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Group by :Switch typeMotif classProteinEnzymePathway            Group Index    Colouring Info              Filtered: PFAM:PF00397 (110 hits) x


x  Coloured by switch type.
  Domain hiding  Altered binding specificity  Motif hiding  Composite binding site formation
  Uncategorised  Rheostatic  Allostery  Avidity-sensing
  Physicochemical compatibility  Pre-translational  Competition

x  Index
Alpha-globin transcription factor CP2Alpha-globin transcription factor CP2 (Mus)Amiloride-sensitive sodium channel subunit gamma
AngiomotinBcl-2-like protein 11 (Mus)Beta-adrenergic receptor kinase 1 (Mus)
CREB-regulated transcription coactivator 2 (Mus)Catenin beta-1Cellular tumor antigen p53
Centrosomal protein of 55 kDa (Mus)Cyclin-dependent kinase inhibitor 1BDeath domain-associated protein 6
DystroglycanF-box only protein 5-A (Xenopus)F-box/WD repeat-containing protein 7
Far upstream element-binding protein 2Focal adhesion kinase 1Focal adhesion kinase 1 (Mus)
G1/S-specific cyclin-D1 (Mus)G1/S-specific cyclin-E1 (Mus)Gephyrin (Mus)
Homeobox protein NANOG (Mus)Insulin receptor substrate 1Interferon regulatory factor 3
Latent membrane protein 2 (Epstein-Barr)Mothers against decapentaplegic homolog 3Myc proto-oncogene protein
Myocyte-specific enhancer factor 2C (Mus)Neurogenic locus notch homolog protein 1Neutrophil cytosol factor 1
Non-POU domain-containing octamer-binding protein (Mus)Nuclear receptor corepressor 2Nuclear receptor subfamily 4 group A member 1
POU domain, class 5, transcription factor 1Protein AATFProtein BTG2
Protein PMLProtein SPT23 (Saccharomyces)Protein Tax-1 (Human)
Protein X (Hepatitis)Proto-oncogene c-Fos (Mus)RAC-alpha serine/threonine-protein kinase
Receptor tyrosine-protein kinase erbB-4Retinoic acid receptor alphaSerine/threonine-protein kinase Nek6
Signal transducer and activator of transcription 3Steroidogenic factor 1 (Mus)Sulfotransferase 4A1
Synphilin-1Telomeric repeat-binding factor 1Transcription factor AP-1
Transcription factor AP-1 (Mus)Transcription factor p65Transcriptional activator Myb (Mus)
Tumor protein p73Tyrosine-protein kinase BTK (Mus)Wee1-like protein kinase 1-B (Xenopus)


MotifStartEndSwitch TypeSwitch SubtypeSwitch DescriptionInformation

Alpha-globin transcription factor CP2 - TFCP2 -  Homo sapiens
DOC_WW_Pin1_4326331BinaryPhysicochemical compatibilityPhosphorylation of T329 in the Pin1-binding motif of Alpha-globin transcription factor CP2 (TFCP2) induces binding to Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), which isomerises the peptide bonds at the nearby-phosphorylated SP motifs (S291 and S309) to the trans configuration, thereby facilitating their dephosphorylation, which is required for the transcriptional activity of Alpha-globin transcription factor CP2 (TFCP2).
details

Alpha-globin transcription factor CP2 - Tcfcp2 -  Mus musculus
DOC_WW_Pin1_4288293BinaryPhysicochemical compatibilityPhosphorylation of S291 in the Pin1-binding motif of Alpha-globin transcription factor CP2 (Tcfcp2) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details
DOC_WW_Pin1_4306311BinaryPhysicochemical compatibilityPhosphorylation of S309 in the Pin1-binding motif of Alpha-globin transcription factor CP2 (Tcfcp2) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details
DOC_WW_Pin1_4326331BinaryPhysicochemical compatibilityPhosphorylation of T329 in the Pin1-binding motif of Alpha-globin transcription factor CP2 (Tcfcp2) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details

Amiloride-sensitive sodium channel subunit gamma - SCNN1G -  Homo sapiens
LIG_WW_1624627SpecificityDomain 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

Angiomotin - AMOT -  Homo sapiens
LIG_WW_1239242BinaryPre‑translationalAlternative splicing removes the WW-binding motif of Angiomotin (AMOT), abrogating binding to Yorkie homolog (YAP1). The splice specific Isoform p130 of Angiomotin (AMOT) of AMOT works within the Hippo pathway to sequester the transcription coactivator YAP1 away at tight junction. In contrast Isoform p80 of Angiomotin (AMOT) of AMOT lacks WW-binding motif.
details
LIG_WW_1239242BinaryPre‑translationalAlternative splicing removes the WW-binding motif of Angiomotin (AMOT), abrogating binding to WW domain-containing transcription regulator protein 1 (WWTR1). The splice specific Isoform p130 of Angiomotin (AMOT) of AMOT works within the Hippo pathway to sequester the transcription coactivator YAP1 away at tight junction. In contrast Isoform p80 of Angiomotin (AMOT) of AMOT lacks WW-binding motif.
details
LIG_WW_1239242BinaryPre‑translationalAlternative splicing removes the WW-binding motif of Angiomotin (AMOT), abrogating binding to Yorkie homolog (YAP1). The splice specific Isoform p130 of Angiomotin (AMOT) of AMOT works within the Hippo pathway to sequester the transcription coactivator YAP1 away at tight junction. In contrast Isoform p80 of Angiomotin (AMOT) of AMOT lacks WW-binding motif.
details

Bcl-2-like protein 11 - Bcl2l11 -  Mus musculus
DOC_WW_Pin1_46267BinaryPhysicochemical 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

Beta-adrenergic receptor kinase 1 - Adrbk1 -  Mus musculus
DOC_WW_Pin1_4667672BinaryPhysicochemical compatibilityPhosphorylation of S670 in the Pin1-binding motif of Beta-adrenergic receptor kinase 1 (Adrbk1) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details

CREB-regulated transcription coactivator 2 - Crtc2 -  Mus musculus
DOC_WW_Pin1_4133138BinaryPhysicochemical compatibilityPhosphorylation of S136 in the Pin1-binding motif of CREB-regulated transcription coactivator 2 (Crtc2) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details

Catenin beta-1 - CTNNB1 -  Homo sapiens
DOC_WW_Pin1_4243248BinaryPhysicochemical 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

Cellular tumor antigen p53 - TP53 -  Homo sapiens
DOC_WW_Pin1_43035BinaryPhysicochemical compatibilityPhosphorylation of S33 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
DOC_WW_Pin1_4312317BinaryPhysicochemical 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
DOC_WW_Pin1_47883BinaryPhysicochemical 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

Centrosomal protein of 55 kDa - Cep55 -  Mus musculus
DOC_WW_Pin1_4420425BinaryPhysicochemical compatibilityPhosphorylation of S423 in the Pin1-binding motif of Centrosomal protein of 55 kDa (Cep55) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details
DOC_WW_Pin1_4423428BinaryPhysicochemical compatibilityPhosphorylation of S426 in the Pin1-binding motif of Centrosomal protein of 55 kDa (Cep55) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details

Cyclin-dependent kinase inhibitor 1B - CDKN1B -  Homo sapiens
DOC_WW_Pin1_4184189BinaryPhysicochemical 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

Death domain-associated protein 6 - DAXX -  Homo sapiens
DOC_WW_Pin1_4175180BinaryPhysicochemical compatibilityPhosphorylation of S178 in the Pin1-binding motif of Death domain-associated protein 6 (DAXX) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details

Dystroglycan - DAG1 -  Homo sapiens
LIG_WW_1889892SpecificityAltered 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
LIG_WW_1889892SpecificityAltered 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
LIG_WW_1889892SpecificityCompetitionThe WW-binding motif for Dystrophin (DMD) and the SH3-binding motif for Growth factor receptor-bound protein 2 (GRB2) on Dystroglycan (DAG1) overlap, making their interactions mutually exclusive and competitive.
details
LIG_WW_1889892SpecificityCompetitionThe WW-binding motif for Dystrophin (DMD) and the SH3-binding motif for Growth factor receptor-bound protein 2 (GRB2) on Dystroglycan (DAG1) overlap, making their interactions mutually exclusive and competitive.
details

F-box only protein 5-A - fbxo5-a -  Xenopus laevis
DOC_WW_Pin1_4712BinaryPhysicochemical compatibilityPhosphorylation of S10 in the Pin1-binding motif of F-box only protein 5-A (fbxo5-a) induces binding to the pin1 protein.
details

F-box/WD repeat-containing protein 7 - FBXW7 -  Homo sapiens
DOC_WW_Pin1_4202207BinaryPhysicochemical compatibilityPhosphorylation of T205 in the Pin1-binding motif of F-box/WD repeat-containing protein 7 (FBXW7) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein. Pin1 interacts with Fbw7 in a phoshorylation-dependent manner and promotes Fbw7 self-ubiquitination and protein degradation by disrupting Fbw7 dimerization. Paper also shows the over-expression of Pin1 suppresses the ability of Fbw7 to inhibit cell transformation and proliferation, suggesting a link between Pin1 overexpression and cancer.
details

Far upstream element-binding protein 2 - KHSRP -  Homo sapiens
DOC_WW_Pin1_4178183BinaryPhysicochemical compatibilityPhosphorylation of S181 in the Pin1-binding motif of Far upstream element-binding protein 2 (KHSRP) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details

Focal adhesion kinase 1 - Ptk2 -  Mus musculus
DOC_WW_Pin1_4907912BinaryPhysicochemical compatibilityPhosphorylation of S910 in the Pin1-binding motif of Isoform 3 of Focal adhesion kinase 1 (Ptk2) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details

Focal adhesion kinase 1 - PTK2 -  Homo sapiens
DOC_WW_Pin1_4907912BinaryPhysicochemical 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

G1/S-specific cyclin-D1 - Ccnd1 -  Mus musculus
DOC_WW_Pin1_4283288BinaryPhysicochemical 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

G1/S-specific cyclin-E1 - Ccne1 -  Mus musculus
DOC_WW_Pin1_4382387BinaryPhysicochemical compatibilityPhosphorylation of S385 in the Pin1-binding motif of G1/S-specific cyclin-E1 (Ccne1) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details

Gephyrin - Gphn -  Mus musculus
DOC_WW_Pin1_4185190BinaryPhysicochemical compatibilityPhosphorylation of S188 in the Pin1-binding motif of Gephyrin (Gphn) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details
DOC_WW_Pin1_4191196BinaryPhysicochemical compatibilityPhosphorylation of S194 in the Pin1-binding motif of Gephyrin (Gphn) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details
DOC_WW_Pin1_4197202BinaryPhysicochemical compatibilityPhosphorylation of S200 in the Pin1-binding motif of Gephyrin (Gphn) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details

Homeobox protein NANOG - Nanog -  Mus musculus
DOC_WW_Pin1_44954BinaryPhysicochemical compatibilityPhosphorylation of S52 in the Pin1-binding motif of Homeobox protein NANOG (Nanog) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details
DOC_WW_Pin1_46267BinaryPhysicochemical compatibilityPhosphorylation of S65 in the Pin1-binding motif of Homeobox protein NANOG (Nanog) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details

Insulin receptor substrate 1 - IRS1 -  Homo sapiens
DOC_WW_Pin1_4431436BinaryPhysicochemical compatibilityPhosphorylation of S434 in the Pin1-binding motif of Insulin receptor substrate 1 (IRS1) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details

Interferon regulatory factor 3 - IRF3 -  Homo sapiens
DOC_WW_Pin1_4336341BinaryPhysicochemical compatibilityPhosphorylation of S339 in the Pin1-binding motif of Interferon regulatory factor 3 (IRF3) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details

Latent membrane protein 2 - LMP2 -  Epstein-Barr virus (strain B95-8)
LIG_WW_15760BinaryPre‑translationalAlternative splicing removes the WW-binding motif of Latent membrane protein 2 (LMP2), abrogating binding to E3 ubiquitin-protein ligase Itchy (Itch).
details
LIG_WW_198101BinaryPre‑translationalAlternative splicing removes the WW-binding motif of Latent membrane protein 2 (LMP2), abrogating binding to E3 ubiquitin-protein ligase Itchy (Itch).
details
LIG_WW_15760BinaryPre‑translationalAlternative splicing removes the WW-binding motif of Latent membrane protein 2 (LMP2), abrogating binding to E3 ubiquitin-protein ligase Itchy (Itch).
details

Mothers against decapentaplegic homolog 3 - SMAD3 -  Homo sapiens
DOC_WW_Pin1_4176181BinaryPhysicochemical 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
DOC_WW_Pin1_4201206BinaryPhysicochemical 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
DOC_WW_Pin1_4205210BinaryPhysicochemical 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
DOC_WW_Pin1_4210215BinaryPhysicochemical 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
DOC_WW_Pin1_4176181SpecificityAltered 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
LIG_WW_Nedd4L203210SpecificityAltered 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
LIG_WW_1181184SpecificityAltered 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
LIG_WW_1181184Avidity‑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
LIG_WW_Nedd4L203210Avidity‑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
LIG_WW_Nedd4L203210CumulativeRheostaticCDK8/9 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

Myc proto-oncogene protein - MYC -  Homo sapiens
DOC_WW_Pin1_45560BinaryPhysicochemical 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

Myocyte-specific enhancer factor 2C - Mef2c -  Mus musculus
DOC_WW_Pin1_4107112BinaryPhysicochemical compatibilityPhosphorylation of S110 in the Pin1-binding motif of Myocyte-specific enhancer factor 2C (Mef2c) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details
DOC_WW_Pin1_495100BinaryPhysicochemical compatibilityPhosphorylation of S98 in the Pin1-binding motif of Myocyte-specific enhancer factor 2C (Mef2c) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details

Neurogenic locus notch homolog protein 1 - NOTCH1 -  Homo sapiens
DOC_WW_Pin1_421182123BinaryPhysicochemical compatibilityPhosphorylation of S2121 in the Pin1-binding motif of Neurogenic locus notch homolog protein 1 (NOTCH1) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
DOC_WW_Pin1_421292134BinaryPhysicochemical compatibilityPhosphorylation of T2132 in the Pin1-binding motif of Neurogenic locus notch homolog protein 1 (NOTCH1) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
DOC_WW_Pin1_421332138BinaryPhysicochemical compatibilityPhosphorylation of S2136 in the Pin1-binding motif of Neurogenic locus notch homolog protein 1 (NOTCH1) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details

Neutrophil cytosol factor 1 - NCF1 -  Homo sapiens
DOC_WW_Pin1_4342347BinaryPhysicochemical 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

Non-POU domain-containing octamer-binding protein - Nono -  Mus musculus
DOC_WW_Pin1_4409414BinaryPhysicochemical compatibilityPhosphorylation of T412 in the Pin1-binding motif of Non-POU domain-containing octamer-binding protein (Nono) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details
DOC_WW_Pin1_4427432BinaryPhysicochemical compatibilityPhosphorylation of T430 in the Pin1-binding motif of Non-POU domain-containing octamer-binding protein (Nono) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details
DOC_WW_Pin1_4449454BinaryPhysicochemical compatibilityPhosphorylation of T452 in the Pin1-binding motif of Non-POU domain-containing octamer-binding protein (Nono) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details

Nuclear receptor corepressor 2 - NCOR2 -  Homo sapiens
DOC_WW_Pin1_412381243BinaryPhysicochemical compatibilityPhosphorylation of T1241 in the Pin1-binding motif of Nuclear receptor corepressor 2 (NCOR2) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
DOC_WW_Pin1_414411446BinaryPhysicochemical compatibilityPhosphorylation of T1444 in the Pin1-binding motif of Nuclear receptor corepressor 2 (NCOR2) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details

Nuclear receptor subfamily 4 group A member 1 - NR4A1 -  Homo sapiens
DOC_WW_Pin1_4137142BinaryPhysicochemical compatibilityPhosphorylation of S140 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
DOC_WW_Pin1_4428433BinaryPhysicochemical 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
DOC_WW_Pin1_49297BinaryPhysicochemical 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

POU domain, class 5, transcription factor 1 - POU5F1 -  Homo sapiens
DOC_WW_Pin1_4914BinaryPhysicochemical compatibilityPhosphorylation of S12 in the Pin1-binding motif of POU domain, class 5, transcription factor 1 (POU5F1) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details

Protein AATF - AATF -  Homo sapiens
DOC_WW_Pin1_4143148BinaryPhysicochemical compatibilityPhosphorylation of T146 in the Pin1-binding motif of Protein AATF (AATF) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details

Protein BTG2 - BTG2 -  Homo sapiens
DOC_WW_Pin1_4144149BinaryPhysicochemical compatibilityPhosphorylation of S147 in the Pin1-binding motif of Protein BTG2 (BTG2) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details

Protein PML - PML -  Homo sapiens
DOC_WW_Pin1_4400405BinaryPhysicochemical 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
DOC_WW_Pin1_4502507BinaryPhysicochemical compatibilityPhosphorylation of S505 in the Pin1-binding motif of Protein PML (PML) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
DOC_WW_Pin1_4515520BinaryPhysicochemical compatibilityPhosphorylation of S518 in the Pin1-binding motif of Protein PML (PML) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
DOC_WW_Pin1_4524529BinaryPhysicochemical compatibilityPhosphorylation of S527 in the Pin1-binding motif of Protein PML (PML) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details

Protein SPT23 - SPT23 -  Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
DOC_WW_Pin1_4651656BinaryPhysicochemical compatibilityPhosphorylation of S654 in the Pin1-binding motif of Protein SPT23 (SPT23) induces binding to the Peptidyl-prolyl cis-trans isomerase ESS1 (ESS1) protein.
details

Protein Tax-1 - tax -  Human T-cell leukemia virus 1 (strain Japan ATK-1 subtype A)
DOC_WW_Pin1_4157162BinaryPhysicochemical compatibilityPhosphorylation of S160 in the Pin1-binding motif of Protein Tax-1 (tax) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details

Protein X - X -  Hepatitis B virus genotype A2 subtype adw2 (strain Rutter 1979)
DOC_WW_Pin1_43843BinaryPhysicochemical compatibilityPhosphorylation of S41 in the Pin1-binding motif of Protein X (X) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details

Proto-oncogene c-Fos - Fos -  Mus musculus
DOC_WW_Pin1_4229234BinaryPhysicochemical 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
DOC_WW_Pin1_4322327BinaryPhysicochemical compatibilityPhosphorylation of T325 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
DOC_WW_Pin1_4328333BinaryPhysicochemical compatibilityPhosphorylation of T331 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
DOC_WW_Pin1_4371376BinaryPhysicochemical compatibilityPhosphorylation of S374 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.
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RAC-alpha serine/threonine-protein kinase - AKT1 -  Homo sapiens
DOC_WW_Pin1_4447452BinaryPhysicochemical 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
DOC_WW_Pin1_48994BinaryPhysicochemical compatibilityPhosphorylation of T92 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

Receptor tyrosine-protein kinase erbB-4 - ERBB4 -  Homo sapiens
LIG_WW_110531056SpecificityAltered 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
LIG_WW_110531056BinaryPre‑translationalAlternative splicing removes the WW-binding motif of Receptor tyrosine-protein kinase erbB-4 (ERBB4), abrogating binding to E3 ubiquitin-protein ligase Itchy homolog (ITCH). The presence of a WW-binding motif mediates ERBB4 mono-ubiquitination and endocytosis by the WW domain-containing HECT-type E3 ubiquitin ligase ITCH.
details
LIG_WW_110531056BinaryPre‑translationalAlternative splicing removes the WW-binding motif of Receptor tyrosine-protein kinase erbB-4 (ERBB4), abrogating binding to E3 ubiquitin-protein ligase Itchy homolog (ITCH). The presence of a WW-binding motif mediates ERBB4 mono-ubiquitination and endocytosis by the WW domain-containing HECT-type E3 ubiquitin ligase ITCH.
details

Retinoic acid receptor alpha - RARA -  Homo sapiens
DOC_WW_Pin1_47479BinaryPhysicochemical 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

Serine/threonine-protein kinase Nek6 - NEK6 -  Homo sapiens
DOC_WW_Pin1_4212217BinaryPhysicochemical compatibilityPhosphorylation of S215 in the Pin1-binding motif of Serine/threonine-protein kinase Nek6 (NEK6) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
DOC_WW_Pin1_4242247BinaryPhysicochemical compatibilityPhosphorylation of S245 in the Pin1-binding motif of Serine/threonine-protein kinase Nek6 (NEK6) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details

Signal transducer and activator of transcription 3 - STAT3 -  Homo sapiens
DOC_WW_Pin1_4724729BinaryPhysicochemical 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

Steroidogenic factor 1 - Nr5a1 -  Mus musculus
DOC_WW_Pin1_4200205BinaryPhysicochemical 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

Sulfotransferase 4A1 - SULT4A1 -  Homo sapiens
DOC_WW_Pin1_4510BinaryPhysicochemical compatibilityPhosphorylation of T8 in the Pin1-binding motif of Sulfotransferase 4A1 (SULT4A1) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
DOC_WW_Pin1_4813BinaryPhysicochemical 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

Synphilin-1 - SNCAIP -  Homo sapiens
DOC_WW_Pin1_4208213BinaryPhysicochemical compatibilityPhosphorylation of S211 in the Pin1-binding motif of Synphilin-1 (SNCAIP) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
DOC_WW_Pin1_4212217BinaryPhysicochemical compatibilityPhosphorylation of S215 in the Pin1-binding motif of Synphilin-1 (SNCAIP) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details

Telomeric repeat-binding factor 1 - TERF1 -  Homo sapiens
DOC_WW_Pin1_4146151BinaryPhysicochemical compatibilityPhosphorylation of T149 in the Pin1-binding motif of Telomeric repeat-binding factor 1 (TERF1) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details

Transcription factor AP-1 - JUN -  Homo sapiens
DOC_WW_Pin1_46065BinaryPhysicochemical 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
DOC_WW_Pin1_47075BinaryPhysicochemical 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

Transcription factor AP-1 - Jun -  Mus musculus
LIG_WW_1167170BinaryPhysicochemical 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

Transcription factor p65 - RELA -  Homo sapiens
DOC_WW_Pin1_4251256BinaryPhysicochemical compatibilityPhosphorylation of T254 in the Pin1-binding motif of Transcription factor p65 (RELA) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details

Transcriptional activator Myb - Myb -  Mus musculus
DOC_WW_Pin1_4525530BinaryPhysicochemical compatibilityPhosphorylation of S528 in the Pin1-binding motif of Transcriptional activator Myb (Myb) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details

Tumor protein p73 - TP73 -  Homo sapiens
DOC_WW_Pin1_4409414BinaryPhysicochemical compatibilityPhosphorylation of S412 in the Pin1-binding motif of Tumor protein p73 (TP73) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
DOC_WW_Pin1_4439444BinaryPhysicochemical compatibilityPhosphorylation of T442 in the Pin1-binding motif of Tumor protein p73 (TP73) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
DOC_WW_Pin1_4479484BinaryPhysicochemical compatibilityPhosphorylation of T482 in the Pin1-binding motif of Tumor protein p73 (TP73) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
details
DOC_WW_Pin1_4479484BinaryPre‑translationalAlternative splicing removes the WW-binding motif of Tumor protein p73 (TP73), abrogating binding to Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1). Isoforms lacking WW-binding motifs have decreased transcriptional activity.
details
DOC_WW_Pin1_4439444BinaryPre‑translationalAlternative splicing removes the WW-binding motif of Tumor protein p73 (TP73), abrogating binding to Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1). Isoforms lacking WW-binding motifs have decreased transcriptional activity.
details
DOC_WW_Pin1_4409414BinaryPre‑translationalAlternative splicing removes the WW-binding motif of Tumor protein p73 (TP73), abrogating binding to Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1). Isoforms lacking WW-binding motifs have decreased transcriptional activity.
details
LIG_WW_1484487SpecificityCompetitionThe transcriptional coactivator YAP1 and the ubiquitin ligase Itch competitively bind to the same WW-binding motif of p73. Binding of YAP1 prevents Itch-mediated ubiquitylation of p73, resulting in stabilisation, and increases trancriptional activity of p73.
details
LIG_WW_1484487SpecificityCompetitionThe transcriptional coactivator YAP1 and the ubiquitin ligase Itch competitively bind to the same WW-binding motif of p73. Binding of YAP1 prevents Itch-mediated ubiquitylation of p73, resulting in stabilisation, and increases trancriptional activity of p73.
details

Tyrosine-protein kinase BTK - Btk -  Mus musculus
DOC_WW_Pin1_4112117BinaryPhysicochemical compatibilityPhosphorylation of S115 in the Pin1-binding motif of Tyrosine-protein kinase BTK (Btk) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details
DOC_WW_Pin1_41823BinaryPhysicochemical compatibilityPhosphorylation of S21 in the Pin1-binding motif of Tyrosine-protein kinase BTK (Btk) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein.
details

Wee1-like protein kinase 1-B - wee1-b -  Xenopus laevis
DOC_WW_Pin1_4183188BinaryPhysicochemical compatibilityPhosphorylation of T186 in the Pin1-binding motif of Wee1-like protein kinase 1-B (wee1-b) induces binding to the pin1 protein.
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