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UNIPROT:P51812 ()1-phosphatidylinositol 3-phosphate 5-kinase3-phosphoinositide-dependent protein kinase 1
3-phosphoinositide-dependent protein kinase 1 (Mus)3-phosphoinositide-dependent protein kinase 1 (Rattus)5'-AMP-activated protein kinase catalytic subunit alpha-1
5'-AMP-activated protein kinase catalytic subunit alpha-1 (Mus)AP2-associated protein kinase 1Abelson tyrosine-protein kinase 2 (Mus)
Activated CDC42 kinase 1Aurora kinase AAurora kinase B
Beta-adrenergic receptor kinase 1Beta-adrenergic receptor kinase 1 (Bos)CDC2/CDKX subfamily ()
CK2 subfamily ()Calcium/calmodulin-dependent protein kinase type II alpha chain (Drosophila)Calcium/calmodulin-dependent protein kinase type II subunit alpha
Calcium/calmodulin-dependent protein kinase type II subunit alpha (Rattus)Calcium/calmodulin-dependent protein kinase type IVCasein kinase I isoform alpha
Casein kinase I isoform deltaCasein kinase I subfamily ()Casein kinase II subunit alpha
Casein kinase II subunit alpha'Cyclin-dependent kinase 1Cyclin-dependent kinase 2
Cyclin-dependent kinase 2 (Mus)Cyclin-dependent kinase 3Cyclin-dependent kinase 4
Cyclin-dependent kinase 4 (Mus)Cyclin-dependent kinase 5Cyclin-dependent kinase 5 (Mus)
Cyclin-dependent kinase 6Cyclin-dependent kinase 7Cyclin-dependent kinase 8
Cyclin-dependent kinase 9Cyclin-dependent protein kinase PHO85 (Saccharomyces)DNA-dependent protein kinase catalytic subunit
Death-associated protein kinase 1Death-associated protein kinase 3Dual specificity protein kinase TTK
Dual specificity tyrosine-phosphorylation-regulated kinase 1ADual specificity tyrosine-phosphorylation-regulated kinase 1B (Mus)Dual specificity tyrosine-phosphorylation-regulated kinase 2
Egl nine homolog 1Ephrin type-A receptor 3Ephrin type-B receptor 2
Ephrin type-B receptor 2 (Mus)Epidermal growth factor receptorFocal adhesion kinase 1
G protein-coupled receptor kinase 5GSK-3 subfamily ()Glycogen synthase kinase-3 alpha
Glycogen synthase kinase-3 betaGlycogen synthase kinase-3 beta (Mus)Glycogen synthase kinase-3 beta (Rattus)
Hepatocyte growth factor receptorHigh affinity nerve growth factor receptorHistone acetyltransferase p300
Homeodomain-interacting protein kinase 2Hypoxia-inducible factor 1-alpha inhibitorI-kappa-B kinase subfamily ()
Inhibitor of nuclear factor kappa-B kinase subunit alphaInhibitor of nuclear factor kappa-B kinase subunit betaInhibitor of nuclear factor kappa-B kinase subunit epsilon
Insulin receptorInsulin receptor (Rattus)Insulin-like growth factor 1 receptor
Integrin-linked protein kinaseInterleukin-1 receptor-associated kinase 1Interleukin-1 receptor-associated kinase 4
Leucine-rich repeat serine/threonine-protein kinase 2MAP kinase-activated protein kinase 2MAP kinase-activated protein kinase 5
MAP/microtubule affinity-regulating kinase 3MAP/microtubule affinity-regulating kinase 3 (Mus)Macrophage-stimulating protein receptor
Maternal embryonic leucine zipper kinase (Mus)Mitogen-activated protein kinase 1Mitogen-activated protein kinase 1 (Mus)
Mitogen-activated protein kinase 10Mitogen-activated protein kinase 10 (Mus)Mitogen-activated protein kinase 14
Mitogen-activated protein kinase 15Mitogen-activated protein kinase 3Mitogen-activated protein kinase 3 (Mus)
Mitogen-activated protein kinase 3 (Rattus)Mitogen-activated protein kinase 7Mitogen-activated protein kinase 8
Mitogen-activated protein kinase 8 (Mus)Mitogen-activated protein kinase 9Mitogen-activated protein kinase 9
Mitogen-activated protein kinase 9 (Mus)Mitogen-activated protein kinase kinase kinase 14Mitogen-activated protein kinase kinase kinase 5
Mitogen-activated protein kinase kinase kinase 7 (Mus)Mitogen-activated protein kinase kinase kinase MLTNP_000042 (?)
NP_446294 (?)NUAK family SNF1-like kinase 1Negative regulator of sexual conjugation and meiosis (Schizosaccharomyces)
Neuronal proto-oncogene tyrosine-protein kinase Src (Mus)Non-receptor tyrosine-protein kinase TYK2Nucleoside diphosphate kinase A
PKC subfamily ()Platelet-derived growth factor receptor betaProbable serine/threonine-protein kinase pknG (Mycobacterium)
Protein kinase C alpha typeProtein kinase C beta typeProtein kinase C beta type
Protein kinase C delta typeProtein kinase C delta type (Mus)Protein kinase C epsilon type
Protein kinase C eta typeProtein-tyrosine kinase 2-betaProto-oncogene tyrosine-protein kinase LCK (Mus)
Proto-oncogene tyrosine-protein kinase SrcProto-oncogene tyrosine-protein kinase Src (Rattus)Proto-oncogene tyrosine-protein kinase receptor Ret
Proto-oncogene tyrosine-protein kinase receptor Ret (Mus)RAC subfamily ()RAC-alpha serine/threonine-protein kinase
RAC-alpha serine/threonine-protein kinase (Mus)RAC-alpha serine/threonine-protein kinase (Rattus)RAF proto-oncogene serine/threonine-protein kinase
Receptor tyrosine-protein kinase erbB-2Receptor tyrosine-protein kinase erbB-4Ribosomal protein S6 kinase alpha-1
Ribosomal protein S6 kinase alpha-1 (Rattus)Ribosomal protein S6 kinase alpha-2Ribosomal protein S6 kinase alpha-3 (Mus)
Ribosomal protein S6 kinase beta-1Ribosomal protein S6 kinase beta-1 (Rattus)Serine-protein kinase ATM
Serine-protein kinase ATM (Mus)Serine/threonine-protein kinase 17ASerine/threonine-protein kinase 4
Serine/threonine-protein kinase ATRSerine/threonine-protein kinase BRSK1Serine/threonine-protein kinase BRSK1
Serine/threonine-protein kinase CBK1 (Saccharomyces)Serine/threonine-protein kinase Chk1Serine/threonine-protein kinase Chk2
Serine/threonine-protein kinase D1Serine/threonine-protein kinase Nek6Serine/threonine-protein kinase PAK 1
Serine/threonine-protein kinase PLK1Serine/threonine-protein kinase PLK3Serine/threonine-protein kinase SMG1
Serine/threonine-protein kinase STK11Serine/threonine-protein kinase Sgk1Serine/threonine-protein kinase TBK1
Serine/threonine-protein kinase TOR1 (Saccharomyces)Serine/threonine-protein kinase VRK1Serine/threonine-protein kinase mTOR
Serine/threonine-protein kinase mTOR (Mus)Serine/threonine-protein kinase pim-1Serine/threonine-protein kinase pim-1 (Mus)
Serine/threonine-protein kinase pim-2Serine/threonine-protein kinase pim-3Serine/threonine-protein kinase pim-3 (Mus)
Serine/threonine-protein kinase pknB (Mycobacterium)TP53-regulating kinaseTranscription initiation factor TFIID subunit 1
Tyrosine-protein kinase ABL1Tyrosine-protein kinase ABL1 (Mus)Tyrosine-protein kinase BTK
Tyrosine-protein kinase BlkTyrosine-protein kinase CSKTyrosine-protein kinase FRK
Tyrosine-protein kinase FgrTyrosine-protein kinase FynTyrosine-protein kinase Fyn (Mus)
Tyrosine-protein kinase HCKTyrosine-protein kinase HCK (Mus)Tyrosine-protein kinase JAK1
Tyrosine-protein kinase JAK2Tyrosine-protein kinase JAK2 (Mus)Tyrosine-protein kinase JAK3
Tyrosine-protein kinase LckTyrosine-protein kinase LynTyrosine-protein kinase Lyn (Mus)
Tyrosine-protein kinase SYKTyrosine-protein kinase TXKTyrosine-protein kinase Yes
Tyrosine-protein kinase ZAP-70Tyrosine-protein kinase ZAP-70 (Mus)Vascular endothelial growth factor receptor 3
cAMP subfamily ()cAMP-dependent protein kinase catalytic subunit alphacAMP-dependent protein kinase catalytic subunit alpha (Bos)
cAMP-dependent protein kinase catalytic subunit alpha (Mus)cAMP-dependent protein kinase catalytic subunit alpha (Rattus)cGMP-dependent protein kinase 1


MotifProteinStartEndSwitch TypeSwitch SubtypeSwitch descriptionInformationEvidence

1-phosphatidylinositol 3-phosphate 5-kinase - PIKFYVE -  Homo sapiens
DOC_AGCK_PIF_1 AKT1_HUMAN469474BinaryPhysicochemical compatibilityPhosphorylation of S473 in the PIF motif of RAC-alpha serine/threonine-protein kinase (AKT1) by Serine/threonine-protein kinase mTOR (MTOR) (as part of mTORC2 complex) induces intramolecular interaction with the PIF-binding pocket, resulting in cis-activation of RAC-alpha serine/threonine-protein kinase (AKT1). Dephosphorylation of the PIF motif by PHLPP1/2 (PHLPP1 for Akt2/3 and PHLPP2 for Akt1/3) results in reduced Akt activity, probably by disrupting the interaction with the Akt PIF pocket and thus cis-activation.
details
Inferred

3-phosphoinositide-dependent protein kinase 1 - PDPK1 -  Homo sapiens
DOC_AGCK_PIF_1 AKT1_HUMAN469474BinaryPhysicochemical compatibilityPhosphorylation of S473 in the PIF motif of RAC-alpha serine/threonine-protein kinase (AKT1) by Serine/threonine-protein kinase mTOR (MTOR) (as part of mTORC2 complex) induces intramolecular interaction with the PIF-binding pocket, resulting in cis-activation of RAC-alpha serine/threonine-protein kinase (AKT1). Dephosphorylation of the PIF motif by PHLPP1/2 (PHLPP1 for Akt2/3 and PHLPP2 for Akt1/3) results in reduced Akt activity, probably by disrupting the interaction with the Akt PIF pocket and thus cis-activation.
details
Inferred
DOC_AGCK_PIF_1 AKT1_HUMAN469474BinaryPhysicochemical compatibilityPhosphorylation of S473 in the PIF motif of RAC-alpha serine/threonine-protein kinase (AKT1) by Serine/threonine-protein kinase mTOR (MTOR) (as part of mTORC2 complex) induces intramolecular interaction with the PIF-binding pocket, resulting in cis-activation of RAC-alpha serine/threonine-protein kinase (AKT1). Dephosphorylation of the PIF motif by PHLPP1/2 (PHLPP1 for Akt2/3 and PHLPP2 for Akt1/3) results in reduced Akt activity, probably by disrupting the interaction with the Akt PIF pocket and thus cis-activation.
details
Inferred
LIG_14-3-3_1 M3K5_HUMAN963968BinaryPhysicochemical compatibilityPhosphorylation of S966 in the 14-3-3-binding motif of Mitogen-activated protein kinase kinase kinase 5 (MAP3K5) induces binding to the 14-3-3 protein zeta/delta (YWHAZ) protein. This interaction inhibits the pro-apoptotic activity of Mitogen-activated protein kinase kinase kinase 5 (MAP3K5).
details
Inferred
DOC_AGCK_PIF_1 SGK1_HUMAN418423BinaryPhysicochemical compatibilityPhosphorylation of S422 by Serine/threonine-protein kinase mTOR (MTOR) (as part of mTORC2 complex) in the PIF pocket-binding motif of Serine/threonine-protein kinase Sgk1 (SGK1) induces intramolecular binding and kinase cis-activation.
details
Inferred
LIG_PTB_Phospho_1 ITB3_HUMAN779785BinaryPhysicochemical compatibilityPhosphorylation of T779 in the PTB-binding motif of Integrin beta-3 (ITGB3) inhibits its interaction with SHC-transforming protein 1 (SHC1).
details
Inferred

3-phosphoinositide-dependent protein kinase 1 - PDPK1 -  Mus musculus
DOC_AGCK_PIF_1 KS6A3_MOUSE382387BinaryPhysicochemical compatibilityAuto-phosphorylation of S386 in the PIF pocket-binding motif of Ribosomal protein S6 kinase alpha-3 (Rps6ka3) induces intramolecular binding and kinase cis-activation.
details
Inferred

3-phosphoinositide-dependent protein kinase 1 - PDPK1 -  Rattus norvegicus
DOC_AGCK_PIF_1 KS6B1_RAT408413BinaryPhysicochemical compatibilityPhosphorylation of T412 in the PIF pocket-binding motif of Ribosomal protein S6 kinase beta-1 (Rps6kb1) induces intramolecular binding and kinase cis-activation.
details
Inferred

5'-AMP-activated protein kinase catalytic subunit alpha-1 - PRKAA1 -  Mus musculus
LIG_14-3-3_1 RAF1_HUMAN256261Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in RAF proto-oncogene serine/threonine-protein kinase (RAF1) in response to growth factors induces high-avidity binding to dimeric 14-3-3 protein zeta/delta (YWHAZ), with pS621 being the high-affinity interaction site. This interaction locks RAF proto-oncogene serine/threonine-protein kinase (RAF1) in an inhibited conformation.
details
Inferred
LIG_14-3-3_1 RAF1_HUMAN618623Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in RAF proto-oncogene serine/threonine-protein kinase (RAF1) in response to growth factors induces high-avidity binding to dimeric 14-3-3 protein zeta/delta (YWHAZ), with pS621 being the high-affinity interaction site. This interaction locks RAF proto-oncogene serine/threonine-protein kinase (RAF1) in an inhibited conformation.
details
Inferred

5'-AMP-activated protein kinase catalytic subunit alpha-1 - PRKAA1 -  Homo sapiens
DEG_MDM2_1 P53_HUMAN1926BinaryPhysicochemical compatibilityPhosphorylation of Cellular tumor antigen p53 (TP53) on T18 (in vitro by Casein kinase I subfamily, requiring prior phosphorylation of S15) inhibits its binding to E3 ubiquitin-protein ligase Mdm2 (MDM2). In vivo, T18 is phosphorylated in response to DNA damage.
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_14-3-3_3 CDN1B_HUMAN154159Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in Cyclin-dependent kinase inhibitor 1B (CDKN1B) by RAC-alpha serine/threonine-protein kinase (AKT1) and ribosomal protein S6 kinases (Ribosomal protein S6 kinase alpha-1 (RPS6KA1), Ribosomal protein S6 kinase alpha-3 (RPS6KA3)) induces binding of 14-3-3 dimer. Binding of 14-3-3 results in cytoplasmic localisation of Cyclin-dependent kinase inhibitor 1B (CDKN1B) (see switch details), thereby alleviating Cyclin-dependent kinase inhibitor 1B (CDKN1B)-mediated inhibition of cyclin-dependent kinases and cell cycle progression.
details
Inferred
LIG_14-3-3_3 CDN1B_HUMAN193198Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in Cyclin-dependent kinase inhibitor 1B (CDKN1B) by RAC-alpha serine/threonine-protein kinase (AKT1) and ribosomal protein S6 kinases (Ribosomal protein S6 kinase alpha-1 (RPS6KA1), Ribosomal protein S6 kinase alpha-3 (RPS6KA3)) induces binding of 14-3-3 dimer. Binding of 14-3-3 results in cytoplasmic localisation of Cyclin-dependent kinase inhibitor 1B (CDKN1B) (see switch details), thereby alleviating Cyclin-dependent kinase inhibitor 1B (CDKN1B)-mediated inhibition of cyclin-dependent kinases and cell cycle progression.
details
Inferred

CDC2/CDKX subfamily
DOC_WW_Pin1_4 SMAD3_HUMAN176181SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Curated
MOD_GSK3_1 SMAD3_HUMAN201208SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Curated
LIG_WW_Nedd4L SMAD3_HUMAN203210SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Curated
LIG_WW_1 SMAD3_HUMAN181184SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Curated
LIG_WW_1 SMAD3_HUMAN181184Avidity‑sensingCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Dual phosphorylation of the two NEDD4L-binding sites mediates high-avidity binding of two WW domains of NEDD4L to SMAD3. See also switch details and switch details.
details
Curated
LIG_WW_Nedd4L SMAD3_HUMAN203210Avidity‑sensingCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Dual phosphorylation of the two NEDD4L-binding sites mediates high-avidity binding of two WW domains of NEDD4L to SMAD3. See also switch details and switch details.
details
Curated
LIG_WW_Nedd4L SMAD3_HUMAN203210CumulativeRheostaticCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Phosphorylation of S208 in SMAD3 induces binding of the third WW domain of NEDD4L, while additional phosphorylation of S204 in SMAD3 further increases the affinity of this interaction. See also switch details and switch details.
details
Curated

CK2 subfamily
CLV_C14_caspase-8-10 CASP3_HUMAN172175BinaryPhysicochemical compatibilityPhosphorylation of S176 adjacent to the cleavage motif of Caspase-3 (CASP3) by CK2 subfamily prevents cleavage by Caspase-8 (CASP8) and thus activation of Caspase-3 (CASP3).
details
Curated
CLV_C14_Caspase3-7 PTEN_HUMAN381385BinaryPhysicochemical compatibilityPhosphorylation of S385 adjacent to the cleavage motif of Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (PTEN) by CK2 subfamily prevents cleavage by Caspase-3 (CASP3).
details
Curated
LIG_SUMO_SBM_1 DAXX_HUMAN734740CumulativeRheostaticMultisite phosphorylation of S737 and S739 in the SUMO-binding motif of Death domain-associated protein 6 (DAXX) by CK2 subfamily and CK2 subfamily increases the strength of the interaction with Small ubiquitin-related modifier 1 (SUMO1).
details
Curated
LIG_SUMO_SBM_1 DAXX_HUMAN734740CumulativeRheostaticMultisite phosphorylation of S737 and S739 in the SUMO-binding motif of Death domain-associated protein 6 (DAXX) by CK2 subfamily and CK2 subfamily increases the strength of the interaction with Small ubiquitin-related modifier 1 (SUMO1).
details
Curated
LIG_SUMO_SBM_1 PIAS1_HUMAN457461BinaryPhysicochemical compatibilityPhosphorylation of S466 and S467 and S468 in the SUMO-binding motif of E3 SUMO-protein ligase PIAS1 (PIAS1) by CK2 subfamily and CK2 subfamily and CK2 subfamily increases the strength of its interaction with Small ubiquitin-related modifier 1 (SUMO1).
details
Curated
LIG_SUMO_SBM_1 PIAS1_HUMAN457461BinaryPhysicochemical compatibilityPhosphorylation of S466 and S467 and S468 in the SUMO-binding motif of E3 SUMO-protein ligase PIAS1 (PIAS1) by CK2 subfamily and CK2 subfamily and CK2 subfamily increases the strength of its interaction with Small ubiquitin-related modifier 1 (SUMO1).
details
Curated
LIG_SUMO_SBM_1 PIAS1_HUMAN457461BinaryPhysicochemical compatibilityPhosphorylation of S466 and S467 and S468 in the SUMO-binding motif of E3 SUMO-protein ligase PIAS1 (PIAS1) by CK2 subfamily and CK2 subfamily and CK2 subfamily increases the strength of its interaction with Small ubiquitin-related modifier 1 (SUMO1).
details
Curated
LIG_Clathr_ClatBox_1 AMPH_HUMAN351355BinaryPhysicochemical compatibilityPhosphorylation of T350 adjacent to the clathrin-binding motif of Amphiphysin (AMPH) by CK2 subfamily inhibits binding to the Clathrin heavy chain 1 (CLTC). A second clathrin-binding motif in Amphiphysin (AMPH) is regulated in a similar manner (see switch details). Both these motifs cooperate in avidity-based binding to Clathrin heavy chain 1 (CLTC) (see switch details).
details
Curated
LIG_Clathr_ClatBox_2 AMPH_HUMAN380385BinaryPhysicochemical compatibilityPhosphorylation of T387 adjacent to the clathrin-binding motif of Amphiphysin (AMPH) by CK2 subfamily inhibits binding to the Clathrin heavy chain 1 (CLTC). A second clathrin-binding motif in Amphiphysin (AMPH) is regulated in a similar manner (see switch details). Both these motifs cooperate in avidity-based binding to Clathrin heavy chain 1 (CLTC) (see switch details).
details
Curated

Casein kinase I subfamily
DEG_MDM2_1 P53_HUMAN1926BinaryPhysicochemical compatibilityPhosphorylation of Cellular tumor antigen p53 (TP53) on T18 (in vitro by Casein kinase I subfamily, requiring prior phosphorylation of S15) inhibits its binding to E3 ubiquitin-protein ligase Mdm2 (MDM2). In vivo, T18 is phosphorylated in response to DNA damage.
details
Curated

GSK-3 subfamily
LIG_SH3_2 MYC_HUMAN6065BinaryPhysicochemical compatibilityPhosphorylation of S62 in the SH3-binding motif of Myc proto-oncogene protein (MYC) by GSK-3 subfamily disrupts its interaction with Myc box-dependent-interacting protein 1 (BIN1).
details
Curated
LIG_SxIP_EBH_1 APC_HUMAN28012811CumulativeRheostaticPhosphorylation of S2789 and S2793 adjacent to the EBH-binding motif of Adenomatous polyposis coli protein (APC), by , respectively, gradually reduces the affinity of its interaction with Microtubule-associated protein RP/EB family member 1 (MAPRE1).
details
Curated

I-kappa-B kinase subfamily
LIG_14-3-3_2 TF65_HUMAN4147BinaryPhysicochemical compatibilityPhosphorylation of S45 by in the 14-3-3-binding motif of Transcription factor p65 (RELA) induces binding to the 14-3-3 protein eta (YWHAH) protein.
details
Curated

PKC subfamily
LIG_14-3-3_2 PDE3A_HUMAN424430BinaryPhysicochemical compatibilityPhosphorylation of S428 by in the 14-3-3-binding motif of cGMP-inhibited 3',5'-cyclic phosphodiesterase A (PDE3A) induces binding to the 14-3-3 protein zeta/delta (YWHAZ) protein.
details
Curated
TRG_ER_diArg_1 NMDZ1_HUMAN893895BinaryPhysicochemical compatibilityPhosphorylation of S896 adjacent to the ER retention motif of Glutamate [NMDA] receptor subunit zeta-1 (GRIN1) by PKC subfamily (and possibly S897 by PKA) inactivates the motif and promotes delivery of the receptor to the plasma membrane. Optimal trafficking upon dual phosphorylation of S896 and S897 allows regulation of receptor trafficking by coordinated PKA and PKC signaling.
details
Curated
DOC_CYCLIN_1 AKA12_MOUSE501504BinaryPhysicochemical compatibilityPhosphorylation of S507 adjacent to the cyclin-binding motif of A-kinase anchor protein 12 (Akap12) by PKC subfamily blocks binding to the G1/S-specific cyclin-D1 (Ccnd1). As a result, the function of A-kinase anchor protein 12 (Akap12) as a scaffold is inhibited and G1/S-specific cyclin-D1 (Ccnd1) is translocated to the nucleus where it regulates progression of the cell cycle from G1 to S phase.
details
Curated
LIG_PCNA_PIPBox_1 CDN1A_HUMAN144153BinaryPhysicochemical compatibilityPhosphorylation of S146 in the PCNA-binding motif of Cyclin-dependent kinase inhibitor 1 (CDKN1A) by PKC subfamily inhibits binding to Proliferating cell nuclear antigen (PCNA). As a result, Cyclin-dependent kinase inhibitor 1 (CDKN1A) no longer inhibits Proliferating cell nuclear antigen (PCNA) and blocking of DNA replication is relieved.
details
Curated

RAC subfamily
LIG_SH3_2 PAK1_HUMAN1318BinaryPhysicochemical compatibilityPhosphorylation of S21 adjacent to the SH3-binding motif of Serine/threonine-protein kinase PAK 1 (PAK1) by RAC subfamily inhibits binding to Cytoplasmic protein NCK1 (NCK1), which regulates its localization to focal contacts.
details
Curated

cAMP subfamily
MOD_GSK3_1 NFAC1_HUMAN287294BinaryPhysicochemical compatibilityPhosphorylation of S294 adjacent to the NLS of Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1) by cAMP subfamily primes Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1) for subsequent phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which results in inhibition of nuclear import of Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1).
details
Curated
MOD_GSK3_1 NFAC1_HUMAN238245BinaryPhysicochemical compatibilityPhosphorylation of S245 adjacent to the NLS of Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1) by cAMP subfamily primes Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1) for subsequent phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which results in inhibition of nuclear import of Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1).
details
Curated
LIG_PDZ_Class_1 CCG2_MOUSE318323BinaryPhysicochemical compatibilityPhosphorylation of T321 in the PDZ-binding motif of Voltage-dependent calcium channel gamma-2 subunit (Cacng2) by cAMP subfamily prevents binding to the PDZ domain of Disks large homolog 4 (Dlg4), an interaction involved in regulating synaptic targeting of AMPA-selective glutamate receptors.
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Curated
LIG_PDZ_Class_1 IRK4_HUMAN440445BinaryPhysicochemical compatibilityPhosphorylation of S443 in the PDZ-binding motif of Inward rectifier potassium channel 4 (KCNJ4) by inhibits its interaction with the Disks large homolog 4 (DLG4) protein.
details
Curated
DOC_PP1 NEB1_RAT455461BinaryPhysicochemical compatibilityPhosphorylation of S461 in the PP1-binding motif of Neurabin-1 (Ppp1r9a) by cAMP subfamily inhibits binding to the Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (Ppp1ca). Binding of Neurabin-1 (Ppp1r9a) inhibits activity of the phosphatase.
details
Curated
LIG_PCNA_PIPBox_1 DPOD3_HUMAN456465BinaryPhysicochemical compatibilityPhosphorylation of S458 in the PCNA-binding motif of DNA polymerase delta subunit 3 (POLD3) by cAMP subfamily reduces the affinity of binding to the Proliferating cell nuclear antigen (PCNA) and decreases the processivity of the polymerase complex.
details
Curated

AP2-associated protein kinase 1 - AAK1 -  Homo sapiens
TRG_ENDOCYTIC_2 PPAL_HUMAN413416UncategorisedUncategorisedPhosphorylation of T156 in AP-2 complex subunit mu (AP2M1) by AP2-associated protein kinase 1 (AAK1) upon clathrin recruitment strengthens the interaction between AP-2 complex subunit mu (AP2M1) and cargo proteins.
details
Curated

Abelson tyrosine-protein kinase 2 - ABL2 -  Mus musculus
LIG_GBD_WASP_1 WASL_HUMAN467477UncategorisedUncategorisedPhosphorylation of Neural Wiskott-Aldrich syndrome protein (WASL) at Y256 destabilises the auto-inhibitory intramolecular interaction of Neural Wiskott-Aldrich syndrome protein (WASL).
details
Inferred

Activated CDC42 kinase 1 - TNK2 -  Homo sapiens
LIG_GBD_WASP_1 WASP_HUMAN466476UncategorisedUncategorisedPhosphorylation of Wiskott-Aldrich syndrome protein (WAS) at Y291 by Src kinases, e.g. , destabilises the auto-inhibitory intramolecular interaction of Wiskott-Aldrich syndrome protein (WAS).
details
Inferred

Aurora kinase A - AURKA -  Homo sapiens
DOC_WW_Pin1_4 P53_HUMAN312317BinaryPhysicochemical compatibilityPhosphorylation of S315 in the Pin1-binding motif of Cellular tumor antigen p53 (TP53) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 P53_HUMAN312317BinaryPhysicochemical compatibilityPhosphorylation of S315 in the Pin1-binding motif of Cellular tumor antigen p53 (TP53) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred

Aurora kinase B - AURKB -  Homo sapiens
LIG_SxIP_EBH_1 KIF2C_HUMAN93104BinaryPhysicochemical compatibilityPhosphorylation of S95 and S109 and S111 adjacent to the EB1-binding motif of Kinesin-like protein KIF2C (KIF2C) by Aurora kinase B (AURKB) and Aurora kinase B (AURKB) and Aurora kinase B (AURKB) inhibits its interaction with Microtubule-associated protein RP/EB family member 1 (MAPRE1), thereby inhibiting microtubule tip tracking.
details
Curated
LIG_SxIP_EBH_1 KIF2C_HUMAN93104BinaryPhysicochemical compatibilityPhosphorylation of S95 and S109 and S111 adjacent to the EB1-binding motif of Kinesin-like protein KIF2C (KIF2C) by Aurora kinase B (AURKB) and Aurora kinase B (AURKB) and Aurora kinase B (AURKB) inhibits its interaction with Microtubule-associated protein RP/EB family member 1 (MAPRE1), thereby inhibiting microtubule tip tracking.
details
Curated
LIG_SxIP_EBH_1 KIF2C_HUMAN93104BinaryPhysicochemical compatibilityPhosphorylation of S95 and S109 and S111 adjacent to the EB1-binding motif of Kinesin-like protein KIF2C (KIF2C) by Aurora kinase B (AURKB) and Aurora kinase B (AURKB) and Aurora kinase B (AURKB) inhibits its interaction with Microtubule-associated protein RP/EB family member 1 (MAPRE1), thereby inhibiting microtubule tip tracking.
details
Curated

Beta-adrenergic receptor kinase 1 - ADRBK1 -  Bos taurus
LIG_PDZ_Class_1 PGFRB_HUMAN11011106BinaryPhysicochemical compatibilityPhosphorylation of S1104 in the PDZ-binding motif of Platelet-derived growth factor receptor beta (PDGFRB) by Beta-adrenergic receptor kinase 1 (ADRBK1) inhibits binding to Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (SLC9A3R1). Binding of Platelet-derived growth factor receptor beta (PDGFRB) to Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (SLC9A3R1) potentiates dimerisation and signalling of the receptor, while phosphorylation at S1104 desensitises the receptor.
details
Inferred

Beta-adrenergic receptor kinase 1 - ADRBK1 -  Homo sapiens
LIG_PDZ_Class_1 PGFRB_HUMAN11011106BinaryPhysicochemical compatibilityPhosphorylation of S1104 in the PDZ-binding motif of Platelet-derived growth factor receptor beta (PDGFRB) by Beta-adrenergic receptor kinase 1 (ADRBK1) inhibits binding to Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (SLC9A3R1). Binding of Platelet-derived growth factor receptor beta (PDGFRB) to Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (SLC9A3R1) potentiates dimerisation and signalling of the receptor, while phosphorylation at S1104 desensitises the receptor.
details
Curated

Calcium/calmodulin-dependent protein kinase type II alpha chain - CAMKII -  Drosophila melanogaster
LIG_14-3-3_3 SLOB_DROME5156Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in Slowpoke-binding protein (Slob) by Calcium/calmodulin-dependent protein kinase type II alpha chain (CaMKII) induces high-avidity binding to dimeric 14-3-3 protein zeta (14-3-3zeta). This interaction recruits 14-3-3 protein zeta (14-3-3zeta) to Calcium-activated potassium channel slowpoke (slo) in the presynapse of neuromuscular junctions.
details
Curated
LIG_14-3-3_3 SLOB_DROME7681Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in Slowpoke-binding protein (Slob) by Calcium/calmodulin-dependent protein kinase type II alpha chain (CaMKII) induces high-avidity binding to dimeric 14-3-3 protein zeta (14-3-3zeta). This interaction recruits 14-3-3 protein zeta (14-3-3zeta) to Calcium-activated potassium channel slowpoke (slo) in the presynapse of neuromuscular junctions.
details
Curated

Calcium/calmodulin-dependent protein kinase type II subunit alpha - CAMK2A -  Homo sapiens
LIG_TKB EGFR_HUMAN10691074CumulativeRheostaticWhile phosphorylation of Y1069 induces binding, additional phosphorylation of S1070 and S1071 in the TKB-binding motif of Epidermal growth factor receptor (EGFR) gradually lowers its binding affinity for E3 ubiquitin-protein ligase CBL (CBL).
details
Inferred
LIG_TKB EGFR_HUMAN10691074CumulativeRheostaticWhile phosphorylation of Y1069 induces binding, additional phosphorylation of S1070 and S1071 in the TKB-binding motif of Epidermal growth factor receptor (EGFR) gradually lowers its binding affinity for E3 ubiquitin-protein ligase CBL (CBL).
details
Inferred

Calcium/calmodulin-dependent protein kinase type II subunit alpha - CAMK2A -  Rattus norvegicus
LIG_TKB EGFR_HUMAN10691074CumulativeRheostaticWhile phosphorylation of Y1069 induces binding, additional phosphorylation of S1070 and S1071 in the TKB-binding motif of Epidermal growth factor receptor (EGFR) gradually lowers its binding affinity for E3 ubiquitin-protein ligase CBL (CBL).
details
Inferred
LIG_TKB EGFR_HUMAN10691074CumulativeRheostaticWhile phosphorylation of Y1069 induces binding, additional phosphorylation of S1070 and S1071 in the TKB-binding motif of Epidermal growth factor receptor (EGFR) gradually lowers its binding affinity for E3 ubiquitin-protein ligase CBL (CBL).
details
Inferred

Calcium/calmodulin-dependent protein kinase type IV - CAMK4 -  Homo sapiens
LIG_14-3-3_3 HDAC4_HUMAN629634BinaryPhysicochemical compatibilityPhosphorylation of S632 in the 14-3-3-binding motif of Histone deacetylase 4 (HDAC4) induces binding to the 14-3-3 protein beta/alpha (YWHAB) protein. This interaction sequesters Histone deacetylase 4 (HDAC4) in the cytoplasm, thereby inhibiting their transcription repression activity.
details
Inferred

Casein kinase I isoform alpha - CSNK1A1 -  Homo sapiens
DEG_MDM2_1 P53_HUMAN1926BinaryPhysicochemical compatibilityPhosphorylation of Cellular tumor antigen p53 (TP53) on T18 (in vitro by Casein kinase I subfamily, requiring prior phosphorylation of S15) inhibits its binding to E3 ubiquitin-protein ligase Mdm2 (MDM2). In vivo, T18 is phosphorylated in response to DNA damage.
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred

Casein kinase I isoform delta - CSNK1D -  Homo sapiens
DEG_MDM2_1 P53_HUMAN1926BinaryPhysicochemical compatibilityPhosphorylation of Cellular tumor antigen p53 (TP53) on T18 (in vitro by Casein kinase I subfamily, requiring prior phosphorylation of S15) inhibits its binding to E3 ubiquitin-protein ligase Mdm2 (MDM2). In vivo, T18 is phosphorylated in response to DNA damage.
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred

Casein kinase II subunit alpha - CSNK2A1 -  Homo sapiens
MOD_GSK3_1 JUN_HUMAN236243BinaryPhysicochemical compatibilityPhosphorylation of Transcription factor AP-1 (JUN) at S243 primes the protein for phosphorylation at T239 by Glycogen synthase kinase-3 beta (GSK3B).
details
Inferred
LIG_FHA_2 XRCC1_HUMAN521527BinaryPhysicochemical compatibilityPhosphorylation of T523 in the FHA-binding motif of DNA repair protein XRCC1 (XRCC1) by Casein kinase II subunit alpha (CSNK2A1) induces binding to the Aprataxin (APTX) protein.
details
Curated
LIG_FHA_2 XRCC4_HUMAN231237BinaryPhysicochemical compatibilityPhosphorylation of T233 in the FHA-binding motif of DNA repair protein XRCC4 (XRCC4) by Casein kinase II subunit alpha (CSNK2A1) induces binding to the Bifunctional polynucleotide phosphatase/kinase (PNKP) protein.
details
Curated
DEG_SCF_TRCP1_1 IKBA_HUMAN3136BinaryPhysicochemical compatibilityDual phosphorylation of S32 and S36 in the TrCP1-binding motif of NF-kappa-B inhibitor alpha (NFKBIA) targets the protein to the SCF ubiquitin ligase complex, which marks it for degradation.
details
Inferred
DEG_SCF_TRCP1_1 IKBA_HUMAN3136BinaryPhysicochemical compatibilityDual phosphorylation of S32 and S36 in the TrCP1-binding motif of NF-kappa-B inhibitor alpha (NFKBIA) targets the protein to the SCF ubiquitin ligase complex, which marks it for degradation.
details
Inferred
CLV_C14_Caspase3-7 PTEN_HUMAN381385BinaryPhysicochemical compatibilityPhosphorylation of S385 adjacent to the cleavage motif of Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (PTEN) by CK2 subfamily prevents cleavage by Caspase-3 (CASP3).
details
Inferred
CLV_C14_Caspase3-7 PTEN_HUMAN381385BinaryPhysicochemical compatibilityPhosphorylation of S385 adjacent to the cleavage motif of Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (PTEN) by CK2 subfamily prevents cleavage by Caspase-3 (CASP3).
details
Inferred
LIG_FHA_2 XRCC1_HUMAN517
521
523
527
CumulativeRheostaticTwo Bifunctional polynucleotide phosphatase/kinase (PNKP) molecules interact with two FHA-binding motifs in DNA repair protein XRCC1 (XRCC1) upon phosphorylation of T519 and T523 in the motifs. Additional phosphorylation of S518 and S525 further increases the affinity of the interaction. S518 and T523 are consensus CK2 phosphorylation sites, T519 and S525 atypical.
details
Curated
LIG_FHA_2 XRCC1_HUMAN517
521
523
527
CumulativeRheostaticTwo Bifunctional polynucleotide phosphatase/kinase (PNKP) molecules interact with two FHA-binding motifs in DNA repair protein XRCC1 (XRCC1) upon phosphorylation of T519 and T523 in the motifs. Additional phosphorylation of S518 and S525 further increases the affinity of the interaction. S518 and T523 are consensus CK2 phosphorylation sites, T519 and S525 atypical.
details
Curated
LIG_FHA_2 XRCC1_HUMAN517
521
523
527
CumulativeRheostaticTwo Bifunctional polynucleotide phosphatase/kinase (PNKP) molecules interact with two FHA-binding motifs in DNA repair protein XRCC1 (XRCC1) upon phosphorylation of T519 and T523 in the motifs. Additional phosphorylation of S518 and S525 further increases the affinity of the interaction. S518 and T523 are consensus CK2 phosphorylation sites, T519 and S525 atypical.
details
Curated
LIG_FHA_2 XRCC1_HUMAN517
521
523
527
CumulativeRheostaticTwo Bifunctional polynucleotide phosphatase/kinase (PNKP) molecules interact with two FHA-binding motifs in DNA repair protein XRCC1 (XRCC1) upon phosphorylation of T519 and T523 in the motifs. Additional phosphorylation of S518 and S525 further increases the affinity of the interaction. S518 and T523 are consensus CK2 phosphorylation sites, T519 and S525 atypical.
details
Curated
MOD_GSK3_1 JUN_HUMAN236243SpecificityAltered binding specificityTranscription factor AP-1 (JUN) is primed by an unknown kinase for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets JUN to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks JUN for degradation. In v-Jun (Viral jun-transforming protein (JUN)) the residue corresponding to S243 is mutated to phenylalanine, which protects v-Jun (JUN) from degradation.
details
Inferred
DEG_SCF_FBW7_1 JUN_HUMAN236243SpecificityAltered binding specificityTranscription factor AP-1 (JUN) is primed by an unknown kinase for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets JUN to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks JUN for degradation. In v-Jun (Viral jun-transforming protein (JUN)) the residue corresponding to S243 is mutated to phenylalanine, which protects v-Jun (JUN) from degradation.
details
Inferred
LIG_FHA_2 XRCC1_HUMAN517523Avidity‑sensingHierarchical cooperative binding of two Bifunctional polynucleotide phosphatase/kinase (PNKP) molecules to one DNA repair protein XRCC1 (XRCC1) molecule upon phosphorylation of a primary and secondary FHA-binding motif in DNA repair protein XRCC1 (XRCC1) by Casein kinase II subunit alpha (CSNK2A1).
details
Curated
LIG_FHA_2 XRCC1_HUMAN521527Avidity‑sensingHierarchical cooperative binding of two Bifunctional polynucleotide phosphatase/kinase (PNKP) molecules to one DNA repair protein XRCC1 (XRCC1) molecule upon phosphorylation of a primary and secondary FHA-binding motif in DNA repair protein XRCC1 (XRCC1) by Casein kinase II subunit alpha (CSNK2A1).
details
Curated
LIG_SUMO_SBM_1 DAXX_HUMAN734740CumulativeRheostaticMultisite phosphorylation of S737 and S739 in the SUMO-binding motif of Death domain-associated protein 6 (DAXX) by CK2 subfamily and CK2 subfamily increases the strength of the interaction with Small ubiquitin-related modifier 1 (SUMO1).
details
Inferred
LIG_SUMO_SBM_1 DAXX_HUMAN734740CumulativeRheostaticMultisite phosphorylation of S737 and S739 in the SUMO-binding motif of Death domain-associated protein 6 (DAXX) by CK2 subfamily and CK2 subfamily increases the strength of the interaction with Small ubiquitin-related modifier 1 (SUMO1).
details
Inferred
LIG_SUMO_SBM_1 PIAS1_HUMAN457461BinaryPhysicochemical compatibilityPhosphorylation of S466 and S467 and S468 in the SUMO-binding motif of E3 SUMO-protein ligase PIAS1 (PIAS1) by CK2 subfamily and CK2 subfamily and CK2 subfamily increases the strength of its interaction with Small ubiquitin-related modifier 1 (SUMO1).
details
Inferred
LIG_SUMO_SBM_1 PIAS1_HUMAN457461BinaryPhysicochemical compatibilityPhosphorylation of S466 and S467 and S468 in the SUMO-binding motif of E3 SUMO-protein ligase PIAS1 (PIAS1) by CK2 subfamily and CK2 subfamily and CK2 subfamily increases the strength of its interaction with Small ubiquitin-related modifier 1 (SUMO1).
details
Inferred
LIG_SUMO_SBM_1 PIAS1_HUMAN457461BinaryPhysicochemical compatibilityPhosphorylation of S466 and S467 and S468 in the SUMO-binding motif of E3 SUMO-protein ligase PIAS1 (PIAS1) by CK2 subfamily and CK2 subfamily and CK2 subfamily increases the strength of its interaction with Small ubiquitin-related modifier 1 (SUMO1).
details
Inferred
LIG_Clathr_ClatBox_1 AMPH_HUMAN351355BinaryPhysicochemical compatibilityPhosphorylation of T350 adjacent to the clathrin-binding motif of Amphiphysin (AMPH) by CK2 subfamily inhibits binding to the Clathrin heavy chain 1 (CLTC). A second clathrin-binding motif in Amphiphysin (AMPH) is regulated in a similar manner (see switch details). Both these motifs cooperate in avidity-based binding to Clathrin heavy chain 1 (CLTC) (see switch details).
details
Inferred
LIG_Clathr_ClatBox_2 AMPH_HUMAN380385BinaryPhysicochemical compatibilityPhosphorylation of T387 adjacent to the clathrin-binding motif of Amphiphysin (AMPH) by CK2 subfamily inhibits binding to the Clathrin heavy chain 1 (CLTC). A second clathrin-binding motif in Amphiphysin (AMPH) is regulated in a similar manner (see switch details). Both these motifs cooperate in avidity-based binding to Clathrin heavy chain 1 (CLTC) (see switch details).
details
Inferred

Casein kinase II subunit alpha' - CSNK2A2 -  Homo sapiens
LIG_FHA_2 XRCC1_HUMAN521527BinaryPhysicochemical compatibilityPhosphorylation of T523 in the FHA-binding motif of DNA repair protein XRCC1 (XRCC1) by Casein kinase II subunit alpha (CSNK2A1) induces binding to the Aprataxin (APTX) protein.
details
Inferred
LIG_FHA_2 XRCC1_HUMAN517
521
523
527
CumulativeRheostaticTwo Bifunctional polynucleotide phosphatase/kinase (PNKP) molecules interact with two FHA-binding motifs in DNA repair protein XRCC1 (XRCC1) upon phosphorylation of T519 and T523 in the motifs. Additional phosphorylation of S518 and S525 further increases the affinity of the interaction. S518 and T523 are consensus CK2 phosphorylation sites, T519 and S525 atypical.
details
Inferred
LIG_FHA_2 XRCC1_HUMAN517
521
523
527
CumulativeRheostaticTwo Bifunctional polynucleotide phosphatase/kinase (PNKP) molecules interact with two FHA-binding motifs in DNA repair protein XRCC1 (XRCC1) upon phosphorylation of T519 and T523 in the motifs. Additional phosphorylation of S518 and S525 further increases the affinity of the interaction. S518 and T523 are consensus CK2 phosphorylation sites, T519 and S525 atypical.
details
Inferred
LIG_FHA_2 XRCC1_HUMAN517
521
523
527
CumulativeRheostaticTwo Bifunctional polynucleotide phosphatase/kinase (PNKP) molecules interact with two FHA-binding motifs in DNA repair protein XRCC1 (XRCC1) upon phosphorylation of T519 and T523 in the motifs. Additional phosphorylation of S518 and S525 further increases the affinity of the interaction. S518 and T523 are consensus CK2 phosphorylation sites, T519 and S525 atypical.
details
Inferred
LIG_FHA_2 XRCC1_HUMAN517523Avidity‑sensingHierarchical cooperative binding of two Bifunctional polynucleotide phosphatase/kinase (PNKP) molecules to one DNA repair protein XRCC1 (XRCC1) molecule upon phosphorylation of a primary and secondary FHA-binding motif in DNA repair protein XRCC1 (XRCC1) by Casein kinase II subunit alpha (CSNK2A1).
details
Inferred
LIG_FHA_2 XRCC1_HUMAN521527Avidity‑sensingHierarchical cooperative binding of two Bifunctional polynucleotide phosphatase/kinase (PNKP) molecules to one DNA repair protein XRCC1 (XRCC1) molecule upon phosphorylation of a primary and secondary FHA-binding motif in DNA repair protein XRCC1 (XRCC1) by Casein kinase II subunit alpha (CSNK2A1).
details
Inferred

Cyclin-dependent kinase 1 - CDK1 -  Homo sapiens
LIG_PLK MPIP3_HUMAN129131BinaryPhysicochemical compatibilityPhosphorylation of T130 in the PLK-docking motif of M-phase inducer phosphatase 3 (CDC25C) by Cyclin-dependent kinase 1 (CDK1)-Cyclin AB subfamily generates a recruitment site for Serine/threonine-protein kinase PLK1 (PLK1), which then phosphorylates M-phase inducer phosphatase 3 (CDC25C). This results in inactivation of the NES of M-phase inducer phosphatase 3 (CDC25C), thereby promoting its nuclear localization.
details
Curated
LIG_PLK MPIP2_HUMAN4951BinaryPhysicochemical compatibilityPhosphorylation of S50 in the PLK-docking motif of M-phase inducer phosphatase 2 (CDC25B) by Cyclin-dependent kinase 1 (CDK1)-Cyclin AB subfamily generates a recruitment site for Serine/threonine-protein kinase PLK1 (PLK1), which then phosphorylates and activates M-phase inducer phosphatase 2 (CDC25B).
details
Curated
DOC_WW_Pin1_4 P53_HUMAN312317BinaryPhysicochemical compatibilityPhosphorylation of S315 in the Pin1-binding motif of Cellular tumor antigen p53 (TP53) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
LIG_14-3-3_3 MPIP2_HUMAN320325BinaryPhysicochemical compatibilityPhosphorylation of S321 in the 14-3-3-binding motif of M-phase inducer phosphatase 2 (CDC25B) by Cyclin-dependent kinase 1 (CDK1) during mitosis abolishes binding of the motif, phosphorylated at S323, to 14-3-3 protein beta/alpha (YWHAB), thereby maintaining active Cdc25B.
details
Curated
LIG_PTB_Apo_2 A4_HUMAN756763BinaryPhysicochemical compatibilityPhosphorylation of T743 adjacent to the PTB-binding motif of Amyloid beta A4 protein (APP) reduces the affinity for Amyloid beta A4 precursor protein-binding family B member 1 (APBB1).
details
Inferred
LIG_SxIP_EBH_1 CLAP2_HUMAN515525BinaryPhysicochemical compatibilityPhosphorylation of several serine residues surrounding the EB1-binding motifs of CLIP-associating protein 2 (CLASP2) by Glycogen synthase kinase-3 beta (GSK3B) and Glycogen synthase kinase-3 beta (GSK3B) and Glycogen synthase kinase-3 beta (GSK3B) and Glycogen synthase kinase-3 beta (GSK3B) and Glycogen synthase kinase-3 beta (GSK3B) inhibits its interaction with Microtubule-associated protein RP/EB family member 1 (MAPRE1).
details
Inferred
LIG_SH2_GRB2 A4_HUMAN757760CumulativeRheostaticWhile phosphorylation of Y757 in the SH2-binding motif of Amyloid beta A4 protein (APP) induces binding to Growth factor receptor-bound protein 2 (GRB2), additional phosphorylation of T743 further increases the strength of the interaction.
details
Inferred
LIG_SxIP_EBH_1 APC_HUMAN28012811CumulativeRheostaticPhosphorylation of S2789 and S2793 adjacent to the EBH-binding motif of Adenomatous polyposis coli protein (APC), by , respectively, gradually reduces the affinity of its interaction with Microtubule-associated protein RP/EB family member 1 (MAPRE1).
details
Curated
MOD_CDK MK67I_HUMAN235241SpecificityAltered binding specificityPhosphorylation of T238 of MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by GSK3B. Triple-phosphorylated hNIFK (MKI67IP) binds strongly to Antigen KI-67 (MKI67).
details
Inferred
MOD_GSK3_1 MK67I_HUMAN231238SpecificityAltered binding specificityPhosphorylation of T238 of MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by GSK3B. Triple-phosphorylated hNIFK (MKI67IP) binds strongly to Antigen KI-67 (MKI67).
details
Curated
MOD_GSK3_1 MK67I_HUMAN227234SpecificityAltered binding specificityPhosphorylation of T238 of MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by GSK3B. Triple-phosphorylated hNIFK (MKI67IP) binds strongly to Antigen KI-67 (MKI67).
details
Inferred
LIG_FHA_2 MK67I_HUMAN238244SpecificityAltered binding specificityPhosphorylation of T238 of MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by GSK3B. Triple-phosphorylated hNIFK (MKI67IP) binds strongly to Antigen KI-67 (MKI67).
details
Curated

Cyclin-dependent kinase 2 - CDK2 -  Homo sapiens
MOD_GSK3_1 CCNE1_HUMAN392399BinaryPhysicochemical compatibilityPhosphorylation of G1/S-specific cyclin-E1 (CCNE1) at S399 by Cyclin-dependent kinase 2 (CDK2) primes the protein for subsequent phosphorylation at T395 by Glycogen synthase kinase-3 beta (GSK3B).
details
Curated
DOC_WW_Pin1_4 P53_HUMAN312317BinaryPhysicochemical compatibilityPhosphorylation of S315 in the Pin1-binding motif of Cellular tumor antigen p53 (TP53) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 CDN1B_HUMAN184189BinaryPhysicochemical compatibilityPhosphorylation of T187 in the Pin1-binding motif of Cyclin-dependent kinase inhibitor 1B (CDKN1B) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 CDN1B_HUMAN184189BinaryPhysicochemical compatibilityPhosphorylation of T187 in the Pin1-binding motif of Cyclin-dependent kinase inhibitor 1B (CDKN1B) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 SMAD3_HUMAN176181BinaryPhysicochemical compatibilityPhosphorylation of T179 in the Pin1-binding motif of Mothers against decapentaplegic homolog 3 (SMAD3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 SMAD3_HUMAN210215BinaryPhysicochemical compatibilityPhosphorylation of S213 in the Pin1-binding motif of Mothers against decapentaplegic homolog 3 (SMAD3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
LIG_BRCT_BRCA1_1 ATRIP_HUMAN238242BinaryPhysicochemical compatibilityPhosphorylation of S239 in the BRCT-binding motif of ATR-interacting protein (ATRIP) induces binding to the Breast cancer type 1 susceptibility protein (BRCA1) protein.
details
Inferred
TRG_NLS_Bipartite_1 PTHR_HUMAN124144BinaryPhysicochemical compatibilityPhosphorylation of T121 adjacent to the NLS of Parathyroid hormone-related protein (PTHLH) by Cyclin-dependent kinase 2 (CDK2) disrupts the interaction with Importin subunit beta-1 (KPNB1) and down-regulates nuclear import.
details
Curated
MOD_GSK3_1 CCNE1_HUMAN377384SpecificityAltered binding specificityPhosphorylation of Isoform E-S of G1/S-specific cyclin-E1 (CCNE1) at S384 by CDK2 primes CCNE1 for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B) at T380, which creates a recognition site for F box proteins of the SCF ubiquitin ligase complex (F-box/WD repeat-containing protein 7 (FBXW7)) that target CCNE1 for degradation.
details
Curated
DEG_SCF_FBW7_1 CCNE1_HUMAN378384SpecificityAltered binding specificityPhosphorylation of Isoform E-S of G1/S-specific cyclin-E1 (CCNE1) at S384 by CDK2 primes CCNE1 for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B) at T380, which creates a recognition site for F box proteins of the SCF ubiquitin ligase complex (F-box/WD repeat-containing protein 7 (FBXW7)) that target CCNE1 for degradation.
details
Curated
DOC_WW_Pin1_4 SMAD3_HUMAN176181SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Inferred
MOD_GSK3_1 SMAD3_HUMAN201208SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Inferred
LIG_WW_Nedd4L SMAD3_HUMAN203210SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Inferred
LIG_WW_1 SMAD3_HUMAN181184SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Inferred
MOD_GSK3_1 CCNE1_HUMAN392399SpecificityAltered binding specificityPhosphorylation of G1/S-specific cyclin-E1 (CCNE1) at S399 generates a docking site for Glycogen synthase kinase-3 beta (GSK3B). Subsequent phosphorylation of CCNE1 by Glycogen synthase kinase-3 beta (GSK3B) at T395 switches the specificity of CCNE1 to the F-box/WD repeat-containing protein 7 (FBXW7), which recruits CCNE1 to the SCF ubiquitin ligase complex to mark CCNE1 for degradation.
details
Curated
DEG_SCF_FBW7_1 CCNE1_HUMAN393399SpecificityAltered binding specificityPhosphorylation of G1/S-specific cyclin-E1 (CCNE1) at S399 generates a docking site for Glycogen synthase kinase-3 beta (GSK3B). Subsequent phosphorylation of CCNE1 by Glycogen synthase kinase-3 beta (GSK3B) at T395 switches the specificity of CCNE1 to the F-box/WD repeat-containing protein 7 (FBXW7), which recruits CCNE1 to the SCF ubiquitin ligase complex to mark CCNE1 for degradation.
details
Curated
MOD_CDK_1 CDN1B_HUMAN184190Pre‑assemblyComposite binding site formationBinding of Cyclin-dependent kinase inhibitor 1B (CDKN1B) (p27) to the SCF-Skp2 ubiquitin ligase complex requires phosphorylation of p27 (CDKN1B) at T187, and association of the F-box protein S-phase kinase-associated protein 2 (SKP2) with the regulatory Cyclin-dependent kinases regulatory subunit 1 (CKS1B). SKP2 and CKS1B together generate a composite binding site for p27 (CDKN1B). While some residues, including the phosphorylated T187, bind to CKS1B and others to SKP2, the E185 makes contact with residues of both CKS1B and SKP2.
details
Inferred
MOD_CDK_1 CDN1B_HUMAN184190Pre‑assemblyComposite binding site formationBinding of Cyclin-dependent kinase inhibitor 1B (CDKN1B) (p27) to the SCF-Skp2 ubiquitin ligase complex requires phosphorylation of p27 (CDKN1B) at T187, and association of the F-box protein S-phase kinase-associated protein 2 (SKP2) with the regulatory Cyclin-dependent kinases regulatory subunit 1 (CKS1B). SKP2 and CKS1B together generate a composite binding site for p27 (CDKN1B). While some residues, including the phosphorylated T187, bind to CKS1B and others to SKP2, the E185 makes contact with residues of both CKS1B and SKP2.
details
Inferred
DEG_SCF_SKP2-CKS1_1 CDN1B_HUMAN183190Pre‑assemblyComposite binding site formationBinding of Cyclin-dependent kinase inhibitor 1B (CDKN1B) (p27) to the SCF-Skp2 ubiquitin ligase complex requires phosphorylation of p27 (CDKN1B) at T187, and association of the F-box protein S-phase kinase-associated protein 2 (SKP2) with the regulatory Cyclin-dependent kinases regulatory subunit 1 (CKS1B). SKP2 and CKS1B together generate a composite binding site for p27 (CDKN1B). While some residues, including the phosphorylated T187, bind to CKS1B and others to SKP2, the E185 makes contact with residues of both CKS1B and SKP2.
details
Curated
DEG_SCF_SKP2-CKS1_1 CDN1C_HUMAN306313Pre‑assemblyComposite binding site formationBinding of Cyclin-dependent kinase inhibitor 1C (CDKN1C) (p57) to the SCF-Skp2 ubiquitin ligase complex requires phosphorylation of p57 (CDKN1C) at T310, and association of the F-box protein S-phase kinase-associated protein 2 (SKP2) with the regulatory Cyclin-dependent kinases regulatory subunit 1 (CKS1B). SKP2 and CKS1B together generate a composite binding site for p57 (CDKN1C).
details
Curated

Cyclin-dependent kinase 2 - CDK2 -  Mus musculus
DOC_WW_Pin1_4 CDN1B_HUMAN184189BinaryPhysicochemical compatibilityPhosphorylation of T187 in the Pin1-binding motif of Cyclin-dependent kinase inhibitor 1B (CDKN1B) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 SMAD3_HUMAN176181BinaryPhysicochemical compatibilityPhosphorylation of T179 in the Pin1-binding motif of Mothers against decapentaplegic homolog 3 (SMAD3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 SMAD3_HUMAN210215BinaryPhysicochemical compatibilityPhosphorylation of S213 in the Pin1-binding motif of Mothers against decapentaplegic homolog 3 (SMAD3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 SMAD3_HUMAN176181SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Inferred
MOD_GSK3_1 SMAD3_HUMAN201208SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Inferred
LIG_WW_Nedd4L SMAD3_HUMAN203210SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Inferred
LIG_WW_1 SMAD3_HUMAN181184SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Inferred
MOD_CDK_1 CDN1B_HUMAN184190Pre‑assemblyComposite binding site formationBinding of Cyclin-dependent kinase inhibitor 1B (CDKN1B) (p27) to the SCF-Skp2 ubiquitin ligase complex requires phosphorylation of p27 (CDKN1B) at T187, and association of the F-box protein S-phase kinase-associated protein 2 (SKP2) with the regulatory Cyclin-dependent kinases regulatory subunit 1 (CKS1B). SKP2 and CKS1B together generate a composite binding site for p27 (CDKN1B). While some residues, including the phosphorylated T187, bind to CKS1B and others to SKP2, the E185 makes contact with residues of both CKS1B and SKP2.
details
Inferred
DEG_SCF_SKP2-CKS1_1 CDN1B_HUMAN183190Pre‑assemblyComposite binding site formationBinding of Cyclin-dependent kinase inhibitor 1B (CDKN1B) (p27) to the SCF-Skp2 ubiquitin ligase complex requires phosphorylation of p27 (CDKN1B) at T187, and association of the F-box protein S-phase kinase-associated protein 2 (SKP2) with the regulatory Cyclin-dependent kinases regulatory subunit 1 (CKS1B). SKP2 and CKS1B together generate a composite binding site for p27 (CDKN1B). While some residues, including the phosphorylated T187, bind to CKS1B and others to SKP2, the E185 makes contact with residues of both CKS1B and SKP2.
details
Inferred
DEG_SCF_SKP2-CKS1_1 CDN1C_MOUSE338345Pre‑assemblyComposite binding site formationBinding of Cyclin-dependent kinase inhibitor 1C (Cdkn1c) (p57) to the SCF-Skp2 ubiquitin ligase complex requires phosphorylation of p57 (Cdkn1c) at T342, and association of the F-box protein S-phase kinase-associated protein 2 (SKP2) with the regulatory Cyclin-dependent kinases regulatory subunit 1 (CKS1B). SKP2 and CKS1B together generate a composite binding site for p57 (Cdkn1c).
details
Curated

Cyclin-dependent kinase 3 - CDK3 -  Homo sapiens
DOC_WW_Pin1_4 JUN_HUMAN6065BinaryPhysicochemical compatibilityPhosphorylation of S63 in the Pin1-binding motif of Transcription factor AP-1 (JUN) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 JUN_HUMAN7075BinaryPhysicochemical compatibilityPhosphorylation of S73 in the Pin1-binding motif of Transcription factor AP-1 (JUN) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred

Cyclin-dependent kinase 4 - CDK4 -  Homo sapiens
DOC_WW_Pin1_4 SMAD3_HUMAN176181BinaryPhysicochemical compatibilityPhosphorylation of T179 in the Pin1-binding motif of Mothers against decapentaplegic homolog 3 (SMAD3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 SMAD3_HUMAN176181BinaryPhysicochemical compatibilityPhosphorylation of T179 in the Pin1-binding motif of Mothers against decapentaplegic homolog 3 (SMAD3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 SMAD3_HUMAN201206BinaryPhysicochemical compatibilityPhosphorylation of S204 in the Pin1-binding motif of Mothers against decapentaplegic homolog 3 (SMAD3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 SMAD3_HUMAN205210BinaryPhysicochemical compatibilityPhosphorylation of S208 in the Pin1-binding motif of Mothers against decapentaplegic homolog 3 (SMAD3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 SMAD3_HUMAN210215BinaryPhysicochemical compatibilityPhosphorylation of S213 in the Pin1-binding motif of Mothers against decapentaplegic homolog 3 (SMAD3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 SMAD3_HUMAN210215BinaryPhysicochemical compatibilityPhosphorylation of S213 in the Pin1-binding motif of Mothers against decapentaplegic homolog 3 (SMAD3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 SMAD3_HUMAN176181SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Inferred
DOC_WW_Pin1_4 SMAD3_HUMAN176181SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Inferred
MOD_GSK3_1 SMAD3_HUMAN201208SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Inferred
MOD_GSK3_1 SMAD3_HUMAN201208SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Inferred
LIG_WW_Nedd4L SMAD3_HUMAN203210SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Inferred
LIG_WW_Nedd4L SMAD3_HUMAN203210SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Inferred
LIG_WW_1 SMAD3_HUMAN181184SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Inferred
LIG_WW_1 SMAD3_HUMAN181184SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Inferred
LIG_WW_1 SMAD3_HUMAN181184Avidity‑sensingCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Dual phosphorylation of the two NEDD4L-binding sites mediates high-avidity binding of two WW domains of NEDD4L to SMAD3. See also switch details and switch details.
details
Inferred
LIG_WW_1 SMAD3_HUMAN181184Avidity‑sensingCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Dual phosphorylation of the two NEDD4L-binding sites mediates high-avidity binding of two WW domains of NEDD4L to SMAD3. See also switch details and switch details.
details
Inferred
LIG_WW_Nedd4L SMAD3_HUMAN203210Avidity‑sensingCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Dual phosphorylation of the two NEDD4L-binding sites mediates high-avidity binding of two WW domains of NEDD4L to SMAD3. See also switch details and switch details.
details
Inferred
LIG_WW_Nedd4L SMAD3_HUMAN203210Avidity‑sensingCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Dual phosphorylation of the two NEDD4L-binding sites mediates high-avidity binding of two WW domains of NEDD4L to SMAD3. See also switch details and switch details.
details
Inferred
LIG_WW_Nedd4L SMAD3_HUMAN203210CumulativeRheostaticCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Phosphorylation of S208 in SMAD3 induces binding of the third WW domain of NEDD4L, while additional phosphorylation of S204 in SMAD3 further increases the affinity of this interaction. See also switch details and switch details.
details
Inferred
LIG_WW_Nedd4L SMAD3_HUMAN203210CumulativeRheostaticCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Phosphorylation of S208 in SMAD3 induces binding of the third WW domain of NEDD4L, while additional phosphorylation of S204 in SMAD3 further increases the affinity of this interaction. See also switch details and switch details.
details
Inferred

Cyclin-dependent kinase 4 - CDK4 -  Mus musculus
DOC_WW_Pin1_4 SMAD3_HUMAN176181BinaryPhysicochemical compatibilityPhosphorylation of T179 in the Pin1-binding motif of Mothers against decapentaplegic homolog 3 (SMAD3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 SMAD3_HUMAN210215BinaryPhysicochemical compatibilityPhosphorylation of S213 in the Pin1-binding motif of Mothers against decapentaplegic homolog 3 (SMAD3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 SMAD3_HUMAN176181SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Inferred
MOD_GSK3_1 SMAD3_HUMAN201208SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Inferred
LIG_WW_Nedd4L SMAD3_HUMAN203210SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Inferred
LIG_WW_1 SMAD3_HUMAN181184SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Inferred

Cyclin-dependent kinase 5 - CDK5 -  Mus musculus
LIG_PTB_Talin PI51C_MOUSE645648BinaryPhysicochemical compatibilityPhosphorylation of S645 in the PTB-binding motif of Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma (Pip5k1c) by Cyclin-dependent kinase 5 (Cdk5) inhibits its interaction with Talin-1 (Tln1).
details
Curated
TRG_AP2beta_CARGO_2 PI51C_MOUSE633644BinaryPhysicochemical compatibilityPhosphorylation of S645 in Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma (Pip5k1c) impedes binding to AP-2 complex subunit beta (Ap2b1), while dephosphorylation by calcineurin promotes binding. These phosphorylation and dephosphorylation events are important for the regulation of clathrin coat formation associated with synaptic vesicles.
details
Curated
TRG_ENDOCYTIC_2 PI51C_HUMAN649652BinaryPhysicochemical compatibilityPhosphorylation of S645 near the AP2-binding motif of Phosphatidylinositol-4-phosphate 5-kinase type-1 gamma (PIP5K1C) by Cyclin-dependent kinase 5 (Cdk5) inhibits its interaction with AP-2 complex subunit mu (AP2M1).
details
Curated

Cyclin-dependent kinase 5 - CDK5 -  Homo sapiens
MOD_GSK3_1 MYC_HUMAN5562BinaryPhysicochemical compatibilityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 primes the protein for phosphorylation at T58 by Glycogen synthase kinase-3 beta (GSK3B).
details
Inferred
DOC_WW_Pin1_4 CTNB1_HUMAN243248BinaryPhysicochemical compatibilityPhosphorylation of S246 in the Pin1-binding motif of Catenin beta-1 (CTNNB1) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 FAK1_HUMAN907912BinaryPhysicochemical compatibilityPhosphorylation of S910 in the Pin1-binding motif of Focal adhesion kinase 1 (PTK2) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
LIG_SH3_2 MYC_HUMAN6065BinaryPhysicochemical compatibilityPhosphorylation of S62 in the SH3-binding motif of Myc proto-oncogene protein (MYC) by GSK-3 subfamily disrupts its interaction with Myc box-dependent-interacting protein 1 (BIN1).
details
Inferred
LIG_PH_Tfb1 P53_HUMAN5056CumulativeRheostaticMultisite phosphorylation of S46 and T55 in the PH-like binding motif of Cellular tumor antigen p53 (TP53) gradually enhances its affinity for General transcription factor IIH subunit 1 (GTF2H1), an interaction involved in activation of transcription initiation and elongation by Cellular tumor antigen p53 (TP53).
details
Inferred
MOD_ProDKin_1 MYC_HUMAN5965SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Inferred
MOD_GSK3_1 MYC_HUMAN5562SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Inferred
DEG_SCF_FBW7_1 MYC_HUMAN5562SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred

Cyclin-dependent kinase 6 - CDK6 -  Homo sapiens
DOC_WW_Pin1_4 CDN1B_HUMAN184189BinaryPhysicochemical compatibilityPhosphorylation of T187 in the Pin1-binding motif of Cyclin-dependent kinase inhibitor 1B (CDKN1B) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
MOD_CDK_1 CDN1B_HUMAN184190Pre‑assemblyComposite binding site formationBinding of Cyclin-dependent kinase inhibitor 1B (CDKN1B) (p27) to the SCF-Skp2 ubiquitin ligase complex requires phosphorylation of p27 (CDKN1B) at T187, and association of the F-box protein S-phase kinase-associated protein 2 (SKP2) with the regulatory Cyclin-dependent kinases regulatory subunit 1 (CKS1B). SKP2 and CKS1B together generate a composite binding site for p27 (CDKN1B). While some residues, including the phosphorylated T187, bind to CKS1B and others to SKP2, the E185 makes contact with residues of both CKS1B and SKP2.
details
Inferred
DEG_SCF_SKP2-CKS1_1 CDN1B_HUMAN183190Pre‑assemblyComposite binding site formationBinding of Cyclin-dependent kinase inhibitor 1B (CDKN1B) (p27) to the SCF-Skp2 ubiquitin ligase complex requires phosphorylation of p27 (CDKN1B) at T187, and association of the F-box protein S-phase kinase-associated protein 2 (SKP2) with the regulatory Cyclin-dependent kinases regulatory subunit 1 (CKS1B). SKP2 and CKS1B together generate a composite binding site for p27 (CDKN1B). While some residues, including the phosphorylated T187, bind to CKS1B and others to SKP2, the E185 makes contact with residues of both CKS1B and SKP2.
details
Inferred

Cyclin-dependent kinase 7 - CDK7 -  Homo sapiens
DOC_WW_Pin1_4 RARA_HUMAN7479BinaryPhysicochemical compatibilityPhosphorylation of S77 in the Pin1-binding motif of Retinoic acid receptor alpha (RARA) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 RARA_HUMAN7479BinaryPhysicochemical compatibilityPhosphorylation of S77 in the Pin1-binding motif of Retinoic acid receptor alpha (RARA) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 STF1_MOUSE200205BinaryPhysicochemical compatibilityPhosphorylation of S203 in the Pin1-binding motif of Steroidogenic factor 1 (Nr5a1) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred

Cyclin-dependent kinase 8 - CDK8 -  Homo sapiens
DOC_WW_Pin1_4 SMAD3_HUMAN176181BinaryPhysicochemical compatibilityPhosphorylation of T179 in the Pin1-binding motif of Mothers against decapentaplegic homolog 3 (SMAD3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 SMAD3_HUMAN205210BinaryPhysicochemical compatibilityPhosphorylation of S208 in the Pin1-binding motif of Mothers against decapentaplegic homolog 3 (SMAD3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 SMAD3_HUMAN210215BinaryPhysicochemical compatibilityPhosphorylation of S213 in the Pin1-binding motif of Mothers against decapentaplegic homolog 3 (SMAD3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 SMAD3_HUMAN176181SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Inferred
MOD_GSK3_1 SMAD3_HUMAN201208SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Inferred
LIG_WW_Nedd4L SMAD3_HUMAN203210SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Inferred
LIG_WW_1 SMAD3_HUMAN181184SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Inferred
LIG_WW_1 SMAD3_HUMAN181184Avidity‑sensingCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Dual phosphorylation of the two NEDD4L-binding sites mediates high-avidity binding of two WW domains of NEDD4L to SMAD3. See also switch details and switch details.
details
Inferred
LIG_WW_Nedd4L SMAD3_HUMAN203210Avidity‑sensingCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Dual phosphorylation of the two NEDD4L-binding sites mediates high-avidity binding of two WW domains of NEDD4L to SMAD3. See also switch details and switch details.
details
Inferred
LIG_WW_Nedd4L SMAD3_HUMAN203210CumulativeRheostaticCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Phosphorylation of S208 in SMAD3 induces binding of the third WW domain of NEDD4L, while additional phosphorylation of S204 in SMAD3 further increases the affinity of this interaction. See also switch details and switch details.
details
Inferred

Cyclin-dependent kinase 9 - CDK9 -  Homo sapiens
DOC_WW_Pin1_4 P53_HUMAN312317BinaryPhysicochemical compatibilityPhosphorylation of S315 in the Pin1-binding motif of Cellular tumor antigen p53 (TP53) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 SMAD3_HUMAN176181BinaryPhysicochemical compatibilityPhosphorylation of T179 in the Pin1-binding motif of Mothers against decapentaplegic homolog 3 (SMAD3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 SMAD3_HUMAN205210BinaryPhysicochemical compatibilityPhosphorylation of S208 in the Pin1-binding motif of Mothers against decapentaplegic homolog 3 (SMAD3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 SMAD3_HUMAN210215BinaryPhysicochemical compatibilityPhosphorylation of S213 in the Pin1-binding motif of Mothers against decapentaplegic homolog 3 (SMAD3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 SMAD3_HUMAN176181SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Inferred
MOD_GSK3_1 SMAD3_HUMAN201208SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Inferred
LIG_WW_Nedd4L SMAD3_HUMAN203210SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Inferred
LIG_WW_1 SMAD3_HUMAN181184SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_WW_1 SMAD3_HUMAN181184Avidity‑sensingCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Dual phosphorylation of the two NEDD4L-binding sites mediates high-avidity binding of two WW domains of NEDD4L to SMAD3. See also switch details and switch details.
details
Inferred
LIG_WW_Nedd4L SMAD3_HUMAN203210Avidity‑sensingCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Dual phosphorylation of the two NEDD4L-binding sites mediates high-avidity binding of two WW domains of NEDD4L to SMAD3. See also switch details and switch details.
details
Inferred
LIG_WW_Nedd4L SMAD3_HUMAN203210CumulativeRheostaticCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Phosphorylation of S208 in SMAD3 induces binding of the third WW domain of NEDD4L, while additional phosphorylation of S204 in SMAD3 further increases the affinity of this interaction. See also switch details and switch details.
details
Inferred

Cyclin-dependent protein kinase PHO85 - PHO85 -  Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
LIG_14-3-3_3 RIM15_YEAST10721077BinaryPhysicochemical compatibilityPhosphorylation of T1075 in the 14-3-3-binding motif of Serine/threonine-protein kinase RIM15 (RIM15) induces binding to the Protein BMH2 (BMH2) protein. This interaction sequesters Serine/threonine-protein kinase RIM15 (RIM15) in the cytoplasm, thereby inhibiting its function.
details
Curated
TRG_NLS_MonoExtC_3 PHO4_YEAST156161BinaryPhysicochemical compatibilityPhosphorylation of S152 adjacent to the NLS of Phosphate system positive regulatory protein PHO4 (PHO4) by the Pho80-Pho85 CDK-Cyclin complex inhibits nuclear import this protein by blocking its interaction with Importin subunit beta-3 (PSE1). Upon phosphate starvation, Pho81 inhibits the Pho80-Pho85 complex, leading to translocation of Phosphate system positive regulatory protein PHO4 (PHO4) to the nucleus, where it regulates expression of phosphate-responsive genes.
details
Curated

DNA-dependent protein kinase catalytic subunit - PRKDC -  Homo sapiens
DOC_AGCK_PIF_1 AKT1_HUMAN469474BinaryPhysicochemical compatibilityPhosphorylation of S473 in the PIF motif of RAC-alpha serine/threonine-protein kinase (AKT1) by Serine/threonine-protein kinase mTOR (MTOR) (as part of mTORC2 complex) induces intramolecular interaction with the PIF-binding pocket, resulting in cis-activation of RAC-alpha serine/threonine-protein kinase (AKT1). Dephosphorylation of the PIF motif by PHLPP1/2 (PHLPP1 for Akt2/3 and PHLPP2 for Akt1/3) results in reduced Akt activity, probably by disrupting the interaction with the Akt PIF pocket and thus cis-activation.
details
Inferred
MOD_GSK3_1 P53_HUMAN3037BinaryPhysicochemical compatibilityPhosphorylation of Cellular tumor antigen p53 (TP53) at S37 primes the protein for phosphorylation at S33 by Glycogen synthase kinase-3 beta (GSK3B).
details
Curated
LIG_BRCT_MDC1_1 H2AX_HUMAN139143BinaryPhysicochemical compatibilityPhosphorylation of S140 in the BRCT-binding motif of Histone H2A.x (H2AFX) induces binding to the Mediator of DNA damage checkpoint protein 1 (MDC1) protein.
details
Curated
LIG_FHA_1 CHK2_HUMAN6672BinaryPhysicochemical compatibilityPhosphorylation of T68 in the FHA-binding motif of Serine/threonine-protein kinase Chk2 (CHEK2) induces binding to the Serine/threonine-protein kinase Chk2 (CHEK2) protein.
details
Inferred
LIG_PH_Tfb1 P53_HUMAN5056CumulativeRheostaticMultisite phosphorylation of S46 and T55 in the PH-like binding motif of Cellular tumor antigen p53 (TP53) gradually enhances its affinity for General transcription factor IIH subunit 1 (GTF2H1), an interaction involved in activation of transcription initiation and elongation by Cellular tumor antigen p53 (TP53).
details
Inferred
DEG_MDM2_1 P53_HUMAN1926BinaryPhysicochemical compatibilityPhosphorylation of Cellular tumor antigen p53 (TP53) on T18 (in vitro by Casein kinase I subfamily, requiring prior phosphorylation of S15) inhibits its binding to E3 ubiquitin-protein ligase Mdm2 (MDM2). In vivo, T18 is phosphorylated in response to DNA damage.
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred

Death-associated protein kinase 1 - DAPK1 -  Homo sapiens
DEG_MDM2_1 P53_HUMAN1926BinaryPhysicochemical compatibilityPhosphorylation of Cellular tumor antigen p53 (TP53) on T18 (in vitro by Casein kinase I subfamily, requiring prior phosphorylation of S15) inhibits its binding to E3 ubiquitin-protein ligase Mdm2 (MDM2). In vivo, T18 is phosphorylated in response to DNA damage.
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred

Death-associated protein kinase 3 - DAPK3 -  Homo sapiens
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_PCNA_PIPBox_1 CDN1A_HUMAN144153BinaryPhysicochemical compatibilityPhosphorylation of T145 in the PCNA-binding motif of Cyclin-dependent kinase inhibitor 1 (CDKN1A) by RAC-alpha serine/threonine-protein kinase (AKT1) inhibits binding to Proliferating cell nuclear antigen (PCNA). As a result, Cyclin-dependent kinase inhibitor 1 (CDKN1A) no longer inhibits Proliferating cell nuclear antigen (PCNA) and blocking of DNA replication is relieved.
details
Inferred

Dual specificity protein kinase TTK - TTK -  Homo sapiens
LIG_FHA_1 CHK2_HUMAN6672BinaryPhysicochemical compatibilityPhosphorylation of T68 in the FHA-binding motif of Serine/threonine-protein kinase Chk2 (CHEK2) induces binding to the Serine/threonine-protein kinase Chk2 (CHEK2) protein.
details
Inferred
LIG_FHA_1 CHK2_HUMAN6672BinaryPhysicochemical compatibilityPhosphorylation of T68 in the FHA-binding motif of Serine/threonine-protein kinase Chk2 (CHEK2) induces binding to the Serine/threonine-protein kinase Chk2 (CHEK2) protein.
details
Inferred
DEG_MDM2_1 P53_HUMAN1926BinaryPhysicochemical compatibilityPhosphorylation of Cellular tumor antigen p53 (TP53) on T18 (in vitro by Casein kinase I subfamily, requiring prior phosphorylation of S15) inhibits its binding to E3 ubiquitin-protein ligase Mdm2 (MDM2). In vivo, T18 is phosphorylated in response to DNA damage.
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred

Dual specificity tyrosine-phosphorylation-regulated kinase 1A - DYRK1A -  Homo sapiens
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred

Dual specificity tyrosine-phosphorylation-regulated kinase 1B - DYRK1B -  Mus musculus
DOC_WW_Pin1_4 CCND1_MOUSE283288BinaryPhysicochemical compatibilityPhosphorylation of T286 in the Pin1-binding motif of G1/S-specific cyclin-D1 (Ccnd1) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details
Inferred

Dual specificity tyrosine-phosphorylation-regulated kinase 2 - DYRK2 -  Homo sapiens
LIG_PH_Tfb1 P53_HUMAN5056CumulativeRheostaticMultisite phosphorylation of S46 and T55 in the PH-like binding motif of Cellular tumor antigen p53 (TP53) gradually enhances its affinity for General transcription factor IIH subunit 1 (GTF2H1), an interaction involved in activation of transcription initiation and elongation by Cellular tumor antigen p53 (TP53).
details
Inferred
LIG_PH_Tfb1 P53_HUMAN5056CumulativeRheostaticMultisite phosphorylation of S46 and T55 in the PH-like binding motif of Cellular tumor antigen p53 (TP53) gradually enhances its affinity for General transcription factor IIH subunit 1 (GTF2H1), an interaction involved in activation of transcription initiation and elongation by Cellular tumor antigen p53 (TP53).
details
Inferred
LIG_PH_Tfb1 P53_HUMAN5056CumulativeRheostaticMultisite phosphorylation of S46 and T55 in the PH-like binding motif of Cellular tumor antigen p53 (TP53) gradually enhances its affinity for General transcription factor IIH subunit 1 (GTF2H1), an interaction involved in activation of transcription initiation and elongation by Cellular tumor antigen p53 (TP53).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_eIF4E_1 4EBP1_HUMAN5460BinaryPhysicochemical compatibilityPhosphorylation of S65 flanking the eIF4E-binding motif of Eukaryotic translation initiation factor 4E-binding protein 1 (EIF4EBP1) by Serine/threonine-protein kinase mTOR (MTOR) inhibits binding to Eukaryotic translation initiation factor 4E (EIF4E) in response to growth factors and nutrients. This results in release of Eukaryotic translation initiation factor 4E (EIF4E), which associates with other initiation factors to form the eIF-4F complex that mediates initiation of translation. However, disruption of the interaction between Eukaryotic translation initiation factor 4E-binding protein 1 (EIF4EBP1) and Eukaryotic translation initiation factor 4E (EIF4E) has been shown to be dependent on hyperphosphorylation of Eukaryotic translation initiation factor 4E-binding protein 1 (EIF4EBP1) by FRAP/mTOR, PI3K and ERK pathways. According to the current model, Eukaryotic translation initiation factor 4E-binding protein 1 (EIF4EBP1) is phosphorylated on multiple residues in a well-defined order. Basal phosphorylation of T37 and T46 serves as a priming event for subsequent serum-induced phosphorylation of T70, which primes for subsequent phosphorylation of S65.
details
Inferred

Egl nine homolog 1 - EGLN1 -  Homo sapiens
DEG_ODPH_VHL_1 HIF1A_HUMAN400413BinaryPhysicochemical compatibilityHydroxylation of P402 in the VHL-binding motif of Hypoxia-inducible factor 1-alpha (HIF1A) induces binding to the Von Hippel-Lindau disease tumor suppressor (VHL) protein.
details
Curated
DEG_ODPH_VHL_1 HIF1A_HUMAN562574BinaryPhysicochemical compatibilityHydroxylation of P564 in the VHL-binding motif of Hypoxia-inducible factor 1-alpha (HIF1A) induces binding to the Von Hippel-Lindau disease tumor suppressor (VHL) protein.
details
Curated
DEG_ODPH_VHL_1 EPAS1_HUMAN403416BinaryPhysicochemical compatibilityHydroxylation of P405 in the VHL-binding motif of Endothelial PAS domain-containing protein 1 (EPAS1) induces binding to the Von Hippel-Lindau disease tumor suppressor (VHL) protein.
details
Curated
DEG_ODPH_VHL_1 EPAS1_HUMAN529542BinaryPhysicochemical compatibilityHydroxylation of P531 in the VHL-binding motif of Endothelial PAS domain-containing protein 1 (EPAS1) induces binding to the Von Hippel-Lindau disease tumor suppressor (VHL) protein.
details
Curated
DEG_ODPH_VHL_1 HIF3A_HUMAN490502BinaryPhysicochemical compatibilityHydroxylation of P492 in the VHL-binding motif of Hypoxia-inducible factor 3-alpha (HIF3A) induces binding to the Von Hippel-Lindau disease tumor suppressor (VHL) protein.
details
Curated

Ephrin type-A receptor 3 - EPHA3 -  Homo sapiens
LIG_SH2_IA EPHA3_HUMAN597606BinaryPhysicochemical compatibilityPhosphorylation of Y602 in the SH2-binding motif of Ephrin type-A receptor 3 (EPHA3) induces binding to the Cytoplasmic protein NCK1 (NCK1) protein.
details
Inferred

Ephrin type-B receptor 2 - EPHB2 -  Homo sapiens
LIG_SH2_IB EPHB2_MOUSE601610BinaryPhysicochemical compatibilityPhosphorylation of Y604 in the SH2-binding motif of Ephrin type-B receptor 2 (Ephb2) induces binding to the Adapter molecule crk (CRK) protein.
details
Inferred
LIG_SH2_IB EPHB2_MOUSE606620BinaryPhysicochemical compatibilityPhosphorylation of Y610 in the SH2-binding motif of Ephrin type-B receptor 2 (Ephb2) induces binding to the Adapter molecule crk (CRK) protein.
details
Inferred
LIG_SH2_IB EPHB2_MOUSE606620BinaryPhysicochemical compatibilityPhosphorylation of Y610 in the SH2-binding motif of Ephrin type-B receptor 2 (Ephb2) induces binding to the Adapter molecule crk (CRK) protein.
details
Inferred
LIG_SH2_IB EPHB2_MOUSE606620BinaryPhysicochemical compatibilityPhosphorylation of Y610 in the SH2-binding motif of Ephrin type-B receptor 2 (Ephb2) induces binding to the Adapter molecule crk (CRK) protein.
details
Inferred

Ephrin type-B receptor 2 - EPHB2 -  Mus musculus
LIG_SH2_IB EPHB2_MOUSE601610BinaryPhysicochemical compatibilityPhosphorylation of Y604 in the SH2-binding motif of Ephrin type-B receptor 2 (Ephb2) induces binding to the Adapter molecule crk (CRK) protein.
details
Inferred
LIG_SH2_IB EPHB2_MOUSE606620BinaryPhysicochemical compatibilityPhosphorylation of Y610 in the SH2-binding motif of Ephrin type-B receptor 2 (Ephb2) induces binding to the Adapter molecule crk (CRK) protein.
details
Inferred

Epidermal growth factor receptor - EGFR -  Homo sapiens
LIG_PTB_Phospho_1 EGFR_HUMAN11041110BinaryPhysicochemical compatibilityPhosphorylation of Y1110 in the PTB-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Docking protein 1 (DOK1) protein.
details
Inferred
LIG_PTB_Phospho_1 EGFR_HUMAN11041110BinaryPhysicochemical compatibilityPhosphorylation of Y1110 in the PTB-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Docking protein 1 (DOK1) protein.
details
Inferred
LIG_SH2_IC EGFR_HUMAN10921100BinaryPhysicochemical compatibilityPhosphorylation of Y1092 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.
details
Inferred
LIG_SH2_IC EGFR_HUMAN10921100BinaryPhysicochemical compatibilityPhosphorylation of Y1092 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.
details
Inferred
LIG_SH2_IE EGFR_HUMAN10111020BinaryPhysicochemical compatibilityPhosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Ras and Rab interactor 1 (RIN1) protein.
details
Inferred
LIG_SH2_IE EGFR_HUMAN11911200BinaryPhysicochemical compatibilityPhosphorylation of Y1197 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Ras and Rab interactor 1 (RIN1) protein.
details
Inferred
LIG_SH2_IE EGFR_HUMAN11911200BinaryPhysicochemical compatibilityPhosphorylation of Y1197 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Ras and Rab interactor 1 (RIN1) protein.
details
Inferred
LIG_SH2_IE EGFR_HUMAN10081024BinaryPhysicochemical compatibilityPhosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Tyrosine-protein kinase JAK1 (JAK1) protein.
details
Inferred
LIG_SH2_IE EGFR_HUMAN10081024BinaryPhysicochemical compatibilityPhosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Tyrosine-protein kinase JAK2 (JAK2) protein.
details
Inferred
LIG_SH2_ID EGFR_HUMAN10081024BinaryPhysicochemical compatibilityPhosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the SH2 domain-containing protein 3C (SH2D3C) protein.
details
Inferred
LIG_SH2_ID EGFR_HUMAN10081024BinaryPhysicochemical compatibilityPhosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the SH2 domain-containing protein 3A (SH2D3A) protein.
details
Inferred
LIG_SH2_III EGFR_HUMAN10081024BinaryPhysicochemical compatibilityPhosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Signal transducer and activator of transcription 6 (STAT6) protein.
details
Inferred
LIG_SH2_SRC EGFR_HUMAN10161019BinaryPhysicochemical compatibilityPhosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1 (PLCG1).
details
Inferred
LIG_SH2_SRC EGFR_HUMAN10161019BinaryPhysicochemical compatibilityPhosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to Cytoplasmic protein NCK1 (NCK1).
details
Inferred
LIG_SH2_STAT5 GAB1_HUMAN472475BinaryPhysicochemical compatibilityPhosphorylation of Y472 in the SH2-binding motif of GRB2-associated-binding protein 1 (GAB1) induces binding to Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1).
details
Inferred
LIG_SH2_STAT5 GAB1_HUMAN472475BinaryPhysicochemical compatibilityPhosphorylation of Y472 in the SH2-binding motif of GRB2-associated-binding protein 1 (GAB1) induces binding to Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1).
details
Inferred
LIG_SH2_STAT5 GAB1_HUMAN447450BinaryPhysicochemical compatibilityPhosphorylation of Y447 in the SH2-binding motif of GRB2-associated-binding protein 1 (GAB1) induces binding to Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1).
details
Inferred
LIG_SH2_STAT5 GAB1_HUMAN447450BinaryPhysicochemical compatibilityPhosphorylation of Y447 in the SH2-binding motif of GRB2-associated-binding protein 1 (GAB1) induces binding to Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1).
details
Inferred

Focal adhesion kinase 1 - PTK2 -  Homo sapiens
LIG_SH2_IA FAK1_HUMAN389405BinaryPhysicochemical compatibilityPhosphorylation of Y397 in the SH2-binding motif of Focal adhesion kinase 1 (PTK2) induces binding to the Cytoplasmic protein NCK2 (NCK2) protein.
details
Inferred
LIG_SH2_IA FAK1_HUMAN389405BinaryPhysicochemical compatibilityPhosphorylation of Y397 in the SH2-binding motif of Focal adhesion kinase 1 (PTK2) induces binding to the Cytoplasmic protein NCK2 (NCK2) protein.
details
Inferred
LIG_SH2_SRC FAK1_HUMAN397400BinaryPhysicochemical compatibilityPhosphorylation of Y397 in the SH2-binding motif of Focal adhesion kinase 1 (PTK2) induces binding to Neuronal proto-oncogene tyrosine-protein kinase Src (Src).
details
Inferred
LIG_SH2_SRC FAK1_HUMAN397400BinaryPhysicochemical compatibilityPhosphorylation of Y397 in the SH2-binding motif of Focal adhesion kinase 1 (PTK2) induces binding to Neuronal proto-oncogene tyrosine-protein kinase Src (Src).
details
Inferred

G protein-coupled receptor kinase 5 - GRK5 -  Homo sapiens
LIG_PDZ_Class_1 ADRB2_HUMAN408413BinaryPhysicochemical compatibilityPhosphorylation of S411 in the PDZ-binding motif of Beta-2 adrenergic receptor (ADRB2) by inhibits its interaction with the Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (SLC9A3R1) protein.
details
Curated
LIG_PH_Tfb1 P53_HUMAN5056CumulativeRheostaticMultisite phosphorylation of S46 and T55 in the PH-like binding motif of Cellular tumor antigen p53 (TP53) gradually enhances its affinity for General transcription factor IIH subunit 1 (GTF2H1), an interaction involved in activation of transcription initiation and elongation by Cellular tumor antigen p53 (TP53).
details
Inferred

Glycogen synthase kinase-3 alpha - GSK3A -  Homo sapiens
MOD_GSK3_1 JUN_HUMAN236243BinaryPhysicochemical compatibilityPhosphorylation of Transcription factor AP-1 (JUN) at S243 primes the protein for phosphorylation at T239 by Glycogen synthase kinase-3 beta (GSK3B).
details
Inferred
DOC_WW_Pin1_4 MYC_HUMAN5560BinaryPhysicochemical compatibilityPhosphorylation of T58 in the Pin1-binding motif of Myc proto-oncogene protein (MYC) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 MYC_HUMAN5560BinaryPhysicochemical compatibilityPhosphorylation of T58 in the Pin1-binding motif of Myc proto-oncogene protein (MYC) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
MOD_CDK MK67I_HUMAN235241SpecificityAltered binding specificityPhosphorylation of T238 of MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by GSK3B. Triple-phosphorylated hNIFK (MKI67IP) binds strongly to Antigen KI-67 (MKI67).
details
Inferred
MOD_CDK MK67I_HUMAN235241SpecificityAltered binding specificityPhosphorylation of T238 of MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by GSK3B. Triple-phosphorylated hNIFK (MKI67IP) binds strongly to Antigen KI-67 (MKI67).
details
Inferred
MOD_CDK MK67I_HUMAN235241SpecificityAltered binding specificityPhosphorylation of T238 of MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by GSK3B. Triple-phosphorylated hNIFK (MKI67IP) binds strongly to Antigen KI-67 (MKI67).
details
Inferred
MOD_CDK MK67I_HUMAN235241SpecificityAltered binding specificityPhosphorylation of T238 of MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by GSK3B. Triple-phosphorylated hNIFK (MKI67IP) binds strongly to Antigen KI-67 (MKI67).
details
Inferred
MOD_GSK3_1 MK67I_HUMAN231238SpecificityAltered binding specificityPhosphorylation of T238 of MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by GSK3B. Triple-phosphorylated hNIFK (MKI67IP) binds strongly to Antigen KI-67 (MKI67).
details
Inferred
MOD_GSK3_1 MK67I_HUMAN231238SpecificityAltered binding specificityPhosphorylation of T238 of MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by GSK3B. Triple-phosphorylated hNIFK (MKI67IP) binds strongly to Antigen KI-67 (MKI67).
details
Inferred
MOD_GSK3_1 MK67I_HUMAN231238SpecificityAltered binding specificityPhosphorylation of T238 of MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by GSK3B. Triple-phosphorylated hNIFK (MKI67IP) binds strongly to Antigen KI-67 (MKI67).
details
Inferred
MOD_GSK3_1 MK67I_HUMAN231238SpecificityAltered binding specificityPhosphorylation of T238 of MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by GSK3B. Triple-phosphorylated hNIFK (MKI67IP) binds strongly to Antigen KI-67 (MKI67).
details
Inferred
MOD_GSK3_1 MK67I_HUMAN227234SpecificityAltered binding specificityPhosphorylation of T238 of MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by GSK3B. Triple-phosphorylated hNIFK (MKI67IP) binds strongly to Antigen KI-67 (MKI67).
details
Inferred
MOD_GSK3_1 MK67I_HUMAN227234SpecificityAltered binding specificityPhosphorylation of T238 of MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by GSK3B. Triple-phosphorylated hNIFK (MKI67IP) binds strongly to Antigen KI-67 (MKI67).
details
Inferred
MOD_GSK3_1 MK67I_HUMAN227234SpecificityAltered binding specificityPhosphorylation of T238 of MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by GSK3B. Triple-phosphorylated hNIFK (MKI67IP) binds strongly to Antigen KI-67 (MKI67).
details
Inferred
MOD_GSK3_1 MK67I_HUMAN227234SpecificityAltered binding specificityPhosphorylation of T238 of MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by GSK3B. Triple-phosphorylated hNIFK (MKI67IP) binds strongly to Antigen KI-67 (MKI67).
details
Inferred
LIG_FHA_2 MK67I_HUMAN238244SpecificityAltered binding specificityPhosphorylation of T238 of MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by GSK3B. Triple-phosphorylated hNIFK (MKI67IP) binds strongly to Antigen KI-67 (MKI67).
details
Inferred
LIG_FHA_2 MK67I_HUMAN238244SpecificityAltered binding specificityPhosphorylation of T238 of MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by GSK3B. Triple-phosphorylated hNIFK (MKI67IP) binds strongly to Antigen KI-67 (MKI67).
details
Inferred
LIG_FHA_2 MK67I_HUMAN238244SpecificityAltered binding specificityPhosphorylation of T238 of MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by GSK3B. Triple-phosphorylated hNIFK (MKI67IP) binds strongly to Antigen KI-67 (MKI67).
details
Inferred
LIG_FHA_2 MK67I_HUMAN238244SpecificityAltered binding specificityPhosphorylation of T238 of MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by GSK3B. Triple-phosphorylated hNIFK (MKI67IP) binds strongly to Antigen KI-67 (MKI67).
details
Inferred
MOD_ProDKin_1 MYC_HUMAN5965SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Inferred
MOD_ProDKin_1 MYC_HUMAN5965SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Inferred
MOD_GSK3_1 MYC_HUMAN5562SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Inferred
MOD_GSK3_1 MYC_HUMAN5562SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Inferred
DEG_SCF_FBW7_1 MYC_HUMAN5562SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Inferred
DEG_SCF_FBW7_1 MYC_HUMAN5562SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Inferred
MOD_GSK3_1 JUN_HUMAN236243SpecificityAltered binding specificityTranscription factor AP-1 (JUN) is primed by an unknown kinase for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets JUN to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks JUN for degradation. In v-Jun (Viral jun-transforming protein (JUN)) the residue corresponding to S243 is mutated to phenylalanine, which protects v-Jun (JUN) from degradation.
details
Inferred
MOD_GSK3_1 JUN_HUMAN236243SpecificityAltered binding specificityTranscription factor AP-1 (JUN) is primed by an unknown kinase for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets JUN to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks JUN for degradation. In v-Jun (Viral jun-transforming protein (JUN)) the residue corresponding to S243 is mutated to phenylalanine, which protects v-Jun (JUN) from degradation.
details
Inferred
MOD_GSK3_1 JUN_HUMAN236243SpecificityAltered binding specificityTranscription factor AP-1 (JUN) is primed by an unknown kinase for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets JUN to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks JUN for degradation. In v-Jun (Viral jun-transforming protein (JUN)) the residue corresponding to S243 is mutated to phenylalanine, which protects v-Jun (JUN) from degradation.
details
Inferred
DEG_SCF_FBW7_1 JUN_HUMAN236243SpecificityAltered binding specificityTranscription factor AP-1 (JUN) is primed by an unknown kinase for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets JUN to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks JUN for degradation. In v-Jun (Viral jun-transforming protein (JUN)) the residue corresponding to S243 is mutated to phenylalanine, which protects v-Jun (JUN) from degradation.
details
Inferred
DEG_SCF_FBW7_1 JUN_HUMAN236243SpecificityAltered binding specificityTranscription factor AP-1 (JUN) is primed by an unknown kinase for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets JUN to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks JUN for degradation. In v-Jun (Viral jun-transforming protein (JUN)) the residue corresponding to S243 is mutated to phenylalanine, which protects v-Jun (JUN) from degradation.
details
Inferred
DEG_SCF_FBW7_1 JUN_HUMAN236243SpecificityAltered binding specificityTranscription factor AP-1 (JUN) is primed by an unknown kinase for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets JUN to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks JUN for degradation. In v-Jun (Viral jun-transforming protein (JUN)) the residue corresponding to S243 is mutated to phenylalanine, which protects v-Jun (JUN) from degradation.
details
Inferred
MOD_GSK3_1 CCNE1_HUMAN392399SpecificityAltered binding specificityPhosphorylation of G1/S-specific cyclin-E1 (CCNE1) at S399 generates a docking site for Glycogen synthase kinase-3 beta (GSK3B). Subsequent phosphorylation of CCNE1 by Glycogen synthase kinase-3 beta (GSK3B) at T395 switches the specificity of CCNE1 to the F-box/WD repeat-containing protein 7 (FBXW7), which recruits CCNE1 to the SCF ubiquitin ligase complex to mark CCNE1 for degradation.
details
Inferred
MOD_GSK3_1 CCNE1_HUMAN392399SpecificityAltered binding specificityPhosphorylation of G1/S-specific cyclin-E1 (CCNE1) at S399 generates a docking site for Glycogen synthase kinase-3 beta (GSK3B). Subsequent phosphorylation of CCNE1 by Glycogen synthase kinase-3 beta (GSK3B) at T395 switches the specificity of CCNE1 to the F-box/WD repeat-containing protein 7 (FBXW7), which recruits CCNE1 to the SCF ubiquitin ligase complex to mark CCNE1 for degradation.
details
Inferred
DEG_SCF_FBW7_1 CCNE1_HUMAN393399SpecificityAltered binding specificityPhosphorylation of G1/S-specific cyclin-E1 (CCNE1) at S399 generates a docking site for Glycogen synthase kinase-3 beta (GSK3B). Subsequent phosphorylation of CCNE1 by Glycogen synthase kinase-3 beta (GSK3B) at T395 switches the specificity of CCNE1 to the F-box/WD repeat-containing protein 7 (FBXW7), which recruits CCNE1 to the SCF ubiquitin ligase complex to mark CCNE1 for degradation.
details
Inferred
DEG_SCF_FBW7_1 CCNE1_HUMAN393399SpecificityAltered binding specificityPhosphorylation of G1/S-specific cyclin-E1 (CCNE1) at S399 generates a docking site for Glycogen synthase kinase-3 beta (GSK3B). Subsequent phosphorylation of CCNE1 by Glycogen synthase kinase-3 beta (GSK3B) at T395 switches the specificity of CCNE1 to the F-box/WD repeat-containing protein 7 (FBXW7), which recruits CCNE1 to the SCF ubiquitin ligase complex to mark CCNE1 for degradation.
details
Inferred
MOD_GSK3_1 CTNB1_HUMAN3441SpecificityAltered binding specificityPhosphorylation of Catenin beta-1 (CTNNB1) at T41 generates a docking site for Glycogen synthase kinase-3 beta (GSK3B), which then phosphorylates S37, thereby generating a new docking site for GSK3B. Subsequent phosphorylation of S33 by GSK3B switches the specificity of CTNNB1 to the F-box/WD repeat-containing protein 1A (BTRC), which recruits CTNNB1 to the SCF ubiquitin ligase complex.
details
Inferred
MOD_GSK3_1 CTNB1_HUMAN3441SpecificityAltered binding specificityPhosphorylation of Catenin beta-1 (CTNNB1) at T41 generates a docking site for Glycogen synthase kinase-3 beta (GSK3B), which then phosphorylates S37, thereby generating a new docking site for GSK3B. Subsequent phosphorylation of S33 by GSK3B switches the specificity of CTNNB1 to the F-box/WD repeat-containing protein 1A (BTRC), which recruits CTNNB1 to the SCF ubiquitin ligase complex.
details
Inferred
MOD_GSK3_1 CTNB1_HUMAN3037SpecificityAltered binding specificityPhosphorylation of Catenin beta-1 (CTNNB1) at T41 generates a docking site for Glycogen synthase kinase-3 beta (GSK3B), which then phosphorylates S37, thereby generating a new docking site for GSK3B. Subsequent phosphorylation of S33 by GSK3B switches the specificity of CTNNB1 to the F-box/WD repeat-containing protein 1A (BTRC), which recruits CTNNB1 to the SCF ubiquitin ligase complex.
details
Inferred
MOD_GSK3_1 CTNB1_HUMAN3037SpecificityAltered binding specificityPhosphorylation of Catenin beta-1 (CTNNB1) at T41 generates a docking site for Glycogen synthase kinase-3 beta (GSK3B), which then phosphorylates S37, thereby generating a new docking site for GSK3B. Subsequent phosphorylation of S33 by GSK3B switches the specificity of CTNNB1 to the F-box/WD repeat-containing protein 1A (BTRC), which recruits CTNNB1 to the SCF ubiquitin ligase complex.
details
Inferred
DEG_SCF_TRCP1_1 CTNB1_HUMAN3237SpecificityAltered binding specificityPhosphorylation of Catenin beta-1 (CTNNB1) at T41 generates a docking site for Glycogen synthase kinase-3 beta (GSK3B), which then phosphorylates S37, thereby generating a new docking site for GSK3B. Subsequent phosphorylation of S33 by GSK3B switches the specificity of CTNNB1 to the F-box/WD repeat-containing protein 1A (BTRC), which recruits CTNNB1 to the SCF ubiquitin ligase complex.
details
Inferred
DEG_SCF_TRCP1_1 CTNB1_HUMAN3237SpecificityAltered binding specificityPhosphorylation of Catenin beta-1 (CTNNB1) at T41 generates a docking site for Glycogen synthase kinase-3 beta (GSK3B), which then phosphorylates S37, thereby generating a new docking site for GSK3B. Subsequent phosphorylation of S33 by GSK3B switches the specificity of CTNNB1 to the F-box/WD repeat-containing protein 1A (BTRC), which recruits CTNNB1 to the SCF ubiquitin ligase complex.
details
Inferred
LIG_FHA_2 MK67I_HUMAN238244CumulativeRheostaticPhosphorylation of T238 in MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by Glycogen synthase kinase-3 beta (GSK3B). Triple-phosphorylated hNIFK (MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP)) binds strongly to Antigen KI-67 (MKI67). See also switch details
details
Inferred
LIG_FHA_2 MK67I_HUMAN238244CumulativeRheostaticPhosphorylation of T238 in MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by Glycogen synthase kinase-3 beta (GSK3B). Triple-phosphorylated hNIFK (MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP)) binds strongly to Antigen KI-67 (MKI67). See also switch details
details
Inferred
LIG_FHA_2 MK67I_HUMAN238244CumulativeRheostaticPhosphorylation of T238 in MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by Glycogen synthase kinase-3 beta (GSK3B). Triple-phosphorylated hNIFK (MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP)) binds strongly to Antigen KI-67 (MKI67). See also switch details
details
Inferred
LIG_FHA_2 MK67I_HUMAN238244CumulativeRheostaticPhosphorylation of T238 in MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by Glycogen synthase kinase-3 beta (GSK3B). Triple-phosphorylated hNIFK (MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP)) binds strongly to Antigen KI-67 (MKI67). See also switch details
details
Inferred

Glycogen synthase kinase-3 beta - GSK3B -  Rattus norvegicus
DOC_WW_Pin1_4 MYC_HUMAN5560BinaryPhysicochemical compatibilityPhosphorylation of T58 in the Pin1-binding motif of Myc proto-oncogene protein (MYC) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
MOD_ProDKin_1 MYC_HUMAN5965SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Inferred
MOD_GSK3_1 MYC_HUMAN5562SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Inferred
DEG_SCF_FBW7_1 MYC_HUMAN5562SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Inferred

Glycogen synthase kinase-3 beta - GSK3B -  Mus musculus
DOC_WW_Pin1_4 CCND1_MOUSE283288BinaryPhysicochemical compatibilityPhosphorylation of T286 in the Pin1-binding motif of G1/S-specific cyclin-D1 (Ccnd1) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details
Inferred

Glycogen synthase kinase-3 beta - GSK3B -  Homo sapiens
MOD_GSK3_1 JUN_HUMAN236243BinaryPhysicochemical compatibilityPhosphorylation of Transcription factor AP-1 (JUN) at S243 primes the protein for phosphorylation at T239 by Glycogen synthase kinase-3 beta (GSK3B).
details
Inferred
DOC_WW_Pin1_4 MYC_HUMAN5560BinaryPhysicochemical compatibilityPhosphorylation of T58 in the Pin1-binding motif of Myc proto-oncogene protein (MYC) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 MYC_HUMAN5560BinaryPhysicochemical compatibilityPhosphorylation of T58 in the Pin1-binding motif of Myc proto-oncogene protein (MYC) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 CCND1_MOUSE283288BinaryPhysicochemical compatibilityPhosphorylation of T286 in the Pin1-binding motif of G1/S-specific cyclin-D1 (Ccnd1) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details
Inferred
DOC_WW_Pin1_4 CCND1_MOUSE283288BinaryPhysicochemical compatibilityPhosphorylation of T286 in the Pin1-binding motif of G1/S-specific cyclin-D1 (Ccnd1) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details
Inferred
TRG_NLS_MonoExtN_4 NFAC1_HUMAN262269BinaryPhysicochemical compatibilityPhosphorylation of S241 and S290 adjacent to the NLS of Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1) by Glycogen synthase kinase-3 beta (GSK3B) and Glycogen synthase kinase-3 beta (GSK3B) inhibits nuclear import of Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1) by disrupting its interaction with Importin subunit alpha-2 (KPNA2). Calcium-dependent dephosphorylation by calcineurin promotes nuclear import.
details
Curated
TRG_NLS_MonoExtN_4 NFAC1_HUMAN262269BinaryPhysicochemical compatibilityPhosphorylation of S241 and S290 adjacent to the NLS of Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1) by Glycogen synthase kinase-3 beta (GSK3B) and Glycogen synthase kinase-3 beta (GSK3B) inhibits nuclear import of Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1) by disrupting its interaction with Importin subunit alpha-2 (KPNA2). Calcium-dependent dephosphorylation by calcineurin promotes nuclear import.
details
Curated
LIG_PTB_Apo_2 A4_HUMAN756763BinaryPhysicochemical compatibilityPhosphorylation of T743 adjacent to the PTB-binding motif of Amyloid beta A4 protein (APP) reduces the affinity for Amyloid beta A4 precursor protein-binding family B member 1 (APBB1).
details
Inferred
LIG_SxIP_EBH_1 CLAP2_HUMAN515525BinaryPhysicochemical compatibilityPhosphorylation of several serine residues surrounding the EB1-binding motifs of CLIP-associating protein 2 (CLASP2) by Glycogen synthase kinase-3 beta (GSK3B) and Glycogen synthase kinase-3 beta (GSK3B) and Glycogen synthase kinase-3 beta (GSK3B) and Glycogen synthase kinase-3 beta (GSK3B) and Glycogen synthase kinase-3 beta (GSK3B) inhibits its interaction with Microtubule-associated protein RP/EB family member 1 (MAPRE1).
details
Curated
LIG_SxIP_EBH_1 CLAP2_HUMAN515525BinaryPhysicochemical compatibilityPhosphorylation of several serine residues surrounding the EB1-binding motifs of CLIP-associating protein 2 (CLASP2) by Glycogen synthase kinase-3 beta (GSK3B) and Glycogen synthase kinase-3 beta (GSK3B) and Glycogen synthase kinase-3 beta (GSK3B) and Glycogen synthase kinase-3 beta (GSK3B) and Glycogen synthase kinase-3 beta (GSK3B) inhibits its interaction with Microtubule-associated protein RP/EB family member 1 (MAPRE1).
details
Curated
LIG_SxIP_EBH_1 CLAP2_HUMAN515525BinaryPhysicochemical compatibilityPhosphorylation of several serine residues surrounding the EB1-binding motifs of CLIP-associating protein 2 (CLASP2) by Glycogen synthase kinase-3 beta (GSK3B) and Glycogen synthase kinase-3 beta (GSK3B) and Glycogen synthase kinase-3 beta (GSK3B) and Glycogen synthase kinase-3 beta (GSK3B) and Glycogen synthase kinase-3 beta (GSK3B) inhibits its interaction with Microtubule-associated protein RP/EB family member 1 (MAPRE1).
details
Curated
LIG_SxIP_EBH_1 CLAP2_HUMAN515525BinaryPhysicochemical compatibilityPhosphorylation of several serine residues surrounding the EB1-binding motifs of CLIP-associating protein 2 (CLASP2) by Glycogen synthase kinase-3 beta (GSK3B) and Glycogen synthase kinase-3 beta (GSK3B) and Glycogen synthase kinase-3 beta (GSK3B) and Glycogen synthase kinase-3 beta (GSK3B) and Glycogen synthase kinase-3 beta (GSK3B) inhibits its interaction with Microtubule-associated protein RP/EB family member 1 (MAPRE1).
details
Curated
LIG_SxIP_EBH_1 CLAP2_HUMAN515525BinaryPhysicochemical compatibilityPhosphorylation of several serine residues surrounding the EB1-binding motifs of CLIP-associating protein 2 (CLASP2) by Glycogen synthase kinase-3 beta (GSK3B) and Glycogen synthase kinase-3 beta (GSK3B) and Glycogen synthase kinase-3 beta (GSK3B) and Glycogen synthase kinase-3 beta (GSK3B) and Glycogen synthase kinase-3 beta (GSK3B) inhibits its interaction with Microtubule-associated protein RP/EB family member 1 (MAPRE1).
details
Curated
LIG_SH2_GRB2 A4_HUMAN757760CumulativeRheostaticWhile phosphorylation of Y757 in the SH2-binding motif of Amyloid beta A4 protein (APP) induces binding to Growth factor receptor-bound protein 2 (GRB2), additional phosphorylation of T743 further increases the strength of the interaction.
details
Inferred
DEG_SCF_FBW7_1 CCNE1_HUMAN378384SpecificityAltered binding specificityPhosphorylation of Isoform E-S of G1/S-specific cyclin-E1 (CCNE1) at S384 by CDK2 primes CCNE1 for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B) at T380, which creates a recognition site for F box proteins of the SCF ubiquitin ligase complex (F-box/WD repeat-containing protein 7 (FBXW7)) that target CCNE1 for degradation.
details
Curated
LIG_WW_Nedd4L SMAD3_HUMAN203210SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Curated
DEG_SCF_TRCP1_1 FGD1_HUMAN282287SpecificityAltered binding specificityPhosphorylation of FYVE, RhoGEF and PH domain-containing protein 1 (FGD1), a GEF for CDC42 small effector protein 2 (CDC42SE2), by Glycogen synthase kinase-3 beta (GSK3B) targets FGD1 to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 1A (BTRC), which marks FGD1 for degradation.
details
Curated
MOD_GSK3_1 FGD3_HUMAN7380SpecificityAltered binding specificityPhosphorylation of FYVE, RhoGEF and PH domain-containing protein 3 (FGD3), a GEF for CDC42 small effector protein 2 (CDC42SE2), by Glycogen synthase kinase-3 beta (GSK3B) targets FGD3 to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 1A (BTRC), which marks FGD3 for degradation.
details
Curated
DEG_SCF_TRCP1_1 FGD3_HUMAN7580SpecificityAltered binding specificityPhosphorylation of FYVE, RhoGEF and PH domain-containing protein 3 (FGD3), a GEF for CDC42 small effector protein 2 (CDC42SE2), by Glycogen synthase kinase-3 beta (GSK3B) targets FGD3 to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 1A (BTRC), which marks FGD3 for degradation.
details
Curated
DEG_SCF_TRCP1_1 FGD3_HUMAN7580SpecificityAltered binding specificityPhosphorylation of FYVE, RhoGEF and PH domain-containing protein 3 (FGD3), a GEF for CDC42 small effector protein 2 (CDC42SE2), by Glycogen synthase kinase-3 beta (GSK3B) targets FGD3 to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 1A (BTRC), which marks FGD3 for degradation.
details
Curated
MOD_CDK MK67I_HUMAN235241SpecificityAltered binding specificityPhosphorylation of T238 of MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by GSK3B. Triple-phosphorylated hNIFK (MKI67IP) binds strongly to Antigen KI-67 (MKI67).
details
Inferred
MOD_CDK MK67I_HUMAN235241SpecificityAltered binding specificityPhosphorylation of T238 of MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by GSK3B. Triple-phosphorylated hNIFK (MKI67IP) binds strongly to Antigen KI-67 (MKI67).
details
Inferred
MOD_CDK MK67I_HUMAN235241SpecificityAltered binding specificityPhosphorylation of T238 of MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by GSK3B. Triple-phosphorylated hNIFK (MKI67IP) binds strongly to Antigen KI-67 (MKI67).
details
Inferred
MOD_CDK MK67I_HUMAN235241SpecificityAltered binding specificityPhosphorylation of T238 of MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by GSK3B. Triple-phosphorylated hNIFK (MKI67IP) binds strongly to Antigen KI-67 (MKI67).
details
Inferred
MOD_GSK3_1 MK67I_HUMAN231238SpecificityAltered binding specificityPhosphorylation of T238 of MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by GSK3B. Triple-phosphorylated hNIFK (MKI67IP) binds strongly to Antigen KI-67 (MKI67).
details
Inferred
MOD_GSK3_1 MK67I_HUMAN231238SpecificityAltered binding specificityPhosphorylation of T238 of MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by GSK3B. Triple-phosphorylated hNIFK (MKI67IP) binds strongly to Antigen KI-67 (MKI67).
details
Inferred
MOD_GSK3_1 MK67I_HUMAN231238SpecificityAltered binding specificityPhosphorylation of T238 of MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by GSK3B. Triple-phosphorylated hNIFK (MKI67IP) binds strongly to Antigen KI-67 (MKI67).
details
Inferred
MOD_GSK3_1 MK67I_HUMAN231238SpecificityAltered binding specificityPhosphorylation of T238 of MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by GSK3B. Triple-phosphorylated hNIFK (MKI67IP) binds strongly to Antigen KI-67 (MKI67).
details
Inferred
MOD_GSK3_1 MK67I_HUMAN227234SpecificityAltered binding specificityPhosphorylation of T238 of MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by GSK3B. Triple-phosphorylated hNIFK (MKI67IP) binds strongly to Antigen KI-67 (MKI67).
details
Curated
LIG_FHA_2 MK67I_HUMAN238244SpecificityAltered binding specificityPhosphorylation of T238 of MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by GSK3B. Triple-phosphorylated hNIFK (MKI67IP) binds strongly to Antigen KI-67 (MKI67).
details
Curated
LIG_FHA_2 MK67I_HUMAN238244SpecificityAltered binding specificityPhosphorylation of T238 of MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by GSK3B. Triple-phosphorylated hNIFK (MKI67IP) binds strongly to Antigen KI-67 (MKI67).
details
Curated
MOD_ProDKin_1 MYC_HUMAN5965SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Inferred
MOD_ProDKin_1 MYC_HUMAN5965SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Inferred
MOD_GSK3_1 MYC_HUMAN5562SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Inferred
MOD_GSK3_1 MYC_HUMAN5562SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Inferred
DEG_SCF_FBW7_1 MYC_HUMAN5562SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Curated
MOD_GSK3_1 JUN_HUMAN236243SpecificityAltered binding specificityTranscription factor AP-1 (JUN) is primed by an unknown kinase for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets JUN to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks JUN for degradation. In v-Jun (Viral jun-transforming protein (JUN)) the residue corresponding to S243 is mutated to phenylalanine, which protects v-Jun (JUN) from degradation.
details
Inferred
MOD_GSK3_1 JUN_HUMAN236243SpecificityAltered binding specificityTranscription factor AP-1 (JUN) is primed by an unknown kinase for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets JUN to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks JUN for degradation. In v-Jun (Viral jun-transforming protein (JUN)) the residue corresponding to S243 is mutated to phenylalanine, which protects v-Jun (JUN) from degradation.
details
Inferred
DEG_SCF_FBW7_1 JUN_HUMAN236243SpecificityAltered binding specificityTranscription factor AP-1 (JUN) is primed by an unknown kinase for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets JUN to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks JUN for degradation. In v-Jun (Viral jun-transforming protein (JUN)) the residue corresponding to S243 is mutated to phenylalanine, which protects v-Jun (JUN) from degradation.
details
Curated
MOD_GSK3_1 CCNE1_HUMAN392399SpecificityAltered binding specificityPhosphorylation of G1/S-specific cyclin-E1 (CCNE1) at S399 generates a docking site for Glycogen synthase kinase-3 beta (GSK3B). Subsequent phosphorylation of CCNE1 by Glycogen synthase kinase-3 beta (GSK3B) at T395 switches the specificity of CCNE1 to the F-box/WD repeat-containing protein 7 (FBXW7), which recruits CCNE1 to the SCF ubiquitin ligase complex to mark CCNE1 for degradation.
details
Inferred
MOD_GSK3_1 CCNE1_HUMAN392399SpecificityAltered binding specificityPhosphorylation of G1/S-specific cyclin-E1 (CCNE1) at S399 generates a docking site for Glycogen synthase kinase-3 beta (GSK3B). Subsequent phosphorylation of CCNE1 by Glycogen synthase kinase-3 beta (GSK3B) at T395 switches the specificity of CCNE1 to the F-box/WD repeat-containing protein 7 (FBXW7), which recruits CCNE1 to the SCF ubiquitin ligase complex to mark CCNE1 for degradation.
details
Inferred
DEG_SCF_FBW7_1 CCNE1_HUMAN393399SpecificityAltered binding specificityPhosphorylation of G1/S-specific cyclin-E1 (CCNE1) at S399 generates a docking site for Glycogen synthase kinase-3 beta (GSK3B). Subsequent phosphorylation of CCNE1 by Glycogen synthase kinase-3 beta (GSK3B) at T395 switches the specificity of CCNE1 to the F-box/WD repeat-containing protein 7 (FBXW7), which recruits CCNE1 to the SCF ubiquitin ligase complex to mark CCNE1 for degradation.
details
Curated
MOD_GSK3_1 SRBP1_HUMAN422430SpecificityAltered binding specificityPhosphorylation of SREBP-1 (Sterol regulatory element-binding protein 1 (SREBF1)) at S430 generates a docking site for Glycogen synthase kinase-3 beta (GSK3B). Subsequent phosphorylation of SREBP-1 (SREBF1) by GSK3B at T426 switches the specificity of SREBP-1 (SREBF1) to the F-box/WD repeat-containing protein 7 (FBXW7), which recruits SREBP-1 (SREBF1) to the SCF ubiquitin ligase complex to mark SREBP-1 (SREBF1) for degradation.
details
Inferred
MOD_GSK3_1 SRBP1_HUMAN422430SpecificityAltered binding specificityPhosphorylation of SREBP-1 (Sterol regulatory element-binding protein 1 (SREBF1)) at S430 generates a docking site for Glycogen synthase kinase-3 beta (GSK3B). Subsequent phosphorylation of SREBP-1 (SREBF1) by GSK3B at T426 switches the specificity of SREBP-1 (SREBF1) to the F-box/WD repeat-containing protein 7 (FBXW7), which recruits SREBP-1 (SREBF1) to the SCF ubiquitin ligase complex to mark SREBP-1 (SREBF1) for degradation.
details
Inferred
DEG_SCF_FBW7_1 SRBP1_HUMAN425430SpecificityAltered binding specificityPhosphorylation of SREBP-1 (Sterol regulatory element-binding protein 1 (SREBF1)) at S430 generates a docking site for Glycogen synthase kinase-3 beta (GSK3B). Subsequent phosphorylation of SREBP-1 (SREBF1) by GSK3B at T426 switches the specificity of SREBP-1 (SREBF1) to the F-box/WD repeat-containing protein 7 (FBXW7), which recruits SREBP-1 (SREBF1) to the SCF ubiquitin ligase complex to mark SREBP-1 (SREBF1) for degradation.
details
Curated
MOD_GSK3_1 CTNB1_HUMAN3441SpecificityAltered binding specificityPhosphorylation of Catenin beta-1 (CTNNB1) at T41 generates a docking site for Glycogen synthase kinase-3 beta (GSK3B), which then phosphorylates S37, thereby generating a new docking site for GSK3B. Subsequent phosphorylation of S33 by GSK3B switches the specificity of CTNNB1 to the F-box/WD repeat-containing protein 1A (BTRC), which recruits CTNNB1 to the SCF ubiquitin ligase complex.
details
Inferred
MOD_GSK3_1 CTNB1_HUMAN3441SpecificityAltered binding specificityPhosphorylation of Catenin beta-1 (CTNNB1) at T41 generates a docking site for Glycogen synthase kinase-3 beta (GSK3B), which then phosphorylates S37, thereby generating a new docking site for GSK3B. Subsequent phosphorylation of S33 by GSK3B switches the specificity of CTNNB1 to the F-box/WD repeat-containing protein 1A (BTRC), which recruits CTNNB1 to the SCF ubiquitin ligase complex.
details
Inferred
MOD_GSK3_1 CTNB1_HUMAN3037SpecificityAltered binding specificityPhosphorylation of Catenin beta-1 (CTNNB1) at T41 generates a docking site for Glycogen synthase kinase-3 beta (GSK3B), which then phosphorylates S37, thereby generating a new docking site for GSK3B. Subsequent phosphorylation of S33 by GSK3B switches the specificity of CTNNB1 to the F-box/WD repeat-containing protein 1A (BTRC), which recruits CTNNB1 to the SCF ubiquitin ligase complex.
details
Curated
DEG_SCF_TRCP1_1 CTNB1_HUMAN3237SpecificityAltered binding specificityPhosphorylation of Catenin beta-1 (CTNNB1) at T41 generates a docking site for Glycogen synthase kinase-3 beta (GSK3B), which then phosphorylates S37, thereby generating a new docking site for GSK3B. Subsequent phosphorylation of S33 by GSK3B switches the specificity of CTNNB1 to the F-box/WD repeat-containing protein 1A (BTRC), which recruits CTNNB1 to the SCF ubiquitin ligase complex.
details
Curated
DEG_SCF_TRCP1_1 CTNB1_HUMAN3237SpecificityAltered binding specificityPhosphorylation of Catenin beta-1 (CTNNB1) at T41 generates a docking site for Glycogen synthase kinase-3 beta (GSK3B), which then phosphorylates S37, thereby generating a new docking site for GSK3B. Subsequent phosphorylation of S33 by GSK3B switches the specificity of CTNNB1 to the F-box/WD repeat-containing protein 1A (BTRC), which recruits CTNNB1 to the SCF ubiquitin ligase complex.
details
Curated
MOD_GSK3_1 SNAI1_HUMAN93100SpecificityAltered binding specificityPhosphorylation of Zinc finger protein SNAI1 (SNAI1) at S100 generates a docking site for Glycogen synthase kinase-3 beta (GSK3B). Subsequent phosphorylation of S96 by GSK3B targets Zinc finger protein SNAI1 (SNAI1) to the SCF ubiquitin ligase complexes F-box/WD repeat-containing protein 1A (BTRC), which marks it for degradation.
details
Inferred
MOD_GSK3_1 SNAI1_HUMAN93100SpecificityAltered binding specificityPhosphorylation of Zinc finger protein SNAI1 (SNAI1) at S100 generates a docking site for Glycogen synthase kinase-3 beta (GSK3B). Subsequent phosphorylation of S96 by GSK3B targets Zinc finger protein SNAI1 (SNAI1) to the SCF ubiquitin ligase complexes F-box/WD repeat-containing protein 1A (BTRC), which marks it for degradation.
details
Inferred
DEG_SCF_TRCP1_1 SNAI1_HUMAN95100SpecificityAltered binding specificityPhosphorylation of Zinc finger protein SNAI1 (SNAI1) at S100 generates a docking site for Glycogen synthase kinase-3 beta (GSK3B). Subsequent phosphorylation of S96 by GSK3B targets Zinc finger protein SNAI1 (SNAI1) to the SCF ubiquitin ligase complexes F-box/WD repeat-containing protein 1A (BTRC), which marks it for degradation.
details
Curated
LIG_FHA_2 MK67I_HUMAN238244CumulativeRheostaticPhosphorylation of T238 in MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by Glycogen synthase kinase-3 beta (GSK3B). Triple-phosphorylated hNIFK (MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP)) binds strongly to Antigen KI-67 (MKI67). See also switch details
details
Curated
LIG_FHA_2 MK67I_HUMAN238244CumulativeRheostaticPhosphorylation of T238 in MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by Glycogen synthase kinase-3 beta (GSK3B). Triple-phosphorylated hNIFK (MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP)) binds strongly to Antigen KI-67 (MKI67). See also switch details
details
Curated
LIG_WW_Nedd4L SMAD3_HUMAN203210Avidity‑sensingCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Dual phosphorylation of the two NEDD4L-binding sites mediates high-avidity binding of two WW domains of NEDD4L to SMAD3. See also switch details and switch details.
details
Curated
LIG_WW_Nedd4L SMAD3_HUMAN203210CumulativeRheostaticCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Phosphorylation of S208 in SMAD3 induces binding of the third WW domain of NEDD4L, while additional phosphorylation of S204 in SMAD3 further increases the affinity of this interaction. See also switch details and switch details.
details
Curated

Hepatocyte growth factor receptor - MET -  Homo sapiens
LIG_SH2_IC MET_HUMAN13511360BinaryPhysicochemical compatibilityPhosphorylation of Y1356 in the SH2-binding motif of Hepatocyte growth factor receptor (MET) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.
details
Inferred
LIG_SH2_IC MET_HUMAN13511360BinaryPhysicochemical compatibilityPhosphorylation of Y1356 in the SH2-binding motif of Hepatocyte growth factor receptor (MET) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.
details
Inferred
LIG_SH2_IC MET_HUMAN13511360BinaryPhysicochemical compatibilityPhosphorylation of Y1356 in the SH2-binding motif of Hepatocyte growth factor receptor (MET) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.
details
Inferred
LIG_SH2_IC MET_HUMAN13511360BinaryPhysicochemical compatibilityPhosphorylation of Y1356 in the SH2-binding motif of Hepatocyte growth factor receptor (MET) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.
details
Inferred
LIG_SH2_IC SHC1_HUMAN423435BinaryPhysicochemical compatibilityPhosphorylation of Y427 in the SH2-binding motif of SHC-transforming protein 1 (SHC1) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.
details
Inferred
LIG_SH2_IA FAK1_HUMAN389405BinaryPhysicochemical compatibilityPhosphorylation of Y397 in the SH2-binding motif of Focal adhesion kinase 1 (PTK2) induces binding to the Cytoplasmic protein NCK2 (NCK2) protein.
details
Inferred
LIG_SH2_SRC FAK1_HUMAN397400BinaryPhysicochemical compatibilityPhosphorylation of Y397 in the SH2-binding motif of Focal adhesion kinase 1 (PTK2) induces binding to Neuronal proto-oncogene tyrosine-protein kinase Src (Src).
details
Inferred
LIG_SH2_STAT5 GAB1_HUMAN472475BinaryPhysicochemical compatibilityPhosphorylation of Y472 in the SH2-binding motif of GRB2-associated-binding protein 1 (GAB1) induces binding to Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1).
details
Inferred
LIG_SH2_STAT5 GAB1_HUMAN447450BinaryPhysicochemical compatibilityPhosphorylation of Y447 in the SH2-binding motif of GRB2-associated-binding protein 1 (GAB1) induces binding to Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1).
details
Inferred

High affinity nerve growth factor receptor - NTRK1 -  Homo sapiens
LIG_PTB_Phospho_1 NTRK1_HUMAN490496BinaryPhysicochemical compatibilityPhosphorylation of Y496 in the PTB-binding motif of High affinity nerve growth factor receptor (NTRK1) induces binding to the SHC-transforming protein 1 (SHC1) protein.
details
Inferred
LIG_PTB_Phospho_1 NTRK1_HUMAN490496BinaryPhysicochemical compatibilityPhosphorylation of Y496 in the PTB-binding motif of High affinity nerve growth factor receptor (NTRK1) induces binding to the SHC-transforming protein 1 (SHC1) protein.
details
Inferred
LIG_PTB_Phospho_1 NTRK1_HUMAN490496BinaryPhysicochemical compatibilityPhosphorylation of Y496 in the PTB-binding motif of High affinity nerve growth factor receptor (NTRK1) induces binding to the SHC-transforming protein 1 (SHC1) protein.
details
Inferred
LIG_SH2_IIB NTRK1_HUMAN782796BinaryPhysicochemical compatibilityPhosphorylation of Y791 in the SH2-binding motif of High affinity nerve growth factor receptor (NTRK1) induces binding to the SHC-transforming protein 1 (SHC1) protein.
details
Inferred
LIG_SH2_IIB NTRK1_HUMAN782796BinaryPhysicochemical compatibilityPhosphorylation of Y791 in the SH2-binding motif of High affinity nerve growth factor receptor (NTRK1) induces binding to the SHC-transforming protein 1 (SHC1) protein.
details
Inferred
LIG_SH2_IB NTRK1_HUMAN783796BinaryPhysicochemical compatibilityPhosphorylation of Y791 in the SH2-binding motif of High affinity nerve growth factor receptor (NTRK1) induces binding to the Megakaryocyte-associated tyrosine-protein kinase (MATK) protein.
details
Inferred
LIG_SH2_IB NTRK1_HUMAN783796BinaryPhysicochemical compatibilityPhosphorylation of Y791 in the SH2-binding motif of High affinity nerve growth factor receptor (NTRK1) induces binding to the Megakaryocyte-associated tyrosine-protein kinase (MATK) protein.
details
Inferred

Histone acetyltransferase p300 - EP300 -  Homo sapiens
TRG_NLS_MonoExtN_4 SKP2_HUMAN6572BinaryPhysicochemical compatibilityAcetylation of S-phase kinase-associated protein 2 (SKP2) in its NLS inhibits binding to the Importin subunit alpha-6 (KPNA5). p300 acetylates SKP2 at K68 and K71 within SKP2's nuclear localisation signal, this stabilises SKP2 from Fizzy-related protein homolog (FZR1)-mediated degradation and facilitates its translocation into the cytoplasm. This process can be reversed by NAD-dependent protein deacetylase sirtuin-3, mitochondrial (SIRT3) that specifically deacetylates SKP2 facilitating its translocation back into the nucleus. In the cytosol, SKP2 acts to promote Cadherin-1 (CDH1) degradation in a Casein Kinase I dependent manner to promote cell migration. Casein kinase I recognises the MOD_CK1_1 motif in CDH1 phosphorylating at residues Ser840 and Ser842.
details
Curated
TRG_NLS_MonoExtN_4 SKP2_HUMAN6572BinaryPhysicochemical compatibilityAcetylation of S-phase kinase-associated protein 2 (SKP2) in its NLS inhibits binding to the Importin subunit alpha-7 (KPNA6). p300 acetylates SKP2 at K68 and K71 within SKP2's nuclear localisation signal, this stabilises SKP2 from Fizzy-related protein homolog (FZR1)-mediated degradation and facilitates its translocation into the cytoplasm. This process can be reversed by NAD-dependent protein deacetylase sirtuin-3, mitochondrial (SIRT3) that specifically deacetylates SKP2 facilitating its translocation back into the nucleus. In the cytosol, SKP2 acts to promote Cadherin-1 (CDH1) degradation in a Casein Kinase I dependent manner to promote cell migration. Casein kinase I recognises the MOD_CK1_1 motif in CDH1 phosphorylating at residues Ser840 and Ser842.
details
Curated

Homeodomain-interacting protein kinase 2 - HIPK2 -  Homo sapiens
LIG_PH_Tfb1 P53_HUMAN5056CumulativeRheostaticMultisite phosphorylation of S46 and T55 in the PH-like binding motif of Cellular tumor antigen p53 (TP53) gradually enhances its affinity for General transcription factor IIH subunit 1 (GTF2H1), an interaction involved in activation of transcription initiation and elongation by Cellular tumor antigen p53 (TP53).
details
Inferred
LIG_PH_Tfb1 P53_HUMAN5056CumulativeRheostaticMultisite phosphorylation of S46 and T55 in the PH-like binding motif of Cellular tumor antigen p53 (TP53) gradually enhances its affinity for General transcription factor IIH subunit 1 (GTF2H1), an interaction involved in activation of transcription initiation and elongation by Cellular tumor antigen p53 (TP53).
details
Inferred
LIG_PH_Tfb1 P53_HUMAN5056CumulativeRheostaticMultisite phosphorylation of S46 and T55 in the PH-like binding motif of Cellular tumor antigen p53 (TP53) gradually enhances its affinity for General transcription factor IIH subunit 1 (GTF2H1), an interaction involved in activation of transcription initiation and elongation by Cellular tumor antigen p53 (TP53).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred

Hypoxia-inducible factor 1-alpha inhibitor - HIF1AN -  Homo sapiens
LIG_TAZ1 HIF1A_HUMAN792795BinaryPhysicochemical compatibilityUnder normoxic conditions interaction of Hypoxia-inducible factor 1-alpha (HIF1A) with transcriptional coactivators such as CREB-binding protein (Crebbp) is inhibited by hydroxylation of N803.
details
Curated

Inhibitor of nuclear factor kappa-B kinase subunit alpha - CHUK -  Homo sapiens
DEG_SCF_TRCP1_1 NFKB1_HUMAN926932BinaryPhysicochemical compatibilityDual phosphorylation of S927 and S932 in the TrCP1-binding motif of Nuclear factor NF-kappa-B p105 subunit (NFKB1) targets the protein to the SCF ubiquitin ligase complex, which marks it for degradation.
details
Inferred
DEG_SCF_TRCP1_1 NFKB1_HUMAN926932BinaryPhysicochemical compatibilityDual phosphorylation of S927 and S932 in the TrCP1-binding motif of Nuclear factor NF-kappa-B p105 subunit (NFKB1) targets the protein to the SCF ubiquitin ligase complex, which marks it for degradation.
details
Inferred
DEG_SCF_TRCP1_1 NFKB1_HUMAN926932BinaryPhysicochemical compatibilityDual phosphorylation of S927 and S932 in the TrCP1-binding motif of Nuclear factor NF-kappa-B p105 subunit (NFKB1) targets the protein to the SCF ubiquitin ligase complex, which marks it for degradation.
details
Inferred
DEG_SCF_TRCP1_1 NFKB1_HUMAN926932BinaryPhysicochemical compatibilityDual phosphorylation of S927 and S932 in the TrCP1-binding motif of Nuclear factor NF-kappa-B p105 subunit (NFKB1) targets the protein to the SCF ubiquitin ligase complex, which marks it for degradation.
details
Inferred
DEG_SCF_TRCP1_1 NFKB1_HUMAN926932BinaryPhysicochemical compatibilityDual phosphorylation of S927 and S932 in the TrCP1-binding motif of Nuclear factor NF-kappa-B p105 subunit (NFKB1) targets the protein to the SCF ubiquitin ligase complex, which marks it for degradation.
details
Inferred
DEG_SCF_TRCP1_1 IKBA_HUMAN3136BinaryPhysicochemical compatibilityDual phosphorylation of S32 and S36 in the TrCP1-binding motif of NF-kappa-B inhibitor alpha (NFKBIA) targets the protein to the SCF ubiquitin ligase complex, which marks it for degradation.
details
Inferred
DEG_SCF_TRCP1_1 IKBA_HUMAN3136BinaryPhysicochemical compatibilityDual phosphorylation of S32 and S36 in the TrCP1-binding motif of NF-kappa-B inhibitor alpha (NFKBIA) targets the protein to the SCF ubiquitin ligase complex, which marks it for degradation.
details
Inferred
MOD_GSK3_1 CTNB1_HUMAN3441SpecificityAltered binding specificityPhosphorylation of Catenin beta-1 (CTNNB1) at T41 generates a docking site for Glycogen synthase kinase-3 beta (GSK3B), which then phosphorylates S37, thereby generating a new docking site for GSK3B. Subsequent phosphorylation of S33 by GSK3B switches the specificity of CTNNB1 to the F-box/WD repeat-containing protein 1A (BTRC), which recruits CTNNB1 to the SCF ubiquitin ligase complex.
details
Inferred
MOD_GSK3_1 CTNB1_HUMAN3441SpecificityAltered binding specificityPhosphorylation of Catenin beta-1 (CTNNB1) at T41 generates a docking site for Glycogen synthase kinase-3 beta (GSK3B), which then phosphorylates S37, thereby generating a new docking site for GSK3B. Subsequent phosphorylation of S33 by GSK3B switches the specificity of CTNNB1 to the F-box/WD repeat-containing protein 1A (BTRC), which recruits CTNNB1 to the SCF ubiquitin ligase complex.
details
Inferred
MOD_GSK3_1 CTNB1_HUMAN3037SpecificityAltered binding specificityPhosphorylation of Catenin beta-1 (CTNNB1) at T41 generates a docking site for Glycogen synthase kinase-3 beta (GSK3B), which then phosphorylates S37, thereby generating a new docking site for GSK3B. Subsequent phosphorylation of S33 by GSK3B switches the specificity of CTNNB1 to the F-box/WD repeat-containing protein 1A (BTRC), which recruits CTNNB1 to the SCF ubiquitin ligase complex.
details
Inferred
MOD_GSK3_1 CTNB1_HUMAN3037SpecificityAltered binding specificityPhosphorylation of Catenin beta-1 (CTNNB1) at T41 generates a docking site for Glycogen synthase kinase-3 beta (GSK3B), which then phosphorylates S37, thereby generating a new docking site for GSK3B. Subsequent phosphorylation of S33 by GSK3B switches the specificity of CTNNB1 to the F-box/WD repeat-containing protein 1A (BTRC), which recruits CTNNB1 to the SCF ubiquitin ligase complex.
details
Inferred
DEG_SCF_TRCP1_1 CTNB1_HUMAN3237SpecificityAltered binding specificityPhosphorylation of Catenin beta-1 (CTNNB1) at T41 generates a docking site for Glycogen synthase kinase-3 beta (GSK3B), which then phosphorylates S37, thereby generating a new docking site for GSK3B. Subsequent phosphorylation of S33 by GSK3B switches the specificity of CTNNB1 to the F-box/WD repeat-containing protein 1A (BTRC), which recruits CTNNB1 to the SCF ubiquitin ligase complex.
details
Inferred
DEG_SCF_TRCP1_1 CTNB1_HUMAN3237SpecificityAltered binding specificityPhosphorylation of Catenin beta-1 (CTNNB1) at T41 generates a docking site for Glycogen synthase kinase-3 beta (GSK3B), which then phosphorylates S37, thereby generating a new docking site for GSK3B. Subsequent phosphorylation of S33 by GSK3B switches the specificity of CTNNB1 to the F-box/WD repeat-containing protein 1A (BTRC), which recruits CTNNB1 to the SCF ubiquitin ligase complex.
details
Inferred

Inhibitor of nuclear factor kappa-B kinase subunit beta - IKBKB -  Homo sapiens
DEG_SCF_TRCP1_1 NFKB1_HUMAN926932BinaryPhysicochemical compatibilityDual phosphorylation of S927 and S932 in the TrCP1-binding motif of Nuclear factor NF-kappa-B p105 subunit (NFKB1) targets the protein to the SCF ubiquitin ligase complex, which marks it for degradation.
details
Inferred
DEG_SCF_TRCP1_1 NFKB1_HUMAN926932BinaryPhysicochemical compatibilityDual phosphorylation of S927 and S932 in the TrCP1-binding motif of Nuclear factor NF-kappa-B p105 subunit (NFKB1) targets the protein to the SCF ubiquitin ligase complex, which marks it for degradation.
details
Inferred
DEG_SCF_TRCP1_1 NFKB1_HUMAN926932BinaryPhysicochemical compatibilityDual phosphorylation of S927 and S932 in the TrCP1-binding motif of Nuclear factor NF-kappa-B p105 subunit (NFKB1) targets the protein to the SCF ubiquitin ligase complex, which marks it for degradation.
details
Inferred
DEG_SCF_TRCP1_1 IKBA_HUMAN3136BinaryPhysicochemical compatibilityDual phosphorylation of S32 and S36 in the TrCP1-binding motif of NF-kappa-B inhibitor alpha (NFKBIA) targets the protein to the SCF ubiquitin ligase complex, which marks it for degradation.
details
Inferred
DEG_SCF_TRCP1_1 IKBA_HUMAN3136BinaryPhysicochemical compatibilityDual phosphorylation of S32 and S36 in the TrCP1-binding motif of NF-kappa-B inhibitor alpha (NFKBIA) targets the protein to the SCF ubiquitin ligase complex, which marks it for degradation.
details
Inferred

Inhibitor of nuclear factor kappa-B kinase subunit epsilon - IKBKE -  Homo sapiens
DEG_SCF_TRCP1_1 IKBA_HUMAN3136BinaryPhysicochemical compatibilityDual phosphorylation of S32 and S36 in the TrCP1-binding motif of NF-kappa-B inhibitor alpha (NFKBIA) targets the protein to the SCF ubiquitin ligase complex, which marks it for degradation.
details
Inferred
DEG_SCF_TRCP1_1 IKBA_HUMAN3136BinaryPhysicochemical compatibilityDual phosphorylation of S32 and S36 in the TrCP1-binding motif of NF-kappa-B inhibitor alpha (NFKBIA) targets the protein to the SCF ubiquitin ligase complex, which marks it for degradation.
details
Inferred

Insulin receptor - INSR -  Rattus norvegicus
LIG_SH2_GRB2 IRS1_RAT895898BinaryPhysicochemical compatibilityPhosphorylation of Y895 in the SH2-binding motif of Insulin receptor substrate 1 (Irs1) induces binding to the Growth factor receptor-bound protein 2 (Grb2) protein.
details
Inferred
LIG_SH2_IB CBL_HUMAN770780BinaryPhysicochemical compatibilityPhosphorylation of Y774 in the SH2-binding motif of E3 ubiquitin-protein ligase CBL (CBL) induces binding to the Adapter molecule crk (CRK) protein.
details
Inferred

Insulin receptor - INSR -  Homo sapiens
LIG_PTB_Phospho_1 INSR_HUMAN993999BinaryPhysicochemical compatibilityPhosphorylation of Y999 in the PTB-binding motif of Insulin receptor (INSR) induces binding to the SHC-transforming protein 1 (SHC1) protein.
details
Inferred
LIG_PTB_Phospho_1 INSR_HUMAN993999BinaryPhysicochemical compatibilityPhosphorylation of Y999 in the PTB-binding motif of Insulin receptor (INSR) induces binding to the SHC-transforming protein 1 (SHC1) protein.
details
Inferred
LIG_PTB_Phospho_1 INSR_HUMAN993999BinaryPhysicochemical compatibilityPhosphorylation of Y999 in the PTB-binding motif of Insulin receptor (INSR) induces binding to the SHC-transforming protein 1 (SHC1) protein.
details
Inferred
LIG_PTB_Phospho_1 INSR_HUMAN993999BinaryPhysicochemical compatibilityPhosphorylation of Y999 in the PTB-binding motif of Insulin receptor (INSR) induces binding to the SHC-transforming protein 1 (SHC1) protein.
details
Inferred
LIG_SH2_GRB2 IRS1_RAT895898BinaryPhysicochemical compatibilityPhosphorylation of Y895 in the SH2-binding motif of Insulin receptor substrate 1 (Irs1) induces binding to the Growth factor receptor-bound protein 2 (Grb2) protein.
details
Inferred
LIG_SH2_GRB2 IRS1_RAT895898BinaryPhysicochemical compatibilityPhosphorylation of Y895 in the SH2-binding motif of Insulin receptor substrate 1 (Irs1) induces binding to the Growth factor receptor-bound protein 2 (Grb2) protein.
details
Inferred
LIG_SH2_STAT5 GAB1_HUMAN472475BinaryPhysicochemical compatibilityPhosphorylation of Y472 in the SH2-binding motif of GRB2-associated-binding protein 1 (GAB1) induces binding to Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1).
details
Inferred
LIG_SH2_STAT5 GAB1_HUMAN472475BinaryPhysicochemical compatibilityPhosphorylation of Y472 in the SH2-binding motif of GRB2-associated-binding protein 1 (GAB1) induces binding to Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1).
details
Inferred
LIG_SH2_STAT5 GAB1_HUMAN447450BinaryPhysicochemical compatibilityPhosphorylation of Y447 in the SH2-binding motif of GRB2-associated-binding protein 1 (GAB1) induces binding to Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1).
details
Inferred
LIG_SH2_STAT5 GAB1_HUMAN447450BinaryPhysicochemical compatibilityPhosphorylation of Y447 in the SH2-binding motif of GRB2-associated-binding protein 1 (GAB1) induces binding to Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1).
details
Inferred

Insulin-like growth factor 1 receptor - IGF1R -  Homo sapiens
LIG_SH2_GRB2 IRS1_RAT895898BinaryPhysicochemical compatibilityPhosphorylation of Y895 in the SH2-binding motif of Insulin receptor substrate 1 (Irs1) induces binding to the Growth factor receptor-bound protein 2 (Grb2) protein.
details
Inferred
LIG_SH2_IC PDPK1_HUMAN376379BinaryPhysicochemical compatibilityPhosphorylation of Y376 in the SH2-binding motif of 3-phosphoinositide-dependent protein kinase 1 (PDPK1) induces binding to the Tensin-1 (TNS1) protein.
details
Inferred

Integrin-linked protein kinase - ILK -  Homo sapiens
DOC_AGCK_PIF_1 AKT1_HUMAN469474BinaryPhysicochemical compatibilityPhosphorylation of S473 in the PIF motif of RAC-alpha serine/threonine-protein kinase (AKT1) by Serine/threonine-protein kinase mTOR (MTOR) (as part of mTORC2 complex) induces intramolecular interaction with the PIF-binding pocket, resulting in cis-activation of RAC-alpha serine/threonine-protein kinase (AKT1). Dephosphorylation of the PIF motif by PHLPP1/2 (PHLPP1 for Akt2/3 and PHLPP2 for Akt1/3) results in reduced Akt activity, probably by disrupting the interaction with the Akt PIF pocket and thus cis-activation.
details
Inferred
DOC_AGCK_PIF_1 AKT1_HUMAN469474BinaryPhysicochemical compatibilityPhosphorylation of S473 in the PIF motif of RAC-alpha serine/threonine-protein kinase (AKT1) by Serine/threonine-protein kinase mTOR (MTOR) (as part of mTORC2 complex) induces intramolecular interaction with the PIF-binding pocket, resulting in cis-activation of RAC-alpha serine/threonine-protein kinase (AKT1). Dephosphorylation of the PIF motif by PHLPP1/2 (PHLPP1 for Akt2/3 and PHLPP2 for Akt1/3) results in reduced Akt activity, probably by disrupting the interaction with the Akt PIF pocket and thus cis-activation.
details
Inferred

Interleukin-1 receptor-associated kinase 1 - IRAK1 -  Homo sapiens
DOC_WW_Pin1_4 STAT3_HUMAN724729BinaryPhysicochemical compatibilityPhosphorylation of S727 in the Pin1-binding motif of Signal transducer and activator of transcription 3 (STAT3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 STAT3_HUMAN724729BinaryPhysicochemical compatibilityPhosphorylation of S727 in the Pin1-binding motif of Signal transducer and activator of transcription 3 (STAT3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred

Interleukin-1 receptor-associated kinase 4 - IRAK4 -  Homo sapiens
DOC_WW_Pin1_4 NCF1_HUMAN342347BinaryPhysicochemical compatibilityPhosphorylation of S345 in the Pin1-binding motif of Neutrophil cytosol factor 1 (NCF1) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred

Leucine-rich repeat serine/threonine-protein kinase 2 - LRRK2 -  Homo sapiens
DOC_AGCK_PIF_1 AKT1_HUMAN469474BinaryPhysicochemical compatibilityPhosphorylation of S473 in the PIF motif of RAC-alpha serine/threonine-protein kinase (AKT1) by Serine/threonine-protein kinase mTOR (MTOR) (as part of mTORC2 complex) induces intramolecular interaction with the PIF-binding pocket, resulting in cis-activation of RAC-alpha serine/threonine-protein kinase (AKT1). Dephosphorylation of the PIF motif by PHLPP1/2 (PHLPP1 for Akt2/3 and PHLPP2 for Akt1/3) results in reduced Akt activity, probably by disrupting the interaction with the Akt PIF pocket and thus cis-activation.
details
Inferred

MAP kinase-activated protein kinase 2 - MAPKAPK2 -  Homo sapiens
DOC_AGCK_PIF_1 AKT1_HUMAN469474BinaryPhysicochemical compatibilityPhosphorylation of S473 in the PIF motif of RAC-alpha serine/threonine-protein kinase (AKT1) by Serine/threonine-protein kinase mTOR (MTOR) (as part of mTORC2 complex) induces intramolecular interaction with the PIF-binding pocket, resulting in cis-activation of RAC-alpha serine/threonine-protein kinase (AKT1). Dephosphorylation of the PIF motif by PHLPP1/2 (PHLPP1 for Akt2/3 and PHLPP2 for Akt1/3) results in reduced Akt activity, probably by disrupting the interaction with the Akt PIF pocket and thus cis-activation.
details
Inferred
LIG_14-3-3_3 MPIP3_HUMAN213218BinaryPhysicochemical compatibilityPhosphorylation of S216 in a 14-3-3-binding motif of M-phase inducer phosphatase 3 (CDC25C) by Serine/threonine-protein kinase Chk1 (CHEK1) induces binding to 14-3-3 protein beta/alpha (YWHAB), which negatively regulates M-phase inducer phosphatase 3 (CDC25C).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred

MAP kinase-activated protein kinase 5 - MAPKAPK5 -  Homo sapiens
MOD_GSK3_1 P53_HUMAN3037BinaryPhysicochemical compatibilityPhosphorylation of Cellular tumor antigen p53 (TP53) at S37 primes the protein for phosphorylation at S33 by Glycogen synthase kinase-3 beta (GSK3B).
details
Inferred
MOD_GSK3_1 P53_HUMAN3037BinaryPhysicochemical compatibilityPhosphorylation of Cellular tumor antigen p53 (TP53) at S37 primes the protein for phosphorylation at S33 by Glycogen synthase kinase-3 beta (GSK3B).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred

MAP/microtubule affinity-regulating kinase 3 - MARK3 -  Homo sapiens
LIG_14-3-3_3 MPIP3_HUMAN213218BinaryPhysicochemical compatibilityPhosphorylation of S216 in a 14-3-3-binding motif of M-phase inducer phosphatase 3 (CDC25C) by Serine/threonine-protein kinase Chk1 (CHEK1) induces binding to 14-3-3 protein beta/alpha (YWHAB), which negatively regulates M-phase inducer phosphatase 3 (CDC25C).
details
Inferred
LIG_14-3-3_3 PTN3_HUMAN356361Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in Tyrosine-protein phosphatase non-receptor type 3 (PTPN3) induces high-avidity binding to dimeric 14-3-3 protein beta/alpha (YWHAB).
details
Curated

MAP/microtubule affinity-regulating kinase 3 - MARK3 -  Mus musculus
LIG_14-3-3_3 KSR1_MOUSE294299Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in Kinase suppressor of Ras 1 (Ksr1) by Q03141 induces high-avidity binding to dimeric 14-3-3 protein beta/alpha (Ywhab). This interaction prevents Kinase suppressor of Ras 1 (Ksr1) to localise to the membrane where it is involved in activation of MAP kinases by Q99N57 in response to growth factors.
details
Curated
LIG_14-3-3_3 KSR1_MOUSE389394Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in Kinase suppressor of Ras 1 (Ksr1) by Q03141 induces high-avidity binding to dimeric 14-3-3 protein beta/alpha (Ywhab). This interaction prevents Kinase suppressor of Ras 1 (Ksr1) to localise to the membrane where it is involved in activation of MAP kinases by Q99N57 in response to growth factors.
details
Curated

Macrophage-stimulating protein receptor - MST1R -  Homo sapiens
LIG_SH2_IC MET_HUMAN13511360BinaryPhysicochemical compatibilityPhosphorylation of Y1356 in the SH2-binding motif of Hepatocyte growth factor receptor (MET) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.
details
Inferred

Maternal embryonic leucine zipper kinase - MELK -  Mus musculus
DOC_WW_Pin1_4 SMAD3_HUMAN201206BinaryPhysicochemical compatibilityPhosphorylation of S204 in the Pin1-binding motif of Mothers against decapentaplegic homolog 3 (SMAD3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
LIG_WW_1 SMAD3_HUMAN181184Avidity‑sensingCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Dual phosphorylation of the two NEDD4L-binding sites mediates high-avidity binding of two WW domains of NEDD4L to SMAD3. See also switch details and switch details.
details
Inferred
LIG_WW_Nedd4L SMAD3_HUMAN203210Avidity‑sensingCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Dual phosphorylation of the two NEDD4L-binding sites mediates high-avidity binding of two WW domains of NEDD4L to SMAD3. See also switch details and switch details.
details
Inferred
LIG_WW_Nedd4L SMAD3_HUMAN203210CumulativeRheostaticCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Phosphorylation of S208 in SMAD3 induces binding of the third WW domain of NEDD4L, while additional phosphorylation of S204 in SMAD3 further increases the affinity of this interaction. See also switch details and switch details.
details
Inferred

Mitogen-activated protein kinase 1 - MAPK1 -  Mus musculus
DOC_WW_Pin1_4 B2L11_MOUSE6267BinaryPhysicochemical compatibilityPhosphorylation of S65 in the Pin1-binding motif of Bcl-2-like protein 11 (Bcl2l11) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details
Inferred
DOC_WW_Pin1_4 STF1_MOUSE200205BinaryPhysicochemical compatibilityPhosphorylation of S203 in the Pin1-binding motif of Steroidogenic factor 1 (Nr5a1) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred

Mitogen-activated protein kinase 1 - MAPK1 -  Homo sapiens
MOD_GSK3_1 MYC_HUMAN5562BinaryPhysicochemical compatibilityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 primes the protein for phosphorylation at T58 by Glycogen synthase kinase-3 beta (GSK3B).
details
Curated
DOC_WW_Pin1_4 MYC_HUMAN5560BinaryPhysicochemical compatibilityPhosphorylation of T58 in the Pin1-binding motif of Myc proto-oncogene protein (MYC) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 NCF1_HUMAN342347BinaryPhysicochemical compatibilityPhosphorylation of S345 in the Pin1-binding motif of Neutrophil cytosol factor 1 (NCF1) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 NR4A1_HUMAN428433BinaryPhysicochemical compatibilityPhosphorylation of S431 in the Pin1-binding motif of Nuclear receptor subfamily 4 group A member 1 (NR4A1) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 STF1_MOUSE200205BinaryPhysicochemical compatibilityPhosphorylation of S203 in the Pin1-binding motif of Steroidogenic factor 1 (Nr5a1) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details
Inferred
DOC_WW_Pin1_4 STF1_MOUSE200205BinaryPhysicochemical compatibilityPhosphorylation of S203 in the Pin1-binding motif of Steroidogenic factor 1 (Nr5a1) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details
Inferred
DOC_WW_Pin1_4 CDN1B_HUMAN184189BinaryPhysicochemical compatibilityPhosphorylation of T187 in the Pin1-binding motif of Cyclin-dependent kinase inhibitor 1B (CDKN1B) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 SMAD3_HUMAN176181BinaryPhysicochemical compatibilityPhosphorylation of T179 in the Pin1-binding motif of Mothers against decapentaplegic homolog 3 (SMAD3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 SMAD3_HUMAN176181BinaryPhysicochemical compatibilityPhosphorylation of T179 in the Pin1-binding motif of Mothers against decapentaplegic homolog 3 (SMAD3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 SMAD3_HUMAN176181BinaryPhysicochemical compatibilityPhosphorylation of T179 in the Pin1-binding motif of Mothers against decapentaplegic homolog 3 (SMAD3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 SMAD3_HUMAN201206BinaryPhysicochemical compatibilityPhosphorylation of S204 in the Pin1-binding motif of Mothers against decapentaplegic homolog 3 (SMAD3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 SMAD3_HUMAN201206BinaryPhysicochemical compatibilityPhosphorylation of S204 in the Pin1-binding motif of Mothers against decapentaplegic homolog 3 (SMAD3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 SMAD3_HUMAN201206BinaryPhysicochemical compatibilityPhosphorylation of S204 in the Pin1-binding motif of Mothers against decapentaplegic homolog 3 (SMAD3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 SMAD3_HUMAN201206BinaryPhysicochemical compatibilityPhosphorylation of S204 in the Pin1-binding motif of Mothers against decapentaplegic homolog 3 (SMAD3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 SMAD3_HUMAN205210BinaryPhysicochemical compatibilityPhosphorylation of S208 in the Pin1-binding motif of Mothers against decapentaplegic homolog 3 (SMAD3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 SMAD3_HUMAN205210BinaryPhysicochemical compatibilityPhosphorylation of S208 in the Pin1-binding motif of Mothers against decapentaplegic homolog 3 (SMAD3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 SMAD3_HUMAN205210BinaryPhysicochemical compatibilityPhosphorylation of S208 in the Pin1-binding motif of Mothers against decapentaplegic homolog 3 (SMAD3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 SMAD3_HUMAN205210BinaryPhysicochemical compatibilityPhosphorylation of S208 in the Pin1-binding motif of Mothers against decapentaplegic homolog 3 (SMAD3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 SMAD3_HUMAN210215BinaryPhysicochemical compatibilityPhosphorylation of S213 in the Pin1-binding motif of Mothers against decapentaplegic homolog 3 (SMAD3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 SMAD3_HUMAN210215BinaryPhysicochemical compatibilityPhosphorylation of S213 in the Pin1-binding motif of Mothers against decapentaplegic homolog 3 (SMAD3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
LIG_SH3_2 MYC_HUMAN6065BinaryPhysicochemical compatibilityPhosphorylation of S62 in the SH3-binding motif of Myc proto-oncogene protein (MYC) by GSK-3 subfamily disrupts its interaction with Myc box-dependent-interacting protein 1 (BIN1).
details
Inferred
LIG_SH3_2 MYC_HUMAN6065BinaryPhysicochemical compatibilityPhosphorylation of S62 in the SH3-binding motif of Myc proto-oncogene protein (MYC) by GSK-3 subfamily disrupts its interaction with Myc box-dependent-interacting protein 1 (BIN1).
details
Inferred
LIG_PH_Tfb1 P53_HUMAN5056CumulativeRheostaticMultisite phosphorylation of S46 and T55 in the PH-like binding motif of Cellular tumor antigen p53 (TP53) gradually enhances its affinity for General transcription factor IIH subunit 1 (GTF2H1), an interaction involved in activation of transcription initiation and elongation by Cellular tumor antigen p53 (TP53).
details
Inferred
DOC_WW_Pin1_4 SMAD3_HUMAN176181SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Inferred
DOC_WW_Pin1_4 SMAD3_HUMAN176181SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Inferred
DOC_WW_Pin1_4 SMAD3_HUMAN176181SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Inferred
MOD_GSK3_1 SMAD3_HUMAN201208SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Inferred
MOD_GSK3_1 SMAD3_HUMAN201208SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Inferred
MOD_GSK3_1 SMAD3_HUMAN201208SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Inferred
LIG_WW_Nedd4L SMAD3_HUMAN203210SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Inferred
LIG_WW_Nedd4L SMAD3_HUMAN203210SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Inferred
LIG_WW_Nedd4L SMAD3_HUMAN203210SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Inferred
LIG_WW_1 SMAD3_HUMAN181184SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Inferred
LIG_WW_1 SMAD3_HUMAN181184SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Inferred
LIG_WW_1 SMAD3_HUMAN181184SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
Inferred
MOD_ProDKin_1 MYC_HUMAN5965SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Inferred
MOD_ProDKin_1 MYC_HUMAN5965SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Inferred
MOD_ProDKin_1 MYC_HUMAN5965SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Inferred
MOD_GSK3_1 MYC_HUMAN5562SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Curated
DEG_SCF_FBW7_1 MYC_HUMAN5562SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Curated
MOD_CDK_1 CDN1B_HUMAN184190Pre‑assemblyComposite binding site formationBinding of Cyclin-dependent kinase inhibitor 1B (CDKN1B) (p27) to the SCF-Skp2 ubiquitin ligase complex requires phosphorylation of p27 (CDKN1B) at T187, and association of the F-box protein S-phase kinase-associated protein 2 (SKP2) with the regulatory Cyclin-dependent kinases regulatory subunit 1 (CKS1B). SKP2 and CKS1B together generate a composite binding site for p27 (CDKN1B). While some residues, including the phosphorylated T187, bind to CKS1B and others to SKP2, the E185 makes contact with residues of both CKS1B and SKP2.
details
Inferred
DEG_SCF_SKP2-CKS1_1 CDN1B_HUMAN183190Pre‑assemblyComposite binding site formationBinding of Cyclin-dependent kinase inhibitor 1B (CDKN1B) (p27) to the SCF-Skp2 ubiquitin ligase complex requires phosphorylation of p27 (CDKN1B) at T187, and association of the F-box protein S-phase kinase-associated protein 2 (SKP2) with the regulatory Cyclin-dependent kinases regulatory subunit 1 (CKS1B). SKP2 and CKS1B together generate a composite binding site for p27 (CDKN1B). While some residues, including the phosphorylated T187, bind to CKS1B and others to SKP2, the E185 makes contact with residues of both CKS1B and SKP2.
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_WW_1 SMAD3_HUMAN181184Avidity‑sensingCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Dual phosphorylation of the two NEDD4L-binding sites mediates high-avidity binding of two WW domains of NEDD4L to SMAD3. See also switch details and switch details.
details
Inferred
LIG_WW_1 SMAD3_HUMAN181184Avidity‑sensingCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Dual phosphorylation of the two NEDD4L-binding sites mediates high-avidity binding of two WW domains of NEDD4L to SMAD3. See also switch details and switch details.
details
Inferred
LIG_WW_1 SMAD3_HUMAN181184Avidity‑sensingCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Dual phosphorylation of the two NEDD4L-binding sites mediates high-avidity binding of two WW domains of NEDD4L to SMAD3. See also switch details and switch details.
details
Inferred
LIG_WW_1 SMAD3_HUMAN181184Avidity‑sensingCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Dual phosphorylation of the two NEDD4L-binding sites mediates high-avidity binding of two WW domains of NEDD4L to SMAD3. See also switch details and switch details.
details
Inferred
LIG_WW_1 SMAD3_HUMAN181184Avidity‑sensingCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Dual phosphorylation of the two NEDD4L-binding sites mediates high-avidity binding of two WW domains of NEDD4L to SMAD3. See also switch details and switch details.
details
Inferred
LIG_WW_1 SMAD3_HUMAN181184Avidity‑sensingCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Dual phosphorylation of the two NEDD4L-binding sites mediates high-avidity binding of two WW domains of NEDD4L to SMAD3. See also switch details and switch details.
details
Inferred
LIG_WW_1 SMAD3_HUMAN181184Avidity‑sensingCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Dual phosphorylation of the two NEDD4L-binding sites mediates high-avidity binding of two WW domains of NEDD4L to SMAD3. See also switch details and switch details.
details
Inferred
LIG_WW_1 SMAD3_HUMAN181184Avidity‑sensingCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Dual phosphorylation of the two NEDD4L-binding sites mediates high-avidity binding of two WW domains of NEDD4L to SMAD3. See also switch details and switch details.
details
Inferred
LIG_WW_Nedd4L SMAD3_HUMAN203210Avidity‑sensingCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Dual phosphorylation of the two NEDD4L-binding sites mediates high-avidity binding of two WW domains of NEDD4L to SMAD3. See also switch details and switch details.
details
Inferred
LIG_WW_Nedd4L SMAD3_HUMAN203210Avidity‑sensingCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Dual phosphorylation of the two NEDD4L-binding sites mediates high-avidity binding of two WW domains of NEDD4L to SMAD3. See also switch details and switch details.
details
Inferred
LIG_WW_Nedd4L SMAD3_HUMAN203210Avidity‑sensingCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Dual phosphorylation of the two NEDD4L-binding sites mediates high-avidity binding of two WW domains of NEDD4L to SMAD3. See also switch details and switch details.
details
Inferred
LIG_WW_Nedd4L SMAD3_HUMAN203210Avidity‑sensingCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Dual phosphorylation of the two NEDD4L-binding sites mediates high-avidity binding of two WW domains of NEDD4L to SMAD3. See also switch details and switch details.
details
Inferred
LIG_WW_Nedd4L SMAD3_HUMAN203210Avidity‑sensingCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Dual phosphorylation of the two NEDD4L-binding sites mediates high-avidity binding of two WW domains of NEDD4L to SMAD3. See also switch details and switch details.
details
Inferred
LIG_WW_Nedd4L SMAD3_HUMAN203210Avidity‑sensingCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Dual phosphorylation of the two NEDD4L-binding sites mediates high-avidity binding of two WW domains of NEDD4L to SMAD3. See also switch details and switch details.
details
Inferred
LIG_WW_Nedd4L SMAD3_HUMAN203210Avidity‑sensingCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Dual phosphorylation of the two NEDD4L-binding sites mediates high-avidity binding of two WW domains of NEDD4L to SMAD3. See also switch details and switch details.
details
Inferred
LIG_WW_Nedd4L SMAD3_HUMAN203210Avidity‑sensingCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Dual phosphorylation of the two NEDD4L-binding sites mediates high-avidity binding of two WW domains of NEDD4L to SMAD3. See also switch details and switch details.
details
Inferred
LIG_WW_Nedd4L SMAD3_HUMAN203210CumulativeRheostaticCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Phosphorylation of S208 in SMAD3 induces binding of the third WW domain of NEDD4L, while additional phosphorylation of S204 in SMAD3 further increases the affinity of this interaction. See also switch details and switch details.
details
Inferred
LIG_WW_Nedd4L SMAD3_HUMAN203210CumulativeRheostaticCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Phosphorylation of S208 in SMAD3 induces binding of the third WW domain of NEDD4L, while additional phosphorylation of S204 in SMAD3 further increases the affinity of this interaction. See also switch details and switch details.
details
Inferred
LIG_WW_Nedd4L SMAD3_HUMAN203210CumulativeRheostaticCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Phosphorylation of S208 in SMAD3 induces binding of the third WW domain of NEDD4L, while additional phosphorylation of S204 in SMAD3 further increases the affinity of this interaction. See also switch details and switch details.
details
Inferred
LIG_WW_Nedd4L SMAD3_HUMAN203210CumulativeRheostaticCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Phosphorylation of S208 in SMAD3 induces binding of the third WW domain of NEDD4L, while additional phosphorylation of S204 in SMAD3 further increases the affinity of this interaction. See also switch details and switch details.
details
Inferred
LIG_WW_Nedd4L SMAD3_HUMAN203210CumulativeRheostaticCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Phosphorylation of S208 in SMAD3 induces binding of the third WW domain of NEDD4L, while additional phosphorylation of S204 in SMAD3 further increases the affinity of this interaction. See also switch details and switch details.
details
Inferred
LIG_WW_Nedd4L SMAD3_HUMAN203210CumulativeRheostaticCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Phosphorylation of S208 in SMAD3 induces binding of the third WW domain of NEDD4L, while additional phosphorylation of S204 in SMAD3 further increases the affinity of this interaction. See also switch details and switch details.
details
Inferred
LIG_WW_Nedd4L SMAD3_HUMAN203210CumulativeRheostaticCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Phosphorylation of S208 in SMAD3 induces binding of the third WW domain of NEDD4L, while additional phosphorylation of S204 in SMAD3 further increases the affinity of this interaction. See also switch details and switch details.
details
Inferred
LIG_WW_Nedd4L SMAD3_HUMAN203210CumulativeRheostaticCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Phosphorylation of S208 in SMAD3 induces binding of the third WW domain of NEDD4L, while additional phosphorylation of S204 in SMAD3 further increases the affinity of this interaction. See also switch details and switch details.
details
Inferred
LIG_eIF4E_1 4EBP1_HUMAN5460BinaryPhysicochemical compatibilityPhosphorylation of S65 flanking the eIF4E-binding motif of Eukaryotic translation initiation factor 4E-binding protein 1 (EIF4EBP1) by Serine/threonine-protein kinase mTOR (MTOR) inhibits binding to Eukaryotic translation initiation factor 4E (EIF4E) in response to growth factors and nutrients. This results in release of Eukaryotic translation initiation factor 4E (EIF4E), which associates with other initiation factors to form the eIF-4F complex that mediates initiation of translation. However, disruption of the interaction between Eukaryotic translation initiation factor 4E-binding protein 1 (EIF4EBP1) and Eukaryotic translation initiation factor 4E (EIF4E) has been shown to be dependent on hyperphosphorylation of Eukaryotic translation initiation factor 4E-binding protein 1 (EIF4EBP1) by FRAP/mTOR, PI3K and ERK pathways. According to the current model, Eukaryotic translation initiation factor 4E-binding protein 1 (EIF4EBP1) is phosphorylated on multiple residues in a well-defined order. Basal phosphorylation of T37 and T46 serves as a priming event for subsequent serum-induced phosphorylation of T70, which primes for subsequent phosphorylation of S65.
details
Inferred

Mitogen-activated protein kinase 10 - MAPK10 -  Mus musculus
DOC_WW_Pin1_4 B2L11_MOUSE6267BinaryPhysicochemical compatibilityPhosphorylation of S65 in the Pin1-binding motif of Bcl-2-like protein 11 (Bcl2l11) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details
Inferred

Mitogen-activated protein kinase 10 - MAPK10 -  Homo sapiens
MOD_GSK3_1 MYC_HUMAN5562BinaryPhysicochemical compatibilityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 primes the protein for phosphorylation at T58 by Glycogen synthase kinase-3 beta (GSK3B).
details
Inferred
DOC_WW_Pin1_4 B2L11_MOUSE6267BinaryPhysicochemical compatibilityPhosphorylation of S65 in the Pin1-binding motif of Bcl-2-like protein 11 (Bcl2l11) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details
Inferred
DOC_WW_Pin1_4 B2L11_MOUSE6267BinaryPhysicochemical compatibilityPhosphorylation of S65 in the Pin1-binding motif of Bcl-2-like protein 11 (Bcl2l11) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details
Inferred
DOC_WW_Pin1_4 MYC_HUMAN5560BinaryPhysicochemical compatibilityPhosphorylation of T58 in the Pin1-binding motif of Myc proto-oncogene protein (MYC) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
LIG_SH3_2 MYC_HUMAN6065BinaryPhysicochemical compatibilityPhosphorylation of S62 in the SH3-binding motif of Myc proto-oncogene protein (MYC) by GSK-3 subfamily disrupts its interaction with Myc box-dependent-interacting protein 1 (BIN1).
details
Inferred
MOD_ProDKin_1 MYC_HUMAN5965SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Inferred
MOD_ProDKin_1 MYC_HUMAN5965SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Inferred
MOD_GSK3_1 MYC_HUMAN5562SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Inferred
MOD_GSK3_1 MYC_HUMAN5562SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Inferred
DEG_SCF_FBW7_1 MYC_HUMAN5562SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Inferred
DEG_SCF_FBW7_1 MYC_HUMAN5562SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Inferred

Mitogen-activated protein kinase 14 - MAPK14 -  Homo sapiens
DOC_WW_Pin1_4 NCF1_HUMAN342347BinaryPhysicochemical compatibilityPhosphorylation of S345 in the Pin1-binding motif of Neutrophil cytosol factor 1 (NCF1) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 NCF1_HUMAN342347BinaryPhysicochemical compatibilityPhosphorylation of S345 in the Pin1-binding motif of Neutrophil cytosol factor 1 (NCF1) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 STAT3_HUMAN724729BinaryPhysicochemical compatibilityPhosphorylation of S727 in the Pin1-binding motif of Signal transducer and activator of transcription 3 (STAT3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
LIG_PH_Tfb1 P53_HUMAN5056CumulativeRheostaticMultisite phosphorylation of S46 and T55 in the PH-like binding motif of Cellular tumor antigen p53 (TP53) gradually enhances its affinity for General transcription factor IIH subunit 1 (GTF2H1), an interaction involved in activation of transcription initiation and elongation by Cellular tumor antigen p53 (TP53).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred

Mitogen-activated protein kinase 15 - MAPK15 -  Homo sapiens
DOC_WW_Pin1_4 JUN_HUMAN6065BinaryPhysicochemical compatibilityPhosphorylation of S63 in the Pin1-binding motif of Transcription factor AP-1 (JUN) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 JUN_HUMAN7075BinaryPhysicochemical compatibilityPhosphorylation of S73 in the Pin1-binding motif of Transcription factor AP-1 (JUN) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred

Mitogen-activated protein kinase 3 - MAPK3 -  Rattus norvegicus
MOD_GSK3_1 MYC_HUMAN5562BinaryPhysicochemical compatibilityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 primes the protein for phosphorylation at T58 by Glycogen synthase kinase-3 beta (GSK3B).
details
Inferred
LIG_SH3_2 MYC_HUMAN6065BinaryPhysicochemical compatibilityPhosphorylation of S62 in the SH3-binding motif of Myc proto-oncogene protein (MYC) by GSK-3 subfamily disrupts its interaction with Myc box-dependent-interacting protein 1 (BIN1).
details
Inferred
MOD_ProDKin_1 MYC_HUMAN5965SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Inferred
MOD_GSK3_1 MYC_HUMAN5562SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Inferred
DEG_SCF_FBW7_1 MYC_HUMAN5562SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Inferred

Mitogen-activated protein kinase 3 - MAPK3 -  Mus musculus
DOC_WW_Pin1_4 B2L11_MOUSE6267BinaryPhysicochemical compatibilityPhosphorylation of S65 in the Pin1-binding motif of Bcl-2-like protein 11 (Bcl2l11) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details
Inferred
DOC_WW_Pin1_4 STF1_MOUSE200205BinaryPhysicochemical compatibilityPhosphorylation of S203 in the Pin1-binding motif of Steroidogenic factor 1 (Nr5a1) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details
Inferred
DOC_AGCK_PIF_1 KS6A3_MOUSE382387BinaryPhysicochemical compatibilityAuto-phosphorylation of S386 in the PIF pocket-binding motif of Ribosomal protein S6 kinase alpha-3 (Rps6ka3) induces intramolecular binding and kinase cis-activation.
details
Inferred

Mitogen-activated protein kinase 3 - MAPK3 -  Homo sapiens
DOC_WW_Pin1_4 NCF1_HUMAN342347BinaryPhysicochemical compatibilityPhosphorylation of S345 in the Pin1-binding motif of Neutrophil cytosol factor 1 (NCF1) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 NCF1_HUMAN342347BinaryPhysicochemical compatibilityPhosphorylation of S345 in the Pin1-binding motif of Neutrophil cytosol factor 1 (NCF1) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 CDN1B_HUMAN184189BinaryPhysicochemical compatibilityPhosphorylation of T187 in the Pin1-binding motif of Cyclin-dependent kinase inhibitor 1B (CDKN1B) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 ST4A1_HUMAN813BinaryPhysicochemical compatibilityPhosphorylation of T11 in the Pin1-binding motif of Sulfotransferase 4A1 (SULT4A1) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
MOD_CDK_1 CDN1B_HUMAN184190Pre‑assemblyComposite binding site formationBinding of Cyclin-dependent kinase inhibitor 1B (CDKN1B) (p27) to the SCF-Skp2 ubiquitin ligase complex requires phosphorylation of p27 (CDKN1B) at T187, and association of the F-box protein S-phase kinase-associated protein 2 (SKP2) with the regulatory Cyclin-dependent kinases regulatory subunit 1 (CKS1B). SKP2 and CKS1B together generate a composite binding site for p27 (CDKN1B). While some residues, including the phosphorylated T187, bind to CKS1B and others to SKP2, the E185 makes contact with residues of both CKS1B and SKP2.
details
Inferred
DEG_SCF_SKP2-CKS1_1 CDN1B_HUMAN183190Pre‑assemblyComposite binding site formationBinding of Cyclin-dependent kinase inhibitor 1B (CDKN1B) (p27) to the SCF-Skp2 ubiquitin ligase complex requires phosphorylation of p27 (CDKN1B) at T187, and association of the F-box protein S-phase kinase-associated protein 2 (SKP2) with the regulatory Cyclin-dependent kinases regulatory subunit 1 (CKS1B). SKP2 and CKS1B together generate a composite binding site for p27 (CDKN1B). While some residues, including the phosphorylated T187, bind to CKS1B and others to SKP2, the E185 makes contact with residues of both CKS1B and SKP2.
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_eIF4E_1 4EBP1_HUMAN5460BinaryPhysicochemical compatibilityPhosphorylation of S65 flanking the eIF4E-binding motif of Eukaryotic translation initiation factor 4E-binding protein 1 (EIF4EBP1) by Serine/threonine-protein kinase mTOR (MTOR) inhibits binding to Eukaryotic translation initiation factor 4E (EIF4E) in response to growth factors and nutrients. This results in release of Eukaryotic translation initiation factor 4E (EIF4E), which associates with other initiation factors to form the eIF-4F complex that mediates initiation of translation. However, disruption of the interaction between Eukaryotic translation initiation factor 4E-binding protein 1 (EIF4EBP1) and Eukaryotic translation initiation factor 4E (EIF4E) has been shown to be dependent on hyperphosphorylation of Eukaryotic translation initiation factor 4E-binding protein 1 (EIF4EBP1) by FRAP/mTOR, PI3K and ERK pathways. According to the current model, Eukaryotic translation initiation factor 4E-binding protein 1 (EIF4EBP1) is phosphorylated on multiple residues in a well-defined order. Basal phosphorylation of T37 and T46 serves as a priming event for subsequent serum-induced phosphorylation of T70, which primes for subsequent phosphorylation of S65.
details
Inferred

Mitogen-activated protein kinase 7 - MAPK7 -  Homo sapiens
DOC_WW_Pin1_4 PML_HUMAN400405BinaryPhysicochemical compatibilityPhosphorylation of S403 in the Pin1-binding motif of Protein PML (PML) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred

Mitogen-activated protein kinase 8 - MAPK8 -  Homo sapiens
MOD_GSK3_1 MYC_HUMAN5562BinaryPhysicochemical compatibilityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 primes the protein for phosphorylation at T58 by Glycogen synthase kinase-3 beta (GSK3B).
details
Inferred
DOC_WW_Pin1_4 B2L11_MOUSE6267BinaryPhysicochemical compatibilityPhosphorylation of S65 in the Pin1-binding motif of Bcl-2-like protein 11 (Bcl2l11) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details
Inferred
DOC_WW_Pin1_4 B2L11_MOUSE6267BinaryPhysicochemical compatibilityPhosphorylation of S65 in the Pin1-binding motif of Bcl-2-like protein 11 (Bcl2l11) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details
Inferred
DOC_WW_Pin1_4 P53_HUMAN7883BinaryPhysicochemical compatibilityPhosphorylation of T81 in the Pin1-binding motif of Cellular tumor antigen p53 (TP53) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 JUN_HUMAN6065BinaryPhysicochemical compatibilityPhosphorylation of S63 in the Pin1-binding motif of Transcription factor AP-1 (JUN) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 JUN_HUMAN6065BinaryPhysicochemical compatibilityPhosphorylation of S63 in the Pin1-binding motif of Transcription factor AP-1 (JUN) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 JUN_HUMAN6065BinaryPhysicochemical compatibilityPhosphorylation of S63 in the Pin1-binding motif of Transcription factor AP-1 (JUN) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 JUN_HUMAN7075BinaryPhysicochemical compatibilityPhosphorylation of S73 in the Pin1-binding motif of Transcription factor AP-1 (JUN) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 JUN_HUMAN7075BinaryPhysicochemical compatibilityPhosphorylation of S73 in the Pin1-binding motif of Transcription factor AP-1 (JUN) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 NR4A1_HUMAN9297BinaryPhysicochemical compatibilityPhosphorylation of S95 in the Pin1-binding motif of Nuclear receptor subfamily 4 group A member 1 (NR4A1) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 STAT3_HUMAN724729BinaryPhysicochemical compatibilityPhosphorylation of S727 in the Pin1-binding motif of Signal transducer and activator of transcription 3 (STAT3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
LIG_SH3_2 MYC_HUMAN6065BinaryPhysicochemical compatibilityPhosphorylation of S62 in the SH3-binding motif of Myc proto-oncogene protein (MYC) by GSK-3 subfamily disrupts its interaction with Myc box-dependent-interacting protein 1 (BIN1).
details
Inferred
MOD_ProDKin_1 MYC_HUMAN5965SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Inferred
MOD_GSK3_1 MYC_HUMAN5562SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Inferred
DEG_SCF_FBW7_1 MYC_HUMAN5562SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Inferred
MOD_GSK3_1 CTNB1_HUMAN3441SpecificityAltered binding specificityPhosphorylation of Catenin beta-1 (CTNNB1) at T41 generates a docking site for Glycogen synthase kinase-3 beta (GSK3B), which then phosphorylates S37, thereby generating a new docking site for GSK3B. Subsequent phosphorylation of S33 by GSK3B switches the specificity of CTNNB1 to the F-box/WD repeat-containing protein 1A (BTRC), which recruits CTNNB1 to the SCF ubiquitin ligase complex.
details
Inferred
MOD_GSK3_1 CTNB1_HUMAN3441SpecificityAltered binding specificityPhosphorylation of Catenin beta-1 (CTNNB1) at T41 generates a docking site for Glycogen synthase kinase-3 beta (GSK3B), which then phosphorylates S37, thereby generating a new docking site for GSK3B. Subsequent phosphorylation of S33 by GSK3B switches the specificity of CTNNB1 to the F-box/WD repeat-containing protein 1A (BTRC), which recruits CTNNB1 to the SCF ubiquitin ligase complex.
details
Inferred
MOD_GSK3_1 CTNB1_HUMAN3037SpecificityAltered binding specificityPhosphorylation of Catenin beta-1 (CTNNB1) at T41 generates a docking site for Glycogen synthase kinase-3 beta (GSK3B), which then phosphorylates S37, thereby generating a new docking site for GSK3B. Subsequent phosphorylation of S33 by GSK3B switches the specificity of CTNNB1 to the F-box/WD repeat-containing protein 1A (BTRC), which recruits CTNNB1 to the SCF ubiquitin ligase complex.
details
Inferred
MOD_GSK3_1 CTNB1_HUMAN3037SpecificityAltered binding specificityPhosphorylation of Catenin beta-1 (CTNNB1) at T41 generates a docking site for Glycogen synthase kinase-3 beta (GSK3B), which then phosphorylates S37, thereby generating a new docking site for GSK3B. Subsequent phosphorylation of S33 by GSK3B switches the specificity of CTNNB1 to the F-box/WD repeat-containing protein 1A (BTRC), which recruits CTNNB1 to the SCF ubiquitin ligase complex.
details
Inferred
DEG_SCF_TRCP1_1 CTNB1_HUMAN3237SpecificityAltered binding specificityPhosphorylation of Catenin beta-1 (CTNNB1) at T41 generates a docking site for Glycogen synthase kinase-3 beta (GSK3B), which then phosphorylates S37, thereby generating a new docking site for GSK3B. Subsequent phosphorylation of S33 by GSK3B switches the specificity of CTNNB1 to the F-box/WD repeat-containing protein 1A (BTRC), which recruits CTNNB1 to the SCF ubiquitin ligase complex.
details
Inferred
DEG_SCF_TRCP1_1 CTNB1_HUMAN3237SpecificityAltered binding specificityPhosphorylation of Catenin beta-1 (CTNNB1) at T41 generates a docking site for Glycogen synthase kinase-3 beta (GSK3B), which then phosphorylates S37, thereby generating a new docking site for GSK3B. Subsequent phosphorylation of S33 by GSK3B switches the specificity of CTNNB1 to the F-box/WD repeat-containing protein 1A (BTRC), which recruits CTNNB1 to the SCF ubiquitin ligase complex.
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_Dynein_DLC8_1 B2L11_HUMAN5056BinaryPhysicochemical compatibilityPhosphorylation of T56 by Mitogen-activated protein kinase 8 (MAPK8) in the Dynein-binding motif of Isoform Bim(L) of Bcl-2-like protein 11 (BCL2L11) inhibits binding to Dynein light chain 1, cytoplasmic (DYNLL1). Most Bim in healthy cells is sequestered away bound to light chain dynein molecules. Cells exposed to environmental stress up-regulate c-Jun NH(2)-terminal kinase (JNK) that phosphorylates both Bim and Bmf, releasing them from motor complexes and promoting apoptosis.
details
Curated

Mitogen-activated protein kinase 8 - MAPK8 -  Mus musculus
DOC_WW_Pin1_4 B2L11_MOUSE6267BinaryPhysicochemical compatibilityPhosphorylation of S65 in the Pin1-binding motif of Bcl-2-like protein 11 (Bcl2l11) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details
Inferred

Mitogen-activated protein kinase 9 - MAPK9 -  Mus musculus
DOC_WW_Pin1_4 B2L11_MOUSE6267BinaryPhysicochemical compatibilityPhosphorylation of S65 in the Pin1-binding motif of Bcl-2-like protein 11 (Bcl2l11) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details
Inferred

Mitogen-activated protein kinase 9 - MAPK9 -  Homo sapiens
MOD_GSK3_1 MYC_HUMAN5562BinaryPhysicochemical compatibilityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 primes the protein for phosphorylation at T58 by Glycogen synthase kinase-3 beta (GSK3B).
details
Inferred
DOC_WW_Pin1_4 B2L11_MOUSE6267BinaryPhysicochemical compatibilityPhosphorylation of S65 in the Pin1-binding motif of Bcl-2-like protein 11 (Bcl2l11) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details
Inferred
DOC_WW_Pin1_4 B2L11_MOUSE6267BinaryPhysicochemical compatibilityPhosphorylation of S65 in the Pin1-binding motif of Bcl-2-like protein 11 (Bcl2l11) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details
Inferred
DOC_WW_Pin1_4 JUN_HUMAN6065BinaryPhysicochemical compatibilityPhosphorylation of S63 in the Pin1-binding motif of Transcription factor AP-1 (JUN) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 JUN_HUMAN6065BinaryPhysicochemical compatibilityPhosphorylation of S63 in the Pin1-binding motif of Transcription factor AP-1 (JUN) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 JUN_HUMAN7075BinaryPhysicochemical compatibilityPhosphorylation of S73 in the Pin1-binding motif of Transcription factor AP-1 (JUN) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
LIG_SH3_2 MYC_HUMAN6065BinaryPhysicochemical compatibilityPhosphorylation of S62 in the SH3-binding motif of Myc proto-oncogene protein (MYC) by GSK-3 subfamily disrupts its interaction with Myc box-dependent-interacting protein 1 (BIN1).
details
Inferred
MOD_ProDKin_1 MYC_HUMAN5965SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Inferred
MOD_GSK3_1 MYC_HUMAN5562SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Inferred
DEG_SCF_FBW7_1 MYC_HUMAN5562SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred

Mitogen-activated protein kinase 9 - MAPK9 -  Homo sapiens
DOC_WW_Pin1_4 STAT3_HUMAN724729BinaryPhysicochemical compatibilityPhosphorylation of S727 in the Pin1-binding motif of Signal transducer and activator of transcription 3 (STAT3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred

Mitogen-activated protein kinase kinase kinase 14 - MAP3K14 -  Homo sapiens
DEG_SCF_TRCP1_1 IKBA_HUMAN3136BinaryPhysicochemical compatibilityDual phosphorylation of S32 and S36 in the TrCP1-binding motif of NF-kappa-B inhibitor alpha (NFKBIA) targets the protein to the SCF ubiquitin ligase complex, which marks it for degradation.
details
Inferred
DEG_SCF_TRCP1_1 IKBA_HUMAN3136BinaryPhysicochemical compatibilityDual phosphorylation of S32 and S36 in the TrCP1-binding motif of NF-kappa-B inhibitor alpha (NFKBIA) targets the protein to the SCF ubiquitin ligase complex, which marks it for degradation.
details
Inferred

Mitogen-activated protein kinase kinase kinase 5 - MAP3K5 -  Homo sapiens
LIG_14-3-3_1 M3K5_HUMAN963968BinaryPhysicochemical compatibilityPhosphorylation of S966 in the 14-3-3-binding motif of Mitogen-activated protein kinase kinase kinase 5 (MAP3K5) induces binding to the 14-3-3 protein zeta/delta (YWHAZ) protein. This interaction inhibits the pro-apoptotic activity of Mitogen-activated protein kinase kinase kinase 5 (MAP3K5).
details
Inferred
LIG_14-3-3_1 M3K5_HUMAN963968BinaryPhysicochemical compatibilityPhosphorylation of S966 in the 14-3-3-binding motif of Mitogen-activated protein kinase kinase kinase 5 (MAP3K5) induces binding to the 14-3-3 protein zeta/delta (YWHAZ) protein. This interaction inhibits the pro-apoptotic activity of Mitogen-activated protein kinase kinase kinase 5 (MAP3K5).
details
Inferred

Mitogen-activated protein kinase kinase kinase 7 - MAP3K7 -  Mus musculus
LIG_14-3-3_3 KSR1_MOUSE294299Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in Kinase suppressor of Ras 1 (Ksr1) by Q03141 induces high-avidity binding to dimeric 14-3-3 protein beta/alpha (Ywhab). This interaction prevents Kinase suppressor of Ras 1 (Ksr1) to localise to the membrane where it is involved in activation of MAP kinases by Q99N57 in response to growth factors.
details
Inferred
LIG_14-3-3_3 KSR1_MOUSE389394Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in Kinase suppressor of Ras 1 (Ksr1) by Q03141 induces high-avidity binding to dimeric 14-3-3 protein beta/alpha (Ywhab). This interaction prevents Kinase suppressor of Ras 1 (Ksr1) to localise to the membrane where it is involved in activation of MAP kinases by Q99N57 in response to growth factors.
details
Inferred

Mitogen-activated protein kinase kinase kinase MLT - MLTK -  Homo sapiens
LIG_FHA_1 CHK2_HUMAN6672BinaryPhysicochemical compatibilityPhosphorylation of T68 in the FHA-binding motif of Serine/threonine-protein kinase Chk2 (CHEK2) induces binding to the Serine/threonine-protein kinase Chk2 (CHEK2) protein.
details
Inferred

NP_000042 - ? -  ?
DOC_AGCK_PIF_1 AKT1_HUMAN469474BinaryPhysicochemical compatibilityPhosphorylation of S473 in the PIF motif of RAC-alpha serine/threonine-protein kinase (AKT1) by Serine/threonine-protein kinase mTOR (MTOR) (as part of mTORC2 complex) induces intramolecular interaction with the PIF-binding pocket, resulting in cis-activation of RAC-alpha serine/threonine-protein kinase (AKT1). Dephosphorylation of the PIF motif by PHLPP1/2 (PHLPP1 for Akt2/3 and PHLPP2 for Akt1/3) results in reduced Akt activity, probably by disrupting the interaction with the Akt PIF pocket and thus cis-activation.
details
Inferred
LIG_FHA_1 CHK2_HUMAN6672BinaryPhysicochemical compatibilityPhosphorylation of T68 in the FHA-binding motif of Serine/threonine-protein kinase Chk2 (CHEK2) induces binding to the Serine/threonine-protein kinase Chk2 (CHEK2) protein.
details
Inferred
LIG_PH_Tfb1 P53_HUMAN5056CumulativeRheostaticMultisite phosphorylation of S46 and T55 in the PH-like binding motif of Cellular tumor antigen p53 (TP53) gradually enhances its affinity for General transcription factor IIH subunit 1 (GTF2H1), an interaction involved in activation of transcription initiation and elongation by Cellular tumor antigen p53 (TP53).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
DOC_USP7_1 MDM4_HUMAN398402BinaryPhysicochemical compatibilityPhosphorylation of S403 adjacent to the USP7-binding motif of Protein Mdm4 (MDM4) by Serine-protein kinase ATM (ATM) inhibits binding to the Ubiquitin carboxyl-terminal hydrolase 7 (USP7), thereby reducing deubiquitylation of Protein Mdm4 (MDM4). As a result, ubiquitylation by E3 ubiquitin-protein ligase Mdm2 (MDM2) is not countered and Protein Mdm4 (MDM4) is targeted for proteasomal degradation.
details
Inferred

NP_446294 - ? -  ?
MOD_GSK3_1 MYC_HUMAN5562BinaryPhysicochemical compatibilityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 primes the protein for phosphorylation at T58 by Glycogen synthase kinase-3 beta (GSK3B).
details
Inferred
LIG_SH3_2 MYC_HUMAN6065BinaryPhysicochemical compatibilityPhosphorylation of S62 in the SH3-binding motif of Myc proto-oncogene protein (MYC) by GSK-3 subfamily disrupts its interaction with Myc box-dependent-interacting protein 1 (BIN1).
details
Inferred
MOD_ProDKin_1 MYC_HUMAN5965SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Inferred
MOD_GSK3_1 MYC_HUMAN5562SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Inferred
DEG_SCF_FBW7_1 MYC_HUMAN5562SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Inferred

NUAK family SNF1-like kinase 1 - NUAK1 -  Homo sapiens
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred

Negative regulator of sexual conjugation and meiosis - RAN1 -  Schizosaccharomyces pombe (strain 972 / ATCC 24843)
LIG_14-3-3_1 MEI2_SCHPO435440Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in Meiosis protein mei2 (mei2) by Negative regulator of sexual conjugation and meiosis (ran1) induces high-avidity binding to dimeric DNA damage checkpoint protein rad24 (rad24), with pT527 being the high-affinity interaction site.
details
Curated
LIG_14-3-3_2 MEI2_SCHPO523529Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in Meiosis protein mei2 (mei2) by Negative regulator of sexual conjugation and meiosis (ran1) induces high-avidity binding to dimeric DNA damage checkpoint protein rad24 (rad24), with pT527 being the high-affinity interaction site.
details
Curated

Neuronal proto-oncogene tyrosine-protein kinase Src - SRC -  Mus musculus
LIG_SH2_IC EGFR_HUMAN10921100BinaryPhysicochemical compatibilityPhosphorylation of Y1092 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.
details
Inferred
LIG_SH2_IA DAB1_MOUSE212228BinaryPhysicochemical compatibilityPhosphorylation of Y220 in the SH2-binding motif of Disabled homolog 1 (Dab1) induces binding to the Cytoplasmic protein NCK2 (NCK2) protein.
details
Inferred
LIG_SH2_IA DAB1_MOUSE220223BinaryPre‑translationalAlternative splicing removes the SH2-binding motif of Disabled homolog 1 (Dab1), abrogating binding to Cytoplasmic protein NCK2 (NCK2). NCK2-beta has a clear preference for splice variant 2 (with the YQYI motif) over splice variant 3 (with the YQTI motif). The authors theorise that since Adapter molecule crk (Crk) is directly linked to the C3G-Rap1 pathway, and NCK2-beta is linked to the Breast cancer anti-estrogen resistance protein 1 (Bcar1) (p130Cas) pathway, it is likely that isoforms 2 and 3 connect to different downstream cascades. It was suggested that the ability of different Dab1 isoforms to recruit distinct sets of SH2 domains implies a fine-tuning role of Dab1 splicing in the intricate series of events that underlie neuronal migration (Gao et al. (2012) (here)) (See also Katyal and Godbout (2004) (here) and Gao et al. (2010) (here)).
details
Curated
LIG_SH2_IA DAB1_MOUSE220223BinaryPre‑translationalAlternative splicing removes the SH2-binding motif of Disabled homolog 1 (Dab1), abrogating binding to Adapter molecule crk (Crk). Both Adapter molecule crk (Crk) and Crk-like protein (Crkl) bind equally well to variants 2 and 3. The authors theorise that since Adapter molecule crk (Crk) is directly linked to the C3G-Rap1 pathway, and NCK2-beta is linked to the Breast cancer anti-estrogen resistance protein 1 (Bcar1) (p130Cas) pathway, it is likely that isoforms 2 and 3 connect to different downstream cascades. It was suggested that the ability of different Dab1 isoforms to recruit distinct sets of SH2 domains implies a fine-tuning role of Dab1 splicing in the intricate series of events that underlie neuronal migration (Gao et al. (2012) (here)) (See also Katyal and Godbout (2004) (here) and Gao et al. (2010) (here)).
details
Curated
LIG_SH2_SRC DAB1_MOUSE198201BinaryPre‑translationalAlternative splicing removes the SH2-binding motif of Disabled homolog 1 (Dab1), abrogating binding to Neuronal proto-oncogene tyrosine-protein kinase Src (Src). Splice variants 2 and 3 (only containing one of the YQxI motifs, i.e. Y185 and Y198) exhibit decreased tyrosine phosphorylation, suggesting both motifs are required for full activation of Dab1. Dab1 is likely to recruit Neuronal proto-oncogene tyrosine-protein kinase Src (Src) via these two YQxI motifs, which subsequently phosphorylates adjacent YxVP motifs (here). This was also suggested for Phosphatidylinositol 3-kinase regulatory subunit alpha (Pik3r1) and Suppressor of cytokine signaling 2 (Socs2). Gao et al. (2012) (here) suggests that the ability of different Dab1 isoforms to recruit distinct sets of SH2 domains allows a fine-tuning role for Dab1 splicing in the intricate series of events that underlie neuronal migration (See also Katyal & Godbout (2004) (here) and Gao et al. (2010) (here)).
details
Curated
LIG_SH2_SRC DAB1_MOUSE198201BinaryPhysicochemical compatibilityPhosphorylation of Y198 in the SH2-binding motif of Disabled homolog 1 (Dab1) induces binding to Neuronal proto-oncogene tyrosine-protein kinase Src (Src).
details
Curated

Non-receptor tyrosine-protein kinase TYK2 - TYK2 -  Homo sapiens
LIG_SH2_IE INAR1_HUMAN458474BinaryPhysicochemical compatibilityPhosphorylation of Y466 in the SH2-binding motif of Interferon alpha/beta receptor 1 (IFNAR1) induces binding to the Non-receptor tyrosine-protein kinase TYK2 (TYK2) protein.
details
Inferred
LIG_SH2_IE INAR1_HUMAN458474BinaryPhysicochemical compatibilityPhosphorylation of Y466 in the SH2-binding motif of Interferon alpha/beta receptor 1 (IFNAR1) induces binding to the Non-receptor tyrosine-protein kinase TYK2 (TYK2) protein.
details
Inferred
LIG_SH2_IE INAR1_HUMAN458474BinaryPhysicochemical compatibilityPhosphorylation of Y466 in the SH2-binding motif of Interferon alpha/beta receptor 1 (IFNAR1) induces binding to the Non-receptor tyrosine-protein kinase TYK2 (TYK2) protein.
details
Inferred
LIG_SH2_IE INAR1_HUMAN473489BinaryPhysicochemical compatibilityPhosphorylation of Y481 in the SH2-binding motif of Interferon alpha/beta receptor 1 (IFNAR1) induces binding to the Non-receptor tyrosine-protein kinase TYK2 (TYK2) protein.
details
Inferred
LIG_SH2_IE INAR1_HUMAN473489BinaryPhysicochemical compatibilityPhosphorylation of Y481 in the SH2-binding motif of Interferon alpha/beta receptor 1 (IFNAR1) induces binding to the Non-receptor tyrosine-protein kinase TYK2 (TYK2) protein.
details
Inferred

Nucleoside diphosphate kinase A - NME1 -  Homo sapiens
LIG_14-3-3_3 KSR1_MOUSE294299Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in Kinase suppressor of Ras 1 (Ksr1) by Q03141 induces high-avidity binding to dimeric 14-3-3 protein beta/alpha (Ywhab). This interaction prevents Kinase suppressor of Ras 1 (Ksr1) to localise to the membrane where it is involved in activation of MAP kinases by Q99N57 in response to growth factors.
details
Inferred
LIG_14-3-3_3 KSR1_MOUSE389394Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in Kinase suppressor of Ras 1 (Ksr1) by Q03141 induces high-avidity binding to dimeric 14-3-3 protein beta/alpha (Ywhab). This interaction prevents Kinase suppressor of Ras 1 (Ksr1) to localise to the membrane where it is involved in activation of MAP kinases by Q99N57 in response to growth factors.
details
Inferred

Platelet-derived growth factor receptor beta - PDGFRB -  Homo sapiens
LIG_SH2_IIA PGFRB_HUMAN751755BinaryPhysicochemical compatibilityPhosphorylation of Y751 in the SH2-binding motif of Platelet-derived growth factor receptor beta (PDGFRB) induces binding to the Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1) protein.
details
Inferred
LIG_SH2_IIA PGFRB_HUMAN751755BinaryPhysicochemical compatibilityPhosphorylation of Y751 in the SH2-binding motif of Platelet-derived growth factor receptor beta (PDGFRB) induces binding to the Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1) protein.
details
Inferred
LIG_SH2_IIA PGFRB_HUMAN10181029BinaryPhysicochemical compatibilityPhosphorylation of Y1021 in the SH2-binding motif of Platelet-derived growth factor receptor beta (PDGFRB) induces binding to the 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1 (PLCG1) protein.
details
Inferred
LIG_SH2_IIA PGFRB_HUMAN10181029BinaryPhysicochemical compatibilityPhosphorylation of Y1021 in the SH2-binding motif of Platelet-derived growth factor receptor beta (PDGFRB) induces binding to the 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1 (PLCG1) protein.
details
Inferred

Probable serine/threonine-protein kinase pknG - PKNG -  Mycobacterium tuberculosis
LIG_FHA_1 Y1827_MYCTU1925BinaryPhysicochemical compatibilityPhosphorylation of T21 in the FHA-binding motif of Uncharacterized protein Rv1827/MT1875 (Rv1827) by Probable serine/threonine-protein kinase pknG (pknG) results in auto-inhibition due to an intramolecular interaction with the FHA domain. As a result, phosphorylation-independent interactions of the FHA domain with metabolic enzymes, which regulate the catalytic activity of these enzymes, are blocked (See also switch details).
details
Curated

Protein kinase C alpha type - PRKCA -  Homo sapiens
DOC_AGCK_PIF_1 AKT1_HUMAN469474BinaryPhysicochemical compatibilityPhosphorylation of S473 in the PIF motif of RAC-alpha serine/threonine-protein kinase (AKT1) by Serine/threonine-protein kinase mTOR (MTOR) (as part of mTORC2 complex) induces intramolecular interaction with the PIF-binding pocket, resulting in cis-activation of RAC-alpha serine/threonine-protein kinase (AKT1). Dephosphorylation of the PIF motif by PHLPP1/2 (PHLPP1 for Akt2/3 and PHLPP2 for Akt1/3) results in reduced Akt activity, probably by disrupting the interaction with the Akt PIF pocket and thus cis-activation.
details
Inferred
LIG_14-3-3_2 PDE3A_HUMAN424430BinaryPhysicochemical compatibilityPhosphorylation of S428 by in the 14-3-3-binding motif of cGMP-inhibited 3',5'-cyclic phosphodiesterase A (PDE3A) induces binding to the 14-3-3 protein zeta/delta (YWHAZ) protein.
details
Inferred
LIG_Filamin ITB2_HUMAN753763SpecificityAltered binding specificityPhosphorylation of T758 in Integrin beta-2 (ITGB2) switches the specificity of ITGB2 from Filamin-A (FLNA) to 14-3-3 proteins (e.g. 14-3-3 protein zeta/delta (YWHAZ)).
details
Inferred
LIG_Filamin ITB2_HUMAN753763SpecificityAltered binding specificityPhosphorylation of T758 in Integrin beta-2 (ITGB2) switches the specificity of ITGB2 from Filamin-A (FLNA) to 14-3-3 proteins (e.g. 14-3-3 protein zeta/delta (YWHAZ)).
details
Inferred
LIG_14-3-3_3 ITB2_HUMAN755760SpecificityAltered binding specificityPhosphorylation of T758 in Integrin beta-2 (ITGB2) switches the specificity of ITGB2 from Filamin-A (FLNA) to 14-3-3 proteins (e.g. 14-3-3 protein zeta/delta (YWHAZ)).
details
Inferred
LIG_14-3-3_3 ITB2_HUMAN755760SpecificityAltered binding specificityPhosphorylation of T758 in Integrin beta-2 (ITGB2) switches the specificity of ITGB2 from Filamin-A (FLNA) to 14-3-3 proteins (e.g. 14-3-3 protein zeta/delta (YWHAZ)).
details
Inferred
LIG_14-3-3_3 KPCE_HUMAN343348Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in Protein kinase C epsilon type (PRKCE) induces high-avidity binding to dimeric 14-3-3 protein zeta/delta (YWHAZ).
details
Inferred
LIG_14-3-3_3 KPCE_HUMAN365370Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in Protein kinase C epsilon type (PRKCE) induces high-avidity binding to dimeric 14-3-3 protein zeta/delta (YWHAZ).
details
Inferred
LIG_PCNA_PIPBox_1 CDN1A_HUMAN144153BinaryPhysicochemical compatibilityPhosphorylation of T145 in the PCNA-binding motif of Cyclin-dependent kinase inhibitor 1 (CDKN1A) by RAC-alpha serine/threonine-protein kinase (AKT1) inhibits binding to Proliferating cell nuclear antigen (PCNA). As a result, Cyclin-dependent kinase inhibitor 1 (CDKN1A) no longer inhibits Proliferating cell nuclear antigen (PCNA) and blocking of DNA replication is relieved.
details
Inferred
LIG_PCNA_PIPBox_1 CDN1A_HUMAN144153BinaryPhysicochemical compatibilityPhosphorylation of S146 in the PCNA-binding motif of Cyclin-dependent kinase inhibitor 1 (CDKN1A) by PKC subfamily inhibits binding to Proliferating cell nuclear antigen (PCNA). As a result, Cyclin-dependent kinase inhibitor 1 (CDKN1A) no longer inhibits Proliferating cell nuclear antigen (PCNA) and blocking of DNA replication is relieved.
details
Inferred
LIG_PCNA_PIPBox_1 CDN1A_HUMAN144153BinaryPhysicochemical compatibilityPhosphorylation of S146 in the PCNA-binding motif of Cyclin-dependent kinase inhibitor 1 (CDKN1A) by PKC subfamily inhibits binding to Proliferating cell nuclear antigen (PCNA). As a result, Cyclin-dependent kinase inhibitor 1 (CDKN1A) no longer inhibits Proliferating cell nuclear antigen (PCNA) and blocking of DNA replication is relieved.
details
Inferred

Protein kinase C beta type - PRKCB -  Homo sapiens
DOC_AGCK_PIF_1 KPCB_HUMAN656661BinaryPhysicochemical compatibilityDephosphorylation of the PIF motif by PHLPP1/2 results in reduced stability and increased degradation of PKC. This is countered by autophosphorylation of the PIF motif, but mTORC2 might also contribute.
details
Curated
LIG_Filamin ITB2_HUMAN753763SpecificityAltered binding specificityPhosphorylation of T758 in Integrin beta-2 (ITGB2) switches the specificity of ITGB2 from Filamin-A (FLNA) to 14-3-3 proteins (e.g. 14-3-3 protein zeta/delta (YWHAZ)).
details
Inferred
LIG_14-3-3_3 ITB2_HUMAN755760SpecificityAltered binding specificityPhosphorylation of T758 in Integrin beta-2 (ITGB2) switches the specificity of ITGB2 from Filamin-A (FLNA) to 14-3-3 proteins (e.g. 14-3-3 protein zeta/delta (YWHAZ)).
details
Inferred

Protein kinase C beta type - PRKCB -  Homo sapiens
DOC_AGCK_PIF_1 AKT1_HUMAN469474BinaryPhysicochemical compatibilityPhosphorylation of S473 in the PIF motif of RAC-alpha serine/threonine-protein kinase (AKT1) by Serine/threonine-protein kinase mTOR (MTOR) (as part of mTORC2 complex) induces intramolecular interaction with the PIF-binding pocket, resulting in cis-activation of RAC-alpha serine/threonine-protein kinase (AKT1). Dephosphorylation of the PIF motif by PHLPP1/2 (PHLPP1 for Akt2/3 and PHLPP2 for Akt1/3) results in reduced Akt activity, probably by disrupting the interaction with the Akt PIF pocket and thus cis-activation.
details
Inferred
LIG_Filamin ITB2_HUMAN753763SpecificityAltered binding specificityPhosphorylation of T758 in Integrin beta-2 (ITGB2) switches the specificity of ITGB2 from Filamin-A (FLNA) to 14-3-3 proteins (e.g. 14-3-3 protein zeta/delta (YWHAZ)).
details
Inferred
LIG_14-3-3_3 ITB2_HUMAN755760SpecificityAltered binding specificityPhosphorylation of T758 in Integrin beta-2 (ITGB2) switches the specificity of ITGB2 from Filamin-A (FLNA) to 14-3-3 proteins (e.g. 14-3-3 protein zeta/delta (YWHAZ)).
details
Inferred

Protein kinase C delta type - PRKCD -  Homo sapiens
DOC_WW_Pin1_4 STAT3_HUMAN724729BinaryPhysicochemical compatibilityPhosphorylation of S727 in the Pin1-binding motif of Signal transducer and activator of transcription 3 (STAT3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 STAT3_HUMAN724729BinaryPhysicochemical compatibilityPhosphorylation of S727 in the Pin1-binding motif of Signal transducer and activator of transcription 3 (STAT3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
LIG_HP1_1 TIF1B_MOUSE486490BinaryPhysicochemical compatibilityPhosphorylation of S473 close to the Chromo shadow domain-binding motif of Transcription intermediary factor 1-beta (Trim28) by Protein kinase C delta type (Prkcd) negatively regulates its interaction with Chromobox protein homolog 1 (Cbx1), which is crucial for heterochromatin formation and maintenance. This results in relief of transcription repression and promotion of cell cycle progression.
details
Inferred
LIG_PH_Tfb1 P53_HUMAN5056CumulativeRheostaticMultisite phosphorylation of S46 and T55 in the PH-like binding motif of Cellular tumor antigen p53 (TP53) gradually enhances its affinity for General transcription factor IIH subunit 1 (GTF2H1), an interaction involved in activation of transcription initiation and elongation by Cellular tumor antigen p53 (TP53).
details
Inferred
LIG_Filamin ITB2_HUMAN753763SpecificityAltered binding specificityPhosphorylation of T758 in Integrin beta-2 (ITGB2) switches the specificity of ITGB2 from Filamin-A (FLNA) to 14-3-3 proteins (e.g. 14-3-3 protein zeta/delta (YWHAZ)).
details
Inferred
LIG_Filamin ITB2_HUMAN753763SpecificityAltered binding specificityPhosphorylation of T758 in Integrin beta-2 (ITGB2) switches the specificity of ITGB2 from Filamin-A (FLNA) to 14-3-3 proteins (e.g. 14-3-3 protein zeta/delta (YWHAZ)).
details
Inferred
LIG_14-3-3_3 ITB2_HUMAN755760SpecificityAltered binding specificityPhosphorylation of T758 in Integrin beta-2 (ITGB2) switches the specificity of ITGB2 from Filamin-A (FLNA) to 14-3-3 proteins (e.g. 14-3-3 protein zeta/delta (YWHAZ)).
details
Inferred
LIG_14-3-3_3 ITB2_HUMAN755760SpecificityAltered binding specificityPhosphorylation of T758 in Integrin beta-2 (ITGB2) switches the specificity of ITGB2 from Filamin-A (FLNA) to 14-3-3 proteins (e.g. 14-3-3 protein zeta/delta (YWHAZ)).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred

Protein kinase C delta type - PRKCD -  Mus musculus
LIG_HP1_1 TIF1B_MOUSE486490BinaryPhysicochemical compatibilityPhosphorylation of S473 close to the Chromo shadow domain-binding motif of Transcription intermediary factor 1-beta (Trim28) by Protein kinase C delta type (Prkcd) negatively regulates its interaction with Chromobox protein homolog 1 (Cbx1), which is crucial for heterochromatin formation and maintenance. This results in relief of transcription repression and promotion of cell cycle progression.
details
Curated

Protein kinase C epsilon type - PRKCE -  Homo sapiens
DOC_WW_Pin1_4 STAT3_HUMAN724729BinaryPhysicochemical compatibilityPhosphorylation of S727 in the Pin1-binding motif of Signal transducer and activator of transcription 3 (STAT3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
LIG_14-3-3_3 KPCE_HUMAN343348Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in Protein kinase C epsilon type (PRKCE) induces high-avidity binding to dimeric 14-3-3 protein zeta/delta (YWHAZ).
details
Inferred
LIG_14-3-3_3 KPCE_HUMAN365370Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in Protein kinase C epsilon type (PRKCE) induces high-avidity binding to dimeric 14-3-3 protein zeta/delta (YWHAZ).
details
Inferred

Protein kinase C eta type - PRKCH -  Homo sapiens
LIG_Filamin ITB2_HUMAN753763SpecificityAltered binding specificityPhosphorylation of T758 in Integrin beta-2 (ITGB2) switches the specificity of ITGB2 from Filamin-A (FLNA) to 14-3-3 proteins (e.g. 14-3-3 protein zeta/delta (YWHAZ)).
details
Inferred
LIG_Filamin ITB2_HUMAN753763SpecificityAltered binding specificityPhosphorylation of T758 in Integrin beta-2 (ITGB2) switches the specificity of ITGB2 from Filamin-A (FLNA) to 14-3-3 proteins (e.g. 14-3-3 protein zeta/delta (YWHAZ)).
details
Inferred
LIG_14-3-3_3 ITB2_HUMAN755760SpecificityAltered binding specificityPhosphorylation of T758 in Integrin beta-2 (ITGB2) switches the specificity of ITGB2 from Filamin-A (FLNA) to 14-3-3 proteins (e.g. 14-3-3 protein zeta/delta (YWHAZ)).
details
Inferred
LIG_14-3-3_3 ITB2_HUMAN755760SpecificityAltered binding specificityPhosphorylation of T758 in Integrin beta-2 (ITGB2) switches the specificity of ITGB2 from Filamin-A (FLNA) to 14-3-3 proteins (e.g. 14-3-3 protein zeta/delta (YWHAZ)).
details
Inferred

Protein-tyrosine kinase 2-beta - PTK2B -  Homo sapiens
LIG_SH2_IB FAK2_HUMAN394410BinaryPhysicochemical compatibilityPhosphorylation of Y402 in the SH2-binding motif of Protein-tyrosine kinase 2-beta (PTK2B) induces binding to the Megakaryocyte-associated tyrosine-protein kinase (MATK) protein.
details
Inferred
LIG_SH2_IB FAK2_HUMAN394410BinaryPhysicochemical compatibilityPhosphorylation of Y402 in the SH2-binding motif of Protein-tyrosine kinase 2-beta (PTK2B) induces binding to the Megakaryocyte-associated tyrosine-protein kinase (MATK) protein.
details
Inferred

Proto-oncogene tyrosine-protein kinase LCK - LCK -  Mus musculus
TRG_ENDOCYTIC_2 CTLA4_MOUSE201204SpecificityAltered binding specificityDephosphorylation of Y201 of Cytotoxic T-lymphocyte protein 4 (Ctla4) switches the specificity of Ctla4 from SH2 domain-containing proteins like Tyrosine-protein phosphatase non-receptor type 11 (Ptpn11) to the AP-2 complex mu subunit (AP-2 complex subunit mu (Ap2m1)), thereby switching from inhibitory signal transmission and negative regulation of T cell responses to internalization and inactivation of Ctla4.
details
Inferred
LIG_SH2_STAT5 CTLA4_MOUSE201204SpecificityAltered binding specificityDephosphorylation of Y201 of Cytotoxic T-lymphocyte protein 4 (Ctla4) switches the specificity of Ctla4 from SH2 domain-containing proteins like Tyrosine-protein phosphatase non-receptor type 11 (Ptpn11) to the AP-2 complex mu subunit (AP-2 complex subunit mu (Ap2m1)), thereby switching from inhibitory signal transmission and negative regulation of T cell responses to internalization and inactivation of Ctla4.
details
Inferred

Proto-oncogene tyrosine-protein kinase Src - SRC -  Rattus norvegicus
LIG_SH2_SRC SRC_HUMAN530533BinaryPhysicochemical compatibilityPhosphorylation of Y530 in the SH2-binding motif of Proto-oncogene tyrosine-protein kinase Src (SRC) induces an intramolecular interaction with the SH2 domain of Proto-oncogene tyrosine-protein kinase Src (SRC) resulting in inhibition of its activity and preventing intermolecular interactions of its SH2 domain.
details
Inferred

Proto-oncogene tyrosine-protein kinase Src - SRC -  Homo sapiens
LIG_SH2_SRC SRC_HUMAN530533BinaryPhysicochemical compatibilityPhosphorylation of Y530 in the SH2-binding motif of Proto-oncogene tyrosine-protein kinase Src (SRC) induces an intramolecular interaction with the SH2 domain of Proto-oncogene tyrosine-protein kinase Src (SRC) resulting in inhibition of its activity and preventing intermolecular interactions of its SH2 domain.
details
Inferred
LIG_TKB SPY2_HUMAN5560BinaryPhysicochemical compatibilityPhosphorylation of Y55 in Protein sprouty homolog 2 (SPRY2) is necessary for binding to the TKB domain of E3 ubiquitin-protein ligase CBL (CBL).
details
Inferred
LIG_TKB SPY2_HUMAN5560BinaryPhysicochemical compatibilityPhosphorylation of Y55 in Protein sprouty homolog 2 (SPRY2) is necessary for binding to the TKB domain of E3 ubiquitin-protein ligase CBL (CBL).
details
Inferred
LIG_PTB_Phospho_1 ITB3_HUMAN767773BinaryPhysicochemical compatibilityPhosphorylation of Y773 in the PTB-binding motif of Integrin beta-3 (ITGB3) induces binding to the Docking protein 1 (DOK1) protein.
details
Inferred
LIG_PTB_Phospho_1 ITB3_HUMAN767773BinaryPhysicochemical compatibilityPhosphorylation of Y773 in the PTB-binding motif of Integrin beta-3 (ITGB3) induces binding to the Docking protein 1 (DOK1) protein.
details
Inferred
LIG_PTB_Phospho_1 ITB3_HUMAN767773BinaryPhysicochemical compatibilityPhosphorylation of Y773 in the PTB-binding motif of Integrin beta-3 (ITGB3) induces binding to the Docking protein 1 (DOK1) protein.
details
Inferred
LIG_PTB_Phospho_1 ITB3_HUMAN779785BinaryPhysicochemical compatibilityPhosphorylation of Y785 in the PTB-binding motif of Integrin beta-3 (ITGB3) induces binding to the SHC-transforming protein 1 (SHC1) protein.
details
Inferred
LIG_PTB_Phospho_1 ITB3_HUMAN779785BinaryPhysicochemical compatibilityPhosphorylation of Y785 in the PTB-binding motif of Integrin beta-3 (ITGB3) induces binding to the SHC-transforming protein 1 (SHC1) protein.
details
Inferred
LIG_PTB_Phospho_1 LRP1_HUMAN45014507BinaryPhysicochemical compatibilityPhosphorylation of Y4507 in the PTB-binding motif of Prolow-density lipoprotein receptor-related protein 1 (LRP1) induces binding to the SHC-transforming protein 1 (SHC1) protein.
details
Inferred
LIG_PTB_Phospho_1 LRP1_HUMAN45014507BinaryPhysicochemical compatibilityPhosphorylation of Y4507 in the PTB-binding motif of Prolow-density lipoprotein receptor-related protein 1 (LRP1) induces binding to the SHC-transforming protein 1 (SHC1) protein.
details
Inferred
LIG_PTB_Phospho_1 ITB3_HUMAN779785CumulativeRheostaticWhile phosphorylation of Y785 in the PTB-binding motif of Integrin beta-3 (ITGB3) induces binding to SHC-transforming protein 1 (SHC1), additional phosphorylation of Y773 further increases the strength of the interaction.
details
Inferred
LIG_PTB_Phospho_1 ITB3_HUMAN779785CumulativeRheostaticWhile phosphorylation of Y785 in the PTB-binding motif of Integrin beta-3 (ITGB3) induces binding to SHC-transforming protein 1 (SHC1), additional phosphorylation of Y773 further increases the strength of the interaction.
details
Inferred
LIG_PTB_Phospho_1 ITB3_HUMAN779785CumulativeRheostaticWhile phosphorylation of Y785 in the PTB-binding motif of Integrin beta-3 (ITGB3) induces binding to SHC-transforming protein 1 (SHC1), additional phosphorylation of Y773 further increases the strength of the interaction.
details
Inferred
LIG_PTB_Phospho_1 ITB3_HUMAN779785CumulativeRheostaticWhile phosphorylation of Y785 in the PTB-binding motif of Integrin beta-3 (ITGB3) induces binding to SHC-transforming protein 1 (SHC1), additional phosphorylation of Y773 further increases the strength of the interaction.
details
Inferred
LIG_PTB_Phospho_1 ITB3_HUMAN779785CumulativeRheostaticWhile phosphorylation of Y785 in the PTB-binding motif of Integrin beta-3 (ITGB3) induces binding to SHC-transforming protein 1 (SHC1), additional phosphorylation of Y773 further increases the strength of the interaction.
details
Inferred
LIG_PTB_Apo_2 ITB3_HUMAN767774SpecificityAltered binding specificityPhosphorylation of Y773 in Integrin beta-3 (ITGB3) switches the specificity of ITGB3 from Talin-1 (TLN1) to Docking protein 1 (DOK1), with a 2-fold decrease of the affinity for TLN1 and close to a 400-fold increase of the affinity for DOK1. This switch results in negative regulation of integrin activation.
details
Inferred
LIG_PTB_Apo_2 ITB3_HUMAN767774SpecificityAltered binding specificityPhosphorylation of Y773 in Integrin beta-3 (ITGB3) switches the specificity of ITGB3 from Talin-1 (TLN1) to Docking protein 1 (DOK1), with a 2-fold decrease of the affinity for TLN1 and close to a 400-fold increase of the affinity for DOK1. This switch results in negative regulation of integrin activation.
details
Inferred
LIG_PTB_Apo_2 ITB3_HUMAN767774SpecificityAltered binding specificityPhosphorylation of Y773 in Integrin beta-3 (ITGB3) switches the specificity of ITGB3 from Talin-1 (TLN1) to Docking protein 1 (DOK1), with a 2-fold decrease of the affinity for TLN1 and close to a 400-fold increase of the affinity for DOK1. This switch results in negative regulation of integrin activation.
details
Inferred
LIG_PTB_Phospho_1 ITB3_HUMAN767773SpecificityAltered binding specificityPhosphorylation of Y773 in Integrin beta-3 (ITGB3) switches the specificity of ITGB3 from Talin-1 (TLN1) to Docking protein 1 (DOK1), with a 2-fold decrease of the affinity for TLN1 and close to a 400-fold increase of the affinity for DOK1. This switch results in negative regulation of integrin activation.
details
Inferred
LIG_PTB_Phospho_1 ITB3_HUMAN767773SpecificityAltered binding specificityPhosphorylation of Y773 in Integrin beta-3 (ITGB3) switches the specificity of ITGB3 from Talin-1 (TLN1) to Docking protein 1 (DOK1), with a 2-fold decrease of the affinity for TLN1 and close to a 400-fold increase of the affinity for DOK1. This switch results in negative regulation of integrin activation.
details
Inferred
LIG_PTB_Phospho_1 ITB3_HUMAN767773SpecificityAltered binding specificityPhosphorylation of Y773 in Integrin beta-3 (ITGB3) switches the specificity of ITGB3 from Talin-1 (TLN1) to Docking protein 1 (DOK1), with a 2-fold decrease of the affinity for TLN1 and close to a 400-fold increase of the affinity for DOK1. This switch results in negative regulation of integrin activation.
details
Inferred
LIG_WW_1 DAG1_HUMAN889892SpecificityAltered binding specificityAdhesion-dependent phosphorylation of Y892 in Dystroglycan (DAG1) by Src kinase (Proto-oncogene tyrosine-protein kinase Src (SRC)) switches the specificity of DAG1 from the WW domain containing cytoskeletal linker Dystrophin (DMD) to the SH2 domain containing Tyrosine-protein kinase Fyn (FYN).
details
Inferred
LIG_SH2_SRC DAG1_HUMAN892895SpecificityAltered binding specificityAdhesion-dependent phosphorylation of Y892 in Dystroglycan (DAG1) by Src kinase (Proto-oncogene tyrosine-protein kinase Src (SRC)) switches the specificity of DAG1 from the WW domain containing cytoskeletal linker Dystrophin (DMD) to the SH2 domain containing Tyrosine-protein kinase Fyn (FYN).
details
Inferred
LIG_WW_1 DAG1_HUMAN889892SpecificityAltered binding specificityAdhesion-dependent phosphorylation of Y892 in Dystroglycan (DAG1) by c-Src (SRC) switches the specificity of DAG1 from WW domain containing proteins like Utrophin (UTRN) to SH2 domain containing proteins like Tyrosine-protein kinase CSK (CSK).
details
Inferred
LIG_SH2_SRC DAG1_HUMAN892895SpecificityAltered binding specificityAdhesion-dependent phosphorylation of Y892 in Dystroglycan (DAG1) by c-Src (SRC) switches the specificity of DAG1 from WW domain containing proteins like Utrophin (UTRN) to SH2 domain containing proteins like Tyrosine-protein kinase CSK (CSK).
details
Inferred
LIG_PTB_Apo_2 ITB3_HUMAN779786SpecificityAltered binding specificityPhosphorylation of Integrin beta-3 (ITGB3) at Y785 switches the specificity of integrin from Kindlin-2 (Fermitin family homolog 2 (FERMT2)) to the adaptor protein SHC-transforming protein 1 (SHC1).
details
Inferred
LIG_PTB_Apo_2 ITB3_HUMAN779786SpecificityAltered binding specificityPhosphorylation of Integrin beta-3 (ITGB3) at Y785 switches the specificity of integrin from Kindlin-2 (Fermitin family homolog 2 (FERMT2)) to the adaptor protein SHC-transforming protein 1 (SHC1).
details
Inferred
LIG_PTB_Phospho_1 ITB3_HUMAN779785SpecificityAltered binding specificityPhosphorylation of Integrin beta-3 (ITGB3) at Y785 switches the specificity of integrin from Kindlin-2 (Fermitin family homolog 2 (FERMT2)) to the adaptor protein SHC-transforming protein 1 (SHC1).
details
Inferred
LIG_PTB_Phospho_1 ITB3_HUMAN779785SpecificityAltered binding specificityPhosphorylation of Integrin beta-3 (ITGB3) at Y785 switches the specificity of integrin from Kindlin-2 (Fermitin family homolog 2 (FERMT2)) to the adaptor protein SHC-transforming protein 1 (SHC1).
details
Inferred
LIG_TYR_ITSM OX1R_HUMAN7986Avidity‑sensingOrexin-A induced phosphorylation of the ITSM and ITIM motifs in Orexin receptor type 1 (HCRTR1) allows binding of Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) via its two SH2 domains. Mutation of either tyrosine in the motifs abolishes binding of Tyrosine-protein phosphatase non-receptor type 11 (PTPN11).
details
Inferred
LIG_TYR_ITIM OX1R_HUMAN356361Avidity‑sensingOrexin-A induced phosphorylation of the ITSM and ITIM motifs in Orexin receptor type 1 (HCRTR1) allows binding of Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) via its two SH2 domains. Mutation of either tyrosine in the motifs abolishes binding of Tyrosine-protein phosphatase non-receptor type 11 (PTPN11).
details
Inferred
LIG_SH2_IC PDPK1_HUMAN376379BinaryPhysicochemical compatibilityPhosphorylation of Y376 in the SH2-binding motif of 3-phosphoinositide-dependent protein kinase 1 (PDPK1) induces binding to the Tensin-1 (TNS1) protein.
details
Inferred
LIG_SH2_IC PDPK1_HUMAN376379BinaryPhysicochemical compatibilityPhosphorylation of Y376 in the SH2-binding motif of 3-phosphoinositide-dependent protein kinase 1 (PDPK1) induces binding to the Tensin-1 (TNS1) protein.
details
Inferred
LIG_SH2_IE EGFR_HUMAN10111020BinaryPhysicochemical compatibilityPhosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Ras and Rab interactor 1 (RIN1) protein.
details
Inferred
LIG_SH2_IE EGFR_HUMAN10111020BinaryPhysicochemical compatibilityPhosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Ras and Rab interactor 1 (RIN1) protein.
details
Inferred
LIG_SH2_IE EGFR_HUMAN10081024BinaryPhysicochemical compatibilityPhosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Tyrosine-protein kinase JAK1 (JAK1) protein.
details
Inferred
LIG_SH2_IE EGFR_HUMAN10081024BinaryPhysicochemical compatibilityPhosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Tyrosine-protein kinase JAK1 (JAK1) protein.
details
Inferred
LIG_SH2_IE EGFR_HUMAN10081024BinaryPhysicochemical compatibilityPhosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Tyrosine-protein kinase JAK2 (JAK2) protein.
details
Inferred
LIG_SH2_IE EGFR_HUMAN10081024BinaryPhysicochemical compatibilityPhosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Tyrosine-protein kinase JAK2 (JAK2) protein.
details
Inferred
LIG_SH2_ID EGFR_HUMAN10081024BinaryPhysicochemical compatibilityPhosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the SH2 domain-containing protein 3C (SH2D3C) protein.
details
Inferred
LIG_SH2_ID EGFR_HUMAN10081024BinaryPhysicochemical compatibilityPhosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the SH2 domain-containing protein 3C (SH2D3C) protein.
details
Inferred
LIG_SH2_ID EGFR_HUMAN10081024BinaryPhysicochemical compatibilityPhosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the SH2 domain-containing protein 3A (SH2D3A) protein.
details
Inferred
LIG_SH2_ID EGFR_HUMAN10081024BinaryPhysicochemical compatibilityPhosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the SH2 domain-containing protein 3A (SH2D3A) protein.
details
Inferred
LIG_SH2_III EGFR_HUMAN10081024BinaryPhysicochemical compatibilityPhosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Signal transducer and activator of transcription 6 (STAT6) protein.
details
Inferred
LIG_SH2_III EGFR_HUMAN10081024BinaryPhysicochemical compatibilityPhosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Signal transducer and activator of transcription 6 (STAT6) protein.
details
Inferred
LIG_SH2_IB CBL_HUMAN770780BinaryPhysicochemical compatibilityPhosphorylation of Y774 in the SH2-binding motif of E3 ubiquitin-protein ligase CBL (CBL) induces binding to the Adapter molecule crk (CRK) protein.
details
Inferred
LIG_SH2_IC SHC1_HUMAN423435BinaryPhysicochemical compatibilityPhosphorylation of Y427 in the SH2-binding motif of SHC-transforming protein 1 (SHC1) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.
details
Inferred
LIG_SH2_IA FAK1_HUMAN389405BinaryPhysicochemical compatibilityPhosphorylation of Y397 in the SH2-binding motif of Focal adhesion kinase 1 (PTK2) induces binding to the Cytoplasmic protein NCK2 (NCK2) protein.
details
Inferred
LIG_SH2_IB FAK2_HUMAN394410BinaryPhysicochemical compatibilityPhosphorylation of Y402 in the SH2-binding motif of Protein-tyrosine kinase 2-beta (PTK2B) induces binding to the Megakaryocyte-associated tyrosine-protein kinase (MATK) protein.
details
Inferred
LIG_SH2_IA DAB1_MOUSE212228BinaryPhysicochemical compatibilityPhosphorylation of Y220 in the SH2-binding motif of Disabled homolog 1 (Dab1) induces binding to the Cytoplasmic protein NCK2 (NCK2) protein.
details
Inferred
LIG_SH2_IA DAB1_MOUSE212228BinaryPhysicochemical compatibilityPhosphorylation of Y220 in the SH2-binding motif of Disabled homolog 1 (Dab1) induces binding to the Cytoplasmic protein NCK2 (NCK2) protein.
details
Inferred
LIG_SH2_III STA5A_HUMAN686702BinaryPhysicochemical compatibilityPhosphorylation of Y694 in the SH2-binding motif of Signal transducer and activator of transcription 5A (STAT5A) induces binding to the Signal transducer and activator of transcription 5B (STAT5B) protein.
details
Inferred
LIG_SH2_III STA5A_HUMAN686702BinaryPhysicochemical compatibilityPhosphorylation of Y694 in the SH2-binding motif of Signal transducer and activator of transcription 5A (STAT5A) induces binding to the Signal transducer and activator of transcription 5B (STAT5B) protein.
details
Inferred
TRG_ENDOCYTIC_2 L1CAM_HUMAN11761179BinaryPhysicochemical compatibilityPhosphorylation of Y1176 by Proto-oncogene tyrosine-protein kinase Src (SRC) in the endocytosis motif of Neural cell adhesion molecule L1 (L1CAM) inhibits binding to AP-2 complex subunit mu (AP2M1).
details
Curated
LIG_PTB_Talin PI51C_MOUSE645648BinaryPhysicochemical compatibilityPhosphorylation of Y644 in Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma (Pip5k1c) promotes its association with Talin-1 (Tln1).
details
Inferred
LIG_PTB_Talin PI51C_MOUSE645648BinaryPhysicochemical compatibilityPhosphorylation of Y644 in Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma (Pip5k1c) promotes its association with Talin-1 (Tln1).
details
Inferred
LIG_SH2_IA DAB1_MOUSE220223BinaryPre‑translationalAlternative splicing removes the SH2-binding motif of Disabled homolog 1 (Dab1), abrogating binding to Cytoplasmic protein NCK2 (NCK2). NCK2-beta has a clear preference for splice variant 2 (with the YQYI motif) over splice variant 3 (with the YQTI motif). The authors theorise that since Adapter molecule crk (Crk) is directly linked to the C3G-Rap1 pathway, and NCK2-beta is linked to the Breast cancer anti-estrogen resistance protein 1 (Bcar1) (p130Cas) pathway, it is likely that isoforms 2 and 3 connect to different downstream cascades. It was suggested that the ability of different Dab1 isoforms to recruit distinct sets of SH2 domains implies a fine-tuning role of Dab1 splicing in the intricate series of events that underlie neuronal migration (Gao et al. (2012) (here)) (See also Katyal and Godbout (2004) (here) and Gao et al. (2010) (here)).
details
Inferred
LIG_SH2_IA DAB1_MOUSE220223BinaryPre‑translationalAlternative splicing removes the SH2-binding motif of Disabled homolog 1 (Dab1), abrogating binding to Cytoplasmic protein NCK2 (NCK2). NCK2-beta has a clear preference for splice variant 2 (with the YQYI motif) over splice variant 3 (with the YQTI motif). The authors theorise that since Adapter molecule crk (Crk) is directly linked to the C3G-Rap1 pathway, and NCK2-beta is linked to the Breast cancer anti-estrogen resistance protein 1 (Bcar1) (p130Cas) pathway, it is likely that isoforms 2 and 3 connect to different downstream cascades. It was suggested that the ability of different Dab1 isoforms to recruit distinct sets of SH2 domains implies a fine-tuning role of Dab1 splicing in the intricate series of events that underlie neuronal migration (Gao et al. (2012) (here)) (See also Katyal and Godbout (2004) (here) and Gao et al. (2010) (here)).
details
Inferred
LIG_SH2_IA DAB1_MOUSE232235BinaryPre‑translationalAlternative splicing removes the SH2-binding motif of Disabled homolog 1 (Dab1), abrogating binding to Cytoplasmic protein NCK2 (NCK2). The NCK2-beta has a clear preference for splice variant 2 (with YQYI motif) over splice variant 3 (with YQTI motif). The authors theorise that since Adapter molecule crk (Crk) is directly linked to the C3G-Rap1 pathway, and NCK2-beta is linked to the Breast cancer anti-estrogen resistance protein 1 (Bcar1) (p130Cas) pathway, it is likely that isoforms 2 and 3 connect to different downstream cascades. It was suggested that the ability of different Dab1 isoforms to recruit distinct sets of SH2 domains implies a fine-tuning role of Dab1 splicing in the intricate series of events that underlie neuronal migration (Gao et al. (2012) (here)) (See also Katyal and Godbout (2004) (here) and Gao et al. (2010) (here)).
details
Inferred
LIG_SH2_IA DAB1_MOUSE232235BinaryPre‑translationalAlternative splicing removes the SH2-binding motif of Disabled homolog 1 (Dab1), abrogating binding to Cytoplasmic protein NCK2 (NCK2). The NCK2-beta has a clear preference for splice variant 2 (with YQYI motif) over splice variant 3 (with YQTI motif). The authors theorise that since Adapter molecule crk (Crk) is directly linked to the C3G-Rap1 pathway, and NCK2-beta is linked to the Breast cancer anti-estrogen resistance protein 1 (Bcar1) (p130Cas) pathway, it is likely that isoforms 2 and 3 connect to different downstream cascades. It was suggested that the ability of different Dab1 isoforms to recruit distinct sets of SH2 domains implies a fine-tuning role of Dab1 splicing in the intricate series of events that underlie neuronal migration (Gao et al. (2012) (here)) (See also Katyal and Godbout (2004) (here) and Gao et al. (2010) (here)).
details
Inferred
LIG_SH2_IA DAB1_MOUSE232235BinaryPre‑translationalAlternative splicing removes the SH2-binding motif of Disabled homolog 1 (Dab1), abrogating binding to Cytoplasmic protein NCK2 (NCK2). The NCK2-beta has a clear preference for splice variant 2 (with YQYI motif) over splice variant 3 (with YQTI motif). The authors theorise that since Adapter molecule crk (Crk) is directly linked to the C3G-Rap1 pathway, and NCK2-beta is linked to the Breast cancer anti-estrogen resistance protein 1 (Bcar1) (p130Cas) pathway, it is likely that isoforms 2 and 3 connect to different downstream cascades. It was suggested that the ability of different Dab1 isoforms to recruit distinct sets of SH2 domains implies a fine-tuning role of Dab1 splicing in the intricate series of events that underlie neuronal migration (Gao et al. (2012) (here)) (See also Katyal and Godbout (2004) (here) and Gao et al. (2010) (here)).
details
Inferred
LIG_SH2_IA DAB1_MOUSE220223BinaryPre‑translationalAlternative splicing removes the SH2-binding motif of Disabled homolog 1 (Dab1), abrogating binding to Adapter molecule crk (Crk). Both Adapter molecule crk (Crk) and Crk-like protein (Crkl) bind equally well to variants 2 and 3. The authors theorise that since Adapter molecule crk (Crk) is directly linked to the C3G-Rap1 pathway, and NCK2-beta is linked to the Breast cancer anti-estrogen resistance protein 1 (Bcar1) (p130Cas) pathway, it is likely that isoforms 2 and 3 connect to different downstream cascades. It was suggested that the ability of different Dab1 isoforms to recruit distinct sets of SH2 domains implies a fine-tuning role of Dab1 splicing in the intricate series of events that underlie neuronal migration (Gao et al. (2012) (here)) (See also Katyal and Godbout (2004) (here) and Gao et al. (2010) (here)).
details
Inferred
LIG_SH2_IA DAB1_MOUSE220223BinaryPre‑translationalAlternative splicing removes the SH2-binding motif of Disabled homolog 1 (Dab1), abrogating binding to Adapter molecule crk (Crk). Both Adapter molecule crk (Crk) and Crk-like protein (Crkl) bind equally well to variants 2 and 3. The authors theorise that since Adapter molecule crk (Crk) is directly linked to the C3G-Rap1 pathway, and NCK2-beta is linked to the Breast cancer anti-estrogen resistance protein 1 (Bcar1) (p130Cas) pathway, it is likely that isoforms 2 and 3 connect to different downstream cascades. It was suggested that the ability of different Dab1 isoforms to recruit distinct sets of SH2 domains implies a fine-tuning role of Dab1 splicing in the intricate series of events that underlie neuronal migration (Gao et al. (2012) (here)) (See also Katyal and Godbout (2004) (here) and Gao et al. (2010) (here)).
details
Inferred
LIG_SH2_IA DAB1_MOUSE232235BinaryPre‑translationalAlternative splicing removes the SH2-binding motif of Disabled homolog 1 (Dab1), abrogating binding to Adapter molecule crk (Crk). Both Adapter molecule crk (Crk) and Crk-like protein (Crkl) bind equally well to variants 2 and 3. The authors theorise that since Adapter molecule crk (Crk) is directly linked to the C3G-Rap1 pathway, and NCK2-beta is linked to the Breast cancer anti-estrogen resistance protein 1 (Bcar1) (p130Cas) pathway, it is likely that isoforms 2 and 3 connect to different downstream cascades. It was suggested that the ability of different Dab1 isoforms to recruit distinct sets of SH2 domains implies a fine-tuning role of Dab1 splicing in the intricate series of events that underlie neuronal migration (Gao et al. (2012) (here)) (See also Katyal and Godbout (2004) (here) and Gao et al. (2010) (here)).
details
Inferred
LIG_SH2_IA DAB1_MOUSE232235BinaryPre‑translationalAlternative splicing removes the SH2-binding motif of Disabled homolog 1 (Dab1), abrogating binding to Adapter molecule crk (Crk). Both Adapter molecule crk (Crk) and Crk-like protein (Crkl) bind equally well to variants 2 and 3. The authors theorise that since Adapter molecule crk (Crk) is directly linked to the C3G-Rap1 pathway, and NCK2-beta is linked to the Breast cancer anti-estrogen resistance protein 1 (Bcar1) (p130Cas) pathway, it is likely that isoforms 2 and 3 connect to different downstream cascades. It was suggested that the ability of different Dab1 isoforms to recruit distinct sets of SH2 domains implies a fine-tuning role of Dab1 splicing in the intricate series of events that underlie neuronal migration (Gao et al. (2012) (here)) (See also Katyal and Godbout (2004) (here) and Gao et al. (2010) (here)).
details
Inferred
LIG_SH2_IA DAB1_MOUSE232235BinaryPre‑translationalAlternative splicing removes the SH2-binding motif of Disabled homolog 1 (Dab1), abrogating binding to Adapter molecule crk (Crk). Both Adapter molecule crk (Crk) and Crk-like protein (Crkl) bind equally well to variants 2 and 3. The authors theorise that since Adapter molecule crk (Crk) is directly linked to the C3G-Rap1 pathway, and NCK2-beta is linked to the Breast cancer anti-estrogen resistance protein 1 (Bcar1) (p130Cas) pathway, it is likely that isoforms 2 and 3 connect to different downstream cascades. It was suggested that the ability of different Dab1 isoforms to recruit distinct sets of SH2 domains implies a fine-tuning role of Dab1 splicing in the intricate series of events that underlie neuronal migration (Gao et al. (2012) (here)) (See also Katyal and Godbout (2004) (here) and Gao et al. (2010) (here)).
details
Inferred
LIG_SH2_SRC DAB1_MOUSE198201BinaryPre‑translationalAlternative splicing removes the SH2-binding motif of Disabled homolog 1 (Dab1), abrogating binding to Neuronal proto-oncogene tyrosine-protein kinase Src (Src). Splice variants 2 and 3 (only containing one of the YQxI motifs, i.e. Y185 and Y198) exhibit decreased tyrosine phosphorylation, suggesting both motifs are required for full activation of Dab1. Dab1 is likely to recruit Neuronal proto-oncogene tyrosine-protein kinase Src (Src) via these two YQxI motifs, which subsequently phosphorylates adjacent YxVP motifs (here). This was also suggested for Phosphatidylinositol 3-kinase regulatory subunit alpha (Pik3r1) and Suppressor of cytokine signaling 2 (Socs2). Gao et al. (2012) (here) suggests that the ability of different Dab1 isoforms to recruit distinct sets of SH2 domains allows a fine-tuning role for Dab1 splicing in the intricate series of events that underlie neuronal migration (See also Katyal & Godbout (2004) (here) and Gao et al. (2010) (here)).
details
Inferred
LIG_SH2_SRC DAB1_MOUSE198201BinaryPre‑translationalAlternative splicing removes the SH2-binding motif of Disabled homolog 1 (Dab1), abrogating binding to Neuronal proto-oncogene tyrosine-protein kinase Src (Src). Splice variants 2 and 3 (only containing one of the YQxI motifs, i.e. Y185 and Y198) exhibit decreased tyrosine phosphorylation, suggesting both motifs are required for full activation of Dab1. Dab1 is likely to recruit Neuronal proto-oncogene tyrosine-protein kinase Src (Src) via these two YQxI motifs, which subsequently phosphorylates adjacent YxVP motifs (here). This was also suggested for Phosphatidylinositol 3-kinase regulatory subunit alpha (Pik3r1) and Suppressor of cytokine signaling 2 (Socs2). Gao et al. (2012) (here) suggests that the ability of different Dab1 isoforms to recruit distinct sets of SH2 domains allows a fine-tuning role for Dab1 splicing in the intricate series of events that underlie neuronal migration (See also Katyal & Godbout (2004) (here) and Gao et al. (2010) (here)).
details
Inferred
LIG_SH2_IA DAB1_MOUSE232235BinaryPhysicochemical compatibilityPhosphorylation of Y232 in the SH2-binding motif of Disabled homolog 1 (Dab1) induces binding to Cytoplasmic protein NCK2 (NCK2).
details
Inferred
LIG_SH2_IA DAB1_MOUSE232235BinaryPhysicochemical compatibilityPhosphorylation of Y232 in the SH2-binding motif of Disabled homolog 1 (Dab1) induces binding to Cytoplasmic protein NCK2 (NCK2).
details
Inferred
LIG_SH2_IA DAB1_MOUSE232235BinaryPhysicochemical compatibilityPhosphorylation of Y232 in the SH2-binding motif of Disabled homolog 1 (Dab1) induces binding to Cytoplasmic protein NCK2 (NCK2).
details
Inferred
LIG_SH2_IA DAB1_MOUSE232235BinaryPhysicochemical compatibilityPhosphorylation of Y232 in the SH2-binding motif of Disabled homolog 1 (Dab1) induces binding to Adapter molecule crk (Crk).
details
Inferred
LIG_SH2_IA DAB1_MOUSE232235BinaryPhysicochemical compatibilityPhosphorylation of Y232 in the SH2-binding motif of Disabled homolog 1 (Dab1) induces binding to Adapter molecule crk (Crk).
details
Inferred
LIG_SH2_IA DAB1_MOUSE232235BinaryPhysicochemical compatibilityPhosphorylation of Y232 in the SH2-binding motif of Disabled homolog 1 (Dab1) induces binding to Adapter molecule crk (Crk).
details
Inferred
LIG_SH2_SRC DAB1_MOUSE198201BinaryPhysicochemical compatibilityPhosphorylation of Y198 in the SH2-binding motif of Disabled homolog 1 (Dab1) induces binding to Neuronal proto-oncogene tyrosine-protein kinase Src (Src).
details
Inferred
LIG_SH2_SRC DAB1_MOUSE198201BinaryPhysicochemical compatibilityPhosphorylation of Y198 in the SH2-binding motif of Disabled homolog 1 (Dab1) induces binding to Neuronal proto-oncogene tyrosine-protein kinase Src (Src).
details
Inferred
LIG_TYR_ITSM OX1R_HUMAN7986Avidity‑sensingOrexin-A induced phosphorylation of the ITSM and ITIM motifs in Orexin receptor type 1 (HCRTR1) allows binding of Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) via its two SH2 domains. Mutation of either tyrosine in the motifs abolishes binding of Tyrosine-protein phosphatase non-receptor type 11 (PTPN11).
details
Inferred
LIG_TYR_ITIM OX1R_HUMAN356361Avidity‑sensingOrexin-A induced phosphorylation of the ITSM and ITIM motifs in Orexin receptor type 1 (HCRTR1) allows binding of Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) via its two SH2 domains. Mutation of either tyrosine in the motifs abolishes binding of Tyrosine-protein phosphatase non-receptor type 11 (PTPN11).
details
Inferred
TRG_ENDOCYTIC_2 L1CAM_HUMAN11761179BinaryPhysicochemical compatibilityPhosphorylation of Y1176 in the endocytotic motif of Neural cell adhesion molecule L1 (L1CAM) by Proto-oncogene tyrosine-protein kinase Src (SRC) abolishes binding to the AP-2 complex subunit mu (AP2M1) and thereby inhibits internalisation of Neural cell adhesion molecule L1 (L1CAM).
details
Curated
LIG_SH2_SRC EGFR_HUMAN10161019BinaryPhysicochemical compatibilityPhosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1 (PLCG1).
details
Inferred
LIG_SH2_SRC EGFR_HUMAN10161019BinaryPhysicochemical compatibilityPhosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1 (PLCG1).
details
Inferred
LIG_SH2_SRC EGFR_HUMAN11251128BinaryPhysicochemical compatibilityPhosphorylation of Y1125 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to Adapter molecule crk (CRK).
details
Inferred
LIG_SH2_SRC EGFR_HUMAN11251128BinaryPhysicochemical compatibilityPhosphorylation of Y1125 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to Adapter molecule crk (CRK).
details
Inferred
LIG_SH2_SRC EGFR_HUMAN11251128BinaryPhysicochemical compatibilityPhosphorylation of Y1125 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to Adapter molecule crk (CRK).
details
Inferred
LIG_SH2_SRC EGFR_HUMAN11251128BinaryPhysicochemical compatibilityPhosphorylation of Y1125 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to Adapter molecule crk (CRK).
details
Inferred
LIG_SH2_SRC EGFR_HUMAN10161019BinaryPhysicochemical compatibilityPhosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to Cytoplasmic protein NCK1 (NCK1).
details
Inferred
LIG_SH2_SRC EGFR_HUMAN10161019BinaryPhysicochemical compatibilityPhosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to Cytoplasmic protein NCK1 (NCK1).
details
Inferred
LIG_SH2_SRC FAK1_HUMAN397400BinaryPhysicochemical compatibilityPhosphorylation of Y397 in the SH2-binding motif of Focal adhesion kinase 1 (PTK2) induces binding to Neuronal proto-oncogene tyrosine-protein kinase Src (Src).
details
Inferred

Proto-oncogene tyrosine-protein kinase receptor Ret - RET -  Homo sapiens
LIG_SH2_IIB RET_HUMAN976985BinaryPhysicochemical compatibilityPhosphorylation of Y981 in the SH2-binding motif of Proto-oncogene tyrosine-protein kinase receptor Ret (RET) induces binding to the SH2B adapter protein 1 (SH2B1) protein.
details
Inferred
LIG_SH2_IIB RET_HUMAN976985BinaryPhysicochemical compatibilityPhosphorylation of Y981 in the SH2-binding motif of Proto-oncogene tyrosine-protein kinase receptor Ret (RET) induces binding to the SH2B adapter protein 1 (SH2B1) protein.
details
Inferred
LIG_SH2_IIB RET_HUMAN976985BinaryPhysicochemical compatibilityPhosphorylation of Y981 in the SH2-binding motif of Proto-oncogene tyrosine-protein kinase receptor Ret (RET) induces binding to the SH2B adapter protein 1 (SH2B1) protein.
details
Inferred

Proto-oncogene tyrosine-protein kinase receptor Ret - RET -  Mus musculus
LIG_PTB_Phospho_1 RET_MOUSE10571063BinaryPhysicochemical compatibilityPhosphorylation of Y1063 in the PTB-binding motif of Proto-oncogene tyrosine-protein kinase receptor Ret (Ret) induces binding to the Docking protein 1 (Dok1) protein.
details
Inferred

RAC-alpha serine/threonine-protein kinase - AKT1 -  Rattus norvegicus
LIG_14-3-3_1 BAD_RAT134139BinaryPhysicochemical compatibilityPhosphorylation of S137 by RAC-alpha serine/threonine-protein kinase (Akt1) in the 14-3-3-binding motif of Bcl2 antagonist of cell death (Bad) induces binding to the 14-3-3 protein beta/alpha (YWHAB) protein. This interaction inhibits the pro-apoptotic activity of Bcl2 antagonist of cell death (Bad).
details
Curated
LIG_14-3-3_3 FOXO3_HUMAN250255Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in Forkhead box protein O3 (FOXO3) by RAC-alpha serine/threonine-protein kinase (AKT1) induces high-avidity binding to dimeric 14-3-3 protein beta/alpha (YWHAB). This interaction results in cytoplasmic retention and inactivation of Forkhead box protein O3 (FOXO3).
details
Inferred
LIG_14-3-3_3 FOXO3_HUMAN2934Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in Forkhead box protein O3 (FOXO3) by RAC-alpha serine/threonine-protein kinase (AKT1) induces high-avidity binding to dimeric 14-3-3 protein beta/alpha (YWHAB). This interaction results in cytoplasmic retention and inactivation of Forkhead box protein O3 (FOXO3).
details
Inferred

RAC-alpha serine/threonine-protein kinase - AKT1 -  Homo sapiens
DOC_WW_Pin1_4 STAT3_HUMAN724729BinaryPhysicochemical compatibilityPhosphorylation of S727 in the Pin1-binding motif of Signal transducer and activator of transcription 3 (STAT3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DEG_SCF_TRCP1_1 IKBA_HUMAN3136BinaryPhysicochemical compatibilityDual phosphorylation of S32 and S36 in the TrCP1-binding motif of NF-kappa-B inhibitor alpha (NFKBIA) targets the protein to the SCF ubiquitin ligase complex, which marks it for degradation.
details
Inferred
LIG_14-3-3_3 CDN1B_HUMAN193198Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in Cyclin-dependent kinase inhibitor 1B (CDKN1B) by RAC-alpha serine/threonine-protein kinase (AKT1) and ribosomal protein S6 kinases (Ribosomal protein S6 kinase alpha-1 (RPS6KA1), Ribosomal protein S6 kinase alpha-3 (RPS6KA3)) induces binding of 14-3-3 dimer. Binding of 14-3-3 results in cytoplasmic localisation of Cyclin-dependent kinase inhibitor 1B (CDKN1B) (see switch details), thereby alleviating Cyclin-dependent kinase inhibitor 1B (CDKN1B)-mediated inhibition of cyclin-dependent kinases and cell cycle progression.
details
Curated

RAC-alpha serine/threonine-protein kinase - AKT1 -  Homo sapiens
LIG_14-3-3_1 ATX1_HUMAN772777BinaryPhysicochemical compatibilityPhosphorylation of S775 by RAC-alpha serine/threonine-protein kinase (AKT1) in the 14-3-3-binding motif of Ataxin-1 (ATXN1) induces binding to the 14-3-3 protein zeta/delta (YWHAZ) protein.
details
Curated
LIG_14-3-3_2 FOXO4_HUMAN193199BinaryPhysicochemical compatibilityPhosphorylation of S197 by in the 14-3-3-binding motif of Forkhead box protein O4 (FOXO4) induces binding to the 14-3-3 protein zeta/delta (YWHAZ) protein.
details
Curated
LIG_ULM_U2AF65_1 ATX1_HUMAN770775SpecificityAltered binding specificityPhosphorylation of S775 switches binding specificity of Ataxin-1 (ATXN1) from the splicing factor Splicing factor U2AF 65 kDa subunit (U2AF2) to 14-3-3 proteins (e.g. 14-3-3 protein zeta/delta (YWHAZ)). While association with the spliceosome protects ATXN1 from self-association, its phosphorylation-dependent recruitment to 14-3-3 proteins (e.g. YWHAZ) might result in aggregation.
details
Inferred
LIG_14-3-3_1 ATX1_HUMAN772777SpecificityAltered binding specificityPhosphorylation of S775 switches binding specificity of Ataxin-1 (ATXN1) from the splicing factor Splicing factor U2AF 65 kDa subunit (U2AF2) to 14-3-3 proteins (e.g. 14-3-3 protein zeta/delta (YWHAZ)). While association with the spliceosome protects ATXN1 from self-association, its phosphorylation-dependent recruitment to 14-3-3 proteins (e.g. YWHAZ) might result in aggregation.
details
Inferred
LIG_14-3-3_1 RAF1_HUMAN256261Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in RAF proto-oncogene serine/threonine-protein kinase (RAF1) in response to growth factors induces high-avidity binding to dimeric 14-3-3 protein zeta/delta (YWHAZ), with pS621 being the high-affinity interaction site. This interaction locks RAF proto-oncogene serine/threonine-protein kinase (RAF1) in an inhibited conformation.
details
Curated
LIG_14-3-3_3 FOXO3_HUMAN250255Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in Forkhead box protein O3 (FOXO3) by RAC-alpha serine/threonine-protein kinase (AKT1) induces high-avidity binding to dimeric 14-3-3 protein beta/alpha (YWHAB). This interaction results in cytoplasmic retention and inactivation of Forkhead box protein O3 (FOXO3).
details
Curated
LIG_14-3-3_3 FOXO3_HUMAN2934Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in Forkhead box protein O3 (FOXO3) by RAC-alpha serine/threonine-protein kinase (AKT1) induces high-avidity binding to dimeric 14-3-3 protein beta/alpha (YWHAB). This interaction results in cytoplasmic retention and inactivation of Forkhead box protein O3 (FOXO3).
details
Curated
LIG_14-3-3_1 FOXO4_HUMAN2934Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in Foxo4 by PKB induces binding of 14-3-3 dimer. In the nucleus, this blocks binding to DNA, while in the cytoplasm it blocks reimport of Foxo4 into the nucleus by blocking its Nuclear Localisation Signal (NLS). Since binding of 14-3-3 to a single motif occurs with an affinity similar to the affinity of Foxo4 for DNA, multivalent binding of 14-3-3 dimer is required for efficient inhibition of DNA binding.
details
Curated
LIG_14-3-3_2 FOXO4_HUMAN193199Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in Foxo4 by PKB induces binding of 14-3-3 dimer. In the nucleus, this blocks binding to DNA, while in the cytoplasm it blocks reimport of Foxo4 into the nucleus by blocking its Nuclear Localisation Signal (NLS). Since binding of 14-3-3 to a single motif occurs with an affinity similar to the affinity of Foxo4 for DNA, multivalent binding of 14-3-3 dimer is required for efficient inhibition of DNA binding.
details
Curated
TRG_NLS CDN1B_HUMAN152166SpecificityMotif hidingPhosphorylation of a 14-3-3-binding motif in the NLS of Cyclin-dependent kinase inhibitor 1B (CDKN1B) by RAC-alpha serine/threonine-protein kinase (AKT1) induces binding of 14-3-3 protein gamma (YWHAG), which hides the NLS and prevents binding to Importin subunit alpha-1 (KPNA1), thereby mediating cytoplasmic retention of Cyclin-dependent kinase inhibitor 1B (CDKN1B). Binding of 14-3-3 dimer involves an additional C-terminal 14-3-3-binding motif (see switch details).
details
Inferred
LIG_14-3-3_3 CDN1B_HUMAN154159SpecificityMotif hidingPhosphorylation of a 14-3-3-binding motif in the NLS of Cyclin-dependent kinase inhibitor 1B (CDKN1B) by RAC-alpha serine/threonine-protein kinase (AKT1) induces binding of 14-3-3 protein gamma (YWHAG), which hides the NLS and prevents binding to Importin subunit alpha-1 (KPNA1), thereby mediating cytoplasmic retention of Cyclin-dependent kinase inhibitor 1B (CDKN1B). Binding of 14-3-3 dimer involves an additional C-terminal 14-3-3-binding motif (see switch details).
details
Curated
LIG_14-3-3_3 CDN1B_HUMAN154159Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in Cyclin-dependent kinase inhibitor 1B (CDKN1B) by RAC-alpha serine/threonine-protein kinase (AKT1) and ribosomal protein S6 kinases (Ribosomal protein S6 kinase alpha-1 (RPS6KA1), Ribosomal protein S6 kinase alpha-3 (RPS6KA3)) induces binding of 14-3-3 dimer. Binding of 14-3-3 results in cytoplasmic localisation of Cyclin-dependent kinase inhibitor 1B (CDKN1B) (see switch details), thereby alleviating Cyclin-dependent kinase inhibitor 1B (CDKN1B)-mediated inhibition of cyclin-dependent kinases and cell cycle progression.
details
Curated
LIG_14-3-3_3 CDN1B_HUMAN193198Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in Cyclin-dependent kinase inhibitor 1B (CDKN1B) by RAC-alpha serine/threonine-protein kinase (AKT1) and ribosomal protein S6 kinases (Ribosomal protein S6 kinase alpha-1 (RPS6KA1), Ribosomal protein S6 kinase alpha-3 (RPS6KA3)) induces binding of 14-3-3 dimer. Binding of 14-3-3 results in cytoplasmic localisation of Cyclin-dependent kinase inhibitor 1B (CDKN1B) (see switch details), thereby alleviating Cyclin-dependent kinase inhibitor 1B (CDKN1B)-mediated inhibition of cyclin-dependent kinases and cell cycle progression.
details
Curated
LIG_PCNA_PIPBox_1 CDN1A_HUMAN144153BinaryPhysicochemical compatibilityPhosphorylation of T145 in the PCNA-binding motif of Cyclin-dependent kinase inhibitor 1 (CDKN1A) by RAC-alpha serine/threonine-protein kinase (AKT1) inhibits binding to Proliferating cell nuclear antigen (PCNA). As a result, Cyclin-dependent kinase inhibitor 1 (CDKN1A) no longer inhibits Proliferating cell nuclear antigen (PCNA) and blocking of DNA replication is relieved.
details
Curated
LIG_PCNA_PIPBox_1 CDN1A_HUMAN144153BinaryPhysicochemical compatibilityPhosphorylation of S146 in the PCNA-binding motif of Cyclin-dependent kinase inhibitor 1 (CDKN1A) by PKC subfamily inhibits binding to Proliferating cell nuclear antigen (PCNA). As a result, Cyclin-dependent kinase inhibitor 1 (CDKN1A) no longer inhibits Proliferating cell nuclear antigen (PCNA) and blocking of DNA replication is relieved.
details
Inferred
LIG_14-3-3_1 BAD_MOUSE133138BinaryPhysicochemical compatibilityPhosphorylation of S136 in Bcl2 antagonist of cell death (Bad) by RAC-alpha serine/threonine-protein kinase (Akt1) in response to survival and growth signals such as Interleukin-3 (Il3) induces binding to 14-3-3 protein theta (Ywhaq). Binding of 14-3-3 protein theta (Ywhaq) results in dissociation of Bcl2 antagonist of cell death (Bad) from Bcl-2-like protein 1 (Bcl2l1), and thereby inhibits the pro-apoptotic activity of Bcl2 antagonist of cell death (Bad) by allowing liberated Bcl-2-like protein 1 (Bcl2l1) to exert its anti-apoptotic effect on pro-apoptotic proteins like Apoptosis regulator BAX (Bax).
details
Inferred

RAC-alpha serine/threonine-protein kinase - AKT1 -  Mus musculus
LIG_14-3-3_1 BAD_MOUSE133138BinaryPhysicochemical compatibilityPhosphorylation of S136 in Bcl2 antagonist of cell death (Bad) by RAC-alpha serine/threonine-protein kinase (Akt1) in response to survival and growth signals such as Interleukin-3 (Il3) induces binding to 14-3-3 protein theta (Ywhaq). Binding of 14-3-3 protein theta (Ywhaq) results in dissociation of Bcl2 antagonist of cell death (Bad) from Bcl-2-like protein 1 (Bcl2l1), and thereby inhibits the pro-apoptotic activity of Bcl2 antagonist of cell death (Bad) by allowing liberated Bcl-2-like protein 1 (Bcl2l1) to exert its anti-apoptotic effect on pro-apoptotic proteins like Apoptosis regulator BAX (Bax).
details
Curated

RAF proto-oncogene serine/threonine-protein kinase - RAF1 -  Homo sapiens
LIG_14-3-3_1 RAF1_HUMAN256261Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in RAF proto-oncogene serine/threonine-protein kinase (RAF1) in response to growth factors induces high-avidity binding to dimeric 14-3-3 protein zeta/delta (YWHAZ), with pS621 being the high-affinity interaction site. This interaction locks RAF proto-oncogene serine/threonine-protein kinase (RAF1) in an inhibited conformation.
details
Inferred
LIG_14-3-3_1 RAF1_HUMAN618623Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in RAF proto-oncogene serine/threonine-protein kinase (RAF1) in response to growth factors induces high-avidity binding to dimeric 14-3-3 protein zeta/delta (YWHAZ), with pS621 being the high-affinity interaction site. This interaction locks RAF proto-oncogene serine/threonine-protein kinase (RAF1) in an inhibited conformation.
details
Inferred

Receptor tyrosine-protein kinase erbB-2 - ERBB2 -  Homo sapiens
LIG_SH2_IC ERBB2_HUMAN11351144BinaryPhysicochemical compatibilityPhosphorylation of Y1139 in the SH2-binding motif of Receptor tyrosine-protein kinase erbB-2 (ERBB2) induces binding to the Growth factor receptor-bound protein 7 (GRB7) protein.
details
Inferred
LIG_SH2_IC ERBB2_HUMAN11351144BinaryPhysicochemical compatibilityPhosphorylation of Y1139 in the SH2-binding motif of Receptor tyrosine-protein kinase erbB-2 (ERBB2) induces binding to the Growth factor receptor-bound protein 7 (GRB7) protein.
details
Inferred
LIG_SH2_IE ERBB2_HUMAN10151031BinaryPhysicochemical compatibilityPhosphorylation of Y1023 in the SH2-binding motif of Receptor tyrosine-protein kinase erbB-2 (ERBB2) induces binding to the Tyrosine-protein kinase JAK1 (JAK1) protein.
details
Inferred
LIG_SH2_IE ERBB2_HUMAN10151031BinaryPhysicochemical compatibilityPhosphorylation of Y1023 in the SH2-binding motif of Receptor tyrosine-protein kinase erbB-2 (ERBB2) induces binding to the Tyrosine-protein kinase JAK2 (JAK2) protein.
details
Inferred
LIG_SH2_ID ERBB2_HUMAN11311147BinaryPhysicochemical compatibilityPhosphorylation of Y1139 in the SH2-binding motif of Receptor tyrosine-protein kinase erbB-2 (ERBB2) induces binding to the Breast cancer anti-estrogen resistance protein 3 (BCAR3) protein.
details
Inferred
LIG_SH2_ID ERBB2_HUMAN11311147BinaryPhysicochemical compatibilityPhosphorylation of Y1139 in the SH2-binding motif of Receptor tyrosine-protein kinase erbB-2 (ERBB2) induces binding to the Breast cancer anti-estrogen resistance protein 3 (BCAR3) protein.
details
Inferred
LIG_SH2_ID ERBB2_HUMAN10151031BinaryPhysicochemical compatibilityPhosphorylation of Y1023 in the SH2-binding motif of Receptor tyrosine-protein kinase erbB-2 (ERBB2) induces binding to the SH2 domain-containing protein 3A (SH2D3A) protein.
details
Inferred
LIG_SH2_III ERBB2_HUMAN11311147BinaryPhysicochemical compatibilityPhosphorylation of Y1139 in the SH2-binding motif of Receptor tyrosine-protein kinase erbB-2 (ERBB2) induces binding to the Signal transducer and activator of transcription 6 (STAT6) protein.
details
Inferred
LIG_SH2_III ERBB2_HUMAN11311147BinaryPhysicochemical compatibilityPhosphorylation of Y1139 in the SH2-binding motif of Receptor tyrosine-protein kinase erbB-2 (ERBB2) induces binding to the Signal transducer and activator of transcription 6 (STAT6) protein.
details
Inferred

Receptor tyrosine-protein kinase erbB-4 - ERBB4 -  Homo sapiens
LIG_WW_1 ERBB4_HUMAN10531056SpecificityAltered binding specificityPhosphorylation-dependent binding of Receptor tyrosine-protein kinase erbB-4 (ERBB4) to the SH2 domains of Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1) results in signaling activation, while binding to the WW domains of E3 ubiquitin-protein ligase Itchy homolog (ITCH) to unphopshorylated ERBB4 results in ubiquitylation, endocytosis and ultimately degradation of ERBB4.
details
Inferred
LIG_SH2_STAT5 ERBB4_HUMAN10561059SpecificityAltered binding specificityPhosphorylation-dependent binding of Receptor tyrosine-protein kinase erbB-4 (ERBB4) to the SH2 domains of Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1) results in signaling activation, while binding to the WW domains of E3 ubiquitin-protein ligase Itchy homolog (ITCH) to unphopshorylated ERBB4 results in ubiquitylation, endocytosis and ultimately degradation of ERBB4.
details
Inferred

Ribosomal protein S6 kinase alpha-1 - RPS6KA1 -  Rattus norvegicus
LIG_14-3-3_3 CDN1B_HUMAN154159Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in Cyclin-dependent kinase inhibitor 1B (CDKN1B) by RAC-alpha serine/threonine-protein kinase (AKT1) and ribosomal protein S6 kinases (Ribosomal protein S6 kinase alpha-1 (RPS6KA1), Ribosomal protein S6 kinase alpha-3 (RPS6KA3)) induces binding of 14-3-3 dimer. Binding of 14-3-3 results in cytoplasmic localisation of Cyclin-dependent kinase inhibitor 1B (CDKN1B) (see switch details), thereby alleviating Cyclin-dependent kinase inhibitor 1B (CDKN1B)-mediated inhibition of cyclin-dependent kinases and cell cycle progression.
details
Inferred
LIG_14-3-3_3 CDN1B_HUMAN193198Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in Cyclin-dependent kinase inhibitor 1B (CDKN1B) by RAC-alpha serine/threonine-protein kinase (AKT1) and ribosomal protein S6 kinases (Ribosomal protein S6 kinase alpha-1 (RPS6KA1), Ribosomal protein S6 kinase alpha-3 (RPS6KA3)) induces binding of 14-3-3 dimer. Binding of 14-3-3 results in cytoplasmic localisation of Cyclin-dependent kinase inhibitor 1B (CDKN1B) (see switch details), thereby alleviating Cyclin-dependent kinase inhibitor 1B (CDKN1B)-mediated inhibition of cyclin-dependent kinases and cell cycle progression.
details
Inferred

Ribosomal protein S6 kinase alpha-1 - RPS6KA1 -  Homo sapiens
DEG_SCF_TRCP1_1 IKBA_HUMAN3136BinaryPhysicochemical compatibilityDual phosphorylation of S32 and S36 in the TrCP1-binding motif of NF-kappa-B inhibitor alpha (NFKBIA) targets the protein to the SCF ubiquitin ligase complex, which marks it for degradation.
details
Inferred
DEG_SCF_TRCP1_1 IKBB_HUMAN1823BinaryPhysicochemical compatibilityDual phosphorylation of S19 and S23 in the TrCP1-binding motif of NF-kappa-B inhibitor beta (NFKBIB) targets the protein to the SCF ubiquitin ligase complex, which marks it for degradation.
details
Inferred
DEG_SCF_TRCP1_1 IKBB_HUMAN1823BinaryPhysicochemical compatibilityDual phosphorylation of S19 and S23 in the TrCP1-binding motif of NF-kappa-B inhibitor beta (NFKBIB) targets the protein to the SCF ubiquitin ligase complex, which marks it for degradation.
details
Inferred
LIG_14-3-3_3 CDN1B_HUMAN193198Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in Cyclin-dependent kinase inhibitor 1B (CDKN1B) by RAC-alpha serine/threonine-protein kinase (AKT1) and ribosomal protein S6 kinases (Ribosomal protein S6 kinase alpha-1 (RPS6KA1), Ribosomal protein S6 kinase alpha-3 (RPS6KA3)) induces binding of 14-3-3 dimer. Binding of 14-3-3 results in cytoplasmic localisation of Cyclin-dependent kinase inhibitor 1B (CDKN1B) (see switch details), thereby alleviating Cyclin-dependent kinase inhibitor 1B (CDKN1B)-mediated inhibition of cyclin-dependent kinases and cell cycle progression.
details
Curated
LIG_14-3-3_1 BAD_MOUSE133138BinaryPhysicochemical compatibilityPhosphorylation of S136 in Bcl2 antagonist of cell death (Bad) by RAC-alpha serine/threonine-protein kinase (Akt1) in response to survival and growth signals such as Interleukin-3 (Il3) induces binding to 14-3-3 protein theta (Ywhaq). Binding of 14-3-3 protein theta (Ywhaq) results in dissociation of Bcl2 antagonist of cell death (Bad) from Bcl-2-like protein 1 (Bcl2l1), and thereby inhibits the pro-apoptotic activity of Bcl2 antagonist of cell death (Bad) by allowing liberated Bcl-2-like protein 1 (Bcl2l1) to exert its anti-apoptotic effect on pro-apoptotic proteins like Apoptosis regulator BAX (Bax).
details
Inferred

Ribosomal protein S6 kinase alpha-2 - RPS6KA2 -  Homo sapiens
LIG_14-3-3_3 CDN1B_HUMAN154159Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in Cyclin-dependent kinase inhibitor 1B (CDKN1B) by RAC-alpha serine/threonine-protein kinase (AKT1) and ribosomal protein S6 kinases (Ribosomal protein S6 kinase alpha-1 (RPS6KA1), Ribosomal protein S6 kinase alpha-3 (RPS6KA3)) induces binding of 14-3-3 dimer. Binding of 14-3-3 results in cytoplasmic localisation of Cyclin-dependent kinase inhibitor 1B (CDKN1B) (see switch details), thereby alleviating Cyclin-dependent kinase inhibitor 1B (CDKN1B)-mediated inhibition of cyclin-dependent kinases and cell cycle progression.
details
Inferred
LIG_14-3-3_3 CDN1B_HUMAN193198Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in Cyclin-dependent kinase inhibitor 1B (CDKN1B) by RAC-alpha serine/threonine-protein kinase (AKT1) and ribosomal protein S6 kinases (Ribosomal protein S6 kinase alpha-1 (RPS6KA1), Ribosomal protein S6 kinase alpha-3 (RPS6KA3)) induces binding of 14-3-3 dimer. Binding of 14-3-3 results in cytoplasmic localisation of Cyclin-dependent kinase inhibitor 1B (CDKN1B) (see switch details), thereby alleviating Cyclin-dependent kinase inhibitor 1B (CDKN1B)-mediated inhibition of cyclin-dependent kinases and cell cycle progression.
details
Inferred

Ribosomal protein S6 kinase alpha-3 - RPS6KA3 -  Mus musculus
DOC_AGCK_PIF_1 KS6A3_MOUSE382387BinaryPhysicochemical compatibilityAuto-phosphorylation of S386 in the PIF pocket-binding motif of Ribosomal protein S6 kinase alpha-3 (Rps6ka3) induces intramolecular binding and kinase cis-activation.
details
Curated
LIG_14-3-3_3 CDN1B_HUMAN154159Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in Cyclin-dependent kinase inhibitor 1B (CDKN1B) by RAC-alpha serine/threonine-protein kinase (AKT1) and ribosomal protein S6 kinases (Ribosomal protein S6 kinase alpha-1 (RPS6KA1), Ribosomal protein S6 kinase alpha-3 (RPS6KA3)) induces binding of 14-3-3 dimer. Binding of 14-3-3 results in cytoplasmic localisation of Cyclin-dependent kinase inhibitor 1B (CDKN1B) (see switch details), thereby alleviating Cyclin-dependent kinase inhibitor 1B (CDKN1B)-mediated inhibition of cyclin-dependent kinases and cell cycle progression.
details
Inferred
LIG_14-3-3_3 CDN1B_HUMAN193198Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in Cyclin-dependent kinase inhibitor 1B (CDKN1B) by RAC-alpha serine/threonine-protein kinase (AKT1) and ribosomal protein S6 kinases (Ribosomal protein S6 kinase alpha-1 (RPS6KA1), Ribosomal protein S6 kinase alpha-3 (RPS6KA3)) induces binding of 14-3-3 dimer. Binding of 14-3-3 results in cytoplasmic localisation of Cyclin-dependent kinase inhibitor 1B (CDKN1B) (see switch details), thereby alleviating Cyclin-dependent kinase inhibitor 1B (CDKN1B)-mediated inhibition of cyclin-dependent kinases and cell cycle progression.
details
Inferred

Ribosomal protein S6 kinase beta-1 - RPS6KB1 -  Homo sapiens
LIG_14-3-3_1 BAD_RAT134139BinaryPhysicochemical compatibilityPhosphorylation of S137 by RAC-alpha serine/threonine-protein kinase (Akt1) in the 14-3-3-binding motif of Bcl2 antagonist of cell death (Bad) induces binding to the 14-3-3 protein beta/alpha (YWHAB) protein. This interaction inhibits the pro-apoptotic activity of Bcl2 antagonist of cell death (Bad).
details
Inferred

Ribosomal protein S6 kinase beta-1 - RPS6KB1 -  Rattus norvegicus
LIG_14-3-3_1 BAD_RAT134139BinaryPhysicochemical compatibilityPhosphorylation of S137 by RAC-alpha serine/threonine-protein kinase (Akt1) in the 14-3-3-binding motif of Bcl2 antagonist of cell death (Bad) induces binding to the 14-3-3 protein beta/alpha (YWHAB) protein. This interaction inhibits the pro-apoptotic activity of Bcl2 antagonist of cell death (Bad).
details
Inferred

Serine-protein kinase ATM - ATM -  Homo sapiens
LIG_BRCT_MDC1_1 H2AX_HUMAN139143BinaryPhysicochemical compatibilityPhosphorylation of S140 in the BRCT-binding motif of Histone H2A.x (H2AFX) induces binding to the Mediator of DNA damage checkpoint protein 1 (MDC1) protein.
details
Curated
LIG_FHA_1 CHK2_HUMAN6672BinaryPhysicochemical compatibilityPhosphorylation of T68 in the FHA-binding motif of Serine/threonine-protein kinase Chk2 (CHEK2) induces binding to the Serine/threonine-protein kinase Chk2 (CHEK2) protein.
details
Inferred
LIG_PH_Tfb1 P53_HUMAN5056CumulativeRheostaticMultisite phosphorylation of S46 and T55 in the PH-like binding motif of Cellular tumor antigen p53 (TP53) gradually enhances its affinity for General transcription factor IIH subunit 1 (GTF2H1), an interaction involved in activation of transcription initiation and elongation by Cellular tumor antigen p53 (TP53).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
DOC_USP7_1 MDM4_HUMAN398402BinaryPhysicochemical compatibilityPhosphorylation of S403 adjacent to the USP7-binding motif of Protein Mdm4 (MDM4) by Serine-protein kinase ATM (ATM) inhibits binding to the Ubiquitin carboxyl-terminal hydrolase 7 (USP7), thereby reducing deubiquitylation of Protein Mdm4 (MDM4). As a result, ubiquitylation by E3 ubiquitin-protein ligase Mdm2 (MDM2) is not countered and Protein Mdm4 (MDM4) is targeted for proteasomal degradation.
details
Curated

Serine-protein kinase ATM - ATM -  Mus musculus
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred

Serine/threonine-protein kinase 17A - STK17A -  Homo sapiens
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred

Serine/threonine-protein kinase 4 - STK4 -  Homo sapiens
LIG_BRCT_MDC1_1 H2AX_HUMAN139143BinaryPhysicochemical compatibilityPhosphorylation of S140 in the BRCT-binding motif of Histone H2A.x (H2AFX) induces binding to the Mediator of DNA damage checkpoint protein 1 (MDC1) protein.
details
Inferred

Serine/threonine-protein kinase ATR - ATR -  Homo sapiens
MOD_GSK3_1 P53_HUMAN3037BinaryPhysicochemical compatibilityPhosphorylation of Cellular tumor antigen p53 (TP53) at S37 primes the protein for phosphorylation at S33 by Glycogen synthase kinase-3 beta (GSK3B).
details
Inferred
LIG_FHA_1 CHK2_HUMAN6672BinaryPhysicochemical compatibilityPhosphorylation of T68 in the FHA-binding motif of Serine/threonine-protein kinase Chk2 (CHEK2) induces binding to the Serine/threonine-protein kinase Chk2 (CHEK2) protein.
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred

Serine/threonine-protein kinase BRSK1 - BRSK1 -  Homo sapiens
LIG_14-3-3_3 MPIP3_HUMAN213218BinaryPhysicochemical compatibilityPhosphorylation of S216 in a 14-3-3-binding motif of M-phase inducer phosphatase 3 (CDC25C) by Serine/threonine-protein kinase Chk1 (CHEK1) induces binding to 14-3-3 protein beta/alpha (YWHAB), which negatively regulates M-phase inducer phosphatase 3 (CDC25C).
details
Inferred

Serine/threonine-protein kinase BRSK1 - BRSK1 -  Homo sapiens
LIG_14-3-3_3 MPIP3_HUMAN213218BinaryPhysicochemical compatibilityPhosphorylation of S216 in a 14-3-3-binding motif of M-phase inducer phosphatase 3 (CDC25C) by Serine/threonine-protein kinase Chk1 (CHEK1) induces binding to 14-3-3 protein beta/alpha (YWHAB), which negatively regulates M-phase inducer phosphatase 3 (CDC25C).
details
Inferred

Serine/threonine-protein kinase CBK1 - CBK1 -  Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
TRG_NES ACE2_YEAST122150BinaryPhysicochemical compatibilityPhosphorylation of S137 in the NES of Metallothionein expression activator (ACE2) inhibits binding to Exportin-1 (CRM1). Phosphorylation of S137, and to a lesser extent S122, by Cbk1 directly antagonizes the interaction of Ace2 with nuclear export machinery.
details
Curated
TRG_NES ACE2_YEAST122150BinaryPhysicochemical compatibilityPhosphorylation of S122 in the NES of Metallothionein expression activator (ACE2) inhibits binding to Exportin-1 (CRM1). Phosphorylation of S137, and to a lesser extent S122, by Cbk1 directly antagonizes the interaction of Ace2 with nuclear export machinery.
details
Curated

Serine/threonine-protein kinase Chk1 - CHEK1 -  Homo sapiens
LIG_14-3-3_3 MPIP3_HUMAN213218BinaryPhysicochemical compatibilityPhosphorylation of S216 in a 14-3-3-binding motif of M-phase inducer phosphatase 3 (CDC25C) by Serine/threonine-protein kinase Chk1 (CHEK1) induces binding to 14-3-3 protein beta/alpha (YWHAB), which negatively regulates M-phase inducer phosphatase 3 (CDC25C).
details
Curated
MOD_GSK3_1 P53_HUMAN3037BinaryPhysicochemical compatibilityPhosphorylation of Cellular tumor antigen p53 (TP53) at S37 primes the protein for phosphorylation at S33 by Glycogen synthase kinase-3 beta (GSK3B).
details
Inferred
DEG_MDM2_1 P53_HUMAN1926BinaryPhysicochemical compatibilityPhosphorylation of Cellular tumor antigen p53 (TP53) on T18 (in vitro by Casein kinase I subfamily, requiring prior phosphorylation of S15) inhibits its binding to E3 ubiquitin-protein ligase Mdm2 (MDM2). In vivo, T18 is phosphorylated in response to DNA damage.
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_14-3-3_1 MDM4_HUMAN364369Avidity‑sensingOptimal binding of 14-3-3 dimer to Hdmx in response to DNA damage requires phosphorylation of two 14-3-3-binding motifs by Chk2 kinase. Binding of 14-3-3 dimer is involved in inactivation of Hdmx, a negative regulator of p53, in response to DNA damage.
details
Inferred
LIG_14-3-3_3 MDM4_HUMAN339344Avidity‑sensingOptimal binding of 14-3-3 dimer to Hdmx in response to DNA damage requires phosphorylation of two 14-3-3-binding motifs by Chk2 kinase. Binding of 14-3-3 dimer is involved in inactivation of Hdmx, a negative regulator of p53, in response to DNA damage.
details
Inferred

Serine/threonine-protein kinase Chk2 - CHEK2 -  Homo sapiens
LIG_14-3-3_3 MPIP3_HUMAN213218BinaryPhysicochemical compatibilityPhosphorylation of S216 in a 14-3-3-binding motif of M-phase inducer phosphatase 3 (CDC25C) by Serine/threonine-protein kinase Chk1 (CHEK1) induces binding to 14-3-3 protein beta/alpha (YWHAB), which negatively regulates M-phase inducer phosphatase 3 (CDC25C).
details
Inferred
LIG_14-3-3_3 MPIP3_HUMAN213218BinaryPhysicochemical compatibilityPhosphorylation of S216 in a 14-3-3-binding motif of M-phase inducer phosphatase 3 (CDC25C) by Serine/threonine-protein kinase Chk1 (CHEK1) induces binding to 14-3-3 protein beta/alpha (YWHAB), which negatively regulates M-phase inducer phosphatase 3 (CDC25C).
details
Inferred
LIG_14-3-3_3 MPIP3_HUMAN213218BinaryPhysicochemical compatibilityPhosphorylation of S216 in a 14-3-3-binding motif of M-phase inducer phosphatase 3 (CDC25C) by Serine/threonine-protein kinase Chk1 (CHEK1) induces binding to 14-3-3 protein beta/alpha (YWHAB), which negatively regulates M-phase inducer phosphatase 3 (CDC25C).
details
Inferred
MOD_GSK3_1 P53_HUMAN3037BinaryPhysicochemical compatibilityPhosphorylation of Cellular tumor antigen p53 (TP53) at S37 primes the protein for phosphorylation at S33 by Glycogen synthase kinase-3 beta (GSK3B).
details
Inferred
LIG_FHA_1 CHK2_HUMAN6672BinaryPhysicochemical compatibilityPhosphorylation of T68 in the FHA-binding motif of Serine/threonine-protein kinase Chk2 (CHEK2) induces binding to the Serine/threonine-protein kinase Chk2 (CHEK2) protein.
details
Inferred
LIG_FHA_1 CHK2_HUMAN6672BinaryPhysicochemical compatibilityPhosphorylation of T68 in the FHA-binding motif of Serine/threonine-protein kinase Chk2 (CHEK2) induces binding to the Serine/threonine-protein kinase Chk2 (CHEK2) protein.
details
Inferred
DEG_MDM2_1 P53_HUMAN1926BinaryPhysicochemical compatibilityPhosphorylation of Cellular tumor antigen p53 (TP53) on T18 (in vitro by Casein kinase I subfamily, requiring prior phosphorylation of S15) inhibits its binding to E3 ubiquitin-protein ligase Mdm2 (MDM2). In vivo, T18 is phosphorylated in response to DNA damage.
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_14-3-3_1 MDM4_HUMAN364369Avidity‑sensingOptimal binding of 14-3-3 dimer to Hdmx in response to DNA damage requires phosphorylation of two 14-3-3-binding motifs by Chk2 kinase. Binding of 14-3-3 dimer is involved in inactivation of Hdmx, a negative regulator of p53, in response to DNA damage.
details
Curated
LIG_14-3-3_3 MDM4_HUMAN339344Avidity‑sensingOptimal binding of 14-3-3 dimer to Hdmx in response to DNA damage requires phosphorylation of two 14-3-3-binding motifs by Chk2 kinase. Binding of 14-3-3 dimer is involved in inactivation of Hdmx, a negative regulator of p53, in response to DNA damage.
details
Curated

Serine/threonine-protein kinase D1 - PRKD1 -  Homo sapiens
DOC_AGCK_PIF_1 AKT1_HUMAN469474BinaryPhysicochemical compatibilityPhosphorylation of S473 in the PIF motif of RAC-alpha serine/threonine-protein kinase (AKT1) by Serine/threonine-protein kinase mTOR (MTOR) (as part of mTORC2 complex) induces intramolecular interaction with the PIF-binding pocket, resulting in cis-activation of RAC-alpha serine/threonine-protein kinase (AKT1). Dephosphorylation of the PIF motif by PHLPP1/2 (PHLPP1 for Akt2/3 and PHLPP2 for Akt1/3) results in reduced Akt activity, probably by disrupting the interaction with the Akt PIF pocket and thus cis-activation.
details
Inferred
DOC_WW_Pin1_4 JUN_HUMAN6065BinaryPhysicochemical compatibilityPhosphorylation of S63 in the Pin1-binding motif of Transcription factor AP-1 (JUN) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred

Serine/threonine-protein kinase Nek6 - NEK6 -  Homo sapiens
DOC_AGCK_PIF_1 SGK1_HUMAN418423BinaryPhysicochemical compatibilityPhosphorylation of S422 by Serine/threonine-protein kinase mTOR (MTOR) (as part of mTORC2 complex) in the PIF pocket-binding motif of Serine/threonine-protein kinase Sgk1 (SGK1) induces intramolecular binding and kinase cis-activation.
details
Inferred
DOC_AGCK_PIF_1 SGK1_HUMAN418423BinaryPhysicochemical compatibilityPhosphorylation of S422 by Serine/threonine-protein kinase mTOR (MTOR) (as part of mTORC2 complex) in the PIF pocket-binding motif of Serine/threonine-protein kinase Sgk1 (SGK1) induces intramolecular binding and kinase cis-activation.
details
Inferred
DOC_AGCK_PIF_1 KS6B1_RAT408413BinaryPhysicochemical compatibilityPhosphorylation of T412 in the PIF pocket-binding motif of Ribosomal protein S6 kinase beta-1 (Rps6kb1) induces intramolecular binding and kinase cis-activation.
details
Inferred

Serine/threonine-protein kinase PAK 1 - PAK1 -  Homo sapiens
LIG_14-3-3_1 BAD_MOUSE133138BinaryPhysicochemical compatibilityPhosphorylation of S136 in Bcl2 antagonist of cell death (Bad) by RAC-alpha serine/threonine-protein kinase (Akt1) in response to survival and growth signals such as Interleukin-3 (Il3) induces binding to 14-3-3 protein theta (Ywhaq). Binding of 14-3-3 protein theta (Ywhaq) results in dissociation of Bcl2 antagonist of cell death (Bad) from Bcl-2-like protein 1 (Bcl2l1), and thereby inhibits the pro-apoptotic activity of Bcl2 antagonist of cell death (Bad) by allowing liberated Bcl-2-like protein 1 (Bcl2l1) to exert its anti-apoptotic effect on pro-apoptotic proteins like Apoptosis regulator BAX (Bax).
details
Inferred

Serine/threonine-protein kinase PLK1 - PLK1 -  Homo sapiens
LIG_FHA_1 CHK2_HUMAN6672BinaryPhysicochemical compatibilityPhosphorylation of T68 in the FHA-binding motif of Serine/threonine-protein kinase Chk2 (CHEK2) induces binding to the Serine/threonine-protein kinase Chk2 (CHEK2) protein.
details
Inferred
LIG_FHA_1 CHK2_HUMAN6672BinaryPhysicochemical compatibilityPhosphorylation of T68 in the FHA-binding motif of Serine/threonine-protein kinase Chk2 (CHEK2) induces binding to the Serine/threonine-protein kinase Chk2 (CHEK2) protein.
details
Inferred
DEG_SCF_TRCP1_1 BORA_HUMAN496501BinaryPhysicochemical compatibilityDual phosphorylation of S497 and T501 in the TrCP1-binding motif of Protein aurora borealis (BORA) targets the protein to the SCF ubiquitin ligase complex, which marks it for degradation.
details
Inferred
DEG_SCF_TRCP1_1 BORA_HUMAN496501BinaryPhysicochemical compatibilityDual phosphorylation of S497 and T501 in the TrCP1-binding motif of Protein aurora borealis (BORA) targets the protein to the SCF ubiquitin ligase complex, which marks it for degradation.
details
Inferred
DEG_SCF_TRCP1_1 CLSPN_HUMAN2934BinaryPhysicochemical compatibilityDual phosphorylation of S30 and S34 in the TrCP1-binding motif of Claspin (CLSPN) targets the protein to the SCF ubiquitin ligase complex, which marks it for degradation.
details
Inferred
DEG_SCF_TRCP1_1 FBX5_HUMAN144149BinaryPhysicochemical compatibilityDual phosphorylation of S145 and S149 in the TrCP1-binding motif of F-box only protein 5 (FBXO5) targets the protein to the SCF ubiquitin ligase complex, which marks it for degradation.
details
Inferred
DEG_SCF_TRCP1_1 FBX5_HUMAN144149BinaryPhysicochemical compatibilityDual phosphorylation of S145 and S149 in the TrCP1-binding motif of F-box only protein 5 (FBXO5) targets the protein to the SCF ubiquitin ligase complex, which marks it for degradation.
details
Inferred
TRG_NES_CRM1_1 MPIP3_HUMAN189203BinaryPhysicochemical compatibilityPhosphorylation of S198 in the NES of M-phase inducer phosphatase 3 (CDC25C) by Serine/threonine-protein kinase PLK1 (PLK1) inhibits binding to Exportin-1 (XPO1), thus promoting nuclear localization of M-phase inducer phosphatase 3 (CDC25C).
details
Curated

Serine/threonine-protein kinase PLK3 - PLK3 -  Homo sapiens
DOC_WW_Pin1_4 JUN_HUMAN6065BinaryPhysicochemical compatibilityPhosphorylation of S63 in the Pin1-binding motif of Transcription factor AP-1 (JUN) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 JUN_HUMAN7075BinaryPhysicochemical compatibilityPhosphorylation of S73 in the Pin1-binding motif of Transcription factor AP-1 (JUN) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
TRG_NES_CRM1_1 MPIP3_HUMAN189203BinaryPhysicochemical compatibilityPhosphorylation of S198 in the NES of M-phase inducer phosphatase 3 (CDC25C) by Serine/threonine-protein kinase PLK1 (PLK1) inhibits binding to Exportin-1 (XPO1), thus promoting nuclear localization of M-phase inducer phosphatase 3 (CDC25C).
details
Inferred
TRG_NES_CRM1_1 MPIP3_HUMAN189203BinaryPhysicochemical compatibilityPhosphorylation of S198 in the NES of M-phase inducer phosphatase 3 (CDC25C) by Serine/threonine-protein kinase PLK1 (PLK1) inhibits binding to Exportin-1 (XPO1), thus promoting nuclear localization of M-phase inducer phosphatase 3 (CDC25C).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred

Serine/threonine-protein kinase SMG1 - SMG1 -  Homo sapiens
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred

Serine/threonine-protein kinase STK11 - STK11 -  Homo sapiens
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred

Serine/threonine-protein kinase Sgk1 - SGK1 -  Homo sapiens
DEG_SCF_TRCP1_1 IKBA_HUMAN3136BinaryPhysicochemical compatibilityDual phosphorylation of S32 and S36 in the TrCP1-binding motif of NF-kappa-B inhibitor alpha (NFKBIA) targets the protein to the SCF ubiquitin ligase complex, which marks it for degradation.
details
Inferred
LIG_14-3-3_1 NED4L_HUMAN465470SpecificityDomain hidingPhosphorylation of Isoform Nedd4-2a of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L) by Serine/threonine-protein kinase Sgk1 (SGK1) induces binding to 14-3-3 protein eta (YWHAH). This inhibits (whether allosterically or sterically is not known) interactions of NEDD4L via its WW domains with the PY motif in Amiloride-sensitive sodium channel subunit gamma (SCNN1G) (ENaC). As a result, ENaC does not get degraded and ENaC-mediated Na+ currents increase.
details
Curated
TRG_NLS CDN1B_HUMAN152166SpecificityMotif hidingPhosphorylation of a 14-3-3-binding motif in the NLS of Cyclin-dependent kinase inhibitor 1B (CDKN1B) by RAC-alpha serine/threonine-protein kinase (AKT1) induces binding of 14-3-3 protein gamma (YWHAG), which hides the NLS and prevents binding to Importin subunit alpha-1 (KPNA1), thereby mediating cytoplasmic retention of Cyclin-dependent kinase inhibitor 1B (CDKN1B). Binding of 14-3-3 dimer involves an additional C-terminal 14-3-3-binding motif (see switch details).
details
Inferred
LIG_14-3-3_3 CDN1B_HUMAN154159SpecificityMotif hidingPhosphorylation of a 14-3-3-binding motif in the NLS of Cyclin-dependent kinase inhibitor 1B (CDKN1B) by RAC-alpha serine/threonine-protein kinase (AKT1) induces binding of 14-3-3 protein gamma (YWHAG), which hides the NLS and prevents binding to Importin subunit alpha-1 (KPNA1), thereby mediating cytoplasmic retention of Cyclin-dependent kinase inhibitor 1B (CDKN1B). Binding of 14-3-3 dimer involves an additional C-terminal 14-3-3-binding motif (see switch details).
details
Inferred
LIG_14-3-3_3 CDN1B_HUMAN154159Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in Cyclin-dependent kinase inhibitor 1B (CDKN1B) by RAC-alpha serine/threonine-protein kinase (AKT1) and ribosomal protein S6 kinases (Ribosomal protein S6 kinase alpha-1 (RPS6KA1), Ribosomal protein S6 kinase alpha-3 (RPS6KA3)) induces binding of 14-3-3 dimer. Binding of 14-3-3 results in cytoplasmic localisation of Cyclin-dependent kinase inhibitor 1B (CDKN1B) (see switch details), thereby alleviating Cyclin-dependent kinase inhibitor 1B (CDKN1B)-mediated inhibition of cyclin-dependent kinases and cell cycle progression.
details
Inferred
LIG_14-3-3_3 CDN1B_HUMAN193198Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in Cyclin-dependent kinase inhibitor 1B (CDKN1B) by RAC-alpha serine/threonine-protein kinase (AKT1) and ribosomal protein S6 kinases (Ribosomal protein S6 kinase alpha-1 (RPS6KA1), Ribosomal protein S6 kinase alpha-3 (RPS6KA3)) induces binding of 14-3-3 dimer. Binding of 14-3-3 results in cytoplasmic localisation of Cyclin-dependent kinase inhibitor 1B (CDKN1B) (see switch details), thereby alleviating Cyclin-dependent kinase inhibitor 1B (CDKN1B)-mediated inhibition of cyclin-dependent kinases and cell cycle progression.
details
Inferred

Serine/threonine-protein kinase TBK1 - TBK1 -  Homo sapiens
DOC_AGCK_PIF_1 AKT1_HUMAN469474BinaryPhysicochemical compatibilityPhosphorylation of S473 in the PIF motif of RAC-alpha serine/threonine-protein kinase (AKT1) by Serine/threonine-protein kinase mTOR (MTOR) (as part of mTORC2 complex) induces intramolecular interaction with the PIF-binding pocket, resulting in cis-activation of RAC-alpha serine/threonine-protein kinase (AKT1). Dephosphorylation of the PIF motif by PHLPP1/2 (PHLPP1 for Akt2/3 and PHLPP2 for Akt1/3) results in reduced Akt activity, probably by disrupting the interaction with the Akt PIF pocket and thus cis-activation.
details
Inferred

Serine/threonine-protein kinase TOR1 - TOR1 -  Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
DOC_AGCK_PIF_1 SCH9_YEAST733738BinaryPhysicochemical compatibilityPhosphorylation of T737 by Serine/threonine-protein kinase TOR1 (TOR1) in the PIF pocket-binding motif of Serine/threonine-protein kinase SCH9 (SCH9) induces intramolecular binding and kinase cis-activation.
details
Curated

Serine/threonine-protein kinase VRK1 - VRK1 -  Homo sapiens
DOC_WW_Pin1_4 JUN_HUMAN6065BinaryPhysicochemical compatibilityPhosphorylation of S63 in the Pin1-binding motif of Transcription factor AP-1 (JUN) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 JUN_HUMAN6065BinaryPhysicochemical compatibilityPhosphorylation of S63 in the Pin1-binding motif of Transcription factor AP-1 (JUN) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 JUN_HUMAN7075BinaryPhysicochemical compatibilityPhosphorylation of S73 in the Pin1-binding motif of Transcription factor AP-1 (JUN) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_WW_Pin1_4 JUN_HUMAN7075BinaryPhysicochemical compatibilityPhosphorylation of S73 in the Pin1-binding motif of Transcription factor AP-1 (JUN) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DEG_MDM2_1 P53_HUMAN1926BinaryPhysicochemical compatibilityPhosphorylation of Cellular tumor antigen p53 (TP53) on T18 (in vitro by Casein kinase I subfamily, requiring prior phosphorylation of S15) inhibits its binding to E3 ubiquitin-protein ligase Mdm2 (MDM2). In vivo, T18 is phosphorylated in response to DNA damage.
details
Inferred
DEG_MDM2_1 P53_HUMAN1926BinaryPhysicochemical compatibilityPhosphorylation of Cellular tumor antigen p53 (TP53) on T18 (in vitro by Casein kinase I subfamily, requiring prior phosphorylation of S15) inhibits its binding to E3 ubiquitin-protein ligase Mdm2 (MDM2). In vivo, T18 is phosphorylated in response to DNA damage.
details
Inferred
DEG_MDM2_1 P53_HUMAN1926BinaryPhysicochemical compatibilityPhosphorylation of Cellular tumor antigen p53 (TP53) on T18 (in vitro by Casein kinase I subfamily, requiring prior phosphorylation of S15) inhibits its binding to E3 ubiquitin-protein ligase Mdm2 (MDM2). In vivo, T18 is phosphorylated in response to DNA damage.
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred

Serine/threonine-protein kinase mTOR - MTOR -  Homo sapiens
DOC_AGCK_PIF_1 AKT1_HUMAN469474BinaryPhysicochemical compatibilityPhosphorylation of S473 in the PIF motif of RAC-alpha serine/threonine-protein kinase (AKT1) by Serine/threonine-protein kinase mTOR (MTOR) (as part of mTORC2 complex) induces intramolecular interaction with the PIF-binding pocket, resulting in cis-activation of RAC-alpha serine/threonine-protein kinase (AKT1). Dephosphorylation of the PIF motif by PHLPP1/2 (PHLPP1 for Akt2/3 and PHLPP2 for Akt1/3) results in reduced Akt activity, probably by disrupting the interaction with the Akt PIF pocket and thus cis-activation.
details
Curated
MOD_GSK3_1 MYC_HUMAN5562BinaryPhysicochemical compatibilityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 primes the protein for phosphorylation at T58 by Glycogen synthase kinase-3 beta (GSK3B).
details
Inferred
DOC_WW_Pin1_4 AKT1_HUMAN447452BinaryPhysicochemical compatibilityPhosphorylation of T450 in the Pin1-binding motif of RAC-alpha serine/threonine-protein kinase (AKT1) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
DOC_AGCK_PIF_1 SGK1_HUMAN418423BinaryPhysicochemical compatibilityPhosphorylation of S422 by Serine/threonine-protein kinase mTOR (MTOR) (as part of mTORC2 complex) in the PIF pocket-binding motif of Serine/threonine-protein kinase Sgk1 (SGK1) induces intramolecular binding and kinase cis-activation.
details
Curated
DOC_AGCK_PIF_1 KS6B1_RAT408413BinaryPhysicochemical compatibilityPhosphorylation of T412 in the PIF pocket-binding motif of Ribosomal protein S6 kinase beta-1 (Rps6kb1) induces intramolecular binding and kinase cis-activation.
details
Inferred
LIG_SH3_2 MYC_HUMAN6065BinaryPhysicochemical compatibilityPhosphorylation of S62 in the SH3-binding motif of Myc proto-oncogene protein (MYC) by GSK-3 subfamily disrupts its interaction with Myc box-dependent-interacting protein 1 (BIN1).
details
Inferred
MOD_ProDKin_1 MYC_HUMAN5965SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Inferred
MOD_GSK3_1 MYC_HUMAN5562SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Inferred
DEG_SCF_FBW7_1 MYC_HUMAN5562SpecificityAltered binding specificityPhosphorylation of Myc proto-oncogene protein (MYC) at S62 by Mitogen-activated protein kinase 1 (MAPK1) primes MYC for phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which targets MYC to the SCF ubiquitin ligase complex, F-box/WD repeat-containing protein 7 (FBXW7) that marks MYC for degradation.
details
Inferred
LIG_eIF4E_1 4EBP1_HUMAN5460BinaryPhysicochemical compatibilityPhosphorylation of S65 flanking the eIF4E-binding motif of Eukaryotic translation initiation factor 4E-binding protein 1 (EIF4EBP1) by Serine/threonine-protein kinase mTOR (MTOR) inhibits binding to Eukaryotic translation initiation factor 4E (EIF4E) in response to growth factors and nutrients. This results in release of Eukaryotic translation initiation factor 4E (EIF4E), which associates with other initiation factors to form the eIF-4F complex that mediates initiation of translation. However, disruption of the interaction between Eukaryotic translation initiation factor 4E-binding protein 1 (EIF4EBP1) and Eukaryotic translation initiation factor 4E (EIF4E) has been shown to be dependent on hyperphosphorylation of Eukaryotic translation initiation factor 4E-binding protein 1 (EIF4EBP1) by FRAP/mTOR, PI3K and ERK pathways. According to the current model, Eukaryotic translation initiation factor 4E-binding protein 1 (EIF4EBP1) is phosphorylated on multiple residues in a well-defined order. Basal phosphorylation of T37 and T46 serves as a priming event for subsequent serum-induced phosphorylation of T70, which primes for subsequent phosphorylation of S65.
details
Curated

Serine/threonine-protein kinase mTOR - MTOR -  Mus musculus
DOC_WW_Pin1_4 STAT3_HUMAN724729BinaryPhysicochemical compatibilityPhosphorylation of S727 in the Pin1-binding motif of Signal transducer and activator of transcription 3 (STAT3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
Inferred
LIG_eIF4E_1 4EBP1_HUMAN5460BinaryPhysicochemical compatibilityPhosphorylation of S65 flanking the eIF4E-binding motif of Eukaryotic translation initiation factor 4E-binding protein 1 (EIF4EBP1) by Serine/threonine-protein kinase mTOR (MTOR) inhibits binding to Eukaryotic translation initiation factor 4E (EIF4E) in response to growth factors and nutrients. This results in release of Eukaryotic translation initiation factor 4E (EIF4E), which associates with other initiation factors to form the eIF-4F complex that mediates initiation of translation. However, disruption of the interaction between Eukaryotic translation initiation factor 4E-binding protein 1 (EIF4EBP1) and Eukaryotic translation initiation factor 4E (EIF4E) has been shown to be dependent on hyperphosphorylation of Eukaryotic translation initiation factor 4E-binding protein 1 (EIF4EBP1) by FRAP/mTOR, PI3K and ERK pathways. According to the current model, Eukaryotic translation initiation factor 4E-binding protein 1 (EIF4EBP1) is phosphorylated on multiple residues in a well-defined order. Basal phosphorylation of T37 and T46 serves as a priming event for subsequent serum-induced phosphorylation of T70, which primes for subsequent phosphorylation of S65.
details
Inferred

Serine/threonine-protein kinase pim-1 - PIM1 -  Homo sapiens
LIG_14-3-3_3 FOXO3_HUMAN250255Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in Forkhead box protein O3 (FOXO3) by RAC-alpha serine/threonine-protein kinase (AKT1) induces high-avidity binding to dimeric 14-3-3 protein beta/alpha (YWHAB). This interaction results in cytoplasmic retention and inactivation of Forkhead box protein O3 (FOXO3).
details
Inferred
LIG_14-3-3_3 FOXO3_HUMAN2934Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in Forkhead box protein O3 (FOXO3) by RAC-alpha serine/threonine-protein kinase (AKT1) induces high-avidity binding to dimeric 14-3-3 protein beta/alpha (YWHAB). This interaction results in cytoplasmic retention and inactivation of Forkhead box protein O3 (FOXO3).
details
Inferred
TRG_NLS CDN1B_HUMAN152166SpecificityMotif hidingPhosphorylation of a 14-3-3-binding motif in the NLS of Cyclin-dependent kinase inhibitor 1B (CDKN1B) by RAC-alpha serine/threonine-protein kinase (AKT1) induces binding of 14-3-3 protein gamma (YWHAG), which hides the NLS and prevents binding to Importin subunit alpha-1 (KPNA1), thereby mediating cytoplasmic retention of Cyclin-dependent kinase inhibitor 1B (CDKN1B). Binding of 14-3-3 dimer involves an additional C-terminal 14-3-3-binding motif (see switch details).
details
Inferred
LIG_14-3-3_3 CDN1B_HUMAN154159SpecificityMotif hidingPhosphorylation of a 14-3-3-binding motif in the NLS of Cyclin-dependent kinase inhibitor 1B (CDKN1B) by RAC-alpha serine/threonine-protein kinase (AKT1) induces binding of 14-3-3 protein gamma (YWHAG), which hides the NLS and prevents binding to Importin subunit alpha-1 (KPNA1), thereby mediating cytoplasmic retention of Cyclin-dependent kinase inhibitor 1B (CDKN1B). Binding of 14-3-3 dimer involves an additional C-terminal 14-3-3-binding motif (see switch details).
details
Inferred
LIG_14-3-3_3 CDN1B_HUMAN154159Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in Cyclin-dependent kinase inhibitor 1B (CDKN1B) by RAC-alpha serine/threonine-protein kinase (AKT1) and ribosomal protein S6 kinases (Ribosomal protein S6 kinase alpha-1 (RPS6KA1), Ribosomal protein S6 kinase alpha-3 (RPS6KA3)) induces binding of 14-3-3 dimer. Binding of 14-3-3 results in cytoplasmic localisation of Cyclin-dependent kinase inhibitor 1B (CDKN1B) (see switch details), thereby alleviating Cyclin-dependent kinase inhibitor 1B (CDKN1B)-mediated inhibition of cyclin-dependent kinases and cell cycle progression.
details
Inferred
LIG_14-3-3_3 CDN1B_HUMAN193198Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in Cyclin-dependent kinase inhibitor 1B (CDKN1B) by RAC-alpha serine/threonine-protein kinase (AKT1) and ribosomal protein S6 kinases (Ribosomal protein S6 kinase alpha-1 (RPS6KA1), Ribosomal protein S6 kinase alpha-3 (RPS6KA3)) induces binding of 14-3-3 dimer. Binding of 14-3-3 results in cytoplasmic localisation of Cyclin-dependent kinase inhibitor 1B (CDKN1B) (see switch details), thereby alleviating Cyclin-dependent kinase inhibitor 1B (CDKN1B)-mediated inhibition of cyclin-dependent kinases and cell cycle progression.
details
Inferred
LIG_PCNA_PIPBox_1 CDN1A_HUMAN144153BinaryPhysicochemical compatibilityPhosphorylation of T145 in the PCNA-binding motif of Cyclin-dependent kinase inhibitor 1 (CDKN1A) by RAC-alpha serine/threonine-protein kinase (AKT1) inhibits binding to Proliferating cell nuclear antigen (PCNA). As a result, Cyclin-dependent kinase inhibitor 1 (CDKN1A) no longer inhibits Proliferating cell nuclear antigen (PCNA) and blocking of DNA replication is relieved.
details
Inferred
LIG_PCNA_PIPBox_1 CDN1A_HUMAN144153BinaryPhysicochemical compatibilityPhosphorylation of T145 in the PCNA-binding motif of Cyclin-dependent kinase inhibitor 1 (CDKN1A) by RAC-alpha serine/threonine-protein kinase (AKT1) inhibits binding to Proliferating cell nuclear antigen (PCNA). As a result, Cyclin-dependent kinase inhibitor 1 (CDKN1A) no longer inhibits Proliferating cell nuclear antigen (PCNA) and blocking of DNA replication is relieved.
details
Inferred
LIG_PCNA_PIPBox_1 CDN1A_HUMAN144153BinaryPhysicochemical compatibilityPhosphorylation of S146 in the PCNA-binding motif of Cyclin-dependent kinase inhibitor 1 (CDKN1A) by PKC subfamily inhibits binding to Proliferating cell nuclear antigen (PCNA). As a result, Cyclin-dependent kinase inhibitor 1 (CDKN1A) no longer inhibits Proliferating cell nuclear antigen (PCNA) and blocking of DNA replication is relieved.
details
Inferred
LIG_PCNA_PIPBox_1 CDN1A_HUMAN144153BinaryPhysicochemical compatibilityPhosphorylation of S146 in the PCNA-binding motif of Cyclin-dependent kinase inhibitor 1 (CDKN1A) by PKC subfamily inhibits binding to Proliferating cell nuclear antigen (PCNA). As a result, Cyclin-dependent kinase inhibitor 1 (CDKN1A) no longer inhibits Proliferating cell nuclear antigen (PCNA) and blocking of DNA replication is relieved.
details
Inferred
LIG_14-3-3_1 BAD_MOUSE133138BinaryPhysicochemical compatibilityPhosphorylation of S136 in Bcl2 antagonist of cell death (Bad) by RAC-alpha serine/threonine-protein kinase (Akt1) in response to survival and growth signals such as Interleukin-3 (Il3) induces binding to 14-3-3 protein theta (Ywhaq). Binding of 14-3-3 protein theta (Ywhaq) results in dissociation of Bcl2 antagonist of cell death (Bad) from Bcl-2-like protein 1 (Bcl2l1), and thereby inhibits the pro-apoptotic activity of Bcl2 antagonist of cell death (Bad) by allowing liberated Bcl-2-like protein 1 (Bcl2l1) to exert its anti-apoptotic effect on pro-apoptotic proteins like Apoptosis regulator BAX (Bax).
details
Inferred

Serine/threonine-protein kinase pim-1 - PIM1 -  Mus musculus
LIG_14-3-3_1 BAD_MOUSE133138BinaryPhysicochemical compatibilityPhosphorylation of S136 in Bcl2 antagonist of cell death (Bad) by RAC-alpha serine/threonine-protein kinase (Akt1) in response to survival and growth signals such as Interleukin-3 (Il3) induces binding to 14-3-3 protein theta (Ywhaq). Binding of 14-3-3 protein theta (Ywhaq) results in dissociation of Bcl2 antagonist of cell death (Bad) from Bcl-2-like protein 1 (Bcl2l1), and thereby inhibits the pro-apoptotic activity of Bcl2 antagonist of cell death (Bad) by allowing liberated Bcl-2-like protein 1 (Bcl2l1) to exert its anti-apoptotic effect on pro-apoptotic proteins like Apoptosis regulator BAX (Bax).
details
Inferred

Serine/threonine-protein kinase pim-2 - PIM2 -  Homo sapiens
LIG_PCNA_PIPBox_1 CDN1A_HUMAN144153BinaryPhysicochemical compatibilityPhosphorylation of T145 in the PCNA-binding motif of Cyclin-dependent kinase inhibitor 1 (CDKN1A) by RAC-alpha serine/threonine-protein kinase (AKT1) inhibits binding to Proliferating cell nuclear antigen (PCNA). As a result, Cyclin-dependent kinase inhibitor 1 (CDKN1A) no longer inhibits Proliferating cell nuclear antigen (PCNA) and blocking of DNA replication is relieved.
details
Inferred
LIG_PCNA_PIPBox_1 CDN1A_HUMAN144153BinaryPhysicochemical compatibilityPhosphorylation of S146 in the PCNA-binding motif of Cyclin-dependent kinase inhibitor 1 (CDKN1A) by PKC subfamily inhibits binding to Proliferating cell nuclear antigen (PCNA). As a result, Cyclin-dependent kinase inhibitor 1 (CDKN1A) no longer inhibits Proliferating cell nuclear antigen (PCNA) and blocking of DNA replication is relieved.
details
Inferred
LIG_14-3-3_1 BAD_MOUSE133138BinaryPhysicochemical compatibilityPhosphorylation of S136 in Bcl2 antagonist of cell death (Bad) by RAC-alpha serine/threonine-protein kinase (Akt1) in response to survival and growth signals such as Interleukin-3 (Il3) induces binding to 14-3-3 protein theta (Ywhaq). Binding of 14-3-3 protein theta (Ywhaq) results in dissociation of Bcl2 antagonist of cell death (Bad) from Bcl-2-like protein 1 (Bcl2l1), and thereby inhibits the pro-apoptotic activity of Bcl2 antagonist of cell death (Bad) by allowing liberated Bcl-2-like protein 1 (Bcl2l1) to exert its anti-apoptotic effect on pro-apoptotic proteins like Apoptosis regulator BAX (Bax).
details
Inferred

Serine/threonine-protein kinase pim-3 - PIM3 -  Homo sapiens
LIG_14-3-3_1 BAD_MOUSE133138BinaryPhysicochemical compatibilityPhosphorylation of S136 in Bcl2 antagonist of cell death (Bad) by RAC-alpha serine/threonine-protein kinase (Akt1) in response to survival and growth signals such as Interleukin-3 (Il3) induces binding to 14-3-3 protein theta (Ywhaq). Binding of 14-3-3 protein theta (Ywhaq) results in dissociation of Bcl2 antagonist of cell death (Bad) from Bcl-2-like protein 1 (Bcl2l1), and thereby inhibits the pro-apoptotic activity of Bcl2 antagonist of cell death (Bad) by allowing liberated Bcl-2-like protein 1 (Bcl2l1) to exert its anti-apoptotic effect on pro-apoptotic proteins like Apoptosis regulator BAX (Bax).
details
Inferred

Serine/threonine-protein kinase pim-3 - PIM3 -  Mus musculus
LIG_14-3-3_1 BAD_MOUSE133138BinaryPhysicochemical compatibilityPhosphorylation of S136 in Bcl2 antagonist of cell death (Bad) by RAC-alpha serine/threonine-protein kinase (Akt1) in response to survival and growth signals such as Interleukin-3 (Il3) induces binding to 14-3-3 protein theta (Ywhaq). Binding of 14-3-3 protein theta (Ywhaq) results in dissociation of Bcl2 antagonist of cell death (Bad) from Bcl-2-like protein 1 (Bcl2l1), and thereby inhibits the pro-apoptotic activity of Bcl2 antagonist of cell death (Bad) by allowing liberated Bcl-2-like protein 1 (Bcl2l1) to exert its anti-apoptotic effect on pro-apoptotic proteins like Apoptosis regulator BAX (Bax).
details
Inferred

Serine/threonine-protein kinase pknB - PKNB -  Mycobacterium tuberculosis
LIG_FHA_1 Y1827_MYCTU2026BinaryPhysicochemical compatibilityPhosphorylation of T22 in the FHA-binding motif of Uncharacterized protein Rv1827/MT1875 (Rv1827) by Serine/threonine-protein kinase pknB (pknB) results in auto-inhibition due to an intramolecular interaction with the FHA domain. As a result, phosphorylation-independent interactions of the FHA domain with metabolic enzymes, which regulate the catalytic activity of these enzymes, are blocked (See also switch details).
details
Curated

TP53-regulating kinase - TP53RK -  Homo sapiens
LIG_TAZ2 P53_HUMAN1925CumulativeRheostaticMultisite phosphorylation of S15 and T18 and S20 and S33 and S37 and S46 in the TAD region of Cellular tumor antigen p53 (TP53) additively enhances its affinity for CREB-binding protein (CREBBP).
details
Inferred

Transcription initiation factor TFIID subunit 1 - TAF1 -  Homo sapiens
LIG_PH_Tfb1 P53_HUMAN5056CumulativeRheostaticMultisite phosphorylation of S46 and T55 in the PH-like binding motif of Cellular tumor antigen p53 (TP53) gradually enhances its affinity for General transcription factor IIH subunit 1 (GTF2H1), an interaction involved in activation of transcription initiation and elongation by Cellular tumor antigen p53 (TP53).
details
Inferred

Tyrosine-protein kinase ABL1 - ABL1 -  Homo sapiens
LIG_GBD_WASP_1 WASP_HUMAN466476UncategorisedUncategorisedPhosphorylation of Wiskott-Aldrich syndrome protein (WAS) at Y291 by Src kinases, e.g. , destabilises the auto-inhibitory intramolecular interaction of Wiskott-Aldrich syndrome protein (WAS).
details
Inferred
LIG_SH2_IC EGFR_HUMAN10921100BinaryPhysicochemical compatibilityPhosphorylation of Y1092 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.
details
Inferred
LIG_SH2_IE EGFR_HUMAN10111020BinaryPhysicochemical compatibilityPhosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Ras and Rab interactor 1 (RIN1) protein.
details
Inferred
LIG_SH2_IE EGFR_HUMAN11911200BinaryPhysicochemical compatibilityPhosphorylation of Y1197 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Ras and Rab interactor 1 (RIN1) protein.
details
Inferred
LIG_SH2_IE EGFR_HUMAN10081024BinaryPhysicochemical compatibilityPhosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Tyrosine-protein kinase JAK1 (JAK1) protein.
details
Inferred
LIG_SH2_IE EGFR_HUMAN10081024BinaryPhysicochemical compatibilityPhosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Tyrosine-protein kinase JAK2 (JAK2) protein.
details
Inferred
LIG_SH2_ID EGFR_HUMAN10081024BinaryPhysicochemical compatibilityPhosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the SH2 domain-containing protein 3C (SH2D3C) protein.
details
Inferred
LIG_SH2_ID EGFR_HUMAN10081024BinaryPhysicochemical compatibilityPhosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the SH2 domain-containing protein 3A (SH2D3A) protein.
details
Inferred
LIG_SH2_III EGFR_HUMAN10081024BinaryPhysicochemical compatibilityPhosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Signal transducer and activator of transcription 6 (STAT6) protein.
details
Inferred
LIG_SH2_IC MET_HUMAN13511360BinaryPhysicochemical compatibilityPhosphorylation of Y1356 in the SH2-binding motif of Hepatocyte growth factor receptor (MET) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.
details
Inferred
LIG_SH2_IA DAB1_MOUSE212228BinaryPhysicochemical compatibilityPhosphorylation of Y220 in the SH2-binding motif of Disabled homolog 1 (Dab1) induces binding to the Cytoplasmic protein NCK2 (NCK2) protein.
details
Inferred
LIG_SH2_IA DAB1_MOUSE220223BinaryPre‑translationalAlternative splicing removes the SH2-binding motif of Disabled homolog 1 (Dab1), abrogating binding to Cytoplasmic protein NCK2 (NCK2). NCK2-beta has a clear preference for splice variant 2 (with the YQYI motif) over splice variant 3 (with the YQTI motif). The authors theorise that since Adapter molecule crk (Crk) is directly linked to the C3G-Rap1 pathway, and NCK2-beta is linked to the Breast cancer anti-estrogen resistance protein 1 (Bcar1) (p130Cas) pathway, it is likely that isoforms 2 and 3 connect to different downstream cascades. It was suggested that the ability of different Dab1 isoforms to recruit distinct sets of SH2 domains implies a fine-tuning role of Dab1 splicing in the intricate series of events that underlie neuronal migration (Gao et al. (2012) (here)) (See also Katyal and Godbout (2004) (here) and Gao et al. (2010) (here)).
details
Inferred
LIG_SH2_IA DAB1_MOUSE232235BinaryPre‑translationalAlternative splicing removes the SH2-binding motif of Disabled homolog 1 (Dab1), abrogating binding to Cytoplasmic protein NCK2 (NCK2). The NCK2-beta has a clear preference for splice variant 2 (with YQYI motif) over splice variant 3 (with YQTI motif). The authors theorise that since Adapter molecule crk (Crk) is directly linked to the C3G-Rap1 pathway, and NCK2-beta is linked to the Breast cancer anti-estrogen resistance protein 1 (Bcar1) (p130Cas) pathway, it is likely that isoforms 2 and 3 connect to different downstream cascades. It was suggested that the ability of different Dab1 isoforms to recruit distinct sets of SH2 domains implies a fine-tuning role of Dab1 splicing in the intricate series of events that underlie neuronal migration (Gao et al. (2012) (here)) (See also Katyal and Godbout (2004) (here) and Gao et al. (2010) (here)).
details
Inferred
LIG_SH2_IA DAB1_MOUSE220223BinaryPre‑translationalAlternative splicing removes the SH2-binding motif of Disabled homolog 1 (Dab1), abrogating binding to Adapter molecule crk (Crk). Both Adapter molecule crk (Crk) and Crk-like protein (Crkl) bind equally well to variants 2 and 3. The authors theorise that since Adapter molecule crk (Crk) is directly linked to the C3G-Rap1 pathway, and NCK2-beta is linked to the Breast cancer anti-estrogen resistance protein 1 (Bcar1) (p130Cas) pathway, it is likely that isoforms 2 and 3 connect to different downstream cascades. It was suggested that the ability of different Dab1 isoforms to recruit distinct sets of SH2 domains implies a fine-tuning role of Dab1 splicing in the intricate series of events that underlie neuronal migration (Gao et al. (2012) (here)) (See also Katyal and Godbout (2004) (here) and Gao et al. (2010) (here)).
details
Inferred
LIG_SH2_IA DAB1_MOUSE232235BinaryPre‑translationalAlternative splicing removes the SH2-binding motif of Disabled homolog 1 (Dab1), abrogating binding to Adapter molecule crk (Crk). Both Adapter molecule crk (Crk) and Crk-like protein (Crkl) bind equally well to variants 2 and 3. The authors theorise that since Adapter molecule crk (Crk) is directly linked to the C3G-Rap1 pathway, and NCK2-beta is linked to the Breast cancer anti-estrogen resistance protein 1 (Bcar1) (p130Cas) pathway, it is likely that isoforms 2 and 3 connect to different downstream cascades. It was suggested that the ability of different Dab1 isoforms to recruit distinct sets of SH2 domains implies a fine-tuning role of Dab1 splicing in the intricate series of events that underlie neuronal migration (Gao et al. (2012) (here)) (See also Katyal and Godbout (2004) (here) and Gao et al. (2010) (here)).
details
Inferred
LIG_SH2_IA DAB1_MOUSE232235BinaryPhysicochemical compatibilityPhosphorylation of Y232 in the SH2-binding motif of Disabled homolog 1 (Dab1) induces binding to Cytoplasmic protein NCK2 (NCK2).
details
Inferred
LIG_SH2_IA DAB1_MOUSE232235BinaryPhysicochemical compatibilityPhosphorylation of Y232 in the SH2-binding motif of Disabled homolog 1 (Dab1) induces binding to Adapter molecule crk (Crk).
details
Inferred
LIG_SH2_SRC EGFR_HUMAN10161019BinaryPhysicochemical compatibilityPhosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1 (PLCG1).
details
Inferred
LIG_SH2_SRC EGFR_HUMAN10161019BinaryPhysicochemical compatibilityPhosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to Cytoplasmic protein NCK1 (NCK1).
details
Inferred

Tyrosine-protein kinase ABL1 - ABL1 -  Mus musculus
LIG_SH2_IB CBL_HUMAN770780BinaryPhysicochemical compatibilityPhosphorylation of Y774 in the SH2-binding motif of E3 ubiquitin-protein ligase CBL (CBL) induces binding to the Adapter molecule crk (CRK) protein.
details
Inferred
LIG_WW_1 JUN_MOUSE167170BinaryPhysicochemical compatibilityPhosphorylation of Y170 in the WW-binding motif of Transcription factor AP-1 (Jun) by Tyrosine-protein kinase ABL1 (Abl1) blocks binding to the E3 ubiquitin-protein ligase Itchy (Itch). As a result, Transcription factor AP-1 (Jun) is not ubiquitylated by E3 ubiquitin-protein ligase Itchy (Itch), and thus not targeted for proteasomal degradation. Regulation of transcriptional activity of Transcription factor AP-1 (Jun) by Tyrosine-protein kinase ABL1 (Abl1) required translocation of the kinase to the nucleus, which was triggered by T cell activation.
details
Curated

Tyrosine-protein kinase BTK - BTK -  Homo sapiens
LIG_GBD_WASP_1 WASP_HUMAN466476UncategorisedUncategorisedPhosphorylation of Wiskott-Aldrich syndrome protein (WAS) at Y291 by Src kinases, e.g. , destabilises the auto-inhibitory intramolecular interaction of Wiskott-Aldrich syndrome protein (WAS).
details
Inferred

Tyrosine-protein kinase Blk - BLK -  Homo sapiens
LIG_TYR_ITIM FCG2B_HUMAN290295BinaryPhysicochemical compatibilityPhosphorylation of Y292 in the ITIM motif of Low affinity immunoglobulin gamma Fc region receptor II-b (FCGR2B) induces binding of Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 1 (INPP5D) via its SH2 domain.
details
Inferred
LIG_TYR_ITIM FCG2B_HUMAN290295BinaryPhysicochemical compatibilityPhosphorylation of Y292 in the ITIM motif of Low affinity immunoglobulin gamma Fc region receptor II-b (FCGR2B) induces binding of Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 1 (INPP5D) via its SH2 domain.
details
Inferred
LIG_TYR_ITAM FCG2A_HUMAN285307Avidity‑sensingPhosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).
details
Inferred
LIG_TYR_ITAM FCG2A_HUMAN285307Avidity‑sensingPhosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).
details
Inferred
LIG_TYR_ITAM FCG2A_HUMAN285307Avidity‑sensingPhosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).
details
Inferred
LIG_TYR_ITAM FCG2A_HUMAN285307Avidity‑sensingPhosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).
details
Inferred
LIG_TYR_ITAM FCG2A_HUMAN285307Avidity‑sensingPhosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).
details
Inferred
LIG_TYR_ITAM FCG2A_HUMAN285307Avidity‑sensingPhosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).
details
Inferred
LIG_TYR_ITAM FCG2A_HUMAN285307Avidity‑sensingPhosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).
details
Inferred
LIG_TYR_ITAM FCG2A_HUMAN285307Avidity‑sensingPhosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).
details
Inferred

Tyrosine-protein kinase CSK - CSK -  Homo sapiens
LIG_SH2_SRC SRC_HUMAN530533BinaryPhysicochemical compatibilityPhosphorylation of Y530 in the SH2-binding motif of Proto-oncogene tyrosine-protein kinase Src (SRC) induces an intramolecular interaction with the SH2 domain of Proto-oncogene tyrosine-protein kinase Src (SRC) resulting in inhibition of its activity and preventing intermolecular interactions of its SH2 domain.
details
Inferred
LIG_SH2_SRC SRC_HUMAN530533BinaryPhysicochemical compatibilityPhosphorylation of Y530 in the SH2-binding motif of Proto-oncogene tyrosine-protein kinase Src (SRC) induces an intramolecular interaction with the SH2 domain of Proto-oncogene tyrosine-protein kinase Src (SRC) resulting in inhibition of its activity and preventing intermolecular interactions of its SH2 domain.
details
Inferred

Tyrosine-protein kinase FRK - FRK -  Homo sapiens
DOC_WW_Pin1_4 FOS_MOUSE229234BinaryPhysicochemical compatibilityPhosphorylation of T232 in the Pin1-binding motif of Proto-oncogene c-Fos (Fos) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details
Inferred

Tyrosine-protein kinase Fgr - FGR -  Homo sapiens
LIG_SH2_IA FAK1_HUMAN389405BinaryPhysicochemical compatibilityPhosphorylation of Y397 in the SH2-binding motif of Focal adhesion kinase 1 (PTK2) induces binding to the Cytoplasmic protein NCK2 (NCK2) protein.
details
Inferred
LIG_SH2_SRC FAK1_HUMAN397400BinaryPhysicochemical compatibilityPhosphorylation of Y397 in the SH2-binding motif of Focal adhesion kinase 1 (PTK2) induces binding to Neuronal proto-oncogene tyrosine-protein kinase Src (Src).
details
Inferred

Tyrosine-protein kinase Fyn - FYN -  Mus musculus
LIG_SH2_GRB2 IRS1_RAT895898BinaryPhysicochemical compatibilityPhosphorylation of Y895 in the SH2-binding motif of Insulin receptor substrate 1 (Irs1) induces binding to the Growth factor receptor-bound protein 2 (Grb2) protein.
details
Inferred
TRG_ENDOCYTIC_2 CTLA4_MOUSE201204SpecificityAltered binding specificityDephosphorylation of Y201 of Cytotoxic T-lymphocyte protein 4 (Ctla4) switches the specificity of Ctla4 from SH2 domain-containing proteins like Tyrosine-protein phosphatase non-receptor type 11 (Ptpn11) to the AP-2 complex mu subunit (AP-2 complex subunit mu (Ap2m1)), thereby switching from inhibitory signal transmission and negative regulation of T cell responses to internalization and inactivation of Ctla4.
details
Inferred
LIG_SH2_STAT5 CTLA4_MOUSE201204SpecificityAltered binding specificityDephosphorylation of Y201 of Cytotoxic T-lymphocyte protein 4 (Ctla4) switches the specificity of Ctla4 from SH2 domain-containing proteins like Tyrosine-protein phosphatase non-receptor type 11 (Ptpn11) to the AP-2 complex mu subunit (AP-2 complex subunit mu (Ap2m1)), thereby switching from inhibitory signal transmission and negative regulation of T cell responses to internalization and inactivation of Ctla4.
details
Inferred
LIG_TYR_ITAM FCG2A_HUMAN285307Avidity‑sensingPhosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).
details
Inferred
LIG_TYR_ITAM FCG2A_HUMAN285307Avidity‑sensingPhosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).
details
Inferred

Tyrosine-protein kinase Fyn - FYN -  Homo sapiens
LIG_TYR_ITIM FCG2B_HUMAN290295BinaryPhysicochemical compatibilityPhosphorylation of Y292 in the ITIM motif of Low affinity immunoglobulin gamma Fc region receptor II-b (FCGR2B) induces binding of Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 1 (INPP5D) via its SH2 domain.
details
Inferred
LIG_TYR_ITSM SLAF1_HUMAN277284BinaryPhysicochemical compatibilityPhosphorylation of Y281 in the ITSM motif of Signaling lymphocytic activation molecule (SLAMF1) induces binding of Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) via one of its SH2 domains.
details
Inferred
LIG_TYR_ITSM SLAF1_HUMAN277284BinaryPhysicochemical compatibilityPhosphorylation of Y281 in the ITSM motif of Signaling lymphocytic activation molecule (SLAMF1) induces binding of Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) via one of its SH2 domains.
details
Inferred
LIG_TYR_ITSM SLAF1_HUMAN323330BinaryPhysicochemical compatibilityPhosphorylation of Y327 in the ITSM motif of Signaling lymphocytic activation molecule (SLAMF1) induces binding of Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) via one of its SH2 domains.
details
Inferred
LIG_TYR_ITSM SLAF1_HUMAN323330BinaryPhysicochemical compatibilityPhosphorylation of Y327 in the ITSM motif of Signaling lymphocytic activation molecule (SLAMF1) induces binding of Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) via one of its SH2 domains.
details
Inferred
LIG_GBD_WASP_1 WASP_HUMAN466476UncategorisedUncategorisedPhosphorylation of Wiskott-Aldrich syndrome protein (WAS) at Y291 by Src kinases, e.g. , destabilises the auto-inhibitory intramolecular interaction of Wiskott-Aldrich syndrome protein (WAS).
details
Curated
LIG_SH2_GRB2 A4_HUMAN757760CumulativeRheostaticWhile phosphorylation of Y757 in the SH2-binding motif of Amyloid beta A4 protein (APP) induces binding to Growth factor receptor-bound protein 2 (GRB2), additional phosphorylation of T743 further increases the strength of the interaction.
details
Inferred
LIG_SH3_5 CD3E_HUMAN184188SpecificityAltered binding specificityPhosphorylation of T-cell surface glycoprotein CD3 epsilon chain (CD3E) by Lck (Tyrosine-protein kinase Lck (LCK)) during T cell activation switches the specificity of CD3E from SH3 domain containing proteins like Epidermal growth factor receptor kinase substrate 8-like protein 1 (EPS8L1) to SH2 domain containing proteins like Tyrosine-protein kinase ZAP-70 (ZAP70).
details
Inferred
LIG_SH3_5 CD3E_HUMAN184188SpecificityAltered binding specificityPhosphorylation of T-cell surface glycoprotein CD3 epsilon chain (CD3E) by Lck (Tyrosine-protein kinase Lck (LCK)) during T cell activation switches the specificity of CD3E from SH3 domain containing proteins like Epidermal growth factor receptor kinase substrate 8-like protein 1 (EPS8L1) to SH2 domain containing proteins like Tyrosine-protein kinase ZAP-70 (ZAP70).
details
Inferred
LIG_TYR_ITAM CD3E_HUMAN185202SpecificityAltered binding specificityPhosphorylation of T-cell surface glycoprotein CD3 epsilon chain (CD3E) by Lck (Tyrosine-protein kinase Lck (LCK)) during T cell activation switches the specificity of CD3E from SH3 domain containing proteins like Epidermal growth factor receptor kinase substrate 8-like protein 1 (EPS8L1) to SH2 domain containing proteins like Tyrosine-protein kinase ZAP-70 (ZAP70).
details
Inferred
LIG_TYR_ITAM CD3E_HUMAN185202SpecificityAltered binding specificityPhosphorylation of T-cell surface glycoprotein CD3 epsilon chain (CD3E) by Lck (Tyrosine-protein kinase Lck (LCK)) during T cell activation switches the specificity of CD3E from SH3 domain containing proteins like Epidermal growth factor receptor kinase substrate 8-like protein 1 (EPS8L1) to SH2 domain containing proteins like Tyrosine-protein kinase ZAP-70 (ZAP70).
details
Inferred
LIG_PTB_Apo_2 A4_HUMAN756763SpecificityAltered binding specificityPhosphorylation of Y757 in APP (Amyloid beta A4 protein (APP)) switches its specificity from PTB domain containing proteins, like Amyloid beta A4 precursor protein-binding family B member 1 (APBB1), which is involved in trafficking and processing of APP, to SH2 domain containing proteins, such as Growth factor receptor-bound protein 2 (GRB2).
details
Inferred
LIG_SH2_GRB2 A4_HUMAN757760SpecificityAltered binding specificityPhosphorylation of Y757 in APP (Amyloid beta A4 protein (APP)) switches its specificity from PTB domain containing proteins, like Amyloid beta A4 precursor protein-binding family B member 1 (APBB1), which is involved in trafficking and processing of APP, to SH2 domain containing proteins, such as Growth factor receptor-bound protein 2 (GRB2).
details
Inferred
LIG_TYR_ITAM CD3E_HUMAN185202Avidity‑sensingPhosphorylation of Y188 and Y199 in the ITAM motif of T-cell surface glycoprotein CD3 epsilon chain (CD3E) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).
details
Inferred
LIG_TYR_ITAM CD3E_HUMAN185202Avidity‑sensingPhosphorylation of Y188 and Y199 in the ITAM motif of T-cell surface glycoprotein CD3 epsilon chain (CD3E) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).
details
Inferred
LIG_TYR_ITAM CD3E_HUMAN185202Avidity‑sensingPhosphorylation of Y188 and Y199 in the ITAM motif of T-cell surface glycoprotein CD3 epsilon chain (CD3E) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).
details
Inferred
LIG_TYR_ITAM CD3E_HUMAN185202Avidity‑sensingPhosphorylation of Y188 and Y199 in the ITAM motif of T-cell surface glycoprotein CD3 epsilon chain (CD3E) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).
details
Inferred
LIG_TYR_ITAM CD3Z_HUMAN108126Avidity‑sensingPhosphorylation of Y111 and Y123 in the ITAM motif of T-cell surface glycoprotein CD3 zeta chain (CD247) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase ZAP-70 (ZAP70).
details
Inferred
LIG_TYR_ITAM CD3Z_HUMAN108126Avidity‑sensingPhosphorylation of Y111 and Y123 in the ITAM motif of T-cell surface glycoprotein CD3 zeta chain (CD247) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase ZAP-70 (ZAP70).
details
Inferred
LIG_TYR_ITAM CD3Z_HUMAN108126Avidity‑sensingPhosphorylation of Y111 and Y123 in the ITAM motif of T-cell surface glycoprotein CD3 zeta chain (CD247) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase ZAP-70 (ZAP70).
details
Inferred
LIG_TYR_ITAM CD3Z_HUMAN108126Avidity‑sensingPhosphorylation of Y111 and Y123 in the ITAM motif of T-cell surface glycoprotein CD3 zeta chain (CD247) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase ZAP-70 (ZAP70).
details
Inferred
LIG_TYR_ITAM FCG2A_HUMAN285307Avidity‑sensingPhosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).
details
Inferred
LIG_TYR_ITAM FCG2A_HUMAN285307Avidity‑sensingPhosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).
details
Inferred
LIG_TYR_ITAM FCG2A_HUMAN285307Avidity‑sensingPhosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).
details
Inferred
LIG_TYR_ITAM FCG2A_HUMAN285307Avidity‑sensingPhosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).
details
Inferred
LIG_TYR_ITAM FCG2A_HUMAN285307Avidity‑sensingPhosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).
details
Inferred
LIG_TYR_ITAM FCG2A_HUMAN285307Avidity‑sensingPhosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).
details
Inferred
LIG_SH2_IB CBL_HUMAN770780BinaryPhysicochemical compatibilityPhosphorylation of Y774 in the SH2-binding motif of E3 ubiquitin-protein ligase CBL (CBL) induces binding to the Adapter molecule crk (CRK) protein.
details
Inferred
LIG_SH2_IB CBL_HUMAN770780BinaryPhysicochemical compatibilityPhosphorylation of Y774 in the SH2-binding motif of E3 ubiquitin-protein ligase CBL (CBL) induces binding to the Adapter molecule crk (CRK) protein.
details
Inferred
LIG_SH2_IB SLAF1_HUMAN276286BinaryPhysicochemical compatibilityPhosphorylation of Y281 in the SH2-binding motif of Signaling lymphocytic activation molecule (SLAMF1) induces binding to the SH2 domain-containing protein 1A (SH2D1A) protein.
details
Inferred
LIG_SH2_IB SLAF1_HUMAN276286BinaryPhysicochemical compatibilityPhosphorylation of Y281 in the SH2-binding motif of Signaling lymphocytic activation molecule (SLAMF1) induces binding to the SH2 domain-containing protein 1A (SH2D1A) protein.
details
Inferred
LIG_SH2_IB SLAF1_HUMAN273286BinaryPhysicochemical compatibilityPhosphorylation of Y281 in the SH2-binding motif of Signaling lymphocytic activation molecule (SLAMF1) induces binding to the SH2 domain-containing protein 1B (Sh2d1b) protein.
details
Inferred
LIG_SH2_IB SLAF1_HUMAN273286BinaryPhysicochemical compatibilityPhosphorylation of Y281 in the SH2-binding motif of Signaling lymphocytic activation molecule (SLAMF1) induces binding to the SH2 domain-containing protein 1B (Sh2d1b) protein.
details
Inferred

Tyrosine-protein kinase HCK - HCK -  Homo sapiens
LIG_GBD_WASP_1 WASP_HUMAN466476UncategorisedUncategorisedPhosphorylation of Wiskott-Aldrich syndrome protein (WAS) at Y291 by Src kinases, e.g. , destabilises the auto-inhibitory intramolecular interaction of Wiskott-Aldrich syndrome protein (WAS).
details
Curated

Tyrosine-protein kinase HCK - HCK -  Mus musculus
LIG_GBD_WASP_1 WASP_HUMAN466476UncategorisedUncategorisedPhosphorylation of Wiskott-Aldrich syndrome protein (WAS) at Y291 by Src kinases, e.g. , destabilises the auto-inhibitory intramolecular interaction of Wiskott-Aldrich syndrome protein (WAS).
details
Inferred

Tyrosine-protein kinase JAK1 - JAK1 -  Homo sapiens
LIG_SH2_III INGR1_HUMAN457461BinaryPhysicochemical compatibilityPhosphorylation of Y457 in the SH2-binding motif of Interferon gamma receptor 1 (IFNGR1) induces binding to the Signal transducer and activator of transcription 1-alpha/beta (STAT1) protein.
details
Inferred

Tyrosine-protein kinase JAK2 - JAK2 -  Homo sapiens
TRG_ENDOCYTIC_2 CTLA4_MOUSE201204SpecificityAltered binding specificityDephosphorylation of Y201 of Cytotoxic T-lymphocyte protein 4 (Ctla4) switches the specificity of Ctla4 from SH2 domain-containing proteins like Tyrosine-protein phosphatase non-receptor type 11 (Ptpn11) to the AP-2 complex mu subunit (AP-2 complex subunit mu (Ap2m1)), thereby switching from inhibitory signal transmission and negative regulation of T cell responses to internalization and inactivation of Ctla4.
details
Inferred
TRG_ENDOCYTIC_2 CTLA4_MOUSE201204SpecificityAltered binding specificityDephosphorylation of Y201 of Cytotoxic T-lymphocyte protein 4 (Ctla4) switches the specificity of Ctla4 from SH2 domain-containing proteins like Tyrosine-protein phosphatase non-receptor type 11 (Ptpn11) to the AP-2 complex mu subunit (AP-2 complex subunit mu (Ap2m1)), thereby switching from inhibitory signal transmission and negative regulation of T cell responses to internalization and inactivation of Ctla4.
details
Inferred
LIG_SH2_STAT5 CTLA4_MOUSE201204SpecificityAltered binding specificityDephosphorylation of Y201 of Cytotoxic T-lymphocyte protein 4 (Ctla4) switches the specificity of Ctla4 from SH2 domain-containing proteins like Tyrosine-protein phosphatase non-receptor type 11 (Ptpn11) to the AP-2 complex mu subunit (AP-2 complex subunit mu (Ap2m1)), thereby switching from inhibitory signal transmission and negative regulation of T cell responses to internalization and inactivation of Ctla4.
details
Inferred
LIG_SH2_STAT5 CTLA4_MOUSE201204SpecificityAltered binding specificityDephosphorylation of Y201 of Cytotoxic T-lymphocyte protein 4 (Ctla4) switches the specificity of Ctla4 from SH2 domain-containing proteins like Tyrosine-protein phosphatase non-receptor type 11 (Ptpn11) to the AP-2 complex mu subunit (AP-2 complex subunit mu (Ap2m1)), thereby switching from inhibitory signal transmission and negative regulation of T cell responses to internalization and inactivation of Ctla4.
details
Inferred
LIG_SH2_III EPOR_HUMAN360376BinaryPhysicochemical compatibilityPhosphorylation of Y368 in the SH2-binding motif of Erythropoietin receptor (EPOR) induces binding to the Signal transducer and activator of transcription 5B (STAT5B) protein.
details
Inferred
LIG_SH2_III JAK2_MOUSE804820BinaryPhysicochemical compatibilityPhosphorylation of Y813 in the SH2-binding motif of Tyrosine-protein kinase JAK2 (Jak2) induces binding to the Signal transducer and activator of transcription 5B (Stat5b) protein.
details
Inferred
LIG_SH2_III STA5A_HUMAN686702BinaryPhysicochemical compatibilityPhosphorylation of Y694 in the SH2-binding motif of Signal transducer and activator of transcription 5A (STAT5A) induces binding to the Signal transducer and activator of transcription 5B (STAT5B) protein.
details
Inferred
LIG_SH2_III STA5A_HUMAN686702BinaryPhysicochemical compatibilityPhosphorylation of Y694 in the SH2-binding motif of Signal transducer and activator of transcription 5A (STAT5A) induces binding to the Signal transducer and activator of transcription 5B (STAT5B) protein.
details
Inferred

Tyrosine-protein kinase JAK2 - JAK2 -  Mus musculus
LIG_SH2_III JAK2_MOUSE804820BinaryPhysicochemical compatibilityPhosphorylation of Y813 in the SH2-binding motif of Tyrosine-protein kinase JAK2 (Jak2) induces binding to the Signal transducer and activator of transcription 5B (Stat5b) protein.
details
Inferred

Tyrosine-protein kinase JAK3 - JAK3 -  Homo sapiens
LIG_SH2_III STA5A_HUMAN686702BinaryPhysicochemical compatibilityPhosphorylation of Y694 in the SH2-binding motif of Signal transducer and activator of transcription 5A (STAT5A) induces binding to the Signal transducer and activator of transcription 5B (STAT5B) protein.
details
Inferred

Tyrosine-protein kinase Lck - LCK -  Homo sapiens
LIG_GBD_WASP_1 WASP_HUMAN466476UncategorisedUncategorisedPhosphorylation of Wiskott-Aldrich syndrome protein (WAS) at Y291 by Src kinases, e.g. , destabilises the auto-inhibitory intramolecular interaction of Wiskott-Aldrich syndrome protein (WAS).
details
Inferred
TRG_ENDOCYTIC_2 CTLA4_MOUSE201204SpecificityAltered binding specificityDephosphorylation of Y201 of Cytotoxic T-lymphocyte protein 4 (Ctla4) switches the specificity of Ctla4 from SH2 domain-containing proteins like Tyrosine-protein phosphatase non-receptor type 11 (Ptpn11) to the AP-2 complex mu subunit (AP-2 complex subunit mu (Ap2m1)), thereby switching from inhibitory signal transmission and negative regulation of T cell responses to internalization and inactivation of Ctla4.
details
Inferred
LIG_SH2_STAT5 CTLA4_MOUSE201204SpecificityAltered binding specificityDephosphorylation of Y201 of Cytotoxic T-lymphocyte protein 4 (Ctla4) switches the specificity of Ctla4 from SH2 domain-containing proteins like Tyrosine-protein phosphatase non-receptor type 11 (Ptpn11) to the AP-2 complex mu subunit (AP-2 complex subunit mu (Ap2m1)), thereby switching from inhibitory signal transmission and negative regulation of T cell responses to internalization and inactivation of Ctla4.
details
Inferred
LIG_TYR_ITAM CD3Z_HUMAN139156Avidity‑sensingPhosphorylation of Y142 and Y153 in the ITAM motif of T-cell surface glycoprotein CD3 zeta chain (CD247) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase ZAP-70 (ZAP70).
details
Inferred
LIG_TYR_ITAM CD3Z_HUMAN139156Avidity‑sensingPhosphorylation of Y142 and Y153 in the ITAM motif of T-cell surface glycoprotein CD3 zeta chain (CD247) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase ZAP-70 (ZAP70).
details
Inferred
LIG_SH2_IA IL2RB_HUMAN409428BinaryPhysicochemical compatibilityPhosphorylation of Y418 in the SH2-binding motif of Interleukin-2 receptor subunit beta (IL2RB) induces binding to the Tyrosine-protein kinase Lck (LCK) protein.
details
Inferred
LIG_SH2_IA IL2RB_HUMAN409428BinaryPhysicochemical compatibilityPhosphorylation of Y418 in the SH2-binding motif of Interleukin-2 receptor subunit beta (IL2RB) induces binding to the Tyrosine-protein kinase Lck (LCK) protein.
details
Inferred
LIG_SH2_III IL2RB_HUMAN531540BinaryPhysicochemical compatibilityPhosphorylation of Y536 in the SH2-binding motif of Interleukin-2 receptor subunit beta (IL2RB) induces binding to the Signal transducer and activator of transcription 5A (STAT5A) protein.
details
Inferred
LIG_SH2_III IL2RB_HUMAN531540BinaryPhysicochemical compatibilityPhosphorylation of Y536 in the SH2-binding motif of Interleukin-2 receptor subunit beta (IL2RB) induces binding to the Signal transducer and activator of transcription 5A (STAT5A) protein.
details
Inferred
LIG_SH2_III IL2RB_HUMAN528544BinaryPhysicochemical compatibilityPhosphorylation of Y536 in the SH2-binding motif of Interleukin-2 receptor subunit beta (IL2RB) induces binding to the Signal transducer and activator of transcription 5B (STAT5B) protein.
details
Inferred
LIG_SH2_III IL2RB_HUMAN528544BinaryPhysicochemical compatibilityPhosphorylation of Y536 in the SH2-binding motif of Interleukin-2 receptor subunit beta (IL2RB) induces binding to the Signal transducer and activator of transcription 5B (STAT5B) protein.
details
Inferred
LIG_SH2_IIB VAV_HUMAN165180BinaryPhysicochemical compatibilityPhosphorylation of Y174 in the SH2-binding motif of Proto-oncogene vav (VAV1) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.
details
Inferred
LIG_SH2_IB CBL_HUMAN770780BinaryPhysicochemical compatibilityPhosphorylation of Y774 in the SH2-binding motif of E3 ubiquitin-protein ligase CBL (CBL) induces binding to the Adapter molecule crk (CRK) protein.
details
Inferred
LIG_SH2_IIB LCP2_HUMAN105118BinaryPhysicochemical compatibilityPhosphorylation of Y113 in the SH2-binding motif of Lymphocyte cytosolic protein 2 (LCP2) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.
details
Inferred
LIG_SH2_IIB LCP2_HUMAN105118BinaryPhysicochemical compatibilityPhosphorylation of Y113 in the SH2-binding motif of Lymphocyte cytosolic protein 2 (LCP2) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.
details
Inferred
LIG_SH2_IIB LCP2_HUMAN120133BinaryPhysicochemical compatibilityPhosphorylation of Y128 in the SH2-binding motif of Lymphocyte cytosolic protein 2 (LCP2) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.
details
Inferred
LIG_SH2_IIB LCP2_HUMAN120133BinaryPhysicochemical compatibilityPhosphorylation of Y128 in the SH2-binding motif of Lymphocyte cytosolic protein 2 (LCP2) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.
details
Inferred
LIG_SH2_IIB LCP2_HUMAN137150BinaryPhysicochemical compatibilityPhosphorylation of Y145 in the SH2-binding motif of Lymphocyte cytosolic protein 2 (LCP2) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.
details
Inferred
LIG_SH2_III STA5A_HUMAN686702BinaryPhysicochemical compatibilityPhosphorylation of Y694 in the SH2-binding motif of Signal transducer and activator of transcription 5A (STAT5A) induces binding to the Signal transducer and activator of transcription 5B (STAT5B) protein.
details
Inferred
LIG_SH2_IIC ZAP70_HUMAN284300BinaryPhysicochemical compatibilityPhosphorylation of Y292 in the SH2-binding motif of Tyrosine-protein kinase ZAP-70 (ZAP70) induces binding to the E3 ubiquitin-protein ligase CBL-B (CBLB) protein.
details
Inferred
LIG_SH2_IIC ZAP70_HUMAN284300BinaryPhysicochemical compatibilityPhosphorylation of Y292 in the SH2-binding motif of Tyrosine-protein kinase ZAP-70 (ZAP70) induces binding to the E3 ubiquitin-protein ligase CBL-B (CBLB) protein.
details
Inferred
LIG_SH2_IIC ZAP70_HUMAN284300BinaryPhysicochemical compatibilityPhosphorylation of Y292 in the SH2-binding motif of Tyrosine-protein kinase ZAP-70 (ZAP70) induces binding to the E3 ubiquitin-protein ligase CBL-B (CBLB) protein.
details
Inferred

Tyrosine-protein kinase Lyn - LYN -  Homo sapiens
LIG_TYR_ITIM FCG2B_HUMAN290295BinaryPhysicochemical compatibilityPhosphorylation of Y292 in the ITIM motif of Low affinity immunoglobulin gamma Fc region receptor II-b (FCGR2B) induces binding of Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 1 (INPP5D) via its SH2 domain.
details
Inferred
LIG_TYR_ITIM FCG2B_HUMAN290295BinaryPhysicochemical compatibilityPhosphorylation of Y292 in the ITIM motif of Low affinity immunoglobulin gamma Fc region receptor II-b (FCGR2B) induces binding of Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 1 (INPP5D) via its SH2 domain.
details
Inferred
LIG_TYR_ITSM SLAF1_HUMAN323330BinaryPhysicochemical compatibilityPhosphorylation of Y327 in the ITSM motif of Signaling lymphocytic activation molecule (SLAMF1) induces binding of Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) via one of its SH2 domains.
details
Inferred
LIG_TYR_ITSM SLAF1_HUMAN323330BinaryPhysicochemical compatibilityPhosphorylation of Y327 in the ITSM motif of Signaling lymphocytic activation molecule (SLAMF1) induces binding of Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) via one of its SH2 domains.
details
Inferred
LIG_GBD_WASP_1 WASP_HUMAN466476UncategorisedUncategorisedPhosphorylation of Wiskott-Aldrich syndrome protein (WAS) at Y291 by Src kinases, e.g. , destabilises the auto-inhibitory intramolecular interaction of Wiskott-Aldrich syndrome protein (WAS).
details
Inferred
LIG_TYR_ITAM FCG2A_HUMAN285307Avidity‑sensingPhosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).
details
Inferred
LIG_TYR_ITAM FCG2A_HUMAN285307Avidity‑sensingPhosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).
details
Inferred
LIG_TYR_ITAM FCG2A_HUMAN285307Avidity‑sensingPhosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).
details
Inferred
LIG_TYR_ITAM FCG2A_HUMAN285307Avidity‑sensingPhosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).
details
Inferred
LIG_TYR_ITAM FCG2A_HUMAN285307Avidity‑sensingPhosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).
details
Inferred
LIG_TYR_ITAM FCG2A_HUMAN285307Avidity‑sensingPhosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).
details
Inferred
LIG_SH2_III EPOR_HUMAN360376BinaryPhysicochemical compatibilityPhosphorylation of Y368 in the SH2-binding motif of Erythropoietin receptor (EPOR) induces binding to the Signal transducer and activator of transcription 5B (STAT5B) protein.
details
Inferred
LIG_SH2_III STA5A_HUMAN686702BinaryPhysicochemical compatibilityPhosphorylation of Y694 in the SH2-binding motif of Signal transducer and activator of transcription 5A (STAT5A) induces binding to the Signal transducer and activator of transcription 5B (STAT5B) protein.
details
Inferred

Tyrosine-protein kinase Lyn - LYN -  Mus musculus
LIG_TYR_ITAM FCG2A_HUMAN285307Avidity‑sensingPhosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).
details
Inferred
LIG_TYR_ITAM FCG2A_HUMAN285307Avidity‑sensingPhosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).
details
Inferred
LIG_SH2_III STA5A_HUMAN686702BinaryPhysicochemical compatibilityPhosphorylation of Y694 in the SH2-binding motif of Signal transducer and activator of transcription 5A (STAT5A) induces binding to the Signal transducer and activator of transcription 5B (STAT5B) protein.
details
Inferred

Tyrosine-protein kinase SYK - SYK -  Homo sapiens
LIG_PTB_Phospho_1 ITB3_HUMAN779785BinaryPhysicochemical compatibilityPhosphorylation of Y785 in the PTB-binding motif of Integrin beta-3 (ITGB3) induces binding to the SHC-transforming protein 1 (SHC1) protein.
details
Inferred
LIG_PTB_Phospho_1 ITB3_HUMAN779785CumulativeRheostaticWhile phosphorylation of Y785 in the PTB-binding motif of Integrin beta-3 (ITGB3) induces binding to SHC-transforming protein 1 (SHC1), additional phosphorylation of Y773 further increases the strength of the interaction.
details
Inferred
LIG_PTB_Apo_2 ITB3_HUMAN779786SpecificityAltered binding specificityPhosphorylation of Integrin beta-3 (ITGB3) at Y785 switches the specificity of integrin from Kindlin-2 (Fermitin family homolog 2 (FERMT2)) to the adaptor protein SHC-transforming protein 1 (SHC1).
details
Inferred
LIG_PTB_Phospho_1 ITB3_HUMAN779785SpecificityAltered binding specificityPhosphorylation of Integrin beta-3 (ITGB3) at Y785 switches the specificity of integrin from Kindlin-2 (Fermitin family homolog 2 (FERMT2)) to the adaptor protein SHC-transforming protein 1 (SHC1).
details
Inferred
LIG_TYR_ITAM FCG2A_HUMAN285307Avidity‑sensingPhosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).
details
Inferred
LIG_TYR_ITAM FCG2A_HUMAN285307Avidity‑sensingPhosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).
details
Inferred
LIG_TYR_ITAM FCG2A_HUMAN285307Avidity‑sensingPhosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).
details
Inferred
LIG_TYR_ITAM FCG2A_HUMAN285307Avidity‑sensingPhosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).
details
Inferred
LIG_TYR_ITAM FCG2A_HUMAN285307Avidity‑sensingPhosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).
details
Inferred
LIG_TYR_ITAM FCG2A_HUMAN285307Avidity‑sensingPhosphorylation of Y288 and Y304 in the ITAM motif of Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).
details
Inferred
LIG_SH2_IB CBL_HUMAN770780BinaryPhysicochemical compatibilityPhosphorylation of Y774 in the SH2-binding motif of E3 ubiquitin-protein ligase CBL (CBL) induces binding to the Adapter molecule crk (CRK) protein.
details
Inferred
LIG_SH2_IB CBL_HUMAN770780BinaryPhysicochemical compatibilityPhosphorylation of Y774 in the SH2-binding motif of E3 ubiquitin-protein ligase CBL (CBL) induces binding to the Adapter molecule crk (CRK) protein.
details
Inferred
LIG_SH2_IC SHC1_HUMAN423435BinaryPhysicochemical compatibilityPhosphorylation of Y427 in the SH2-binding motif of SHC-transforming protein 1 (SHC1) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.
details
Inferred
LIG_SH2_IIB M4K1_HUMAN372391BinaryPhysicochemical compatibilityPhosphorylation of Y381 in the SH2-binding motif of Mitogen-activated protein kinase kinase kinase kinase 1 (MAP4K1) induces binding to the B-cell linker protein (BLNK) protein.
details
Inferred
LIG_SH2_IIB LCP2_HUMAN105118BinaryPhysicochemical compatibilityPhosphorylation of Y113 in the SH2-binding motif of Lymphocyte cytosolic protein 2 (LCP2) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.
details
Inferred
LIG_SH2_IIB LCP2_HUMAN105118BinaryPhysicochemical compatibilityPhosphorylation of Y113 in the SH2-binding motif of Lymphocyte cytosolic protein 2 (LCP2) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.
details
Inferred
LIG_SH2_IIB LCP2_HUMAN120133BinaryPhysicochemical compatibilityPhosphorylation of Y128 in the SH2-binding motif of Lymphocyte cytosolic protein 2 (LCP2) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.
details
Inferred
LIG_SH2_IIB LCP2_HUMAN120133BinaryPhysicochemical compatibilityPhosphorylation of Y128 in the SH2-binding motif of Lymphocyte cytosolic protein 2 (LCP2) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.
details
Inferred
LIG_SH2_IB FAK2_HUMAN394410BinaryPhysicochemical compatibilityPhosphorylation of Y402 in the SH2-binding motif of Protein-tyrosine kinase 2-beta (PTK2B) induces binding to the Megakaryocyte-associated tyrosine-protein kinase (MATK) protein.
details
Inferred
LIG_SH2_III STA5A_HUMAN686702BinaryPhysicochemical compatibilityPhosphorylation of Y694 in the SH2-binding motif of Signal transducer and activator of transcription 5A (STAT5A) induces binding to the Signal transducer and activator of transcription 5B (STAT5B) protein.
details
Inferred

Tyrosine-protein kinase TXK - TXK -  Homo sapiens
LIG_SH2_IIB LCP2_HUMAN137150BinaryPhysicochemical compatibilityPhosphorylation of Y145 in the SH2-binding motif of Lymphocyte cytosolic protein 2 (LCP2) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.
details
Inferred

Tyrosine-protein kinase Yes - YES1 -  Homo sapiens
LIG_SH2_IB CBL_HUMAN770780BinaryPhysicochemical compatibilityPhosphorylation of Y774 in the SH2-binding motif of E3 ubiquitin-protein ligase CBL (CBL) induces binding to the Adapter molecule crk (CRK) protein.
details
Inferred

Tyrosine-protein kinase ZAP-70 - ZAP70 -  Mus musculus
LIG_SH2_GRB2 LAT_MOUSE175178BinaryPhysicochemical compatibilityPhosphorylation of Y175 in the SH2-binding motif of Linker for activation of T-cells family member 1 (Lat) induces binding to the Growth factor receptor-bound protein 2 (Grb2) protein.
details
Inferred
LIG_SH2_GRB2 LAT_MOUSE195198BinaryPhysicochemical compatibilityPhosphorylation of Y195 in the SH2-binding motif of Linker for activation of T-cells family member 1 (Lat) induces binding to the Growth factor receptor-bound protein 2 (Grb2) protein.
details
Inferred
LIG_SH2_GRB2 LAT_MOUSE235238BinaryPhysicochemical compatibilityPhosphorylation of Y235 in the SH2-binding motif of Linker for activation of T-cells family member 1 (Lat) induces binding to the Growth factor receptor-bound protein 2 (Grb2) protein.
details
Inferred

Tyrosine-protein kinase ZAP-70 - ZAP70 -  Homo sapiens
LIG_SH2_GRB2 LAT_MOUSE175178BinaryPhysicochemical compatibilityPhosphorylation of Y175 in the SH2-binding motif of Linker for activation of T-cells family member 1 (Lat) induces binding to the Growth factor receptor-bound protein 2 (Grb2) protein.
details
Inferred
LIG_SH2_GRB2 LAT_MOUSE195198BinaryPhysicochemical compatibilityPhosphorylation of Y195 in the SH2-binding motif of Linker for activation of T-cells family member 1 (Lat) induces binding to the Growth factor receptor-bound protein 2 (Grb2) protein.
details
Inferred
LIG_SH2_GRB2 LAT_MOUSE235238BinaryPhysicochemical compatibilityPhosphorylation of Y235 in the SH2-binding motif of Linker for activation of T-cells family member 1 (Lat) induces binding to the Growth factor receptor-bound protein 2 (Grb2) protein.
details
Inferred
LIG_SH2_IC SHC1_HUMAN423435BinaryPhysicochemical compatibilityPhosphorylation of Y427 in the SH2-binding motif of SHC-transforming protein 1 (SHC1) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.
details
Inferred
LIG_SH2_IIB LCP2_HUMAN105118BinaryPhysicochemical compatibilityPhosphorylation of Y113 in the SH2-binding motif of Lymphocyte cytosolic protein 2 (LCP2) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.
details
Inferred
LIG_SH2_IIB LCP2_HUMAN105118BinaryPhysicochemical compatibilityPhosphorylation of Y113 in the SH2-binding motif of Lymphocyte cytosolic protein 2 (LCP2) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.
details
Inferred
LIG_SH2_IIB LCP2_HUMAN105118BinaryPhysicochemical compatibilityPhosphorylation of Y113 in the SH2-binding motif of Lymphocyte cytosolic protein 2 (LCP2) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.
details
Inferred
LIG_SH2_IIB LCP2_HUMAN105118BinaryPhysicochemical compatibilityPhosphorylation of Y113 in the SH2-binding motif of Lymphocyte cytosolic protein 2 (LCP2) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.
details
Inferred
LIG_SH2_IIB LCP2_HUMAN120133BinaryPhysicochemical compatibilityPhosphorylation of Y128 in the SH2-binding motif of Lymphocyte cytosolic protein 2 (LCP2) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.
details
Inferred
LIG_SH2_IIB LCP2_HUMAN120133BinaryPhysicochemical compatibilityPhosphorylation of Y128 in the SH2-binding motif of Lymphocyte cytosolic protein 2 (LCP2) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.
details
Inferred
LIG_SH2_IIB LCP2_HUMAN120133BinaryPhysicochemical compatibilityPhosphorylation of Y128 in the SH2-binding motif of Lymphocyte cytosolic protein 2 (LCP2) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.
details
Inferred
LIG_SH2_IIB LCP2_HUMAN120133BinaryPhysicochemical compatibilityPhosphorylation of Y128 in the SH2-binding motif of Lymphocyte cytosolic protein 2 (LCP2) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.
details
Inferred
LIG_SH2_IIB LCP2_HUMAN137150BinaryPhysicochemical compatibilityPhosphorylation of Y145 in the SH2-binding motif of Lymphocyte cytosolic protein 2 (LCP2) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.
details
Inferred
LIG_SH2_IIB LCP2_HUMAN137150BinaryPhysicochemical compatibilityPhosphorylation of Y145 in the SH2-binding motif of Lymphocyte cytosolic protein 2 (LCP2) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.
details
Inferred
LIG_SH2_IIC ZAP70_HUMAN284300BinaryPhysicochemical compatibilityPhosphorylation of Y292 in the SH2-binding motif of Tyrosine-protein kinase ZAP-70 (ZAP70) induces binding to the E3 ubiquitin-protein ligase CBL-B (CBLB) protein.
details
Inferred
LIG_SH2_IIC ZAP70_HUMAN284300BinaryPhysicochemical compatibilityPhosphorylation of Y292 in the SH2-binding motif of Tyrosine-protein kinase ZAP-70 (ZAP70) induces binding to the E3 ubiquitin-protein ligase CBL-B (CBLB) protein.
details
Inferred
LIG_SH2_IIC ZAP70_HUMAN284300BinaryPhysicochemical compatibilityPhosphorylation of Y292 in the SH2-binding motif of Tyrosine-protein kinase ZAP-70 (ZAP70) induces binding to the E3 ubiquitin-protein ligase CBL-B (CBLB) protein.
details
Inferred

Vascular endothelial growth factor receptor 3 - FLT4 -  Homo sapiens
LIG_SH2_IC SHC1_HUMAN423435BinaryPhysicochemical compatibilityPhosphorylation of Y427 in the SH2-binding motif of SHC-transforming protein 1 (SHC1) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.
details
Inferred

cAMP-dependent protein kinase catalytic subunit alpha - PRKACA -  Rattus norvegicus
LIG_14-3-3_1 BAD_RAT134139BinaryPhysicochemical compatibilityPhosphorylation of S137 by RAC-alpha serine/threonine-protein kinase (Akt1) in the 14-3-3-binding motif of Bcl2 antagonist of cell death (Bad) induces binding to the 14-3-3 protein beta/alpha (YWHAB) protein. This interaction inhibits the pro-apoptotic activity of Bcl2 antagonist of cell death (Bad).
details
Inferred
DOC_PP1 NEB1_RAT455461BinaryPhysicochemical compatibilityPhosphorylation of S461 in the PP1-binding motif of Neurabin-1 (Ppp1r9a) by cAMP subfamily inhibits binding to the Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (Ppp1ca). Binding of Neurabin-1 (Ppp1r9a) inhibits activity of the phosphatase.
details
Inferred

cAMP-dependent protein kinase catalytic subunit alpha - PRKACA -  Bos taurus
LIG_14-3-3_1 BAD_MOUSE133138BinaryPhysicochemical compatibilityPhosphorylation of S136 in Bcl2 antagonist of cell death (Bad) by RAC-alpha serine/threonine-protein kinase (Akt1) in response to survival and growth signals such as Interleukin-3 (Il3) induces binding to 14-3-3 protein theta (Ywhaq). Binding of 14-3-3 protein theta (Ywhaq) results in dissociation of Bcl2 antagonist of cell death (Bad) from Bcl-2-like protein 1 (Bcl2l1), and thereby inhibits the pro-apoptotic activity of Bcl2 antagonist of cell death (Bad) by allowing liberated Bcl-2-like protein 1 (Bcl2l1) to exert its anti-apoptotic effect on pro-apoptotic proteins like Apoptosis regulator BAX (Bax).
details
Inferred

cAMP-dependent protein kinase catalytic subunit alpha - PRKACA -  Homo sapiens
MOD_GSK3_1 NFAC1_HUMAN287294BinaryPhysicochemical compatibilityPhosphorylation of S294 adjacent to the NLS of Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1) by cAMP subfamily primes Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1) for subsequent phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which results in inhibition of nuclear import of Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1).
details
Inferred
MOD_GSK3_1 NFAC1_HUMAN238245BinaryPhysicochemical compatibilityPhosphorylation of S245 adjacent to the NLS of Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1) by cAMP subfamily primes Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1) for subsequent phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which results in inhibition of nuclear import of Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1).
details
Inferred
LIG_14-3-3_1 ATX1_HUMAN772777BinaryPhysicochemical compatibilityPhosphorylation of S775 by RAC-alpha serine/threonine-protein kinase (AKT1) in the 14-3-3-binding motif of Ataxin-1 (ATXN1) induces binding to the 14-3-3 protein zeta/delta (YWHAZ) protein.
details
Inferred
LIG_RhoGAP_OCRL_1 DP13A_HUMAN403415BinaryPhysicochemical compatibilityPhosphorylation of S410 in the RhoGAP-binding motif of DCC-interacting protein 13-alpha (APPL1) inhibits its interaction with Inositol polyphosphate 5-phosphatase OCRL-1 (OCRL).
details
Inferred
LIG_ULM_U2AF65_1 ATX1_HUMAN770775SpecificityAltered binding specificityPhosphorylation of S775 switches binding specificity of Ataxin-1 (ATXN1) from the splicing factor Splicing factor U2AF 65 kDa subunit (U2AF2) to 14-3-3 proteins (e.g. 14-3-3 protein zeta/delta (YWHAZ)). While association with the spliceosome protects ATXN1 from self-association, its phosphorylation-dependent recruitment to 14-3-3 proteins (e.g. YWHAZ) might result in aggregation.
details
Inferred
LIG_14-3-3_1 ATX1_HUMAN772777SpecificityAltered binding specificityPhosphorylation of S775 switches binding specificity of Ataxin-1 (ATXN1) from the splicing factor Splicing factor U2AF 65 kDa subunit (U2AF2) to 14-3-3 proteins (e.g. 14-3-3 protein zeta/delta (YWHAZ)). While association with the spliceosome protects ATXN1 from self-association, its phosphorylation-dependent recruitment to 14-3-3 proteins (e.g. YWHAZ) might result in aggregation.
details
Inferred
LIG_14-3-3_1 RAF1_HUMAN256261Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in RAF proto-oncogene serine/threonine-protein kinase (RAF1) in response to growth factors induces high-avidity binding to dimeric 14-3-3 protein zeta/delta (YWHAZ), with pS621 being the high-affinity interaction site. This interaction locks RAF proto-oncogene serine/threonine-protein kinase (RAF1) in an inhibited conformation.
details
Inferred
LIG_14-3-3_1 RAF1_HUMAN618623Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in RAF proto-oncogene serine/threonine-protein kinase (RAF1) in response to growth factors induces high-avidity binding to dimeric 14-3-3 protein zeta/delta (YWHAZ), with pS621 being the high-affinity interaction site. This interaction locks RAF proto-oncogene serine/threonine-protein kinase (RAF1) in an inhibited conformation.
details
Inferred
LIG_PCNA_PIPBox_1 DPOD3_HUMAN456465BinaryPhysicochemical compatibilityPhosphorylation of S458 in the PCNA-binding motif of DNA polymerase delta subunit 3 (POLD3) by cAMP subfamily reduces the affinity of binding to the Proliferating cell nuclear antigen (PCNA) and decreases the processivity of the polymerase complex.
details
Inferred
LIG_14-3-3_1 BAD_MOUSE133138BinaryPhysicochemical compatibilityPhosphorylation of S136 in Bcl2 antagonist of cell death (Bad) by RAC-alpha serine/threonine-protein kinase (Akt1) in response to survival and growth signals such as Interleukin-3 (Il3) induces binding to 14-3-3 protein theta (Ywhaq). Binding of 14-3-3 protein theta (Ywhaq) results in dissociation of Bcl2 antagonist of cell death (Bad) from Bcl-2-like protein 1 (Bcl2l1), and thereby inhibits the pro-apoptotic activity of Bcl2 antagonist of cell death (Bad) by allowing liberated Bcl-2-like protein 1 (Bcl2l1) to exert its anti-apoptotic effect on pro-apoptotic proteins like Apoptosis regulator BAX (Bax).
details
Inferred

cAMP-dependent protein kinase catalytic subunit alpha - PRKACA -  Mus musculus
MOD_GSK3_1 NFAC1_HUMAN238245BinaryPhysicochemical compatibilityPhosphorylation of S245 adjacent to the NLS of Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1) by cAMP subfamily primes Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1) for subsequent phosphorylation by Glycogen synthase kinase-3 beta (GSK3B), which results in inhibition of nuclear import of Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1).
details
Inferred
LIG_PDZ_Class_1 CCG2_MOUSE318323BinaryPhysicochemical compatibilityPhosphorylation of T321 in the PDZ-binding motif of Voltage-dependent calcium channel gamma-2 subunit (Cacng2) by cAMP subfamily prevents binding to the PDZ domain of Disks large homolog 4 (Dlg4), an interaction involved in regulating synaptic targeting of AMPA-selective glutamate receptors.
details
Inferred
LIG_14-3-3_1 RAF1_HUMAN256261Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in RAF proto-oncogene serine/threonine-protein kinase (RAF1) in response to growth factors induces high-avidity binding to dimeric 14-3-3 protein zeta/delta (YWHAZ), with pS621 being the high-affinity interaction site. This interaction locks RAF proto-oncogene serine/threonine-protein kinase (RAF1) in an inhibited conformation.
details
Inferred
LIG_14-3-3_1 RAF1_HUMAN618623Avidity‑sensingPhosphorylation of two 14-3-3-binding motifs in RAF proto-oncogene serine/threonine-protein kinase (RAF1) in response to growth factors induces high-avidity binding to dimeric 14-3-3 protein zeta/delta (YWHAZ), with pS621 being the high-affinity interaction site. This interaction locks RAF proto-oncogene serine/threonine-protein kinase (RAF1) in an inhibited conformation.
details
Inferred
LIG_14-3-3_1 BAD_MOUSE133138BinaryPhysicochemical compatibilityPhosphorylation of S136 in Bcl2 antagonist of cell death (Bad) by RAC-alpha serine/threonine-protein kinase (Akt1) in response to survival and growth signals such as Interleukin-3 (Il3) induces binding to 14-3-3 protein theta (Ywhaq). Binding of 14-3-3 protein theta (Ywhaq) results in dissociation of Bcl2 antagonist of cell death (Bad) from Bcl-2-like protein 1 (Bcl2l1), and thereby inhibits the pro-apoptotic activity of Bcl2 antagonist of cell death (Bad) by allowing liberated Bcl-2-like protein 1 (Bcl2l1) to exert its anti-apoptotic effect on pro-apoptotic proteins like Apoptosis regulator BAX (Bax).
details
Inferred

cGMP-dependent protein kinase 1 - PRKG1 -  Homo sapiens
LIG_SH3_2 PAK1_HUMAN1318BinaryPhysicochemical compatibilityPhosphorylation of S21 adjacent to the SH3-binding motif of Serine/threonine-protein kinase PAK 1 (PAK1) by RAC subfamily inhibits binding to Cytoplasmic protein NCK1 (NCK1), which regulates its localization to focal contacts.
details
Inferred
           
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