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  Domain hiding  Altered binding specificity  Motif hiding  Composite binding site formation
  Uncategorised  Rheostatic  Allostery  Avidity-sensing
  Physicochemical compatibility  Pre-translational  Competition

x  Index
Type: Avidity‑sensing Subtype: Type: Binary Subtype: AllosteryType: Binary Subtype: Physicochemical compatibility
Type: Binary Subtype: Pre‑translationalType: Cumulative Subtype: RheostaticType: Pre‑assembly Subtype: Composite binding site formation
Type: Specificity Subtype: Altered binding specificityType: Specificity Subtype: CompetitionType: Specificity Subtype: Domain hiding
Type: Specificity Subtype: Motif hidingType: Uncategorised Subtype: Uncategorised


ProteinMotifStartEndSwitch descriptionInformation

Type: Specificity Subtype: Domain hiding
A domain can be sterically masked by binding of an effector when there is a large difference in intrinsic affinity of the domain for different binding partners, or a large difference in the local abundance of these partners, thereby precluding further interactions of the domain. Binding of the masking molecule can be PTM-dependent or -independent.
NED4L_HUMANLIG_14-3-3_1465470Phosphorylation 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
SCNNG_HUMANLIG_WW_1624627Phosphorylation 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
BIN1_HUMANLIG_SH3_3305311An intramolecular interaction of an SH3 binding motif, encoded by exon 12A, in Isoform II2 of Myc box-dependent-interacting protein 1 (BIN1) with the SH3 domain of Bin1 prevents interaction of the Bin1 SH3 domain with the SH3 binding motif of Isoform II2 of Myc box-dependent-interacting protein 1 (BIN1).
details
MYC_HUMANLIG_SH3_26065An intramolecular interaction of an SH3 binding motif, encoded by exon 12A, in Isoform II2 of Myc box-dependent-interacting protein 1 (BIN1) with the SH3 domain of Bin1 prevents interaction of the Bin1 SH3 domain with the SH3 binding motif of Myc proto-oncogene protein (MYC).
details
INSR_HUMANLIG_SH2_STAT513611364PIP3 (1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate), a product of PI3-kinase, binds to the SH2 domains of PI3K (Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1)) and thereby blocks its interaction with tyrosine-phosphorylated SH2 motif containing proteins.
details
MEI2_SCHPOLIG_14-3-3_1;ELM435
523
440
529
Binding of meiRNA meiotic non-coding RNA (meiRNA) to the RRM domains of Meiosis protein mei2 (mei2) is essential for promotion of premeiotic DNA synthesis and meiosis I and is blocked by Pat1-mediated phosphorylation-induced binding of the 14-3-3 protein DNA damage checkpoint protein rad24 (rad24) to 2 14-3-3 binding motifs in mei2
details
APBA1_HUMANLIG_PDZ_Class_2832837An intramolecular interaction of the C-terminal PDZ binding motif of Amyloid beta A4 precursor protein-binding family A member 1 (APBA1) (also known as X11alpha/Mint1) with the PDZ domain tandem of APBA1 results in an auto-inhibited conformation of APBA1, where binding of ligands containing a PDZ binding motif such as Presenilin-1 (PSEN1) is blocked. Binding of these ligands might be regulated by phosphorylation of Y836 in the APBA1 PDZ-binding motif, as its mutation to glutamate releases autoinhibition and enhances the interaction of the APBA1 PDZ tandem with presenilin.
details
PSN1_HUMANLIG_PDZ_Class_2462467An intramolecular interaction of the C-terminal PDZ binding motif of Amyloid beta A4 precursor protein-binding family A member 1 (APBA1) (also known as X11alpha/Mint1) with the PDZ domain tandem of APBA1 results in an auto-inhibited conformation of APBA1, where binding of ligands containing a PDZ binding motif such as Presenilin-1 (PSEN1) is blocked. Binding of these ligands might be regulated by phosphorylation of Y836 in the APBA1 PDZ-binding motif, as its mutation to glutamate releases autoinhibition and enhances the interaction of the APBA1 PDZ tandem with presenilin.
details
BIN1_HUMANLIG_SH3_8265268An intramolecular interaction of a Bin1 SH3 binding motif, encoded by exon 10, with the Isoform BIN1 of Myc box-dependent-interacting protein 1 (BIN1) SH3 domain prevents binding of dynamin2 to the Bin1 SH3 domain. Binding of PI(4,5)P2 to the overlapping PI(4,5)P2-binding motif encoded by exon 10 relieves the intramolecular auto-inhibitory interaction and allows the Bin1 SH3 domain to interact with the dynamin2 PxxP motif.
details
DYN2_HUMANLIG_SH3_2829834An intramolecular interaction of a Bin1 SH3 binding motif, encoded by exon 10, with the Dynamin-2 (DNM2) SH3 domain prevents binding of dynamin2 to the Bin1 SH3 domain. Binding of PI(4,5)P2 to the overlapping PI(4,5)P2 binding motif encoded by exon 10 relieves the intramolecular auto-inhibitory interaction and allows the Bin1 SH3 domain to interact with the dynamin2 PxxP motif
details
IMA1_YEASTTRG_NLS_Bipartite_14458An intramolecular interaction between the importin beta-binding (IBB) domain and the NLS-binding pocket of Importin subunit alpha (SRP1) prevents binding of NLS cargo (e.g. Large T antigen) in the absence of Importin subunit beta-1 (KAP95) by hiding of the NLS-binding pocket. Binding of the IBB of Importin subunit alpha (SRP1) to Importin subunit beta-1 (KAP95) relieves this auto-inhibitory interaction and increases the affinity of Importin subunit alpha (SRP1) for NLS cargo.
details
LT_SV40TRG_NLS_MonoExtN_4126132An intramolecular interaction between the importin beta-binding (IBB) domain and the NLS-binding pocket of Importin subunit alpha (SRP1) prevents binding of NLS cargo (e.g. Large T antigen) in the absence of Importin subunit beta-1 (KAP95) by hiding of the NLS-binding pocket. Binding of the IBB of Importin subunit alpha (SRP1) to Importin subunit beta-1 (KAP95) relieves this auto-inhibitory interaction and increases the affinity of Importin subunit alpha (SRP1) for NLS cargo.
details
CDN1B_HUMANDOC_CYCLIN_13033Binding of the CDK-cyclin inhibitor p27 (Cyclin-dependent kinase inhibitor 1B (CDKN1B)) blocks the substrate recruitment site on Cyclin-A2 (CCNA2).
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CDC6_HUMANDOC_CYCLIN_19498Binding of the CDK-cyclin inhibitor p27 (Cyclin-dependent kinase inhibitor 1B (CDKN1B)) blocks the substrate recruitment site on Cyclin-A2 (CCNA2).
details
TEX14_MOUSELIG_EABR_CEP55_1791797The switch from cytokinesis to intracellular bridge formation in differentiating male germ cells is mediated by Testis-expressed protein 14 (Tex14). Binding of Tex14 to Centrosomal protein of 55 kDa (Cep55) prevents binding of ALIX (Programmed cell death 6-interacting protein (Pdcd6ip)) and Tumor susceptibility gene 101 protein (Tsg101) to Cep55, which is required for abscission at the end of cytokinesis. Tex14 uses the same site on Cep55 as ALIX (Pdcd6ip) and Tsg101. The strong interaction between Tex14 and Cep55 together with the avidity effect that results from interaction of MKLP1 with both Tex14 and Cep55 prevent recruitment of ALIX (Pdcd6ip) and Tsg101 for abscission.
details
TS101_MOUSELIG_EABR_CEP55_1158164The switch from cytokinesis to intracellular bridge formation in differentiating male germ cells is mediated by Testis-expressed protein 14 (Tex14). Binding of Tex14 to Centrosomal protein of 55 kDa (Cep55) prevents binding of ALIX (Programmed cell death 6-interacting protein (Pdcd6ip)) and Tumor susceptibility gene 101 protein (Tsg101) to Cep55, which is required for abscission at the end of cytokinesis. Tex14 uses the same site on Cep55 as ALIX (Pdcd6ip) and Tsg101. The strong interaction between Tex14 and Cep55 together with the avidity effect that results from interaction of MKLP1 with both Tex14 and Cep55 prevent recruitment of ALIX (Pdcd6ip) and Tsg101 for abscission.
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TEX14_MOUSELIG_EABR_CEP55_1791797The switch from cytokinesis to intracellular bridge formation in differentiating male germ cells is mediated by Testis-expressed protein 14 (Tex14). Binding of Tex14 to Centrosomal protein of 55 kDa (Cep55) prevents binding of ALIX (Programmed cell death 6-interacting protein (Pdcd6ip)) and Tumor susceptibility gene 101 protein (Tsg101) to Cep55, which is required for abscission at the end of cytokinesis. Tex14 uses the same site on Cep55 as ALIX (Pdcd6ip) and Tsg101. The strong interaction between Tex14 and Cep55 together with the avidity effect that results from interaction of MKLP1 with both Tex14 and Cep55 prevent recruitment of ALIX (Pdcd6ip) and Tsg101 for abscission.
details
PDC6I_MOUSELIG_EABR_CEP55_1801807The switch from cytokinesis to intracellular bridge formation in differentiating male germ cells is mediated by Testis-expressed protein 14 (Tex14). Binding of Tex14 to Centrosomal protein of 55 kDa (Cep55) prevents binding of ALIX (Programmed cell death 6-interacting protein (Pdcd6ip)) and Tumor susceptibility gene 101 protein (Tsg101) to Cep55, which is required for abscission at the end of cytokinesis. Tex14 uses the same site on Cep55 as ALIX (Pdcd6ip) and Tsg101. The strong interaction between Tex14 and Cep55 together with the avidity effect that results from interaction of MKLP1 with both Tex14 and Cep55 prevent recruitment of ALIX (Pdcd6ip) and Tsg101 for abscission.
details
NHRF1_HUMANLIG_PDZ_Class_1353358Binding of Ezrin via its FERM domain to the EB domain of Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (SLC9A3R1) results in allosteric coupling to the second PDZ domain of SLC9A3R1. This relieves the intramolecular interaction with the SLC9A3R1 PDZ-binding ligand and increases the affinity of the PDZ domain for other ligands including Catenin beta-1 (CTNNB1).
details
CTNB1_HUMANLIG_PDZ_Class_1776781Binding of Ezrin via its FERM domain to the EB domain of Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (SLC9A3R1) results in allosteric coupling to the second PDZ domain of SLC9A3R1. This relieves the intramolecular interaction with the SLC9A3R1 PDZ-binding ligand and increases the affinity of the PDZ domain for other ligands including Catenin beta-1 (CTNNB1).
details
GRM5_RATLIG_PDZ_Class_111981203Binding of the PDZ-binding motif of General receptor for phosphoinositides 1-associated scaffold protein (Grasp) (Tamalin) to the Tamalin (Grasp) PDZ domain locks this protein in an auto-inhibited conformation. Binding of the PDZ-binding motif of Metabotropic glutamate receptor 5 (Grm5) to the Tamalin (Grasp) PDZ domain results in disruption of the weaker intramolecular Tamalin (Grasp) interactions. The PDZ-binding motif of Tamalin (Grasp) becomes available to interact with the PDZ domain of Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2 (Magi2) (S-SCAM), which functions as a receptor for kinesin motor proteins. See also switch details.
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GRASP_RATLIG_PDZ_Class_1389394Binding of the PDZ-binding motif of General receptor for phosphoinositides 1-associated scaffold protein (Grasp) (Tamalin) to the Tamalin (Grasp) PDZ domain locks this protein in an auto-inhibited conformation. Binding of the PDZ-binding motif of Metabotropic glutamate receptor 5 (Grm5) to the Tamalin (Grasp) PDZ domain results in disruption of the weaker intramolecular Tamalin (Grasp) interactions. The PDZ-binding motif of Tamalin (Grasp) becomes available to interact with the PDZ domain of Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2 (Magi2) (S-SCAM), which functions as a receptor for kinesin motor proteins. See also switch details.
details
BUB1B_HUMANDEG_APCC_KENBOX_2303307Binding of the second KEN-box motif of Mitotic checkpoint serine/threonine-protein kinase BUB1 beta (BUB1B), a subunit of the Spindle Assembly Checkpoint (SAC), to the substrate recruitment site of Cell division cycle protein 20 homolog (CDC20), the substrate recognition subunit of the Anaphase Promoting Complex/Cyclosome (APC/C), blocks binding of the Cdc20 substrate G2/mitotic-specific cyclin-B1 (CCNB1). As a result, G2/mitotic-specific cyclin-B1 (CCNB1) is not targeted for proteasomal degradation until metaphase, when the SAC is inhibited. Destruction of G2/mitotic-specific cyclin-B1 (CCNB1) is required for progression to the anaphase of the cell cycle.
details
CCNB1_HUMANDEG_APCC_DBOX_14149Binding of the second KEN-box motif of Mitotic checkpoint serine/threonine-protein kinase BUB1 beta (BUB1B), a subunit of the Spindle Assembly Checkpoint (SAC), to the substrate recruitment site of Cell division cycle protein 20 homolog (CDC20), the substrate recognition subunit of the Anaphase Promoting Complex/Cyclosome (APC/C), blocks binding of the Cdc20 substrate G2/mitotic-specific cyclin-B1 (CCNB1). As a result, G2/mitotic-specific cyclin-B1 (CCNB1) is not targeted for proteasomal degradation until metaphase, when the SAC is inhibited. Destruction of G2/mitotic-specific cyclin-B1 (CCNB1) is required for progression to the anaphase of the cell cycle.
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BUB1B_HUMANDEG_APCC_KENBOX_2303307Binding of the second KEN-box motif of Mitotic checkpoint serine/threonine-protein kinase BUB1 beta (BUB1B), a subunit of the Spindle Assembly Checkpoint (SAC), to the substrate recruitment site of Cell division cycle protein 20 homolog (CDC20), the substrate recognition subunit of the Anaphase Promoting Complex/Cyclosome (APC/C), blocks binding of the Cdc20 substrate Securin (PTTG1). As a result, Securin (PTTG1) is not targeted for proteasomal degradation until metaphase, when the SAC is inhibited. Destruction of Securin (PTTG1) is required for progression to the anaphase of the cell cycle.
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PTTG1_HUMANDEG_APCC_DBOX_16068Binding of the second KEN-box motif of Mitotic checkpoint serine/threonine-protein kinase BUB1 beta (BUB1B), a subunit of the Spindle Assembly Checkpoint (SAC), to the substrate recruitment site of Cell division cycle protein 20 homolog (CDC20), the substrate recognition subunit of the Anaphase Promoting Complex/Cyclosome (APC/C), blocks binding of the Cdc20 substrate Securin (PTTG1). As a result, Securin (PTTG1) is not targeted for proteasomal degradation until metaphase, when the SAC is inhibited. Destruction of Securin (PTTG1) is required for progression to the anaphase of the cell cycle.
details
ACM1_YEASTDEG_APCC_KENBOX_297101The KEN-box motif of APC/C-CDH1 modulator 1 (ACM1) binds to the substrate recruitment site of APC/C activator protein CDH1 (CDH1), the substrate recognition subunit of the Anaphase Promoting Complex/Cyclosome (APC/C), and thereby blocks recruitment, and subsequent targeting for proteasomal degradation, of the Cdh1 substrate G2/mitotic-specific cyclin-2 (CLB2). Degradation of G2/mitotic-specific cyclin-2 (CLB2) is required for mitotic exit and maintenance of the G1 phase of the cell cycle and is allowed by Cdc20-dependent degradation of APC/C-CDH1 modulator 1 (ACM1) in anaphase.
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CG22_YEASTDEG_APCC_KENBOX_299103The KEN-box motif of APC/C-CDH1 modulator 1 (ACM1) binds to the substrate recruitment site of APC/C activator protein CDH1 (CDH1), the substrate recognition subunit of the Anaphase Promoting Complex/Cyclosome (APC/C), and thereby blocks recruitment, and subsequent targeting for proteasomal degradation, of the Cdh1 substrate G2/mitotic-specific cyclin-2 (CLB2). Degradation of G2/mitotic-specific cyclin-2 (CLB2) is required for mitotic exit and maintenance of the G1 phase of the cell cycle and is allowed by Cdc20-dependent degradation of APC/C-CDH1 modulator 1 (ACM1) in anaphase.
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ACM1_YEASTDEG_APCC_KENBOX_297101The KEN-box motif of APC/C-CDH1 modulator 1 (ACM1) binds to the substrate recruitment site of APC/C activator protein CDH1 (CDH1), the substrate recognition subunit of the Anaphase Promoting Complex/Cyclosome (APC/C), and thereby blocks recruitment, and subsequent targeting for proteasomal degradation, of the Cdh1 substrate Kinesin-like protein CIN8 (CIN8). Degradation of Kinesin-like protein CIN8 (CIN8) is required for mitotic exit and maintenance of the G1 phase of the cell cycle and is allowed by Cdc20-dependent degradation of APC/C-CDH1 modulator 1 (ACM1) in anaphase.
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CIN8_YEASTDEG_APCC_KENBOX_2931935The KEN-box motif of APC/C-CDH1 modulator 1 (ACM1) binds to the substrate recruitment site of APC/C activator protein CDH1 (CDH1), the substrate recognition subunit of the Anaphase Promoting Complex/Cyclosome (APC/C), and thereby blocks recruitment, and subsequent targeting for proteasomal degradation, of the Cdh1 substrate Kinesin-like protein CIN8 (CIN8). Degradation of Kinesin-like protein CIN8 (CIN8) is required for mitotic exit and maintenance of the G1 phase of the cell cycle and is allowed by Cdc20-dependent degradation of APC/C-CDH1 modulator 1 (ACM1) in anaphase.
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ACM1_YEASTDEG_APCC_KENBOX_297101The KEN-box motif of APC/C-CDH1 modulator 1 (ACM1) binds to the substrate recruitment site of APC/C activator protein CDH1 (CDH1), the substrate recognition subunit of the Anaphase Promoting Complex/Cyclosome (APC/C), and thereby blocks recruitment, and subsequent targeting for proteasomal degradation, of the Cdh1 substrate Probable serine/threonine-protein kinase HSL1 (HSL1). Degradation of Probable serine/threonine-protein kinase HSL1 (HSL1) is required for mitotic exit and maintenance of the G1 phase of the cell cycle and is allowed by Cdc20-dependent degradation of APC/C-CDH1 modulator 1 (ACM1) in anaphase.
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HSL1_YEASTDEG_APCC_KENBOX_2774778The KEN-box motif of APC/C-CDH1 modulator 1 (ACM1) binds to the substrate recruitment site of APC/C activator protein CDH1 (CDH1), the substrate recognition subunit of the Anaphase Promoting Complex/Cyclosome (APC/C), and thereby blocks recruitment, and subsequent targeting for proteasomal degradation, of the Cdh1 substrate Probable serine/threonine-protein kinase HSL1 (HSL1). Degradation of Probable serine/threonine-protein kinase HSL1 (HSL1) is required for mitotic exit and maintenance of the G1 phase of the cell cycle and is allowed by Cdc20-dependent degradation of APC/C-CDH1 modulator 1 (ACM1) in anaphase.
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Type: Specificity Subtype: Competition
Competitive binding of multiple binding partners to overlapping or adjacent, mutually exclusive interaction interfaces depends on local target protein abundance, which can be regulated by changing the expression level or subcellular localisation of the competitors, or by scaffolding.
ITB7_HUMANLIG_Talin770779The integrin regulator Talin-1 (TLN1) and the actin-crosslinking Filamins Filamin-A (FLNA) use overlapping binding sites on the cytoplasmic tails of beta integrin subunits Integrin beta-7 (ITGB7), which makes their interaction with beta integrin mutually exclusive.
details
ITB7_HUMANLIG_Filamin776787The integrin regulator Talin-1 (TLN1) and the actin-crosslinking Filamins Filamin-A (FLNA) use overlapping binding sites on the cytoplasmic tails of beta integrin subunits Integrin beta-7 (ITGB7), which makes their interaction with beta integrin mutually exclusive.
details
HES1_HUMANLIG_WRPW_1275280The Transducin-like enhancer protein 1 (TLE1) can recruit a wide range of transcriptional repressors via its WD domain, to which the WRPW motif of Transcription factor HES-1 (HES1) and the EH1 motif of Homeobox protein goosecoid (GSC) can bind using overlapping sites.
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GSC_HUMANLIG_EH1_1513The Transducin-like enhancer protein 1 (TLE1) can recruit a wide range of transcriptional repressors via its WD domain, to which the WRPW motif of Transcription factor HES-1 (HES1) and the EH1 motif of Homeobox protein goosecoid (GSC) can bind using overlapping sites.
details
CD2_HUMANLIG_GYF295303T-cell surface antigen CD2 (CD2) uses overlapping motifs to bind to CD2 antigen cytoplasmic tail-binding protein 2 (CD2BP2) and Fyn, which makes their interactions mutually exclusive. Since CD2BP2 and Tyrosine-protein kinase Fyn (FYN) reside in different subcellular locations, the specificity of CD2 for the two competitors is switched by changing its cellular localization, from non-raft membranes to lipid raft membranes.
details
CD2_HUMANLIG_SH3_3294300T-cell surface antigen CD2 (CD2) uses overlapping motifs to bind to CD2 antigen cytoplasmic tail-binding protein 2 (CD2BP2) and Fyn, which makes their interactions mutually exclusive. Since CD2BP2 and Tyrosine-protein kinase Fyn (FYN) reside in different subcellular locations, the specificity of CD2 for the two competitors is switched by changing its cellular localization, from non-raft membranes to lipid raft membranes.
details
CDN1A_HUMANDOC_CYCLIN_11922Cyclin-dependent kinase inhibitor 1 (CDKN1A) (p21) and the M-phase inducer phosphatase 1 (CDC25A) bind the same site on Cyclin proteins (e.g. G1/S-specific cyclin-E1 (CCNE1)), making their interactions mutually exclusive.
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MPIP1_HUMANDOC_CYCLIN_11115Cyclin-dependent kinase inhibitor 1 (CDKN1A) (p21) and the M-phase inducer phosphatase 1 (CDC25A) bind the same site on Cyclin proteins (e.g. G1/S-specific cyclin-E1 (CCNE1)), making their interactions mutually exclusive.
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RB_HUMANDOC_CYCLIN_1873877The docking sites for PP1 (e.g. Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (PPP1CA)) and Cdk-Cyclins (e.g. Cyclin-A2 (CCNA2)) on Retinoblastoma-associated protein (RB1) overlap, which makes their binding to RB1 mutually exclusive. Hypophosphorylated RB1 blocks E2F-dependent transcription, while hyperphosphorylation inactivates RB1 as a repressor, thereby promoting cell cycle progression.
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RB_HUMANDOC_PP1872878The docking sites for PP1 (e.g. Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (PPP1CA)) and Cdk-Cyclins (e.g. Cyclin-A2 (CCNA2)) on Retinoblastoma-associated protein (RB1) overlap, which makes their binding to RB1 mutually exclusive. Hypophosphorylated RB1 blocks E2F-dependent transcription, while hyperphosphorylation inactivates RB1 as a repressor, thereby promoting cell cycle progression.
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SNX9_HUMANLIG_Glycolytic_Aldolase165169Sorting nexin-9 (SNX9) and fructose-1,6-bisphosphate (D-fructose 1,6-bisphosphate) bind mutually exclusive and with similar affinities to Fructose-bisphosphate aldolase A (ALDOA).
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DAG1_HUMANLIG_WW_1889892The 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.
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DAG1_HUMANLIG_SH3_3888894The 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.
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CFTR_HUMANLIG_PDZ_Class_114751480The PDZ domains of Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (SLC9A3R1) and SH3 and multiple ankyrin repeat domains protein 2 (SHANK2) compete for the PDZ-binding motif of Cystic fibrosis transmembrane conductance regulator (CFTR). SLC9A3R1 positively regulates CFTR activity by recruiting a PKA-containing complex, while SH3 and multiple ankyrin repeat domains protein 2 (SHANK2) negatively affects CFTR activity by recruiting PDE4D.
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CFTR_HUMANLIG_PDZ_Class_114751480The PDZ domains of Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (SLC9A3R1) and SH3 and multiple ankyrin repeat domains protein 2 (SHANK2) compete for the PDZ-binding motif of Cystic fibrosis transmembrane conductance regulator (CFTR). SLC9A3R1 positively regulates CFTR activity by recruiting a PKA-containing complex, while SH3 and multiple ankyrin repeat domains protein 2 (SHANK2) negatively affects CFTR activity by recruiting PDE4D.
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DAG1_HUMANLIG_WW_1889892The 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
DAG1_HUMANLIG_SH3_3888894The 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.
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P73_HUMANLIG_WW_1484487The 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.
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P73_HUMANLIG_WW_1484487The 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.
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Type: Specificity Subtype: Motif hiding
Motif hiding occurs when there is a large difference in intrinsic affinity of overlapping or adjacent motifs for their respective binding partners, or a large difference in the local abundance of these partners. Binding of an effector to one motif sterically masks the overlapping or adjacent motif, thereby precluding it from binding. Binding of the masking molecule can be PTM-dependent or -independent.
LT_SV40TRG_NLS_MonoExtN_4126132Inhibition of nuclear import of Large T antigen by phosphorylation-dependent (T124) binding of BRCA1-associated protein (BRAP).
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LT_SV40TRG_NLS_MonoExtN_4126132Inhibition of nuclear import of Large T antigen by phosphorylation-dependent (T124) binding of BRCA1-associated protein (BRAP).
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VPAP_HCMVATRG_NLS_MonoExtN_4425432Inhibition of nuclear import of DNA polymerase processivity factor (UL44) by phosphorylation-dependent (T427) binding of BRCA1-associated protein (BRAP).
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VPAP_HCMVATRG_NLS_MonoExtN_4425432Inhibition of nuclear import of DNA polymerase processivity factor (UL44) by phosphorylation-dependent (T427) binding of BRCA1-associated protein (BRAP).
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ADA22_HUMANLIG_14-3-3_3831
854
836
859
Phosphorylation-induced binding of dimeric 14-3-3 protein beta/alpha (YWHAB) to Disintegrin and metalloproteinase domain-containing protein 22 (ADAM22) blocks ER retention motifs in Disintegrin and metalloproteinase domain-containing protein 22 (ADAM22) and regulates transport of this protein to the membrane.
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ADA22_HUMANTRG_ER_diArg_1829
851
831
854
Phosphorylation-induced binding of dimeric 14-3-3 protein beta/alpha (YWHAB) to Disintegrin and metalloproteinase domain-containing protein 22 (ADAM22) blocks ER retention motifs in Disintegrin and metalloproteinase domain-containing protein 22 (ADAM22) and regulates transport of this protein to the membrane.
details
MKL1_MOUSELIG_Actin_RPEL_317
61
105
36
80
124
Hiding of the NLS of MKL/myocardin-like protein 1 (Mkl1) by binding of G-actin to the RPEL motifs of MKL/myocardin-like protein 1 (Mkl1) prevents translocation of this transcription factor to the nucleus.
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MKL1_MOUSETRG_NLS_MonoExtN_462
95
67
101
Hiding of the NLS of MKL/myocardin-like protein 1 (Mkl1) by binding of G-actin to the RPEL motifs of MKL/myocardin-like protein 1 (Mkl1) prevents translocation of this transcription factor to the nucleus.
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GPR15_HUMANLIG_14-3-3_4356360Phosphorylation-induced binding of 14-3-3 protein beta/alpha (YWHAB) promotes cell surface expression of G-protein coupled receptor 15 (GPR15) by releasing the receptor from the ER retrieval/retention pathway that is mediated by the interaction of its ER retention motif with Coatomer subunit beta (COPB1).
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GPR15_HUMANTRG_ER_diArg_1352354Phosphorylation-induced binding of 14-3-3 protein beta/alpha (YWHAB) promotes cell surface expression of G-protein coupled receptor 15 (GPR15) by releasing the receptor from the ER retrieval/retention pathway that is mediated by the interaction of its ER retention motif with Coatomer subunit beta (COPB1).
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HG2A_HUMANLIG_14-3-3_3510The basic ER retention motif of HLA class II histocompatibility antigen gamma chain (CD74) is blocked from binding to Coatomer subunit beta (COPB1) by phosphorylation-induced binding of 14-3-3 protein beta/alpha (YWHAB), regulating its release from the ER and trafficking to the plasma membrane.
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HG2A_HUMANTRG_ER_diArg_135The basic ER retention motif of HLA class II histocompatibility antigen gamma chain (CD74) is blocked from binding to Coatomer subunit beta (COPB1) by phosphorylation-induced binding of 14-3-3 protein beta/alpha (YWHAB), regulating its release from the ER and trafficking to the plasma membrane.
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GABR1_HUMANTRG_ER_diArg_1923926Interaction of the GABA receptor R2 subunit (Gamma-aminobutyric acid type B receptor subunit 2 (GABBR2)) with the R1 subunit (Gamma-aminobutyric acid type B receptor subunit 1 (GABBR1)) via coiled-coil forming domains masks the ER retention motif in the R1 subunit (Gamma-aminobutyric acid type B receptor subunit 1 (GABBR1)), thereby promoting surface expression of fully assembled GABA receptors.
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GRASP_RATLIG_PDZ_Class_1389394Binding of the PDZ-binding motif of General receptor for phosphoinositides 1-associated scaffold protein (Grasp) (Tamalin) to the Tamalin Grasp PDZ domain locks this protein in an auto-inhibited conformation. Binding of the PDZ-binding motif of Metabotropic glutamate receptor 5 (Grm5) to the Tamalin GraspPDZ domain results in disruption of the weaker intramolecular Tamalin (Grasp) interactions. The PDZ-binding motif of Tamalin (General receptor for phosphoinositides 1-associated scaffold protein (Grasp)) becomes available to interact with the PDZ domain of Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2 (Magi2) (S-SCAM), which functions as a receptor for kinesin motor proteins. See also switch details.
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GRASP_RATLIG_PDZ_Class_1389394Binding of the PDZ-binding motif of General receptor for phosphoinositides 1-associated scaffold protein (Grasp) (Tamalin) to the Tamalin Grasp PDZ domain locks this protein in an auto-inhibited conformation. Binding of the PDZ-binding motif of Metabotropic glutamate receptor 5 (Grm5) to the Tamalin GraspPDZ domain results in disruption of the weaker intramolecular Tamalin (Grasp) interactions. The PDZ-binding motif of Tamalin (General receptor for phosphoinositides 1-associated scaffold protein (Grasp)) becomes available to interact with the PDZ domain of Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2 (Magi2) (S-SCAM), which functions as a receptor for kinesin motor proteins. See also switch details.
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NMDZ1_HUMANLIG_PDZ_Class_1917922Binding of the PDZ domain of Disks large homolog 4 (DLG4) suppresses the ER-retention motif of Isoform 4 of Glutamate receptor subunit zeta-1 (GRIN1) in a splice variant-specific manner, thereby promoting cell surface expression of this particular isoform. This supports the hypothesis that local regulation of receptor exit from neuronal ER plays a role in modifying discrete synaptic receptor number.
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NMDZ1_HUMANTRG_ER_diArg_1893895Binding of the PDZ domain of Disks large homolog 4 (DLG4) suppresses the ER-retention motif of Isoform 4 of Glutamate receptor subunit zeta-1 (GRIN1) in a splice variant-specific manner, thereby promoting cell surface expression of this particular isoform. This supports the hypothesis that local regulation of receptor exit from neuronal ER plays a role in modifying discrete synaptic receptor number.
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NMDZ1_HUMANLIG_PDZ_Class_1917922Binding of the PDZ domain of Disks large homolog 4 (DLG4) suppresses the ER-retention motif of Isoform 4 of Glutamate receptor subunit zeta-1 (GRIN1) in a splice variant-specific manner, thereby promoting cell surface expression of this particular isoform. This supports the hypothesis that local regulation of receptor exit from neuronal ER plays a role in modifying discrete synaptic receptor number.
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NMDZ1_HUMANTRG_ER_diArg_1893895Binding of the PDZ domain of Disks large homolog 4 (DLG4) suppresses the ER-retention motif of Isoform 4 of Glutamate receptor subunit zeta-1 (GRIN1) in a splice variant-specific manner, thereby promoting cell surface expression of this particular isoform. This supports the hypothesis that local regulation of receptor exit from neuronal ER plays a role in modifying discrete synaptic receptor number.
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NMDZ1_HUMANLIG_PDZ_Class_1917922Binding of the PDZ domain of Disks large homolog 4 (DLG4) suppresses the ER-retention motif of Isoform 4 of Glutamate receptor subunit zeta-1 (GRIN1) in a splice variant-specific manner, thereby promoting cell surface expression of this particular isoform. This supports the hypothesis that local regulation of receptor exit from neuronal ER plays a role in modifying discrete synaptic receptor number.
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NMDZ1_HUMANTRG_ER_diArg_1893895Binding of the PDZ domain of Disks large homolog 4 (DLG4) suppresses the ER-retention motif of Isoform 4 of Glutamate receptor subunit zeta-1 (GRIN1) in a splice variant-specific manner, thereby promoting cell surface expression of this particular isoform. This supports the hypothesis that local regulation of receptor exit from neuronal ER plays a role in modifying discrete synaptic receptor number.
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CDN1B_HUMANTRG_NLS152166Phosphorylation 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).
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CDN1B_HUMANLIG_14-3-3_3154159Phosphorylation 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).
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Type: Avidity‑sensing Subtype:
Multiple low-affinity interactions give rise to high-avidity interactions that have increased binding strength, with more than additive affinity.
XRCC1_HUMANLIG_FHA_2517523Hierarchical 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).
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XRCC1_HUMANLIG_FHA_2521527Hierarchical 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).
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CD3Z_HUMANLIG_TYR_ITAM6986Phosphorylation of Y72 and Y83 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).
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CD3Z_HUMANLIG_TYR_ITAM6986Phosphorylation of Y72 and Y83 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).
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CD79A_MOUSELIG_TYR_ITAM179196Phosphorylation of Y182 and Y193 in the ITAM motif of B-cell antigen receptor complex-associated protein alpha chain (Cd79a) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (Syk). Maximal Syk activation requires both Syk SH2 domains and phosphorylation of both ITAM tyrosine residues.
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CD79A_MOUSELIG_TYR_ITAM179196Phosphorylation of Y182 and Y193 in the ITAM motif of B-cell antigen receptor complex-associated protein alpha chain (Cd79a) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (Syk). Maximal Syk activation requires both Syk SH2 domains and phosphorylation of both ITAM tyrosine residues.
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CD3E_HUMANLIG_TYR_ITAM185202Phosphorylation 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).
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CD3E_HUMANLIG_TYR_ITAM185202Phosphorylation 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).
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CD3Z_HUMANLIG_TYR_ITAM108126Phosphorylation 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).
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CD3Z_HUMANLIG_TYR_ITAM108126Phosphorylation 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).
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CD3Z_HUMANLIG_TYR_ITAM139156Phosphorylation 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).
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CD3Z_HUMANLIG_TYR_ITAM139156Phosphorylation 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).
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CD3G_HUMANLIG_TYR_ITAM157174Phosphorylation of Y160 and Y171 in the ITAM motif of T-cell surface glycoprotein CD3 gamma chain (CD3G) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase ZAP-70 (ZAP70).
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CD3G_HUMANLIG_TYR_ITAM157174Phosphorylation of Y160 and Y171 in the ITAM motif of T-cell surface glycoprotein CD3 gamma chain (CD3G) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase ZAP-70 (ZAP70).
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OX1R_HUMANLIG_TYR_ITSM7986Orexin-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).
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OX1R_HUMANLIG_TYR_ITIM356361Orexin-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).
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FCG2A_HUMANLIG_TYR_ITAM285307Phosphorylation 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).
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FCG2A_HUMANLIG_TYR_ITAM285307Phosphorylation 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).
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FCERG_HUMANLIG_TYR_ITAM6279Phosphorylation of Y65 and Y76 in the ITAM motif of High affinity immunoglobulin epsilon receptor subunit gamma (FCER1G) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).
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FCERG_HUMANLIG_TYR_ITAM6279Phosphorylation of Y65 and Y76 in the ITAM motif of High affinity immunoglobulin epsilon receptor subunit gamma (FCER1G) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).
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KPCE_HUMANLIG_14-3-3_3343348Phosphorylation 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).
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KPCE_HUMANLIG_14-3-3_3365370Phosphorylation 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).
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RAF1_HUMANLIG_14-3-3_1256261Phosphorylation 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.
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RAF1_HUMANLIG_14-3-3_1618623Phosphorylation 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.
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FOXO3_HUMANLIG_14-3-3_3250255Phosphorylation 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).
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FOXO3_HUMANLIG_14-3-3_32934Phosphorylation 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).
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PTN3_HUMANLIG_14-3-3_3356361Phosphorylation 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).
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PTN3_HUMANLIG_14-3-3_3832837Phosphorylation 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).
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KSR1_MOUSELIG_14-3-3_3294299Phosphorylation 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.
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KSR1_MOUSELIG_14-3-3_3389394Phosphorylation 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.
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SLOB_DROMELIG_14-3-3_35156Phosphorylation 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.
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SLOB_DROMELIG_14-3-3_37681Phosphorylation 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.
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IRS1_HUMANLIG_14-3-3_3371376Phosphorylation of two 14-3-3-binding motifs in Insulin receptor substrate 1 (IRS1) induces high-avidity binding to dimeric 14-3-3 protein epsilon (YWHAE).
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IRS1_HUMANLIG_14-3-3_3638643Phosphorylation of two 14-3-3-binding motifs in Insulin receptor substrate 1 (IRS1) induces high-avidity binding to dimeric 14-3-3 protein epsilon (YWHAE).
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MEI2_SCHPOLIG_14-3-3_1435440Phosphorylation 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.
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MEI2_SCHPOLIG_14-3-3_2523529Phosphorylation 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.
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SMAD3_HUMANLIG_WW_1181184CDK8/9 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.
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SMAD3_HUMANLIG_WW_Nedd4L203210CDK8/9 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.
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OX1R_HUMANLIG_TYR_ITSM7986Orexin-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).
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OX1R_HUMANLIG_TYR_ITIM356361Orexin-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).
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AMPH_HUMANLIG_Clathr_ClatBox_1351355Amphiphysin 1 contains two distinct motifs that bind to distinct sites on N-terminal beta-propeller domain of clathrin, resulting in increased binding strength to free domain. This, in combination with binding of its BAR domain to curved membranes, results in localisation of amphipysin to the periphery of the assembling clathrin lattice. The two clathrin-binding motifs are regulated by phosphorylation of adjacent modification sites (see switch details and switch details).
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AMPH_HUMANLIG_Clathr_ClatBox_2380385Amphiphysin 1 contains two distinct motifs that bind to distinct sites on N-terminal beta-propeller domain of clathrin, resulting in increased binding strength to free domain. This, in combination with binding of its BAR domain to curved membranes, results in localisation of amphipysin to the periphery of the assembling clathrin lattice. The two clathrin-binding motifs are regulated by phosphorylation of adjacent modification sites (see switch details and switch details).
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MDM4_HUMANLIG_14-3-3_1364369Optimal 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.
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MDM4_HUMANLIG_14-3-3_3339344Optimal 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.
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FOXO4_HUMANLIG_14-3-3_12934Phosphorylation 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.
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FOXO4_HUMANLIG_14-3-3_2193199Phosphorylation 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.
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CDN1B_HUMANLIG_14-3-3_3154159Phosphorylation 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.
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CDN1B_HUMANLIG_14-3-3_3193198Phosphorylation 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.
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Type: Binary Subtype: Physicochemical compatibility
PTM of a residue in a motif or in its flanking regions alters the physicochemical and/or structural compatibility of the motif with its binding partner. This can either induce or enhance an interaction, or result in inhibition or even abrogation of an interaction.
LAT_HUMANLIG_SH2_STAT5161164Phosphorylation of Y161 in the SH2-binding motif of Linker for activation of T-cells family member 1 (LAT) induces binding to the 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1 (PLCG1) protein.
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AKT1_HUMANDOC_AGCK_PIF_1469474Phosphorylation 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.
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KPCB_HUMANDOC_AGCK_PIF_1656661Dephosphorylation 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.
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TFCP2_HUMANDOC_WW_Pin1_4326331Phosphorylation 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).
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MPIP3_HUMANLIG_PLK129131Phosphorylation 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.
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MPIP2_HUMANLIG_PLK4951Phosphorylation 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).
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Y1827_MYCTULIG_FHA_11925Phosphorylation 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).
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MPIP3_HUMANLIG_14-3-3_3213218Phosphorylation 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).
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SRC_HUMANLIG_SH2_SRC530533Phosphorylation 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.
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NFAC1_HUMANMOD_GSK3_1287294Phosphorylation 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).
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NFAC1_HUMANMOD_GSK3_1238245Phosphorylation 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
EGFR_HUMANLIG_TKB10691074Phosphorylation of Y1069 in Epidermal growth factor receptor (EGFR) is necessary for binding to the TKB domain of E3 ubiquitin-protein ligase CBL (CBL).
details
SPY2_HUMANLIG_TKB5560Phosphorylation of Y55 in Protein sprouty homolog 2 (SPRY2) is necessary for binding to the TKB domain of E3 ubiquitin-protein ligase CBL (CBL).
details
MYC_HUMANMOD_GSK3_15562Phosphorylation of Myc proto-oncogene protein (MYC) at S62 primes the protein for phosphorylation at T58 by Glycogen synthase kinase-3 beta (GSK3B).
details
P53_HUMANMOD_GSK3_13037Phosphorylation of Cellular tumor antigen p53 (TP53) at S37 primes the protein for phosphorylation at S33 by Glycogen synthase kinase-3 beta (GSK3B).
details
JUN_HUMANMOD_GSK3_1236243Phosphorylation of Transcription factor AP-1 (JUN) at S243 primes the protein for phosphorylation at T239 by Glycogen synthase kinase-3 beta (GSK3B).
details
CCNE1_HUMANMOD_GSK3_1392399Phosphorylation 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
ATX3_HUMANMOD_GSK3_1253260Phosphorylation of Ataxin-3 (ATXN3) at S260 primes the protein for subsequent phosphorylation at S256 by Glycogen synthase kinase-3 beta (GSK3B).
details
LT_SV40DEG_SCF_FBW7_2699705Phosphorylation of T701 in the degron of Large T antigen induces binding to the F-box/WD repeat-containing protein 7 (FBXW7) protein, which recruits it to the SCF ubiquitin ligase complex where it is marked for degradation.
details
NOTC1_HUMANDEG_SCF_FBW7_225082515Phosphorylation of T2511 in the degron of Neurogenic locus notch homolog protein 1 (NOTCH1) induces binding to the F-box/WD repeat-containing protein 7 (FBXW7) protein, which recruits it to the SCF ubiquitin ligase complex where it is marked for degradation.
details
HIF1A_HUMANDEG_ODPH_VHL_1400413Hydroxylation 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
HIF1A_HUMANDEG_ODPH_VHL_1562574Hydroxylation 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
EPAS1_HUMANDEG_ODPH_VHL_1403416Hydroxylation 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
EPAS1_HUMANDEG_ODPH_VHL_1529542Hydroxylation 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
HIF3A_HUMANDEG_ODPH_VHL_1490502Hydroxylation 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
P73_HUMANDOC_WW_Pin1_4409414Phosphorylation 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
P73_HUMANDOC_WW_Pin1_4439444Phosphorylation 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
P73_HUMANDOC_WW_Pin1_4479484Phosphorylation 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
B2L11_MOUSEDOC_WW_Pin1_46267Phosphorylation 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
FOS_MOUSEDOC_WW_Pin1_4229234Phosphorylation 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
FOS_MOUSEDOC_WW_Pin1_4322327Phosphorylation 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
FOS_MOUSEDOC_WW_Pin1_4328333Phosphorylation 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
FOS_MOUSEDOC_WW_Pin1_4371376Phosphorylation 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.
details
MYC_HUMANDOC_WW_Pin1_45560Phosphorylation 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
TAX_HTL1ADOC_WW_Pin1_4157162Phosphorylation 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
P53_HUMANDOC_WW_Pin1_43035Phosphorylation 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
P53_HUMANDOC_WW_Pin1_4312317Phosphorylation 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
P53_HUMANDOC_WW_Pin1_47883Phosphorylation 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
JUN_HUMANDOC_WW_Pin1_46065Phosphorylation 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
JUN_HUMANDOC_WW_Pin1_47075Phosphorylation 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
MYB_MOUSEDOC_WW_Pin1_4525530Phosphorylation 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
RARA_HUMANDOC_WW_Pin1_47479Phosphorylation 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
NCF1_HUMANDOC_WW_Pin1_4342347Phosphorylation 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
NR4A1_HUMANDOC_WW_Pin1_4137142Phosphorylation 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
NR4A1_HUMANDOC_WW_Pin1_4428433Phosphorylation 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
NR4A1_HUMANDOC_WW_Pin1_49297Phosphorylation 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
CCND1_MOUSEDOC_WW_Pin1_4283288Phosphorylation 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
PML_HUMANDOC_WW_Pin1_4400405Phosphorylation 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
PML_HUMANDOC_WW_Pin1_4502507Phosphorylation 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
PML_HUMANDOC_WW_Pin1_4515520Phosphorylation 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
PML_HUMANDOC_WW_Pin1_4524529Phosphorylation 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
AKT1_HUMANDOC_WW_Pin1_4447452Phosphorylation 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
AKT1_HUMANDOC_WW_Pin1_48994Phosphorylation 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
STF1_MOUSEDOC_WW_Pin1_4200205Phosphorylation 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
CTNB1_HUMANDOC_WW_Pin1_4243248Phosphorylation 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
IRS1_HUMANDOC_WW_Pin1_4431436Phosphorylation 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
BTK_MOUSEDOC_WW_Pin1_4112117Phosphorylation 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
BTK_MOUSEDOC_WW_Pin1_41823Phosphorylation 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
STAT3_HUMANDOC_WW_Pin1_4724729Phosphorylation 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
CDN1B_HUMANDOC_WW_Pin1_4184189Phosphorylation 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
NOTC1_HUMANDOC_WW_Pin1_421182123Phosphorylation 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
NOTC1_HUMANDOC_WW_Pin1_421292134Phosphorylation 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
NOTC1_HUMANDOC_WW_Pin1_421332138Phosphorylation 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
TERF1_HUMANDOC_WW_Pin1_4146151Phosphorylation 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
X_HBVA3DOC_WW_Pin1_43843Phosphorylation 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
BTG2_HUMANDOC_WW_Pin1_4144149Phosphorylation 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
SMAD3_HUMANDOC_WW_Pin1_4176181Phosphorylation 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
SMAD3_HUMANDOC_WW_Pin1_4201206Phosphorylation 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
SMAD3_HUMANDOC_WW_Pin1_4205210Phosphorylation 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
SMAD3_HUMANDOC_WW_Pin1_4210215Phosphorylation 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
PO5F1_HUMANDOC_WW_Pin1_4914Phosphorylation 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
TF65_HUMANDOC_WW_Pin1_4251256Phosphorylation 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
FAK1_HUMANDOC_WW_Pin1_4907912Phosphorylation 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
IRF3_HUMANDOC_WW_Pin1_4336341Phosphorylation 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
CRTC2_MOUSEDOC_WW_Pin1_4133138Phosphorylation 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
CCNE1_MOUSEDOC_WW_Pin1_4382387Phosphorylation 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
NANOG_MOUSEDOC_WW_Pin1_44954Phosphorylation 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
NANOG_MOUSEDOC_WW_Pin1_46267Phosphorylation 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
CEP55_MOUSEDOC_WW_Pin1_4420425Phosphorylation 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
CEP55_MOUSEDOC_WW_Pin1_4423428Phosphorylation 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
GEPH_MOUSEDOC_WW_Pin1_4185190Phosphorylation 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
GEPH_MOUSEDOC_WW_Pin1_4191196Phosphorylation 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
GEPH_MOUSEDOC_WW_Pin1_4197202Phosphorylation 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
MEF2C_MOUSEDOC_WW_Pin1_4107112Phosphorylation 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
MEF2C_MOUSEDOC_WW_Pin1_495100Phosphorylation 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
FUBP2_HUMANDOC_WW_Pin1_4178183Phosphorylation 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
NONO_MOUSEDOC_WW_Pin1_4409414Phosphorylation 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
NONO_MOUSEDOC_WW_Pin1_4427432Phosphorylation 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
NONO_MOUSEDOC_WW_Pin1_4449454Phosphorylation 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
ARBK1_MOUSEDOC_WW_Pin1_4667672Phosphorylation 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
ST4A1_HUMANDOC_WW_Pin1_4510Phosphorylation 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
ST4A1_HUMANDOC_WW_Pin1_4813Phosphorylation 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
TFCP2_MOUSEDOC_WW_Pin1_4288293Phosphorylation 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
TFCP2_MOUSEDOC_WW_Pin1_4306311Phosphorylation 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
TFCP2_MOUSEDOC_WW_Pin1_4326331Phosphorylation 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
NEK6_HUMANDOC_WW_Pin1_4212217Phosphorylation 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
NEK6_HUMANDOC_WW_Pin1_4242247Phosphorylation 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
AATF_HUMANDOC_WW_Pin1_4143148Phosphorylation 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
DAXX_HUMANDOC_WW_Pin1_4175180Phosphorylation 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
NCOR2_HUMANDOC_WW_Pin1_412381243Phosphorylation 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
NCOR2_HUMANDOC_WW_Pin1_414411446Phosphorylation 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
SNCAP_HUMANDOC_WW_Pin1_4208213Phosphorylation 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
SNCAP_HUMANDOC_WW_Pin1_4212217Phosphorylation 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
BAD_RATLIG_14-3-3_1134139Phosphorylation 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
MT_POVM3LIG_14-3-3_1254259Phosphorylation of S257 in the 14-3-3-binding motif of Middle T antigen induces binding to the 14-3-3 protein zeta/delta (YWHAZ) protein.
details
ATX1_HUMANLIG_14-3-3_1772777Phosphorylation 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
M3K5_HUMANLIG_14-3-3_1963968Phosphorylation 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
PTPN3_MOUSELIG_14-3-3_2355361Phosphorylation of S359 in the 14-3-3-binding motif of Tyrosine-protein phosphatase non-receptor type 3 (Ptpn3) induces binding to the 14-3-3 protein beta/alpha (Ywhab) protein.
details
NAC1_HUMANLIG_14-3-3_2388394Phosphorylation of S392 in the 14-3-3-binding motif of Sodium/calcium exchanger 1 (SLC8A1) induces binding to the 14-3-3 protein epsilon (YWHAE) protein. This interaction inhibits the activity of Sodium/calcium exchanger 1 (SLC8A1).
details
FOXO4_HUMANLIG_14-3-3_2193199Phosphorylation 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
TF65_HUMANLIG_14-3-3_24147Phosphorylation 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
PDE3A_HUMANLIG_14-3-3_2424430Phosphorylation 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
TESK1_RATLIG_14-3-3_2435441Phosphorylation of S439 in the 14-3-3-binding motif of Dual specificity testis-specific protein kinase 1 (Tesk1) induces binding to the 14-3-3 protein beta/alpha (Ywhab) protein. This interaction inhibits the kinase activity of Dual specificity testis-specific protein kinase 1 (Tesk1).
details
RIM15_YEASTLIG_14-3-3_310721077Phosphorylation 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
HDAC4_HUMANLIG_14-3-3_3629634Phosphorylation 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
ACACA_HUMANLIG_BRCT_BRCA1_112621266Phosphorylation of S1263 in the BRCT-binding motif of Acetyl-CoA carboxylase 1 (ACACA) induces binding to the Breast cancer type 1 susceptibility protein (BRCA1) protein.
details
F175A_HUMANLIG_BRCT_BRCA1_1405409Phosphorylation of S406 in the BRCT-binding motif of BRCA1-A complex subunit Abraxas (FAM175A) induces binding to the Breast cancer type 1 susceptibility protein (BRCA1) protein.
details
ATRIP_HUMANLIG_BRCT_BRCA1_1238242Phosphorylation 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
COM1_HUMANLIG_BRCT_BRCA1_1326330Phosphorylation of S327 in the BRCT-binding motif of DNA endonuclease RBBP8 (RBBP8) induces binding to the Breast cancer type 1 susceptibility protein (BRCA1) protein.
details
FANCJ_HUMANLIG_BRCT_BRCA1_1989993Phosphorylation of S990 in the BRCT-binding motif of Fanconi anemia group J protein (BRIP1) induces binding to the Breast cancer type 1 susceptibility protein (BRCA1) protein.
details
FANCJ_HUMANLIG_BRCT_BRCA1_2989995Phosphorylation of S990 in the BRCT-binding motif of Fanconi anemia group J protein (BRIP1) induces binding to the Breast cancer type 1 susceptibility protein (BRCA1) protein.
details
H2AX_HUMANLIG_BRCT_MDC1_1139143Phosphorylation 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
CHK2_HUMANLIG_FHA_16672Phosphorylation 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
RAD9_YEASTLIG_FHA_1601607Phosphorylation of T603 in the FHA-binding motif of DNA repair protein RAD9 (RAD9) induces binding to the Serine/threonine-protein kinase RAD53 (RAD53) protein.
details
PIN4_YEASTLIG_FHA_1303309Phosphorylation of T305 in the FHA-binding motif of RNA-binding protein PIN4 (PIN4) induces binding to the Serine/threonine-protein kinase RAD53 (RAD53) protein.
details
CLV1_ARATHLIG_FHA_1866872Phosphorylation of T868 in the FHA-binding motif of Receptor protein kinase CLAVATA1 (CLV1) induces binding to the Protein phosphatase 2C 70 (KAPP) protein.
details
RAD9_YEASTLIG_FHA_2153159Phosphorylation of T155 in the FHA-binding motif of DNA repair protein RAD9 (RAD9) induces binding to the Serine/threonine-protein kinase RAD53 (RAD53) protein.
details
RAD9_YEASTLIG_FHA_2190196Phosphorylation of T192 in the FHA-binding motif of DNA repair protein RAD9 (RAD9) induces binding to the Serine/threonine-protein kinase RAD53 (RAD53) protein.
details
XRCC1_HUMANLIG_FHA_2521527Phosphorylation 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
XRCC4_HUMANLIG_FHA_2231237Phosphorylation 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
XRCC4_MOUSELIG_FHA_2229235Phosphorylation of T231 in the FHA-binding motif of DNA repair protein XRCC4 (Xrcc4) induces binding to the Bifunctional polynucleotide phosphatase/kinase (Pnkp) protein.
details
MRC1_SCHPOLIG_FHA_2643649Phosphorylation of T645 in the FHA-binding motif of Mediator of replication checkpoint protein 1 (mrc1) induces binding to the Serine/threonine-protein kinase cds1 (cds1) protein.
details
EGFR_HUMANLIG_PTB_Phospho_111041110Phosphorylation of Y1110 in the PTB-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Docking protein 1 (DOK1) protein.
details
ERBB3_HUMANLIG_PTB_Phospho_113221328Phosphorylation of Y1328 in the PTB-binding motif of Receptor tyrosine-protein kinase erbB-3 (ERBB3) induces binding to the SHC-transforming protein 1 (SHC1) protein.
details
IL2RB_HUMANLIG_PTB_Phospho_1358364Phosphorylation of Y364 in the PTB-binding motif of Interleukin-2 receptor subunit beta (IL2RB) induces binding to the SHC-transforming protein 1 (SHC1) protein.
details
IL4RA_HUMANLIG_PTB_Phospho_1491497Phosphorylation of Y497 in the PTB-binding motif of Interleukin-4 receptor subunit alpha (IL4R) induces binding to the Insulin receptor substrate 1 (IRS1) protein.
details
INSR_HUMANLIG_PTB_Phospho_1993999Phosphorylation of Y999 in the PTB-binding motif of Insulin receptor (INSR) induces binding to the SHC-transforming protein 1 (SHC1) protein.
details
ITB3_HUMANLIG_PTB_Phospho_1767773Phosphorylation of Y773 in the PTB-binding motif of Integrin beta-3 (ITGB3) induces binding to the Docking protein 1 (DOK1) protein.
details
ITB3_HUMANLIG_PTB_Phospho_1779785Phosphorylation of Y785 in the PTB-binding motif of Integrin beta-3 (ITGB3) induces binding to the SHC-transforming protein 1 (SHC1) protein.
details
ITB4_HUMANLIG_PTB_Phospho_115901596Phosphorylation of Y1596 in the PTB-binding motif of Integrin beta-4 (ITGB4) induces binding to the SHC-transforming protein 1 (SHC1) protein.
details
LRP1_HUMANLIG_PTB_Phospho_145014507Phosphorylation 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
MT_POVMALIG_PTB_Phospho_1244250Phosphorylation of Y250 in the PTB-binding motif of Middle T antigen induces binding to the SHC-transforming protein 1 (Shc1) protein.
details
MUSK_MOUSELIG_PTB_Phospho_1547553Phosphorylation of Y553 in the PTB-binding motif of Muscle, skeletal receptor tyrosine-protein kinase (Musk) induces binding to the Protein Dok-7 (Dok7) protein.
details
NTRK1_HUMANLIG_PTB_Phospho_1490496Phosphorylation 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
RET_MOUSELIG_PTB_Phospho_110571063Phosphorylation 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
SHIP1_HUMANLIG_PTB_Phospho_110161022Phosphorylation of Y1022 in the PTB-binding motif of Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 1 (INPP5D) induces binding to the SHC-transforming protein 1 (SHC1) protein.
details
SHIP1_HUMANLIG_PTB_Phospho_1909915Phosphorylation of Y915 in the PTB-binding motif of Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 1 (INPP5D) induces binding to the SHC-transforming protein 1 (SHC1) protein.
details
SGK1_HUMANDOC_AGCK_PIF_1418423Phosphorylation 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
SCH9_YEASTDOC_AGCK_PIF_1733738Phosphorylation 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
KS6A3_MOUSEDOC_AGCK_PIF_1382387Auto-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
AKT2_HUMANDOC_AGCK_PIF_1470475Phosphorylation of S474 in the PIF pocket-binding motif of RAC-beta serine/threonine-protein kinase (AKT2) induces intramolecular binding and kinase cis-activation.
details
KS6B1_RATDOC_AGCK_PIF_1408413Phosphorylation of T412 in the PIF pocket-binding motif of Ribosomal protein S6 kinase beta-1 (Rps6kb1) induces intramolecular binding and kinase cis-activation.
details
ROCK1_HUMANDOC_AGCK_PIF_1394399Phosphorylation of T398 in the PIF pocket-binding motif of Rho-associated protein kinase 1 (ROCK1) induces intramolecular binding and kinase cis-activation.
details
SGK3_HUMANDOC_AGCK_PIF_1482487Phosphorylation of S486 in the PIF pocket-binding motif of Serine/threonine-protein kinase Sgk3 (SGK3) induces intramolecular binding and kinase cis-activation.
details
SGK3_MOUSEDOC_AGCK_PIF_1482487Phosphorylation of S486 in the PIF pocket-binding motif of Serine/threonine-protein kinase Sgk3 (Sgk3) induces intramolecular binding and kinase cis-activation.
details
IKBE_HUMANDEG_SCF_TRCP1_1156161Dual phosphorylation of S157 and S161 in the TrCP1-binding motif of NF-kappa-B inhibitor epsilon (NFKBIE) targets the protein to the SCF ubiquitin ligase complex, which marks it for degradation.
details
LMP1_EBVB9DEG_SCF_TRCP1_1210215Dual phosphorylation of S211 and S215 in the TrCP1-binding motif of Latent membrane protein 1 (LMP1) targets the protein to the SCF ubiquitin ligase complex, which marks it for degradation.
details
VPU_HV1BRDEG_SCF_TRCP1_15156Dual phosphorylation of S52 and S56 in the TrCP1-binding motif of Protein Vpu (vpu) targets the protein to the SCF ubiquitin ligase complex, which marks it for degradation.
details
PRLR_HUMANDEG_SCF_TRCP1_1348353Dual phosphorylation of S349 and S353 in the TrCP1-binding motif of Prolactin receptor (PRLR) targets the protein to the SCF ubiquitin ligase complex, which marks it for degradation.
details
ATF4_HUMANDEG_SCF_TRCP1_1218224Dual phosphorylation of S219 and S224 in the TrCP1-binding motif of Cyclic AMP-dependent transcription factor ATF-4 (ATF4) targets the protein to the SCF ubiquitin ligase complex, which marks it for degradation.
details
NFKB1_HUMANDEG_SCF_TRCP1_1926932Dual 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
IKBA_HUMANDEG_SCF_TRCP1_13136Dual 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
DLG1_HUMANDEG_SCF_TRCP1_1597602Dual phosphorylation of S598 and S602 in the TrCP1-binding motif of Disks large homolog 1 (DLG1) targets the protein to the SCF ubiquitin ligase complex, which marks it for degradation.
details
IKBB_HUMANDEG_SCF_TRCP1_11823Dual 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
PDCD4_HUMANDEG_SCF_TRCP1_17076Dual phosphorylation of S71 and S76 in the TrCP1-binding motif of Programmed cell death protein 4 (PDCD4) targets the protein to the SCF ubiquitin ligase complex, which marks it for degradation.
details
BORA_HUMANDEG_SCF_TRCP1_1496501Dual 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
CLSPN_HUMANDEG_SCF_TRCP1_12934Dual 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
FBX5_HUMANDEG_SCF_TRCP1_1144149Dual 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
WEE1B_XENLADOC_WW_Pin1_4183188Phosphorylation of T186 in the Pin1-binding motif of Wee1-like protein kinase 1-B (wee1-b) induces binding to the pin1 protein.
details
FBX5A_XENLADOC_WW_Pin1_4712Phosphorylation of S10 in the Pin1-binding motif of F-box only protein 5-A (fbxo5-a) induces binding to the pin1 protein.
details
SPT23_YEASTDOC_WW_Pin1_4651656Phosphorylation of S654 in the Pin1-binding motif of Protein SPT23 (SPT23) induces binding to the Peptidyl-prolyl cis-trans isomerase ESS1 (ESS1) protein.
details
SOC1_ARATHDOC_WW_Pin1_4192197Phosphorylation of S195 in the Pin1-binding motif of MADS-box protein SOC1 (SOC1) induces binding to the Peptidyl-prolyl cis-trans isomerase Pin1 (PIN1) protein.
details
SOC1_ARATHDOC_WW_Pin1_44651Phosphorylation of S49 in the Pin1-binding motif of MADS-box protein SOC1 (SOC1) induces binding to the Peptidyl-prolyl cis-trans isomerase Pin1 (PIN1) protein.
details
AGL24_ARATHDOC_WW_Pin1_4199204Phosphorylation of T202 in the Pin1-binding motif of MADS-box protein AGL24 (AGL24) induces binding to the Peptidyl-prolyl cis-trans isomerase Pin1 (PIN1) protein.
details
FAK1_MOUSEDOC_WW_Pin1_4907912Phosphorylation 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
FCG2B_HUMANLIG_TYR_ITIM290295Phosphorylation 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
KI3L2_HUMANLIG_TYR_ITIM396401Phosphorylation of Y398 in the ITIM motif of Killer cell immunoglobulin-like receptor 3DL2 (KIR3DL2) induces binding of Tyrosine-protein phosphatase non-receptor type 6 (PTPN6) via one of its SH2 domains.
details
SLAF1_HUMANLIG_TYR_ITSM277284Phosphorylation 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
SLAF1_HUMANLIG_TYR_ITSM323330Phosphorylation 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
IRS1_RATLIG_SH2_GRB2895898Phosphorylation 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
MYC_HUMANLIG_SH3_26065Phosphorylation 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
SWI6_YEASTTRG_NLS_MonoExtN_4161167Phosphorylation of S160 adjacent to the NLS of Regulatory protein SWI6 (SWI6) decreases nuclear import of this protein by decreasing the affinity for Importin subunit alpha (SRP1).
details
PHO4_YEASTTRG_NLS_MonoExtC_3156161Phosphorylation 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
TIF1B_MOUSELIG_HP1_1486490Phosphorylation 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
MPIP3_HUMANTRG_NES_CRM1_1189203Phosphorylation 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
HIF1A_HUMANLIG_TAZ1792795Under 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
PTHR_HUMANTRG_NLS_Bipartite_1124144Phosphorylation 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
RAF1_HUMANLIG_14-3-3_1256261Phosphorylation of S257 in the 14-3-3-binding motif of RAF proto-oncogene serine/threonine-protein kinase (RAF1) abolishes binding of the motif, phosphorylated at S259, to 14-3-3 protein zeta/delta (YWHAZ).
details
MPIP2_HUMANLIG_14-3-3_3320325Phosphorylation 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
SNX9_HUMANLIG_Glycolytic_Aldolase165169Phosphorylation of the LC4 region of Sorting nexin-9 (SNX9) abolishes its interaction with Fructose-bisphosphate aldolase A (ALDOA). However, the exact position of the residues that are phosphorylated and regulate binding is not known.
details
PI51C_HUMANLIG_PTB_Talin650653Phosphorylation of S650 in the PTB-binding motif of Phosphatidylinositol-4-phosphate 5-kinase type-1 gamma (PIP5K1C) blocks its interaction with Talin-1 (TLN1). Phosphorylation of Y649 by Src kinase enhances the interaction, possibly indirectly by inhibiting S650 phosphorylation.
details
CASP3_HUMANCLV_C14_caspase-8-10172175Phosphorylation 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
PTEN_HUMANCLV_C14_Caspase3-7381385Phosphorylation 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
NMDZ1_HUMANTRG_ER_diArg_1893895Phosphorylation 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
NFAC1_HUMANTRG_NLS_MonoExtN_4262269Phosphorylation 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
PAK1_HUMANLIG_SH3_21318Phosphorylation 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
TAU_HUMANLIG_SH3_3213219Phosphorylation of S210 adjacent to the SH3-binding motif of Isoform Tau-F of Microtubule-associated protein tau (MAPT) inhibits binding to Tyrosine-protein kinase Fyn (Fyn).
details
SDC1_HUMANLIG_PDZ_Class_2305310Phosphorylation of Y309 in the PDZ-binding motif of Syndecan-1 (SDC1) prevents binding to the PDZ domain of Syntenin-1 (SDCBP), an interaction involved in the formation of cellular protrusions.
details
CCG2_MOUSELIG_PDZ_Class_1318323Phosphorylation 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
A4_HUMANLIG_PTB_Apo_2756763Phosphorylation 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
ITB3_HUMANLIG_PTB_Phospho_1779785Phosphorylation of T779 in the PTB-binding motif of Integrin beta-3 (ITGB3) inhibits its interaction with SHC-transforming protein 1 (SHC1).
details
KIF2C_HUMANLIG_SxIP_EBH_193104Phosphorylation 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
CLAP2_HUMANLIG_SxIP_EBH_1515525Phosphorylation 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
DP13A_HUMANLIG_RhoGAP_OCRL_1403415Phosphorylation of S403 in the RhoGAP-binding motif of DCC-interacting protein 13-alpha (APPL1), possibly by PKA, inhibits its interaction with Inositol polyphosphate 5-phosphatase OCRL-1 (OCRL).
details
DP13A_HUMANLIG_RhoGAP_OCRL_1403415Phosphorylation 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
IRK4_HUMANLIG_PDZ_Class_1440445Phosphorylation 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
ADRB2_HUMANLIG_PDZ_Class_1408413Phosphorylation 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
BCR_HUMANLIG_PDZ_Class_112661271Phosphorylation of T1269 in the PDZ-binding motif of Breakpoint cluster region protein (BCR) inhibits its interaction with the Afadin (MLLT4) protein.
details
YAP1_MOUSELIG_14-3-3_1109114Phosphorylation of S112 in the 14-3-3 binding motif of Yorkie homolog (Yap1) induces binding to the 14-3-3 protein epsilon (Ywhae) protein. 14-3-3 retains phosphorylated YAP in the cytosol, negatively regulating its function.
details
A9UF02_HUMANLIG_SH2_IC174180Phosphorylation of Y177 in the SH2-binding motif of BCR/ABL fusion induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.
details
PDPK1_HUMANLIG_SH2_IC376379Phosphorylation of Y376 in the SH2-binding motif of 3-phosphoinositide-dependent protein kinase 1 (PDPK1) induces binding to the Tensin-1 (TNS1) protein.
details
LAT_HUMANLIG_SH2_IC198203Phosphorylation of Y200 in the SH2-binding motif of Linker for activation of T-cells family member 1 (LAT) induces binding to the GRB2-related adaptor protein 2 (Grap2) protein.
details
LAT_HUMANLIG_SH2_IC218223Phosphorylation of Y220 in the SH2-binding motif of Linker for activation of T-cells family member 1 (LAT) induces binding to the GRB2-related adaptor protein 2 (Grap2) protein.
details
LAT_MOUSELIG_SH2_GRB2175178Phosphorylation 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
LAT_MOUSELIG_SH2_GRB2195198Phosphorylation 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
LAT_MOUSELIG_SH2_GRB2235238Phosphorylation 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
DOK2_HUMANLIG_SH2_IC402405Phosphorylation of Y402 in the SH2-binding motif of Docking protein 2 (DOK2) induces binding to the Tensin-1 (TNS1) protein.
details
JAK2_HUMANLIG_SH2_IIB804823Phosphorylation of Y813 in the SH2-binding motif of Tyrosine-protein kinase JAK2 (JAK2) induces binding to the SH2B adapter protein 1 (SH2B1) protein.
details
DAB1_HUMANLIG_SH2_IB211230Phosphorylation of Y220 in the SH2-binding motif of Disabled homolog 1 (DAB1) induces binding to the Adapter molecule crk (CRK) protein.
details
EGFR_HUMANLIG_SH2_IC10921100Phosphorylation 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
EGFR_HUMANLIG_SH2_IE10111020Phosphorylation 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
EGFR_HUMANLIG_SH2_IE11911200Phosphorylation 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
EGFR_HUMANLIG_SH2_IE10081024Phosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Tyrosine-protein kinase JAK1 (JAK1) protein.
details
EGFR_HUMANLIG_SH2_IE10081024Phosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the Tyrosine-protein kinase JAK2 (JAK2) protein.
details
EGFR_HUMANLIG_SH2_ID10081024Phosphorylation 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
EGFR_HUMANLIG_SH2_ID10081024Phosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to the SH2 domain-containing protein 3A (SH2D3A) protein.
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EGFR_HUMANLIG_SH2_III10081024Phosphorylation 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.
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ERBB2_HUMANLIG_SH2_IC11351144Phosphorylation 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.
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ERBB2_HUMANLIG_SH2_IE10151031Phosphorylation 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.
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ERBB2_HUMANLIG_SH2_IE10151031Phosphorylation 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.
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ERBB2_HUMANLIG_SH2_ID11311147Phosphorylation 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.
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ERBB2_HUMANLIG_SH2_ID10151031Phosphorylation 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.
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ERBB2_HUMANLIG_SH2_III11311147Phosphorylation 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.
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NTRK1_HUMANLIG_SH2_IIB782796Phosphorylation 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.
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NTRK1_HUMANLIG_SH2_IB783796Phosphorylation 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.
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RET_HUMANLIG_SH2_IIB976985Phosphorylation 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.
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MET_HUMANLIG_SH2_IC13511360Phosphorylation 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.
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PGFRB_HUMANLIG_SH2_IIA751755Phosphorylation 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.
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PGFRB_HUMANLIG_SH2_IIA10181029Phosphorylation 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.
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GHR_HUMANLIG_SH2_IIA591600Phosphorylation of Y595 in the SH2-binding motif of Growth hormone receptor (GHR) induces binding to the Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) protein.
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GHR_HUMANLIG_SH2_III428444Phosphorylation of Y436 in the SH2-binding motif of Growth hormone receptor (GHR) induces binding to the Signal transducer and activator of transcription 5B (STAT5B) protein.
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IL2RB_HUMANLIG_SH2_IA409428Phosphorylation of Y418 in the SH2-binding motif of Interleukin-2 receptor subunit beta (IL2RB) induces binding to the Tyrosine-protein kinase Lck (LCK) protein.
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IL2RB_HUMANLIG_SH2_III531540Phosphorylation 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.
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IL2RB_HUMANLIG_SH2_IIB361370Phosphorylation of Y364 in the SH2-binding motif of Interleukin-2 receptor subunit beta (IL2RB) induces binding to the SHC-transforming protein 1 (SHC1) protein.
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IL2RB_HUMANLIG_SH2_III528544Phosphorylation 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.
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INGR1_HUMANLIG_SH2_III457461Phosphorylation 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.
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VAV_HUMANLIG_SH2_IIB165180Phosphorylation of Y174 in the SH2-binding motif of Proto-oncogene vav (VAV1) induces binding to the SH2 domain-containing adapter protein B (SHB) protein.
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PGFRA_HUMANLIG_SH2_IIB705729Phosphorylation of Y720 in the SH2-binding motif of Platelet-derived growth factor receptor alpha (PDGFRA) induces binding to the SH2 domain-containing adapter protein F (SHF) protein.
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INAR1_HUMANLIG_SH2_IE458474Phosphorylation 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.
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INAR1_HUMANLIG_SH2_IE473489Phosphorylation 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.
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EPOR_HUMANLIG_SH2_III360376Phosphorylation of Y368 in the SH2-binding motif of Erythropoietin receptor (EPOR) induces binding to the Signal transducer and activator of transcription 5B (STAT5B) protein.
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EPOR_HUMANLIG_SH2_III418434Phosphorylation of Y426 in the SH2-binding motif of Erythropoietin receptor (EPOR) induces binding to the Signal transducer and activator of transcription 5B (STAT5B) protein.
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EPOR_HUMANLIG_SH2_III496508Phosphorylation of Y504 in the SH2-binding motif of Erythropoietin receptor (EPOR) induces binding to the Signal transducer and activator of transcription 5B (STAT5B) protein.
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ERBB3_HUMANLIG_SH2_ID860876Phosphorylation of Y868 in the SH2-binding motif of Receptor tyrosine-protein kinase erbB-3 (ERBB3) induces binding to the Breast cancer anti-estrogen resistance protein 3 (BCAR3) protein.
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ERBB3_HUMANLIG_SH2_ID12681284Phosphorylation of Y1276 in the SH2-binding motif of Receptor tyrosine-protein kinase erbB-3 (ERBB3) induces binding to the Breast cancer anti-estrogen resistance protein 3 (BCAR3) protein.
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ERBB3_HUMANLIG_SH2_ID12811297Phosphorylation of Y1289 in the SH2-binding motif of Receptor tyrosine-protein kinase erbB-3 (ERBB3) induces binding to the Breast cancer anti-estrogen resistance protein 3 (BCAR3) protein.
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ERBB3_HUMANLIG_SH2_ID13201336Phosphorylation of Y1328 in the SH2-binding motif of Receptor tyrosine-protein kinase erbB-3 (ERBB3) induces binding to the Breast cancer anti-estrogen resistance protein 3 (BCAR3) protein.
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ERBB3_HUMANLIG_SH2_ID13201336Phosphorylation of Y1328 in the SH2-binding motif of Receptor tyrosine-protein kinase erbB-3 (ERBB3) induces binding to the SH2 domain-containing protein 3A (SH2D3A) protein.
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ERBB3_HUMANLIG_SH2_III13201336Phosphorylation of Y1328 in the SH2-binding motif of Receptor tyrosine-protein kinase erbB-3 (ERBB3) induces binding to the Signal transducer and activator of transcription 6 (STAT6) protein.
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CBL_HUMANLIG_SH2_IB770780Phosphorylation of Y774 in the SH2-binding motif of E3 ubiquitin-protein ligase CBL (CBL) induces binding to the Adapter molecule crk (CRK) protein.
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IL4RA_HUMANLIG_SH2_III566585Phosphorylation of Y575 in the SH2-binding motif of Interleukin-4 receptor subunit alpha (IL4R) induces binding to the Signal transducer and activator of transcription 6 (STAT6) protein.
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IL4RA_HUMANLIG_SH2_III594613Phosphorylation of Y603 in the SH2-binding motif of Interleukin-4 receptor subunit alpha (IL4R) induces binding to the Signal transducer and activator of transcription 6 (STAT6) protein.
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IL4RA_HUMANLIG_SH2_III622641Phosphorylation of Y631 in the SH2-binding motif of Interleukin-4 receptor subunit alpha (IL4R) induces binding to the Signal transducer and activator of transcription 6 (STAT6) protein.
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IL4RA_HUMANLIG_SH2_IIA706721Phosphorylation of Y713 in the SH2-binding motif of Interleukin-4 receptor subunit alpha (IL4R) induces binding to the Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) protein.
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IL4RA_HUMANLIG_SH2_IIB706721Phosphorylation of Y713 in the SH2-binding motif of Interleukin-4 receptor subunit alpha (IL4R) induces binding to the SHC-transforming protein 1 (SHC1) protein.
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IL4RA_HUMANLIG_SH2_IIB706721Phosphorylation of Y713 in the SH2-binding motif of Interleukin-4 receptor subunit alpha (IL4R) induces binding to the Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 1 (INPP5D) protein.
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EPHA3_HUMANLIG_SH2_IA597606Phosphorylation of Y602 in the SH2-binding motif of Ephrin type-A receptor 3 (EPHA3) induces binding to the Cytoplasmic protein NCK1 (NCK1) protein.
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SHC1_HUMANLIG_SH2_IC423435Phosphorylation 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.
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FCERG_HUMANLIG_SH2_IA7579Phosphorylation of Y76 in the SH2-binding motif of High affinity immunoglobulin epsilon receptor subunit gamma (FCER1G) induces binding to the Tyrosine-protein kinase SYK (SYK) protein.
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FRS2_HUMANLIG_SH2_IC191200Phosphorylation of Y196 in the SH2-binding motif of Fibroblast growth factor receptor substrate 2 (FRS2) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.
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FRS2_HUMANLIG_SH2_IC301310Phosphorylation of Y306 in the SH2-binding motif of Fibroblast growth factor receptor substrate 2 (FRS2) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.
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FRS2_HUMANLIG_SH2_IC345355Phosphorylation of Y349 in the SH2-binding motif of Fibroblast growth factor receptor substrate 2 (FRS2) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.
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FRS2_HUMANLIG_SH2_IC385395Phosphorylation of Y392 in the SH2-binding motif of Fibroblast growth factor receptor substrate 2 (FRS2) induces binding to the Growth factor receptor-bound protein 2 (GRB2) protein.
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FRS2_HUMANLIG_SH2_IIA431440Phosphorylation of Y436 in the SH2-binding motif of Fibroblast growth factor receptor substrate 2 (FRS2) induces binding to the Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) protein.
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FRS2_HUMANLIG_SH2_IIA465475Phosphorylation of Y471 in the SH2-binding motif of Fibroblast growth factor receptor substrate 2 (FRS2) induces binding to the Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) protein.
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M4K1_HUMANLIG_SH2_IIB372391Phosphorylation 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.
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CSF3R_HUMANLIG_SH2_IIA747758Phosphorylation of Y752 in the SH2-binding motif of Granulocyte colony-stimulating factor receptor (CSF3R) induces binding to the Suppressor of cytokine signaling 3 (SOCS3) protein.
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DOK1_HUMANLIG_SH2_IIB203206Phosphorylation of Y203 in the SH2-binding motif of Docking protein 1 (DOK1) induces binding to the Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 1 (INPP5D) protein.
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DOK1_HUMANLIG_SH2_IB447454Phosphorylation of Y449 in the SH2-binding motif of Docking protein 1 (DOK1) induces binding to the SH2 domain-containing protein 1A (SH2D1A) protein.
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FAK1_HUMANLIG_SH2_IA389405Phosphorylation of Y397 in the SH2-binding motif of Focal adhesion kinase 1 (PTK2) induces binding to the Cytoplasmic protein NCK2 (NCK2) protein.
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LCP2_HUMANLIG_SH2_IIB105118Phosphorylation 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.
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LCP2_HUMANLIG_SH2_IIB120133Phosphorylation 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.
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LCP2_HUMANLIG_SH2_IIB137150Phosphorylation 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.
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SLAF1_HUMANLIG_SH2_IB276286Phosphorylation of Y281 in the SH2-binding motif of Signaling lymphocytic activation molecule (SLAMF1) induces binding to the SH2 domain-containing protein 1A (SH2D1A) protein.
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SLAF1_HUMANLIG_SH2_IB273286Phosphorylation of Y281 in the SH2-binding motif of Signaling lymphocytic activation molecule (SLAMF1) induces binding to the SH2 domain-containing protein 1B (Sh2d1b) protein.
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FAK2_HUMANLIG_SH2_IB394410Phosphorylation 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.
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NTRK2_HUMANLIG_SH2_IA714730Phosphorylation of Y727 in the SH2-binding motif of BDNF/NT-3 growth factors receptor (NTRK2) induces binding to the Cytoplasmic protein NCK2 (NCK2) protein.
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LCP2_MOUSELIG_SH2_IA143148Phosphorylation of Y145 in the SH2-binding motif of Lymphocyte cytosolic protein 2 (Lcp2) induces binding to the Tyrosine-protein kinase ITK/TSK (Itk) protein.
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JAK2_MOUSELIG_SH2_III804820Phosphorylation 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.
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BCAR1_HUMANLIG_SH2_IB358368Phosphorylation of Y362 in the SH2-binding motif of Breast cancer anti-estrogen resistance protein 1 (BCAR1) induces binding to the Adapter molecule crk (CRK) protein.
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GBLP_RATLIG_SH2_IA241250Phosphorylation of Y246 in the SH2-binding motif of Guanine nucleotide-binding protein subunit beta-2-like 1 (Gnb2l1) induces binding to the Proto-oncogene tyrosine-protein kinase Src (SRC) protein.
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DCD_HUMANLIG_SH2_IA1525Phosphorylation of Y20 in the SH2-binding motif of Dermcidin (DCD) induces binding to the Cytoplasmic protein NCK1 (NCK1) protein.
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DAB1_MOUSELIG_SH2_IA212228Phosphorylation of Y220 in the SH2-binding motif of Disabled homolog 1 (Dab1) induces binding to the Cytoplasmic protein NCK2 (NCK2) protein.
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IL6RB_MOUSELIG_SH2_IIA750764Phosphorylation of Y757 in the SH2-binding motif of Interleukin-6 receptor subunit beta (Il6st) induces binding to the Suppressor of cytokine signaling 3 (Socs3) protein.
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STA5A_HUMANLIG_SH2_III686702Phosphorylation 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.
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ZAP70_HUMANLIG_SH2_IIC284300Phosphorylation 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.
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KSYK_HUMANLIG_SH2_IIC315331Phosphorylation of Y323 in the SH2-binding motif of Tyrosine-protein kinase SYK (SYK) induces binding to the E3 ubiquitin-protein ligase CBL-B (CBLB) protein.
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EPHB2_MOUSELIG_SH2_IB601610Phosphorylation of Y604 in the SH2-binding motif of Ephrin type-B receptor 2 (Ephb2) induces binding to the Adapter molecule crk (CRK) protein.
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EPHB2_MOUSELIG_SH2_IB606620Phosphorylation of Y610 in the SH2-binding motif of Ephrin type-B receptor 2 (Ephb2) induces binding to the Adapter molecule crk (CRK) protein.
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LEPR_MOUSELIG_SH2_III11291148Phosphorylation of Y1138 in the SH2-binding motif of Leptin receptor (Lepr) induces binding to the Signal transducer and activator of transcription 3 (STAT3) protein.
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ERBB3_HUMANLIG_SH2_IE13201336Phosphorylation of Y1328 in the SH2-binding motif of Receptor tyrosine-protein kinase erbB-3 (ERBB3) induces binding to the Tyrosine-protein kinase JAK1 (JAK1) protein.
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ERBB3_HUMANLIG_SH2_IE13201336Phosphorylation of Y1328 in the SH2-binding motif of Receptor tyrosine-protein kinase erbB-3 (ERBB3) induces binding to the Tyrosine-protein kinase JAK2 (JAK2) protein.
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ERBB3_HUMANLIG_SH2_IE12681284Phosphorylation of Y1276 in the SH2-binding motif of Receptor tyrosine-protein kinase erbB-3 (ERBB3) induces binding to the Tyrosine-protein kinase JAK2 (JAK2) protein.
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ERBB3_HUMANLIG_SH2_IE12681284Phosphorylation of Y1276 in the SH2-binding motif of Receptor tyrosine-protein kinase erbB-3 (ERBB3) induces binding to the Tyrosine-protein kinase JAK3 (JAK3) protein.
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IL4RA_HUMANLIG_SH2_IIA706721Phosphorylation of Y713 in the SH2-binding motif of Interleukin-4 receptor subunit alpha (IL4R) induces binding to the Tyrosine-protein phosphatase non-receptor type 6 (PTPN6) protein.
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P53_HUMANDEG_MDM2_11926Phosphorylation 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.
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L1CAM_HUMANTRG_ENDOCYTIC_211761179Phosphorylation 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).
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B2L11_HUMANLIG_Dynein_DLC8_15056Phosphorylation 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.
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CASP9_HUMANLIG_BIR_III_2315319Binding of the BIR domain-binding motif of Caspase-9 (CASP9) to the BIR domains of Baculoviral IAP repeat-containing protein 4 (XIAP) requires cleavage of Caspase-9 (CASP9) at D315, since this results in a functional neo N-terminal motif. BIR domains are found in Inhibitor of Apoptosis Proteins (IAPs) that suppress the activity of activated caspases, either by directly inhibiting caspase catalytic activity, or by targeting caspases for degradation by ubiquitin modification.
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CASP9_HUMANLIG_BIR_III_2315319Binding of the BIR domain-binding motif of Caspase-9 (CASP9) to the BIR domains of Baculoviral IAP repeat-containing protein 2 (BIRC2) requires cleavage of Caspase-9 (CASP9) at D315, since this results in a functional neo N-terminal motif. BIR domains are found in Inhibitor of Apoptosis Proteins (IAPs) that suppress the activity of activated caspases, either by directly inhibiting caspase catalytic activity, or by targeting caspases for degradation by ubiquitin modification.
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CASP7_HUMANLIG_BIR_III_22327Binding of the BIR domain-binding motif of Caspase-7 (CASP7) to the BIR domains of Baculoviral IAP repeat-containing protein 2 (BIRC2) requires cleavage of Caspase-7 (CASP7) at D23, since this results in a functional neo N-terminal motif. BIR domains are found in Inhibitor of Apoptosis Proteins (IAPs) that suppress the activity of activated caspases, either by directly inhibiting caspase catalytic activity, or by targeting caspases for degradation by ubiquitin modification.
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CASP1_DROMELIG_BIR_III_43337Binding of the BIR domain-binding motif of Caspase-1 (Dcp-1) to the BIR domains of Apoptosis 1 inhibitor (th) requires cleavage of Caspase-1 (Dcp-1) at D33, since this results in a functional neo N-terminal motif. BIR domains are found in Inhibitor of Apoptosis Proteins (IAPs) that suppress the activity of activated caspases, either by directly inhibiting caspase catalytic activity, or by targeting caspases for degradation by ubiquitin modification.
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ICE_DROMELIG_BIR_III_42832Binding of the BIR domain-binding motif of Caspase (Ice) to the BIR domains of Apoptosis 1 inhibitor (th) requires cleavage of Caspase (Ice) at D28, since this results in a functional neo N-terminal motif. BIR domains are found in Inhibitor of Apoptosis Proteins (IAPs) that suppress the activity of activated caspases, either by directly inhibiting caspase catalytic activity, or by targeting caspases for degradation by ubiquitin modification.
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HSF4_HUMANMOD_SUMO292295The phosphorylation-dependent sumoylation of the PDSM (phosphorylation-dependent sumoylation motif) strongly represses Isoform HSF4B of Heat shock factor protein 4 (HSF4) activity.
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WWTR1_HUMANLIG_14-3-3_18691Phosphorylation of S89 in the 14-3-3-binding motif of WW domain-containing transcription regulator protein 1 (WWTR1) induces binding to 14-3-3 protein epsilon (YWHAE), retaining phosphorylated WWTR1 in the cytosol, negatively regulating its function.
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PI51C_MOUSELIG_PTB_Talin645648Phosphorylation 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).
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PI51C_MOUSELIG_PTB_Talin645648Phosphorylation of Y644 in Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma (Pip5k1c) promotes its association with Talin-1 (Tln1).
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PI51C_MOUSETRG_AP2beta_CARGO_2633644Phosphorylation 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.
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PIAS1_HUMANLIG_SUMO_SBM_1457461Phosphorylation 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).
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PI51C_HUMANTRG_ENDOCYTIC_2649652Phosphorylation 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).
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DAB1_MOUSELIG_SH2_IA232235Phosphorylation of Y232 in the SH2-binding motif of Disabled homolog 1 (Dab1) induces binding to Cytoplasmic protein NCK2 (NCK2).
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DAB1_MOUSELIG_SH2_IA232235Phosphorylation of Y232 in the SH2-binding motif of Disabled homolog 1 (Dab1) induces binding to Adapter molecule crk (Crk).
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DAB1_MOUSELIG_SH2_IA185188Phosphorylation of Y185 in the SH2-binding motif of Disabled homolog 1 (Dab1) induces binding to Neuronal proto-oncogene tyrosine-protein kinase Src (Src).
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DAB1_MOUSELIG_SH2_SRC198201Phosphorylation of Y198 in the SH2-binding motif of Disabled homolog 1 (Dab1) induces binding to Neuronal proto-oncogene tyrosine-protein kinase Src (Src).
details
Y1827_MYCTULIG_FHA_12026Phosphorylation 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).
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CASP7_HUMANLIG_BIR_III_22327Binding of the BIR domain-binding motif of Caspase-7 (CASP7) to the BIR domains of Baculoviral IAP repeat-containing protein 2 (BIRC2) requires cleavage of Caspase-7 (CASP7) at D23, since this results in a functional neo N-terminal motif. BIR domains are found in Inhibitor of Apoptosis Proteins (IAPs) that suppress the activity of activated caspases, either by directly inhibiting caspase catalytic activity, or by targeting caspases for degradation by ubiquitin modification.
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CASP7_HUMANLIG_BIR_III_22327Binding of the BIR domain-binding motif of Caspase-7 (CASP7) to the BIR domains of Baculoviral IAP repeat-containing protein 2 (BIRC2) requires cleavage of Caspase-7 (CASP7) at D23, since this results in a functional neo N-terminal motif. BIR domains are found in Inhibitor of Apoptosis Proteins (IAPs) that suppress the activity of activated caspases, either by directly inhibiting caspase catalytic activity, or by targeting caspases for degradation by ubiquitin modification.
details
FBXW7_HUMANDOC_WW_Pin1_4202207Phosphorylation 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.
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PIAS1_HUMANLIG_SUMO_SBM_1457461Acetylation of K33 in Small ubiquitin-related modifier 2 (SUMO2) inhibits binding to E3 SUMO-protein ligase PIAS1 (PIAS1). The acetylation counters SUMO-SIM-dependent transcriptional repression processes. An additional interaction is also possible upon acetylation with the Bromodomain of p300 shown to bind the acetylated version of SUMO2. This does not occur with acetylated SUMO1. Acetylation is countered by Histone deacetylase family, HD type 1 subfamily.
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PIAS1_HUMANLIG_SUMO_SBM_1457461Acetylation of K37 in Small ubiquitin-related modifier 1 (SUMO1) inhibits binding to E3 SUMO-protein ligase PIAS1 (PIAS1). The acetylation counters SUMO-SIM-dependent transcriptional repression processes. Acetylation is countered by Histone deacetylase family, HD type 1 subfamily.
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PIAS2_HUMANLIG_SUMO_SBM_1467471Acetylation of K33 in Small ubiquitin-related modifier 2 (SUMO2) inhibits binding to E3 SUMO-protein ligase PIAS2 (PIAS2). The acetylation counters SUMO-SIM-dependent transcriptional repression processes. An additional interaction is also possible upon acetylation with the Bromodomain of p300 shown to bind the acetylated version of SUMO2. This does not occur with acetylated SUMO1. Acetylation is countered by Histone deacetylase family, HD type 1 subfamily.
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PIAS2_HUMANLIG_SUMO_SBM_1467471Acetylation of K37 in Small ubiquitin-related modifier 1 (SUMO1) inhibits binding to E3 SUMO-protein ligase PIAS2 (PIAS2). The acetylation counters SUMO-SIM-dependent transcriptional repression processes. Acetylation is countered by Histone deacetylase family, HD type 1 subfamily.
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ESR2_HUMANMOD_GSK3_1512The GSK3-beta binding site at S12 in Estrogen receptor beta (ESR2) is primed by (most likely) RAC-alpha serine/threonine-protein kinase (AKT1). This enhances the binding of SUMO-conjugating enzyme UBC9 (UBE2I) at the adjacent Sumoylation site. This site is also primed at S6 (most likely) by AKT1. The addition of SUMO at K4 stabilises ESR2 as it prevents the ubiquitination at K4 (see switch details
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ESR2_HUMANMOD_SUMO_PHOS47The GSK3-beta binding site at S12 in Estrogen receptor beta (ESR2) is primed by (most likely) RAC-alpha serine/threonine-protein kinase (AKT1). This enhances the binding of SUMO-conjugating enzyme UBC9 (UBE2I) at the adjacent Sumoylation site. This site is also primed at S6 (most likely) by AKT1. The addition of SUMO at K4 stabilises ESR2 as it prevents the ubiquitination at K4 (see switch details)
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ESR2_HUMANMOD_SUMO_PHOS47Sumoylation of K4 in Estrogen receptor beta (ESR2) is inhibited by ubiquitination K4. This destabilises ESR2 increasing its turnover (see also switch details)
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SKP2_HUMANTRG_NLS_MonoExtN_46572Acetylation 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.
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SKP2_HUMANTRG_NLS_MonoExtN_46572Acetylation 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.
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NEB1_RATDOC_PP1455461Phosphorylation 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.
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PGFRB_HUMANLIG_PDZ_Class_111011106Phosphorylation 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.
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AMPH_HUMANLIG_Clathr_ClatBox_1351355Phosphorylation 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).
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AMPH_HUMANLIG_Clathr_ClatBox_2380385Phosphorylation 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).
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DPOD3_HUMANLIG_PCNA_PIPBox_1456465Phosphorylation 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.
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L1CAM_HUMANTRG_ENDOCYTIC_211761179Phosphorylation 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).
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MDM4_HUMANDOC_USP7_1398402Phosphorylation 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.
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AKA12_MOUSEDOC_CYCLIN_1501504Phosphorylation 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.
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JUN_MOUSELIG_WW_1167170Phosphorylation 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.
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CDN1A_HUMANLIG_PCNA_PIPBox_1144153Phosphorylation 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.
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CDN1A_HUMANLIG_PCNA_PIPBox_1144153Phosphorylation 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.
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4EBP1_HUMANLIG_eIF4E_15460Phosphorylation 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.
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BAD_MOUSELIG_14-3-3_1133138Phosphorylation 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).
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EGFR_HUMANLIG_SH2_SRC10161019Phosphorylation 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).
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EGFR_HUMANLIG_SH2_SRC11251128Phosphorylation of Y1125 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to Adapter molecule crk (CRK).
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EGFR_HUMANLIG_SH2_SRC10161019Phosphorylation of Y1016 in the SH2-binding motif of Epidermal growth factor receptor (EGFR) induces binding to Cytoplasmic protein NCK1 (NCK1).
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ERBB3_HUMANLIG_SH2_GRB212621265Phosphorylation of Y1262 in the SH2-binding motif of Receptor tyrosine-protein kinase erbB-3 (ERBB3) induces binding to Growth factor receptor-bound protein 2 (GRB2).
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FAK1_HUMANLIG_SH2_SRC397400Phosphorylation of Y397 in the SH2-binding motif of Focal adhesion kinase 1 (PTK2) induces binding to Neuronal proto-oncogene tyrosine-protein kinase Src (Src).
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GAB1_HUMANLIG_SH2_STAT5472475Phosphorylation of Y472 in the SH2-binding motif of GRB2-associated-binding protein 1 (GAB1) induces binding to Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1).
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GAB1_HUMANLIG_SH2_STAT5447450Phosphorylation of Y447 in the SH2-binding motif of GRB2-associated-binding protein 1 (GAB1) induces binding to Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1).
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DAXX_HUMANLIG_SUMO_SBM_1733740Acetylation of K37 in the SUMO1 inhibits binding to the Small ubiquitin-related modifier 1 (SUMO1) protein see switch details. SUMO-modified forms of Protein PML (PML) are essential for the recruitment of DAXX to PML nuclear bodies. The acetylated versions of SUMO1/2 failed to trigger recruitment of DAXX into the nuclear bodies. Acetylation is countered by Histone deacetylase family, HD type 1 subfamily.
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ACE2_YEASTTRG_NES122150Phosphorylation 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.
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ACE2_YEASTTRG_NES122150Phosphorylation 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.
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Type: Binary Subtype: Pre‑translational
Pre-translational mechanisms such as alternative splicing, alternative promoter-usage and/or RNA editing result in inclusion or removal of exons that contain an entire or partial motif.
AMOT_HUMANLIG_WW_1239242Alternative 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.
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AMOT_HUMANLIG_WW_1239242Alternative 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.
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DYN1_HUMANDOC_PP2B_1844849Alternative splicing removes the PP2B-binding motif of Isoform 3 of Dynamin-1 (DNM1), abrogating binding to Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform (PPP3CA). This splice-specific motif in Isoform 3 of Dynamin-1 (DNM1) allows the docking of calcineurin phosphatase. The dephosphorylation of DNM1 by calcineurin, upon NGF stimulation, promotes the internalisation of the High affinity nerve growth factor receptor (NTRK1) (TrkA).
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ADA22_HUMANLIG_PDZ_Class_1901906Alternative splicing removes the PDZ-binding motif of Disintegrin and metalloproteinase domain-containing protein 22 (ADAM22), abrogating binding to Disks large homolog 4 (DLG4). The motif-containing Isoform Epsilon of Disintegrin and metalloproteinase domain-containing protein 22 (ADAM22) forms part of a complex containing Leucine-rich glioma-inactivated protein 1 (LGI1), AMPA-R (e.g. Glutamate receptor 1 (GRIA1)) and AMPA-R regulatory proteins (e.g. Voltage-dependent calcium channel gamma-2 subunit (CACNG2)), and is closely associated with epilepsy.
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MPIP2_HUMANDEG_APCC_KENBOX_2191195Alternative splicing removes the APC/C KEN-box degron motif of M-phase inducer phosphatase 2 (CDC25B), abrogating binding to Fizzy-related protein homolog (FZR1). The motif-lacking Isoform CDC25B2 of M-phase inducer phosphatase 2 (CDC25B) is not degraded during mitosis, unlike other isoforms.
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NEK2_HUMANDOC_PP1380387Alternative splicing removes the PP1-docking motif of Serine/threonine-protein kinase Nek2 (NEK2), abrogating binding to Serine/threonine-protein phosphatase PP1-gamma catalytic subunit (PPP1CC). Isoform Nek2A of Serine/threonine-protein kinase Nek2 (NEK2) is localised at centrosomes and causes centrosome splitting. Isoform Nek2B of Serine/threonine-protein kinase Nek2 (NEK2) is expressed at a different point in the cell cycle and is required for assembly/maintenance of centrosomes.
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NEK2_HUMANDOC_PP1380387Alternative splicing removes the PP1-docking motif of Serine/threonine-protein kinase Nek2 (NEK2), abrogating binding to Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (PPP1CA). Isoform Nek2A of Serine/threonine-protein kinase Nek2 (NEK2) is localised at centrosomes and causes centrosome splitting. Isoform Nek2B of Serine/threonine-protein kinase Nek2 (NEK2) is expressed at a different point in the cell cycle and required for assembly/maintenance of centrosomes.
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NEK2_HUMANDEG_APCC_DBOX_3423445Alternative splicing removes the extended D-box degron motif of Serine/threonine-protein kinase Nek2 (NEK2), abrogating binding to Cell division cycle protein 20 homolog (CDC20). NEK2-A is targeted by APC/C-Cdc20 in early mitosis whereas Isoform Nek2B of Serine/threonine-protein kinase Nek2 (NEK2) persists into late mitosis. Degradation of Isoform Nek2A of Serine/threonine-protein kinase Nek2 (NEK2) may be necessary to allow re-establishment of the intercentriolar linkage in late mitosis.
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B2L11_HUMANDEG_SCF_TRCP1_29398Alternative splicing removes the extended SCF-TrCP degron motif of Bcl-2-like protein 11 (BCL2L11), abrogating binding to F-box/WD repeat-containing protein 1A (BTRC). Upon mitogen survival signals, RPS6KA1 and RPS6KA2 kinases are up-regulated and rapidly phosphorylate the three serines of Isoform Bim(EL) of Bcl-2-like protein 11 (BCL2L11). This facilitates the binding of betaTrCP and subsequent ubiquitination and degradation of Isoform Bim(EL) of Bcl-2-like protein 11 (BCL2L11).
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CACP_HUMANTRG_MLS121Alternative splicing removes the mitochondrial localisation signal (MLS) motif of Carnitine O-acetyltransferase (CRAT), abrogating binding to Mitochondrial import receptor subunit TOM70 (TOMM70A). As a result, Isoform SM-1200 of Carnitine O-acetyltransferase (CRAT), which lacks the MLS, is located in peroxisomes due to a PTS1 motif in its C-terminus.
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ITB1_HUMANLIG_Talin775785Alternative splicing alters the flanking regions of the PTB-binding motif of Isoform Beta-1D of Integrin beta-1 (ITGB1), inducing higher affinity binding to Talin-1 (TLN1). Alteration of residue 788 from G to Q and alteration of residue 786 from A to P increases the binding affinity from 491 micromolar in the canonical Isoform Beta-1A of Integrin beta-1 (ITGB1) to 95 micromolar in Isoform Beta-1D of Integrin beta-1 (ITGB1).
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ITB1_HUMANLIG_Talin775785Alternative splicing alters the flanking regions of the PTB-binding motif of Isoform Beta-1D of Integrin beta-1 (ITGB1), inducing higher affinity binding to Talin-2 (TLN2). The alteration of residue 788 from G to Q and alteration of residue 786 from A to P increases the binding affinity from 652 micromolar in the canonical Isoform Beta-1A of Integrin beta-1 (ITGB1) to 36 micromolar in Isoform Beta-1D of Integrin beta-1 (ITGB1).
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ITB1_HUMANLIG_Filamin_2783791Alternative splicing strongly inhibits the binding of the filamin-binding motif of Integrin beta-1 (ITGB1) to Filamin-A (FLNA), primarily due to the alteration of A to P it seems.
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ITB1_HUMANLIG_Filamin_2783791Alternative splicing strongly inhibits the binding of the filamin-binding motif of Integrin beta-1 (ITGB1) to Filamin-B (FLNB), primarily due to the alteration of A to P it seems. Splicing of FLNB also affects this interaction.
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BIN1_HUMANLIG_Clathr_ClatBox_1390394Alternative splicing removes the Clathrin I-binding motif of Myc box-dependent-interacting protein 1 (BIN1), abrogating binding to Clathrin heavy chain 1 (CLTC).
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BIN1_HUMANLIG_Clathr_ClatBox_2415420Alternative splicing removes the Clathrin II-binding motif of Myc box-dependent-interacting protein 1 (BIN1), abrogating binding to Clathrin heavy chain 1 (CLTC).
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BIN1_HUMANLIG_SH3_8265268Alternative splicing removes the SH3-binding motif of Isoform BIN1 of Myc box-dependent-interacting protein 1 (BIN1), abrogating binding to the SH3 domain of Isoform BIN1 of Myc box-dependent-interacting protein 1 (BIN1). Splice-specific motifs in Isoform BIN1 of Myc box-dependent-interacting protein 1 (BIN1) engage in an intra-molecular interaction with its own SH3 domain. Auto-inhibition is relieved at the plasma membrane when an overlapping lipid-binding motif outcompetes the SH3-binding motif. This means that the SH3 domain is only available for inter-molecular interactions at the plasma membrane.
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BIN1_HUMANLIG_PI(4,5)P2258266Alternative splicing removes the PI(4,5)P2-binding motif of Isoform BIN1 of Myc box-dependent-interacting protein 1 (BIN1), abrogating binding to 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate. Splice-specific motifs in Isoform BIN1 of Myc box-dependent-interacting protein 1 (BIN1) engage in an intra-molecular interaction with its own SH3 domain. Auto-inhibition is relieved at the plasma membrane when an overlapping lipid-binding motif outcompetes the SH3-binding motif. This means that the SH3 domain is only available for inter-molecular interactions at the plasma membrane.
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TRXR1_HUMANLIG_NRBOX4652Alternative splicing removes the NRBOX motif of Isoform TXNRD1_v2 of Thioredoxin reductase 1, cytoplasmic (TXNRD1), abrogating binding to Estrogen receptor (ESR1). Unlike splice variants without the NRBOX motif, TrxR1b (also known as Isoform TXNRD1_v2 of Thioredoxin reductase 1, cytoplasmic (TXNRD1)) is identified within the nucleus. TrxR1b enhanced the transcriptional activity of the estrogen receptors ESR1 and ESR2, possibly by providing a reduced environment in the immediate vicinity of the ERs.
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TRXR1_HUMANLIG_NRBOX4652Alternative splicing removes the NRBOX motif of Isoform TXNRD1_v2 of Thioredoxin reductase 1, cytoplasmic (TXNRD1), abrogating binding to Estrogen receptor beta (ESR2). Unlike splice variants without the NRBOX motif, TrxR1b (also known as Isoform TXNRD1_v2 of Thioredoxin reductase 1, cytoplasmic (TXNRD1)) is identified within the nucleus. TrxR1b enhanced the transcriptional activity of the estrogen receptors ESR1 and ESR2, possibly by providing a reduced environment in the immediate vicinity of the ERs.
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AT2B2_HUMANLIG_PDZ_Class_112381243Alternative splicing removes the PDZ-binding motif of Plasma membrane calcium-transporting ATPase 2 (ATP2B2), abrogating binding to Na(+)/H(+) exchange regulatory cofactor NHE-RF2 (SLC9A3R2), altering the location of this Ca2+ pump. Despite the similarity in C-terminal between the 'b' splice variants of Plasma membrane calcium-transporting ATPase 4 (ATP2B4) (-ETSV) and Plasma membrane calcium-transporting ATPase 2 (ATP2B2) (-ETSL), 'b' splice variants of ATP2B4 did not interact with either of the NHERFs whereas PMCA2b selectively preferred Na(+)/H(+) exchange regulatory cofactor NHE-RF2 (SLC9A3R2) over Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (SLC9A3R1). NHERFs have been previously implicated in the targeting, retention and regulation of membrane proteins including the ╬▓2-adrenergic receptor, cystic fibrosis transmembrane conductance regulator, and Trp4 Ca2+channel. This study suggests Plasma membrane calcium-transporting ATPase 2 (ATP2B2) may be under similar regulation.
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AT2B4_HUMANLIG_PDZ_Class_112361241Alternative splicing removes the PDZ-binding motif of Plasma membrane calcium-transporting ATPase 4 (ATP2B4), abrogating binding to Nitric oxide synthase, brain (NOS1). PMCA4b acts as a negative regulator of Nitric oxide synthase, brain (NOS1), reducing production of nitric oxide in heart tissue. This negative regulation was not dependent on a conformational change due to binding of the PDZ ligand, but on Ca2+ depletion in close proximity of the enzyme. Nitric oxide production by NOS1 is known to be important in the regulation of excitation-contraction (EC) coupling and subsequently contractility.
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AT2B4_HUMANLIG_PDZ_Class_112361241Alternative splicing removes the PDZ-binding motif of Plasma membrane calcium-transporting ATPase 4 (ATP2B4), abrogating binding to Disks large homolog 3 (DLG3). Disks large homolog 3 (DLG3) did not bind to 'b' isoform of PMCA2. There is therefore an interaction selectivity between 'b' isoforms of ATP2B4 and DLG3 as opposed to the promiscuity of 'b' isoforms of ATP2B2 and ATP2B4 in interacting with other SAPs. Same study DLG4, DLG2 and DLG1 shown to bind to PDZ-binding motifs in 'b' isoforms of ATP2B4 and ATP2B2.
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AT2B4_HUMANLIG_PDZ_Class_112361241Alternative splicing removes the PDZ-binding motif of Plasma membrane calcium-transporting ATPase 4 (ATP2B4), abrogating binding to Disks large homolog 1 (DLG1). A much lower affinity was recorded for the third PDZ domain of DLG1 (in in the micromolar range (KD = 1.2 microM) compared to nanomolar affinity (KD = 1.6 nM)). PMCA4b and DLG1 are co-expressed in kidney and intestinal epithelial cells as well as in several areas of the brain. Should be noted that the 'b' isoforms of Plasma membrane calcium-transporting ATPase 2 (ATP2B2) bind much more weakly to all PDZ domains of DLG1
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AT2B4_HUMANLIG_PDZ_Class_112361241Alternative splicing removes the PDZ-binding motif of Plasma membrane calcium-transporting ATPase 4 (ATP2B4), abrogating binding to Peripheral plasma membrane protein CASK (CASK). The PDZ domain-containing protein CASK and PMCA4b co-precipitate in kidney and brain. Similar to NOS1, binding to PMCA4b allows Ca2+ dependent regulation. Depletion of local Ca2+ by PMCA4b in close proximity to CASK may inhibit Ca2+/calmodulin binding. This can subsequently inhibit binding to T-box brain protein 1 (TBR1) and/or translocation of CASK or the CASK/TBR1 complex to the nucleus.
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L1CAM_HUMANTRG_ENDOCYTIC_211761179Alternative splicing removes the endocytosis motif of Neural cell adhesion molecule L1 (L1CAM), abrogating binding to AP-2 complex subunit mu (AP2M1). This motif is required for sorting of L1CAM to the axonal growth cone of neurons and its clathrin-mediated internalisation. Non-neuronal cells, such as Schwann cells, do not require these motifs, probably because these cells are not highly polarised.
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ADA15_HUMANLIG_SH3_2767772Alternative splicing removes the SH3-binding motif of Disintegrin and metalloproteinase domain-containing protein 15 (ADAM15), abrogating binding to Proto-oncogene tyrosine-protein kinase Src (SRC). The overexpression of this splice variant has been linked to clinical aggressiveness of breast cancer.
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ERBB4_HUMANLIG_WW_110531056Alternative 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.
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PDE2A_HUMANMOD_NMyristoyl17Alternative splicing removes the myristoylation motif of cGMP-dependent 3',5'-cyclic phosphodiesterase (PDE2A). The soluble Isoform PDE2A1 of cGMP-dependent 3',5'-cyclic phosphodiesterase (PDE2A) is expressed in a variety of peripheral tissues, whereas the membrane-associated Isoform PDE2A3 of cGMP-dependent 3',5'-cyclic phosphodiesterase (PDE2A) is found exclusively in the brain. Isoform PDE2A3 of cGMP-dependent 3',5'-cyclic phosphodiesterase (PDE2A) requires N-myristoylation together with palmitoylation to be targeted to synapses, allowing control and crosstalk of cyclic nucleotides.
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SPTB2_HUMANMOD_PKA_221572162Alternative splicing removes the PKA-binding motif of Isoform Short of Spectrin beta chain, brain 1 (SPTBN1), abrogating binding to cAMP-dependent protein kinase catalytic subunit alpha (PRKACA). The phosphorylation of the short C-terminal betaII-spectrin (also known as Isoform Short of Spectrin beta chain, brain 1 (SPTBN1)) by PKA is important in allowing neuritogenesis.
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KPCD_HUMANCLV_C14_Caspase3-7326330Alternative splicing inserts exons within the Caspase-3 scission motif of Protein kinase C delta type (PRKCD), abrogating binding to Caspase-3 (CASP3). Cleavage of PKCdeltaI Protein kinase C delta type (PRKCD) by caspase-3 releases a catalytically active C-terminal fragment that is sufficient to induce apoptosis. This inserted exon disrupts scission motifs and therefore the PKCdeltaVIII (GENBANK:DQ516383) splice variant functions as an anti-apoptotic protein in NT2 cells.
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B2L11_HUMANLIG_Dynein_DLC8_1110116Alternative splicing removes the Dynein-binding motif of Bcl-2-like protein 11 (BCL2L11), abrogating binding to Dynein light chain 1, cytoplasmic (DYNLL1). Most BCL2L11 in healthy cells is sequestered away bound to DYNLL1 (the exception is Bim-S Isoform BCL2-like 11 transcript variant 9 of Bcl-2-like protein 11 (BCL2L11)). Cells exposed to environmental stress up-regulate c-Jun NH(2)-terminal kinases (JNK) that phosphorylate both BCL2L11 and BMF, releasing them from motor complexes and promoting apoptosis.
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UNG_HUMANTRG_NLS_MonoExtN_41521Alternative splicing removes the nuclear localisation signal (NLS) of Uracil-DNA glycosylase (UNG), abrogating binding to Importin subunit alpha-1 (KPNA1) and import into the nucleus. In Isoform UNG1 of Uracil-DNA glycosylase (UNG) the NLS present in Isoform UNG2 of Uracil-DNA glycosylase (UNG) is replaced with a mitochondrial localisation signal (MLS), promoting different localisations of the different protein isoforms.
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GRM1_RATLIG_EVH1_211521156Alternative splicing removes the EVH1-binding motif of Metabotropic glutamate receptor 1 (Grm1), abrogating binding to Homer protein homolog 1 (Homer1), which is important for spatial targeting of Grm1.
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5HT4R_MOUSELIG_PDZ_Class_1382387Alternative splicing removes the PDZ-binding motif of Isoform 5-HT4(A) of 5-hydroxytryptamine receptor 4 (Htr4), abrogating binding to Sorting nexin-27 (Snx27). Snx27 is responsible for targeting of the Isoform 5-HT4(A) of 5-hydroxytryptamine receptor 4 (Htr4) to early endosomes.
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5HT4R_MOUSELIG_PDZ_Class_1382387Alternative splicing removes the PDZ-binding motif of Isoform 5-HT4(A) of 5-hydroxytryptamine receptor 4 (Htr4), abrogating binding to Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (Slc9a3r1). Isoform 5-HT4(A) of 5-hydroxytryptamine receptor 4 (Htr4) interacts specifically with a protein complex including Slc9a3r1 and Ezrin (Ezr) that might participate in its targeting to specialised subcellular regions, such as microvilli.
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5HT4R_MOUSELIG_PDZ_Class_2368371Alternative splicing removes the PDZ-binding motif of Isoform 5-HT4(E) of 5-hydroxytryptamine receptor 4 (Htr4), abrogating binding to InaD-like protein (Inadl).
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ERBB4_HUMANLIG_SH2_IIA10561059Alternative splicing removes the SH2-binding motif of Receptor tyrosine-protein kinase erbB-4 (ERBB4), abrogating binding to Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1). The SH2-binding motif overlaps with a WW-binding motif. Binding of these motifs is regulated in a phosphorylation-dependent manner, ensuring ERBB4 is either endocytosed or stabilised.
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PAXI_HUMANLIG_FAT_LD_1412Alternative splicing removes the FAK-binding LD motif of Paxillin (PXN), abrogating binding to Focal adhesion kinase 1 (PTK2).
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PAXI_HUMANLIG_SH2_IB118121Alternative splicing removes the SH2-binding motif of Paxillin (PXN), abrogating binding to Ras GTPase-activating protein 1 (RASA1).
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PAXI_HUMANLIG_SH2_IB118121Alternative splicing removes the SH2-binding motif of Paxillin (PXN), abrogating binding to Adapter molecule crk (CRK).
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PAXI_HUMANLIG_SH2_IB3134Alternative splicing removes the SH2-binding motif of Paxillin (PXN), abrogating binding to Adapter molecule crk (CRK).
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SYNJ1_HUMANLIG_EH_113931397Alternative splicing removes the EH-binding motif of Synaptojanin-1 (SYNJ1), abrogating binding to Epidermal growth factor receptor substrate 15 (EPS15). Isoform Synaptojanin-170 of Synaptojanin-1 (SYNJ1) is associated with clathrin-mediated endocytosis as a negative regulator of coat-membrane interaction. This isoform is virtually absent from mature neuronal synapses, where clathrin-mediated endocytosis plays a critical role and where Isoform Synaptojanin-145 of Synaptojanin-1 (SYNJ1) is by far the major synaptojanin isoform. Isoform Synaptojanin-145 of Synaptojanin-1 (SYNJ1) may be recruited early to clathrin-coated pits of synapses, either indirectly by adaptors that bind clathrin and AP-2, such as Amphiphysin (AMPH), or by interactions of endophilin family dimers with synaptic vesicle cargo, such as the vesicular glutamate transport.
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SYNJ1_HUMANLIG_EH_114031407Alternative splicing removes the EH-binding motif of Synaptojanin-1 (SYNJ1), abrogating binding to Epidermal growth factor receptor substrate 15 (EPS15). Isoform Synaptojanin-170 of Synaptojanin-1 (SYNJ1) is associated with clathrin-mediated endocytosis as a negative regulator of coat-membrane interaction. This isoform is virtually absent from mature neuronal synapses, where clathrin-mediated endocytosis plays a critical role and where Isoform Synaptojanin-145 of Synaptojanin-1 (SYNJ1) is by far the major synaptojanin isoform. Isoform Synaptojanin-145 of Synaptojanin-1 (SYNJ1) may be recruited early to clathrin-coated pits of synapses, either indirectly by adaptors that bind clathrin and AP-2, such as Amphiphysin (AMPH), or by interactions of endophilin family dimers with synaptic vesicle cargo, such as the vesicular glutamate receptor transport.
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SYNJ1_HUMANLIG_EH_114141418Alternative splicing removes the EH-binding motif of Synaptojanin-1 (SYNJ1), abrogating binding to Epidermal growth factor receptor substrate 15 (EPS15). Isoform Synaptojanin-170 of Synaptojanin-1 (SYNJ1) is associated with clathrin-mediated endocytosis as a negative regulator of coat-membrane interaction. This isoform is virtually absent from mature neuronal synapses, where clathrin-mediated endocytosis plays a critical role and where Isoform Synaptojanin-145 of Synaptojanin-1 (SYNJ1) is by far the major synaptojanin isoform. Isoform Synaptojanin-145 of Synaptojanin-1 (SYNJ1) may be recruited early to clathrin-coated pits of synapses, either indirectly by adaptors that bind clathrin and AP-2, such as Amphiphysin (AMPH), or by interactions of endophilin family dimers with synaptic vesicle cargo, such as the vesicular glutamate receptor transport.
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SYNJ1_HUMANLIG_AP2alpha_213231325Alternative splicing removes the AP2alpha-binding motif of Synaptojanin-1 (SYNJ1), abrogating binding to AP-2 complex subunit alpha-2 (AP2A2). Isoform Synaptojanin-170 of Synaptojanin-1 (SYNJ1) is associated with clathrin-mediated endocytosis as a negative regulator of coat-membrane interaction. This isoform is virtually absent from mature neuronal synapses, where clathrin-mediated endocytosis plays a critical role and where Isoform Synaptojanin-145 of Synaptojanin-1 (SYNJ1) is by far the major synaptojanin isoform. Isoform Synaptojanin-145 of Synaptojanin-1 (SYNJ1) may be recruited early to clathrin-coated pits of synapses, either indirectly by adaptors that bind clathrin and AP-2, such as Amphiphysin (AMPH), or by interactions of endophilin family dimers with synaptic vesicle cargo, such as the vesicular glutamate transport.
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SYNJ1_HUMANLIG_AP2alpha_215551557Alternative splicing removes the AP2alpha-binding motif of Synaptojanin-1 (SYNJ1), abrogating binding to AP-2 complex subunit alpha-2 (AP2A2). Isoform Synaptojanin-170 of Synaptojanin-1 (SYNJ1) is associated with clathrin-mediated endocytosis as a negative regulator of coat-membrane interaction. This isoform is virtually absent from mature neuronal synapses, where clathrin-mediated endocytosis plays a critical role and where Isoform Synaptojanin-145 of Synaptojanin-1 (SYNJ1) is by far the major synaptojanin isoform. Isoform Synaptojanin-145 of Synaptojanin-1 (SYNJ1) may be recruited early to clathrin-coated pits of synapses, either indirectly by adaptors that bind clathrin and AP-2, such as Amphiphysin (AMPH), or by interactions of endophilin family dimers with synaptic vesicle cargo, such as the vesicular glutamate transport.
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SLOB_DROMELIG_14-3-3_37681Alternative splicing removes the 14-3-3-binding motif of Slowpoke-binding protein (Slob), abrogating binding to 14-3-3 family. Another 14-3-3 motif exists in this protein (50-RSNS-54) that is not altered by Alternative splicing. The removal of this motif therefore decreases the avidity of the interaction with 14-3-3 proteins.
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MYCD_MOUSELIG_Actin_RPEL_32039Alternative promoter usage removes the RPEL-binding motif of Myocardin (Myocd), abrogating binding to Actin, alpha skeletal muscle (Acta1). 3 RPEL motifs are found in Myocd. The shortened form lacks 2 RPEL motifs but no definitive comparison of binding to actin has been undertaken between isoforms.
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MYCD_MOUSELIG_Actin_RPEL_36483Alternative promoter usage removes the RPEL-binding motif of Myocardin (Myocd), abrogating binding to Actin, alpha skeletal muscle (Acta1). 3 RPEL motifs are found in Myocd. The shortened form lacks 2 RPEL motifs but no definitive comparison of binding to actin has been undertaken between isoforms.
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DMD_HUMANLIG_Actin_DMD510Alternative splicing removes the actin-binding motif of Isoform Dp71 of Dystrophin (DMD), abrogating binding to Actin, alpha skeletal muscle (ACTA1). The presence of the actin-binding motif in Isoform Dp71 of Dystrophin (DMD) may allow it to participate in the clustering of sodium channels by anchoring the syntrophin/channel complex to the actin cytoskeleton.
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AKAP1_HUMANDOC_PP1151158Alternative splicing removes the PP1-binding motif of A-kinase anchor protein 1, mitochondrial (AKAP1), abrogating binding to PP-1 subfamily. Isoform AKAP149 of A-kinase anchor protein 1, mitochondrial (AKAP1) may conceivably position PKA and PP1 in close proximity where they can reversibly modulate the phosphorylation of nuclear substrates such as NPP1, DNA-binding cAMP response elements, B-type lamins and inner nuclear membrane proteins LBR and lamina-associated polypeptides, which all harbor PKA phosphorylation sites.
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DBLOH_HUMANLIG_BIR_internal5659Alternative splicing removes the BIR-binding motif of Diablo homolog, mitochondrial (DIABLO), abrogating binding to Baculoviral IAP repeat-containing protein 4 (XIAP). Isoform SMAC3 of Diablo homolog, mitochondrial (DIABLO) is localised to mitochondria via its mitochondrial localisation signal (MLS). Upon entry in mitochondria the MLS is cleaved and Isoform SMAC3 of Diablo homolog, mitochondrial (DIABLO) is found localised with cytochrome-c. During apoptosis, Isoform SMAC3 of Diablo homolog, mitochondrial (DIABLO) binds to the second/third BIR domain of Baculoviral IAP repeat-containing protein 4 (XIAP). This interaction disrupts binding of XIAP to processed Caspase-9 (CASP9) and promotes Caspase-3 (CASP3) activation. Isoform SMAC3 of Diablo homolog, mitochondrial (DIABLO) also promotes ubiquitination of XIAP and subsequent degradation. Isoform 1 of Diablo homolog, mitochondrial (DIABLO) on the other hand did not cause degradation of XIAP.
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DBLOH_HUMANTRG_MLS155Alternative splicing removes the BIR-binding motif of Diablo homolog, mitochondrial (DIABLO), abrogating binding to Mitochondrial import receptor subunit TOM70 (TOMM70A). Isoform SMAC3 of Diablo homolog, mitochondrial (DIABLO) is localised to mitochondria via its mitochondrial localisation signal (MLS). Upon entry in mitochondria the MLS is cleaved and Isoform SMAC3 of Diablo homolog, mitochondrial (DIABLO) is found localised with cytochrome-c. During apoptosis, Isoform SMAC3 of Diablo homolog, mitochondrial (DIABLO) binds to the second/third BIR domain of Baculoviral IAP repeat-containing protein 4 (XIAP). This interaction disrupts binding of XIAP to processed Caspase-9 (CASP9) and promotes Caspase-3 (CASP3) activation. Isoform SMAC3 of Diablo homolog, mitochondrial (DIABLO) also promotes ubiquitination of XIAP and subsequent degradation. Isoform 1 of Diablo homolog, mitochondrial (DIABLO) on the other hand did not cause degradation of XIAP.
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P53_HUMANDEG_MDM2_11926Alternative promoter usage and alternative splicing removes the E3 ubiquitin ligase MDM2-binding motif of Cellular tumor antigen p53 (TP53), abrogating binding to E3 ubiquitin-protein ligase Mdm2 (MDM2). The splice variant without this motif is resistant to MDM2-mediated degradation, leading to a longer half-life.
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P53_HUMANTRG_NES_CRM1_1339352Alternative splicing removes the nuclear export signal (NES) of Cellular tumor antigen p53 (TP53), abrogating binding to Exportin-1 (XPO1) and export from the nucleus.
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P53_HUMANDOC_USP7_1359363Alternative splicing removes the deubiquitinating enzyme USP7-binding motif of Cellular tumor antigen p53 (TP53), abrogating binding to Ubiquitin carboxyl-terminal hydrolase 7 (USP7).
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P53_HUMANDOC_USP7_1364368Alternative splicing removes the deubiquitinating enzyme USP7-binding motif of Cellular tumor antigen p53 (TP53), abrogating binding to Ubiquitin carboxyl-terminal hydrolase 7 (USP7).
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ING1_HUMANLIG_PCNA_2915Alternative splicing removes the PCNA-binding motif of Isoform Variant A of Inhibitor of growth protein 1 (ING1), abrogating binding to Proliferating cell nuclear antigen (PCNA). P33-ING1b (also known as Isoform Variant A of Inhibitor of growth protein 1 (ING1)) binds specially to PCNA, resulting in a major change in subcellular localisation and the import of this isoform into the nucleus. This is theorised to act by limiting access to the PCNA-binding domain but eventually it promotes apoptosis (though this may not be its physiological effect).
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S35A2_HUMANTRG_ER_diLys_1392396Alternative splicing removes the di-lysine ER-retention motif of UDP-galactose translocator (SLC35A2), abrogating binding to Coatomer subunit alpha (COPA). This motif localises Isoform UGT1 of UDP-galactose translocator (SLC35A2) exclusively in the Golgi whereas Isoform UGT2 of UDP-galactose translocator (SLC35A2) shows dual expression in both the Golgi and the ER. This motif is considered a weak retention signal.
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UNG_HUMANTRG_MLS144Alternative promoter usage removes the mitochondrial localisation signal (MLS) of Isoform UNG1 of Uracil-DNA glycosylase (UNG), abrogating binding to Mitochondrial import receptor subunit TOM70 (TOMM70A) and import into mitochondria. In Isoform UNG2 of Uracil-DNA glycosylase (UNG) the MLS present in Isoform UNG1 of Uracil-DNA glycosylase (UNG) is replaced with a nuclear localisation signal (NLS), promoting different localisations of the different protein isoforms.
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AT2B1_HUMANLIG_IQ_211141128Alternative splicing partially removes the IQ motif of Isoform CI of Plasma membrane calcium-transporting ATPase 1 (ATP2B1), partially inhibiting binding to Calmodulin (CALM1).
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IRK6_MOUSELIG_PDZ_Class_1420425Alternative splicing removes the PDZ-binding motif of G protein-activated inward rectifier potassium channel 2 (Kcnj6), abrogating binding to Sorting nexin-27 (Snx27).
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KCC2D_RATTRG_NLS_MonoCore_2327332Alternative splicing removes the nuclear localisation signal (NLS) of Isoform Delta 3 of Calcium/calmodulin-dependent protein kinase type II subunit delta (Camk2d), abrogating binding to Importin subunit alpha-1 (KPNA1) and nuclear import. This is due to an 11 amino acid insert encoded by exon 14.
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PEX5R_MOUSETRG_ENDOCYTIC_23841Alternative splicing removes the endocytosis motif of Isoform 3 of PEX5-related protein (Pex5l), abrogating binding to AP-2 complex subunit mu (Ap2m1). The motif is present in exon 2, and its absence causes a significant increase in channel density of members from the potassium channel HCN family.
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PEX5R_MOUSETRG_LysEnd_APsAcLL_11419Alternative splicing removes the di-leucine endocytosis motif of PEX5-related protein (Pex5l), abrogating binding to AP-2 complex subunit sigma (Ap2s1). The motif is present in exon 5.
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HSF4_HUMANMOD_SUMO292295Alternative splicing removes the sumoylation motif of Heat shock factor protein 4 (HSF4), abrogating binding to SUMO-conjugating enzyme UBC9 (UBE2I). The phosphorylation-dependent sumoylation of the PDSM (phosphorylation-dependent sumoylation motif) strongly represses Isoform HSF4B of Heat shock factor protein 4 (HSF4) activity.
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P73_HUMANDOC_WW_Pin1_4479484Alternative 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.
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P73_HUMANDOC_WW_Pin1_4439444Alternative 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.
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P73_HUMANDOC_WW_Pin1_4409414Alternative 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.
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MYO5A_HUMANLIG_Dynein_DLC8_212861290Alternative splicing removes the dynein-binding motif of Unconventional myosin-Va (MYO5A), abrogating binding to Dynein light chain 2, cytoplasmic (DYNLL2). DYNLL2 (also known as DLC2) globally protects the tail domains of MYO5A against limited proteolysis.
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REST_HUMANDEG_SCF_TRCP1_210081013Alternative splicing removes the beta-TrCP-binding degron of RE1-silencing transcription factor (REST), abrogating binding to F-box/WD repeat-containing protein 1A (BTRC), and therefore altering the half-life of the variant. Up-regulation of the protein isoform without the degron has been linked to cancer.
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FBXW7_HUMANTRG_NLS_MonoCore_21015Alternative splicing removes the nuclear localisation signal (NLS) of F-box/WD repeat-containing protein 7 (FBXW7), abrogating binding to Importin subunit alpha-1 (KPNA1). There are two other NLS motifs in the protein, meaning the isoform can still enter the nucleus.
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FBXW7_HUMANTRG_NES_CRM1_21926Alternative splicing removes the nuclear export signal (NES) of Isoform Archipelago beta of F-box/WD repeat-containing protein 7 (FBXW7), abrogating binding to Exportin-1 (XPO1) and export from nucleus. The presence of the NES produces an isoform with a cytoplasmic localisation. The two other isoforms of FBXW7 localise to the nucleus and the nucleolus, respectively.
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SORC1_HUMANTRG_LysEnd_APsAcLL_211361140Alternative splicing removes the di-leucine motif of Isoform 4 of VPS10 domain-containing receptor SorCS1 (SORCS1), abrogating binding to AP-2 complex subunit sigma (AP2S1). Human and mouse have completely different C-termini for SorCS1a (also known as Isoform 4 of VPS10 domain-containing receptor SorCS1 (SORCS1)), with only the human splice variant containing the motif.
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SORC1_HUMANTRG_ENDOCYTIC_211321135Alternative splicing removes the endocytosis motif of Isoform 2 of VPS10 domain-containing receptor SorCS1 (SORCS1), abrogating binding to AP-2 complex subunit mu (AP2M1). The sequence is conserved in both human and mouse. Different splice variants have different endocytosis motifs.
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SLAF7_HUMANLIG_TYR_ITSM280287Alternative splicing removes the ITSM (immunoreceptor tyrosine-based switch motif) motif of SLAM family member 7 (SLAMF7), abrogating binding to SH2 domain-containing protein 1A (SH2D1A). The full-length isoform (Isoform CS1-L of SLAM family member 7 (SLAMF7)) has 2 ITSM motifs and only one is missing in the shorter splice variant (Isoform 19A24 of SLAM family member 7 (SLAMF7)). However, experiments showed only Isoform CS1-L of SLAM family member 7 (SLAMF7) binds to SH2D1A.
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CDC42_HUMANMOD_CAAXbox188191Alternative splicing removes the prenylation motif of Cell division control protein 42 homolog (CDC42), abrogating binding to Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha (FNTA). The canonical, prenylated Cdc42 isoform (Cdc42-pren or Isoform Placental of Cell division control protein 42 homolog (CDC42)) is expressed in all tissues, the variant, palmitoylated form (Cdc42-palm or Isoform Brain of Cell division control protein 42 homolog (CDC42)) is expressed only in brain.
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CDC42_HUMANMOD_Spalmitoyl188191Alternative splicing removes the palmitoylation motif of Isoform Brain of Cell division control protein 42 homolog (CDC42), abrogating binding to Palmitoyltransferase ZDHHC9 (ZDHHC9). The splice variant with the palmitoylation motif (Isoform Brain of Cell division control protein 42 homolog (CDC42)) is expressed in brain and is often found within raf-like domain of dendrites. Increased levels of glutamate results in rapid depalmitoylation and dislocation from dendrites.
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CEAM1_MOUSECLV_CASPASE3_1457460Alternative splicing removes the caspase-3 scission site of Carcinoembryonic antigen-related cell adhesion molecule 1 (Ceacam1), preventing cleavage by Caspase-3 (Casp3). The presence of cleavage sites allows production of a stronger adhession molecule.
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SHIP1_HUMANLIG_SH2_IIA918921Alternative splicing partially removes the SH2-binding motif of Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1 (Inpp5d), partially inhibiting binding to Phosphatidylinositol 3-kinase regulatory subunit alpha (Pik3r1).
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LMP2_EBVB9LIG_WW_15760Alternative splicing removes the WW-binding motif of Latent membrane protein 2 (LMP2), abrogating binding to E3 ubiquitin-protein ligase Itchy (Itch).
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LMP2_EBVB9LIG_WW_198101Alternative splicing removes the WW-binding motif of Latent membrane protein 2 (LMP2), abrogating binding to E3 ubiquitin-protein ligase Itchy (Itch).
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KIF1B_MOUSELIG_PDZ_Class_111451150Alternative splicing removes the PDZ-binding motif of Isoform 3 of Kinesin-like protein KIF1B (Kif1b), abrogating binding to PDZ domain-containing protein GIPC1 (Gipc1).
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CYLD_MOUSELIG_TRAF2_3449453Alternative splicing removes the TRAF2-binding motif of Ubiquitin carboxyl-terminal hydrolase CYLD (Cyld), abrogating binding to TNF receptor-associated factor 2 (Traf2). Mice expressing solely the alternatively spliced Isoform 3 of Ubiquitin carboxyl-terminal hydrolase CYLD (Cyld) (sCYLD) show an altered B-cell expansion profile and have more stable NF-kB proteins.
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SIG12_MOUSELIG_TYR_ITIM430435Alternative splicing removes the ITIM (immunoreceptor tyrosine-based inhibitory motif) of Sialic acid-binding Ig-like lectin 12 (Siglec12), abrogating binding to Tyrosine-protein phosphatase non-receptor type 6 (Ptpn6).
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SIG12_MOUSELIG_TYR_ITIM430435Alternative splicing removes the ITIM (immunoreceptor tyrosine-based inhibitory motif) of Sialic acid-binding Ig-like lectin 12 (Siglec12), abrogating binding to Tyrosine-protein phosphatase non-receptor type 11 (Ptpn11).
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TRML1_HUMANLIG_TYR_ITIM279284Alternative splicing removes the ITIM (immunoreceptor tyrosine-based inhibitory motif) of Trem-like transcript 1 protein (TREML1), abrogating binding to Tyrosine-protein phosphatase non-receptor type 11 (PTPN11).
details
GRIK1_RATLIG_PDZ_Class_1900905Alternative splicing removes the PDZ-binding motif of Isoform Glur5-2 of Glutamate receptor ionotropic, kainate 1 (Grik1), abrogating binding to PRKCA-binding protein (Pick1). The ER-retention motif of Grik1 splice variants can be inhibited by PKC phosphorylation and association with a PDZ protein. It has also been shown that the PDZ domain-containing proteins Disks large homolog 4 (Dlg4) and Syntenin-1 (Sdcbp) are able to bind.
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GRIK1_RATLIG_PDZ_Class_1900905Alternative splicing removes the PDZ-binding motif of Glutamate receptor, ionotropic kainate 1 (Grik1), abrogating binding to Glutamate receptor-interacting protein 1 (Grip1). The ER retention of Grik1 splice variants can be inhibited by PKC phosphorylation and association with a PDZ domain-containing protein. Also shown that the PDZ-binding containing proteins PSD95 and syntenin are able to bind.
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GRIK1_RATTRG_ER_diArg_2937941Alternative splicing removes the di-arginine ER-retention motif of Glutamate receptor, ionotropic kainate 1 (Grik1), abrogating binding to Coatomer subunit beta (COPB1).
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ODFP2_HUMANMOD_CDK_1793799Alternative splicing removes the cyclin-dependent kinase (CDK) phosphorylation motif of Isoform Cenexin 1 of Outer dense fiber protein 2 (ODF2), abrogating binding to Cyclin-dependent kinase 1 (CDK1). This phosphorylation is required for the recruitment of Serine/threonine-protein kinase PLK1 (PLK1). The C-terminal extension of Isoform Cenexin 1 of Outer dense fiber protein 2 (ODF2) has the ability to distinctly localise to mother centriole whereas the splice variant (e.g. Isoform Cenexin 1 of Outer dense fiber protein 2 (ODF2)), which does not have this extension, permits ODF2 to associate with sperm tail.
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PIMT_BOVINTRG_ER_KDEL_1225228Alternative splicing removes the KDEL ER-retention motif of Isoform 2 of Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT1).
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P3H1_HUMANTRG_ER_KDEL_1733736Alternative splicing removes the KDEL ER-retention motif of Prolyl 3-hydroxylase 1 (LEPRE1).
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SMAD4_HUMANTRG_NES_CRM1_2142149Alternative splicing removes the nuclear export signal (NES) motif of Mothers against decapentaplegic homolog 4 (SMAD4), thereby inhibiting binding to Exportin-1 (XPO1) and export from the nucleus. A splice variant lacking the NES does not shuttle back and forth between nucleus and cytosol. At present, this particular splice variant is not annotated in UniProtKB.
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TRM1_YEASTTRG_MLS116Alternative initiation removes the mitochondrial localisation signal (MLS) motif of tRNA (guanine(26)-N(2))-dimethyltransferase, mitochondrial (TRM1), abrogating binding to Mitochondrial import receptor subunit TOM70 (TOMM70A). Both variants contain a weak nuclear localisation signal (NLS) (KKSKKKRC). However, this motif is over-powered by the MLS and therefore the full-length variant is localised to mitochondria. Alternative initiation removes the N-terminus and the MLS motif, resulting in a nuclear localisation for the truncated isoform.
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MOD5_MOUSETRG_MLS147Alternative splicing removes the mitochondrial localisation signal (MLS) motif of tRNA dimethylallyltransferase, mitochondrial (Trit1), abrogating binding to Mitochondrial import receptor subunit TOM70 (TOMM70A). The IPPT-I isoform (also known as Isoform 1 of tRNA dimethylallyltransferase, mitochondrial (Trit1)) was found to localise to both the mitochondria and the cytosol whereas the IPPT-II isoform (also known as Isoform 2 of tRNA dimethylallyltransferase, mitochondrial (Trit1)) is only localised to the cytosol and the nucleus. No nuclear localisation signal (NLS) was identified in either splice variant.
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SYK_HUMANTRG_MLS149Alternative splicing removes the mitochondrial localisation signal (MLS) motif of Isoform Mitochondrial of Lysine--tRNA ligase (KARS), abrogating binding to Mitochondrial import receptor subunit TOM70 (TOMM70A) and import into mitochondria. Unusually, the first two exons of Lysine--tRNA ligase (KARS) are non-constitutive. The first exon does not contain a localisation signal (resulting in cytosol localisation) whereas the second exon contains an MLS.
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GLRX2_HUMANTRG_MLS121Alternative splicing removes the mitochondrial localisation signal (MLS) motif of Glutaredoxin-2, mitochondrial (GLRX2), abrogating binding to Mitochondrial import receptor subunit TOM70 (TOMM70A) and import into mitochondria. The Grx2a isoform Isoform Grx2a of Glutaredoxin-2, mitochondrial (GLRX2) is localised to the mitochondria whereas the Isoform Grx2b of Glutaredoxin-2, mitochondrial (GLRX2) is localised to the perinuclear region.
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OGG1_HUMANTRG_NLS_MonoExtN_4332339Alternative splicing removes the nuclear localisation signal (NLS) motif of N-glycosylase/DNA lyase (OGG1), abrogating binding to Importin subunit alpha-1 (KPNA1) and import into the nucleus. OGG1-1a (also known as Isoform Alpha of N-glycosylase/DNA lyase (OGG1)) has a C-terminal NLS motif that is absent in OGG1-2a (also known as Isoform Beta of N-glycosylase/DNA lyase (OGG1)) . Both have a weak mitochondrial localisation signal (MLS) in the N-terminal.
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DUT_HUMANTRG_MLS169Alternative splicing removes the mitochondrial localisation signal (MLS) motif of Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial (DUT), abrogating binding to Mitochondrial import receptor subunit TOM70 (TOMM70A) and import into the mitochondria.
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DAB2_HUMANLIG_AP2alpha_2293295Alternative splicing removes the AP2alpha-binding motifs of Disabled homolog 2 (DAB2), abrogating binding to AP-2 complex subunit alpha-2 (AP2A2). The p67 splice variant of Dab1 (also known as Isoform 2 of Disabled homolog 2 (DAB2)) does not localise to vesicles as it fails to bind the AP-2 complex.
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DAB2_HUMANLIG_AP2alpha_2298300Alternative splicing removes the AP2alpha-binding motifs of Disabled homolog 2 (DAB2), abrogating binding to AP-2 complex subunit alpha-2 (AP2A2). The p67 splice variant of Dab1 (also known as Isoform 2 of Disabled homolog 2 (DAB2)) does not localise to vesicles as it fails to bind the AP-2 complex.
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PML_HUMANTRG_NLS476490Alternative splicing removes the nuclear localisation signal (NLS) of Protein PML (PML), abrogating binding to Importin subunit alpha-1 (KPNA1) and import into the nucleus.
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PML_HUMANMOD_SUMO489492Alternative splicing removes the SUMO motif of Protein PML (PML), abrogating binding to SUMO-conjugating enzyme UBC9 (UBE2I). The study identified a major sumoylation site within the nuclear localisation signal (NLS) of PML. Although they did not determine whether the lysine residue regulates the NLS, they found that sumoylation was not necessary for nuclear localisation and that SUMO-modification only occurs in the nucleus.
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PML_HUMANTRG_NES_CRM1_1702716Alternative splicing removes the nuclear export signal (NES) of Protein PML (PML), abrogating binding to Exportin-1 (XPO1) and export from the nucleus.
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PRLR_RATTRG_LysEnd_APsAcLL_1301306Alternative splicing removes the di-leucine endocytosis motif of Prolactin receptor (Prlr), partially inhibiting binding to AP-2 complex subunit sigma (AP2S1) and the rate of endocytosis. Isoform Long of Prolactin receptor (Prlr) (also known as PRLR-long) has a longer C-terminal tail than the Isoform Short of Prolactin receptor (Prlr) (also known as PRLR-short) splice variant. PRLR-long internalises faster than PRLR-short due to two additional di-leucine motifs in the C-terminus (where the adjacent phenylalanine also plays a role). PRLR-short has two di-leucine motifs whereas PRLR-long has four.
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AMACR_HUMANTRG_PTS1379382Alternative splicing removes the type 1 peroxisomal targeting signal (PTS1) of Alpha-methylacyl-CoA racemase (AMACR), abrogating binding to Peroxisomal targeting signal 1 receptor (PEX5) and import into the peroxisome. Only the major AMACR IA (also known as Isoform 1 of Alpha-methylacyl-CoA racemase (AMACR)) form localises to the peroxisome.
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BRCA1_HUMANTRG_NLS_MonoExtN_4501508Alternative splicing removes the nuclear localisation signal (NLS) of Breast cancer type 1 susceptibility protein (BRCA1), abrogating binding to Importin subunit alpha-1 (KPNA1) and import into the nucleus. The study compared the full-length Brca1 splice variant (Isoform 1 of Breast cancer type 1 susceptibility protein (BRCA1)) to the Delta11b isoform (Isoform Delta11b of Breast cancer type 1 susceptibility protein (BRCA1)). The shorter isoform is missing exon 11b and differs in a number of ways. Firstly, it lacks an NLS and therefore has a cytoplasmic localisation. Also, when over-expressed, the Delta11b isoform was not toxic, suggesting nuclear localisation is important for Brca1's toxic behaviour.
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HIF3A_HUMANDEG_ODPH_VHL_1490502Alternative splicing removes the VHL-hydroxyproline-modified binding motif of Hypoxia-inducible factor 3-alpha (HIF3A), abrogating binding to Von Hippel-Lindau disease tumor suppressor (VHL). Other studies have shown that the HIF-3 alpha-4 splice variant (Isoform HIF-3alpha4 of Hypoxia-inducible factor 3-alpha (HIF3A)) can act as a dominant negative form with tumour-suppressive activity (see Maynard et al. (2007) (here)).
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STA5A_HUMANLIG_SH2_STAT5694697Alternative splicing removes the regulatory Y694 residue of Signal transducer and activator of transcription 5A (STAT5A). The phosphorylation of Y694 by Proto-oncogene tyrosine-protein kinase Src (SRC) has been shown to be essential for DNA binding. This event acts as an important regulatory mechanism (See Clark et al. (2005) (here) and Okutani et al. (2001) (here)). The exact function of Y694 remains uncertain as is binding to STAT5 in dimer. The STAT5A-DeltaE18 does not enter nucleus upon PRLR stimulation.
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HAP1_RATLIG_14-3-3_4594598Alternative splicing removes the 14-3-3-binding motif of Isoform Short of Huntingtin-associated protein 1 (Hap1), abrogating binding to 14-3-3 protein zeta/delta (Ywhaz). The association of HAP1A (Isoform Short of Huntingtin-associated protein 1 (Hap1)) with 14-3-3 protein zeta/delta (Ywhaz) inhibits binding of the splice variant to members of the kinesin light chain family and diminishes trafficking of Hap1 to neural processes and neurite tips. The result is a decrease in neurite outgrowth.
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XIRP1_HUMANLIG_EVH1_12226Alternative splicing removes the EVH1-binding motif of Xin actin-binding repeat-containing protein 1 (XIRP1), abrogating binding to Protein enabled homolog (ENAH).
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XIRP1_HUMANLIG_EVH1_12226Alternative splicing removes the EVH1-binding motif of Xin actin-binding repeat-containing protein 1 (XIRP1), abrogating binding to Vasodilator-stimulated phosphoprotein (VASP).
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GUAD_HUMANLIG_PDZ_Class_1449454Alternative splicing removes the PDZ-binding motif of Guanine deaminase (GDA) (Nedasin), abrogating binding to Disks large homolog 3 (DLG3). Isoform 1 of Guanine deaminase (GDA) (Nedasin S) is predominately expressed in neuronal tissues and binds PDZ domains. Isoform 3 of Guanine deaminase (GDA) (Nedasin V1), which is predominately expressed in non-neuronal tissues, does not bind PDZ domains. The presence of Nedasin S inhibits binding of NMDA receptors and K+ channels to PDZ domain-containing proteins such as members of the MAGUK family. This suggests that GDA might modulate the receptor clustering function of the PDZ domains of MAGUK family members, and this modulation is regulated by alternative splicing of GDA transcripts.
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NMDZ1_HUMANLIG_PDZ_Class_1917922Alternative splicing removes the PDZ-binding motif of Isoform 4 of Glutamate [NMDA] receptor subunit zeta-1 (GRIN1), abrogating binding to Disks large homolog 4 (DLG4). Binding of the PDZ domain of DLG4 suppresses an ER-retention motif in GRIN1, promoting its cell surface expression in a splice variant-specific manner.
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SYNJ2_RATLIG_PDZ_Class_112881293Alternative splicing removes the PDZ-binding motif of Isoform 7.5kb of Synaptojanin-2 (Synj2), abrogating binding to Synaptojanin-2-binding protein (Synj2bp). Isoform 7.5kb of Synaptojanin-2 (Synj2) (Synaptojanin 2A) is recruited to mitochondria through the interaction with the PDZ domain of the mitochondrial outer membrane protein Synj2bp.
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SYNJ2_RATLIG_SH3_211201125Alternative splicing removes the SH3-binding motif of Synaptojanin-2 (Synj2), abrogating binding to Endophilin-A2 (Sh3gl1). Endophilin-A1 (Sh3gl2) and Endophilin-A3 (Sh3gl3) were also shown to bind in this study.
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CLCN3_HUMANLIG_PDZ_Class_1861866Alternative splicing removes the PDZ-binding motif of Isoform ClC-3B of H(+)/Cl(-) exchange transporter 3 (CLCN3), abrogating binding to Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (SLC9A3R1). Isoform ClC-3B of H(+)/Cl(-) exchange transporter 3 (CLCN3) is expressed at the leading edge of membrane ruffles. The interaction of CLCN3 with SLC9A3R1 is important for localising outwardly rectifying chloride channels at the leading edge.
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GRIA2_RATLIG_PDZ_Class_2878883Alternative splicing removes the PDZ-binding motif of Glutamate receptor 2 (Gria2), abrogating binding to PRKCA-binding protein (Pick1). The presence of PDZ-binding motifs is also seen in the short isoforms of Gria3 (Isoform Flop of Glutamate receptor 3 (Gria3)) and Gria4 (Isoform 4C flop of Glutamate receptor 4 (Gria4)). PRKCA-binding protein (Pick1) recruits both Protein kinase C alpha type (Prkca) and Gria2 simultaneously, possibly allowing Pick1 to play a role in the selective targeting to and possible anchoring of GluRshort-containing AMPA receptors to intracellular membrane-associated Prkca.
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PKHG5_MOUSELIG_PDZ_Class_110681073Alternative splicing removes the PDZ-binding motif of Pleckstrin homology domain-containing family G member 5 (Plekhg5), abrogating binding to PDZ domain-containing protein GIPC1 (Gipc1). The PDZ adaptor protein Gipc1 (Synectin) bound the longer splice variant, Isoform SYX1 of Pleckstrin homology domain-containing family G member 5 (Plekhg5) (Syx1), which was targeted to the plasma membrane in a Synectin-dependent manner. The shorter variant, Isoform SYX2 of Pleckstrin homology domain-containing family G member 5 (Plekhg5) (Syx2), was diffusely distributed in the cytoplasm. Expression of Syx1 augmented endothelial cell migration and tube formation, whereas Syx2 expression did not. Significant expression of Syx2 was only seen in brain tumour cells, which also exhibited high basal Transforming protein RhoA (Rhoa) activity.
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KALRN_RATLIG_PDZ_Class_116491654Alternative splicing removes the PDZ-binding motif of Isoform Kalirin-7 of Kalirin (Kalrn), abrogating binding to Disks large homolog 4 (Dlg4). Isoform Kalirin-7 of Kalirin (Kalrn) is the most prevalent isoform in the adult rat hippocampus where it locates to the postsynaptic density via an interaction with Dlg4 and regulates dendritic morphogenesis.
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PLCB1_HUMANLIG_PDZ_Class_112111216Alternative splicing removes the PDZ-binding motif of 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1 (PLCB1), abrogating binding to Partitioning defective 3 homolog (PARD3). The G protein-activated PLCB1 can directly interact with cell polarity proteins Partitioning defective 3 homolog (PARD3) and Partitioning defective 6 homolog alpha (PARD6A) to form protein complexes in the cell, which potentially modulate G protein-activated PLCB1 activity in cell polarity formation and asymmetric cell division.
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PLCB1_MOUSELIG_PDZ_Class_112111216Alternative splicing removes the PDZ-binding motif of 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1 (Plcb1), abrogating binding to Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (Slc9a3r1). Plcb1 does not bind to Slc9a3r2.
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PLCB1_HUMANLIG_SH3_311621168Alternative splicing removes the SH3-binding motif of Isoform B of 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1 (PLCB1), abrogating binding to SH3 and multiple ankyrin repeat domains protein 3 (SHANK3). PLCB1 associates with a SHANK3 complex in cardiomyocytes via its splice variant-specific C-terminal tail. Studies show that Isoform B of 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1 (PLCB1) selectively mediates downstream responses initiated by Gq-coupled receptors, in particular hypertrophy and apoptosis.
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PI51C_MOUSETRG_ENDOCYTIC_2644647Alternative splicing removes the endocytosis motif of Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma (Pip5k1c), abrogating binding to AP-2 complex subunit mu (Ap2m1). The direct interaction between the AP-2 complex and Isoform PIPKIgamma661 of Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma (Pip5k1c) (PIPKIgamma661) targets this isoform to sites of endocytosis at the plasma membrane. Consequently, this results in the generation of a highly concentrated pool of PI(4,5)P2 at these sites.
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PI51C_MOUSELIG_PTB_Talin645648Alternative splicing removes the PTB domain-binding motif of Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma (Pip5k1c), abrogating binding to Talin-1 (Tln1). Integrin receptors, Tln1 and Isoform PIPKIgamma661 of Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma (Pip5k1c) (PIPKIgamma661) are recruited to focal adhesions, inducing synthesis of PI(4,5)P2. The regulated and localised generation of PI(4,5)P2 facilitates the assembly and/or disassembly of focal adhesions.
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PI51C_MOUSETRG_AP2beta_CARGO_2633644Alternative splicing removes the AP-2 beta-appendage-binding motif of Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma (Pip5k1c), abrogating binding to AP-2 complex subunit beta (Ap2b1). With other enzymes (members of the eukaryotic diacylglycerol kinase family, and Synaptojanin-1 (Synj1)), Isoform PIPKIgamma661 of Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma (Pip5k1c) (PIPKIgamma661) optimises the regional lipid environment necessary for clathrin coat formation. There are three different C-terminal splice variants of Pip5k1c: one (PIPKIgamma687) can bind selectively to Talin-1 (Tln1) via the C-terminal extension (switch details), one (PIPKIgamma661) can bind to both Talin-1 (Tln1) and AP-2 complex subunit beta (Ap2b1), and one (PIPKIgamma635) can bind to neither protein. This flexibility could impart importantly different biological functions to each isoform. For example, in humans PIP5K1C (PIPKIgamma661 in mouse) is proposed to act upstream of Rac/Rho and the differential regulation of PIP5K-gamma and -alpha might allow them to work in tandem to modulate the actin cytoskeleton during the attachment and ingestion phases of phagocytosis (See (here)).
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MDM2_HUMANTRG_NLS_MonoExtC_3181187Alternative splicing removes the nuclear localisation signal (NLS) of E3 ubiquitin-protein ligase Mdm2 (MDM2), abrogating binding to Importin subunit alpha-1 (KPNA1). The exclusion from the nucleus is not complete however, as another NLS (466-473) is speculated to target splice variants to the nucleus, however, to the annotator it seems more likely that splice variants can dimerise with full-length MDM2 and be simultaneously transported into nucleus.
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MDM2_HUMANTRG_NES_CRM1_2190202Alternative splicing removes the nuclear export signal (NES) of E3 ubiquitin-protein ligase Mdm2 (MDM2), abrogating binding to Exportin-1 (XPO1).
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CTND1_HUMANTRG_NES_CRM1_1942956Alternative splicing removes the nuclear export signal (NES) of Catenin delta-1 (CTNND1), abrogating binding to Exportin-1 (XPO1). Despite demonstration of the importance of the NES for removing Catenin delta-1 (CTNND1) from the nucleus, those isoforms without NES are rarely found in the nucleus.
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NF2L1_HUMANTRG_NES_CRM1_2251259Alternative splicing removes the nuclear export signal (NES) of Nuclear factor erythroid 2-related factor 1 (NFE2L1), abrogating binding to Exportin-1 (XPO1). Only the full-length variant of NFE2L1 (Isoform 1 of Nuclear factor erythroid 2-related factor 1 (NFE2L1)) contains an NES and shows cytoplasmic localisation. The two other naturally occuring isoforms (of which at present only 1 is annotated in UniProtKB) lack the NES and show exclusive nuclear staining.
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BAIP2_HUMANLIG_PDZ_Class_1516521Alternative splicing removes the PDZ-binding motif of Isoform BAIAP2-alpha of Brain-specific angiogenesis inhibitor 1-associated protein 2 (BAIAP2), abrogating binding to Disks large homolog 3 (DLG3). The SH3 domain of Isoform BAIAP2-alpha of Brain-specific angiogenesis inhibitor 1-associated protein 2 (BAIAP2) also binds to SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), meaning it can link two prominent proteins of the postsynaptic NMDA-receptor complex, namely SHANK1 and DLG3.
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CAC1D_RATLIG_IQ16501669Alternative splicing removes the IQ motif of Voltage-dependent L-type calcium channel subunit alpha-1D (Cacna1d) abrogating binding to Calmodulin (Calm1). CaV1.3IQdelta (IQ-deleted Isoform CACN4B of Voltage-dependent L-type calcium channel subunit alpha-1D (Cacna1d)) channels exhibit a lack of calcium-dependent inactivation. CaV1.3IQdelta channel immunoreactivity was preferentially localised to cochlear outer hair cells (OHCs), whereas that of CaV1.3IQfull channels (IQ-possessing Isoform CACN4A of Voltage-dependent L-type calcium channel subunit alpha-1D (Cacna1d)) labelled inner hair cells (IHCs).
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DAB1_MOUSELIG_SH2_IA220223Alternative 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)).
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DAB1_MOUSELIG_SH2_IA232235Alternative 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)).
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DAB1_MOUSELIG_SH2_IA220223Alternative 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)).
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DAB1_MOUSELIG_SH2_IA232235Alternative 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)).
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DAB1_MOUSELIG_SH2_IA185188Alternative 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)).
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DAB1_MOUSELIG_SH2_SRC198201Alternative 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)).
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PRLR_HUMANDEG_SCF_TRCP1_1348353Alternative Splicing removes the degron motif of Prolactin receptor (PRLR) abrogating binding to F-box/WD repeat-containing protein 11 (FBXW11). SCF-beta-TrCP2 negatively regulates the long isoform of PRLR (Isoform 1 of Prolactin receptor (PRLR)). Should be noted that TrCP2 has a predominately cytoplasmic localisation compared to TrCP1 that is located in the nucleus. The mechanism for the down-regulation of the intermediate (Isoform Intermediate of Prolactin receptor (PRLR)) and short (Isoform Short form 1a of Prolactin receptor (PRLR) and Isoform Short form 1b of Prolactin receptor (PRLR)) that lack the TrCP degron is still not known. However it should be noted that the short and intermediate are either partially deficient or entirely deficient in mediating the signal transduction pathways induced by PRL (see Kine et al. (1999) (here) and Ross et al. (1997) (here)). This though is likely due to the missing STAT5-SH2-binding motif.
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PRLR_HUMANLIG_SH2_STAT5342345Alternative Splicing removes the degron motif of Prolactin receptor (PRLR), abrogating binding to Signal transducer and activator of transcription 5A (STAT5A). The PRLR S1a (Isoform Short form 1a of Prolactin receptor (PRLR)) and S1b and (Isoform Short form 1b of Prolactin receptor (PRLR)) isoforms were unable to mediate the transcriptional activation of the beta-casein promoter via the JAK-STAT5 pathway. Therefore these two splice variants act as dominant negatives on the full-length version LF (Isoform 1 of Prolactin receptor (PRLR)). Another study showed that different splice variants of heterodimers (e.g. LF/S1a, LF/S1b) that were able to induce JAK2 phosphorylation but not further signalling events due to lack of STAT recruitment (Qazi et al. (2006) (here)).
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SYN_DROMEMOD_PKA_139RNA editing removes the degron motif of Synapsin (Syn), abrogating binding to cAMP-dependent protein kinase catalytic subunit (Pka-C1). A genomic version of the protein sequence contains a canonical PKA-recognition motif that is highly conserved, however in Drosophilia, in all except the embryo sequences this sequence was RNA-edited to RGFS (from RRFS).
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AT2B4_HUMANLIG_PDZ_Class_112361241Alternative splicing removes the PDZ-binding motif of Plasma membrane calcium-transporting ATPase 4 (ATP2B4), abrogating binding to Disks large homolog 1 (DLG1). A much lower affinity was recorded for the third PDZ domain of DLG1 (in in the micromolar range (KD = 1.2 microM) compared to nanomolar affinity (KD = 1.6 nM)). PMCA4b and DLG1 are co-expressed in kidney and intestinal epithelial cells as well as in several areas of the brain.
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AT2B4_HUMANLIG_PDZ_Class_112361241Alternative splicing removes the PDZ-binding motif of Plasma membrane calcium-transporting ATPase 4 (ATP2B4), abrogating binding to Disks large homolog 3 (DLG3). Disks large homolog 3 (DLG3) did not bind to 'b' isoform of PMCA2. There is therefore an interaction selectivity between 'b' isoforms of ATP2B4 and DLG3 as opposed to the promiscuity of 'b' isoforms of ATP2B2 and ATP2B4 in interacting with other SAPs. Same study DLG4, DLG2 and DLG1 shown to bind to PDZ-binding motifs in 'b' isoforms of ATP2B4 and ATP2B2.
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KALRN_RATLIG_PDZ_Class_116491654Alternative splicing removes the PDZ-binding motif of Isoform Kalirin-7 of Kalirin (Kalrn), abrogating binding to Disks large homolog 4 (Dlg4). Isoform Kalirin-7 of Kalirin (Kalrn) is the most prevalent isoform in the adult rat hippocampus where it locates to the postsynaptic density via an interaction with Dlg4 and regulates dendritic morphogenesis.
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KALRN_RATLIG_PDZ_Class_116491654Alternative splicing removes the PDZ-binding motif of Isoform Kalirin-7 of Kalirin (Kalrn), abrogating binding to Disks large homolog 4 (Dlg4). Isoform Kalirin-7 of Kalirin (Kalrn) is the most prevalent isoform in the adult rat hippocampus where it locates to the postsynaptic density via an interaction with Dlg4 and regulates dendritic morphogenesis.
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NMDZ1_HUMANLIG_PDZ_Class_1917922Alternative splicing removes the PDZ-binding motif of Isoform 4 of Glutamate [NMDA] receptor subunit zeta-1 (GRIN1), abrogating binding to Disks large homolog 4 (DLG4). Binding of the PDZ domain of DLG4 suppresses an ER-retention motif in GRIN1, promoting its cell surface expression in a splice variant-specific manner.
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NMDZ1_HUMANLIG_PDZ_Class_1917922Alternative splicing removes the PDZ-binding motif of Isoform 4 of Glutamate [NMDA] receptor subunit zeta-1 (GRIN1), abrogating binding to Disks large homolog 4 (DLG4). Binding of the PDZ domain of DLG4 suppresses an ER-retention motif in GRIN1, promoting its cell surface expression in a splice variant-specific manner.
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GUAD_HUMANLIG_PDZ_Class_1449454Alternative splicing removes the PDZ-binding motif of Guanine deaminase (GDA) (Nedasin), abrogating binding to Disks large homolog 3 (DLG3). Isoform 1 of Guanine deaminase (GDA) (Nedasin S) is predominately expressed in neuronal tissues and binds PDZ domains. Isoform 3 of Guanine deaminase (GDA) (Nedasin V1), which is predominately expressed in non-neuronal tissues, does not bind PDZ domains. The presence of Nedasin S inhibits binding of NMDA receptors and K+ channels to PDZ domain-containing proteins such as members of the MAGUK family. This suggests that GDA might modulate the receptor clustering function of the PDZ domains of MAGUK family members, and this modulation is regulated by alternative splicing of GDA transcripts.
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SIG12_MOUSELIG_TYR_ITIM430435Alternative splicing removes the ITIM (immunoreceptor tyrosine-based inhibitory motif) of Sialic acid-binding Ig-like lectin 12 (Siglec12), abrogating binding to Tyrosine-protein phosphatase non-receptor type 6 (Ptpn6).
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SIG12_MOUSELIG_TYR_ITIM430435Alternative splicing removes the ITIM (immunoreceptor tyrosine-based inhibitory motif) of Sialic acid-binding Ig-like lectin 12 (Siglec12), abrogating binding to Tyrosine-protein phosphatase non-receptor type 11 (Ptpn11).
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TRML1_HUMANLIG_TYR_ITIM279284Alternative splicing removes the ITIM (immunoreceptor tyrosine-based inhibitory motif) of Trem-like transcript 1 protein (TREML1), abrogating binding to Tyrosine-protein phosphatase non-receptor type 11 (PTPN11).
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SHIP1_HUMANLIG_SH2_IIA918921Alternative splicing partially removes the SH2-binding motif of Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1 (Inpp5d), partially inhibiting binding to Phosphatidylinositol 3-kinase regulatory subunit alpha (Pik3r1).
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LMP2_EBVB9LIG_WW_15760Alternative splicing removes the WW-binding motif of Latent membrane protein 2 (LMP2), abrogating binding to E3 ubiquitin-protein ligase Itchy (Itch).
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AT2B1_HUMANLIG_IQ_211141128Alternative splicing partially removes the IQ motif of Isoform CI of Plasma membrane calcium-transporting ATPase 1 (ATP2B1), partially inhibiting binding to Calmodulin (CALM1).
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DBLOH_HUMANLIG_BIR_internal5659Alternative splicing removes the BIR-binding motif of Diablo homolog, mitochondrial (DIABLO), abrogating binding to Baculoviral IAP repeat-containing protein 4 (XIAP). Isoform SMAC3 of Diablo homolog, mitochondrial (DIABLO) is localised to mitochondria via its mitochondrial localisation signal (MLS). Upon entry in mitochondria the MLS is cleaved and Isoform SMAC3 of Diablo homolog, mitochondrial (DIABLO) is found localised with cytochrome-c. During apoptosis, Isoform SMAC3 of Diablo homolog, mitochondrial (DIABLO) binds to the second/third BIR domain of Baculoviral IAP repeat-containing protein 4 (XIAP). This interaction disrupts binding of XIAP to processed Caspase-9 (CASP9) and promotes Caspase-3 (CASP3) activation. Isoform SMAC3 of Diablo homolog, mitochondrial (DIABLO) also promotes ubiquitination of XIAP and subsequent degradation. Isoform 1 of Diablo homolog, mitochondrial (DIABLO) on the other hand did not cause degradation of XIAP.
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SYNJ1_HUMANLIG_EH_113931397Alternative splicing removes the EH-binding motif of Synaptojanin-1 (SYNJ1), abrogating binding to Epidermal growth factor receptor substrate 15 (EPS15). Isoform Synaptojanin-170 of Synaptojanin-1 (SYNJ1) is associated with clathrin-mediated endocytosis as a negative regulator of coat-membrane interaction. This isoform is virtually absent from mature neuronal synapses, where clathrin-mediated endocytosis plays a critical role and where Isoform Synaptojanin-145 of Synaptojanin-1 (SYNJ1) is by far the major synaptojanin isoform. Isoform Synaptojanin-145 of Synaptojanin-1 (SYNJ1) may be recruited early to clathrin-coated pits of synapses, either indirectly by adaptors that bind clathrin and AP-2, such as Amphiphysin (AMPH), or by interactions of endophilin family dimers with synaptic vesicle cargo, such as the vesicular glutamate transport.
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SYNJ1_HUMANLIG_EH_114031407Alternative splicing removes the EH-binding motif of Synaptojanin-1 (SYNJ1), abrogating binding to Epidermal growth factor receptor substrate 15 (EPS15). Isoform Synaptojanin-170 of Synaptojanin-1 (SYNJ1) is associated with clathrin-mediated endocytosis as a negative regulator of coat-membrane interaction. This isoform is virtually absent from mature neuronal synapses, where clathrin-mediated endocytosis plays a critical role and where Isoform Synaptojanin-145 of Synaptojanin-1 (SYNJ1) is by far the major synaptojanin isoform. Isoform Synaptojanin-145 of Synaptojanin-1 (SYNJ1) may be recruited early to clathrin-coated pits of synapses, either indirectly by adaptors that bind clathrin and AP-2, such as Amphiphysin (AMPH), or by interactions of endophilin family dimers with synaptic vesicle cargo, such as the vesicular glutamate receptor transport.
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SYNJ1_HUMANLIG_EH_114141418Alternative splicing removes the EH-binding motif of Synaptojanin-1 (SYNJ1), abrogating binding to Epidermal growth factor receptor substrate 15 (EPS15). Isoform Synaptojanin-170 of Synaptojanin-1 (SYNJ1) is associated with clathrin-mediated endocytosis as a negative regulator of coat-membrane interaction. This isoform is virtually absent from mature neuronal synapses, where clathrin-mediated endocytosis plays a critical role and where Isoform Synaptojanin-145 of Synaptojanin-1 (SYNJ1) is by far the major synaptojanin isoform. Isoform Synaptojanin-145 of Synaptojanin-1 (SYNJ1) may be recruited early to clathrin-coated pits of synapses, either indirectly by adaptors that bind clathrin and AP-2, such as Amphiphysin (AMPH), or by interactions of endophilin family dimers with synaptic vesicle cargo, such as the vesicular glutamate receptor transport.
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SYNJ1_HUMANLIG_EH_113931397Alternative splicing removes the EH-binding motif of Synaptojanin-1 (SYNJ1), abrogating binding to Epidermal growth factor receptor substrate 15 (EPS15). Isoform Synaptojanin-170 of Synaptojanin-1 (SYNJ1) is associated with clathrin-mediated endocytosis as a negative regulator of coat-membrane interaction. This isoform is virtually absent from mature neuronal synapses, where clathrin-mediated endocytosis plays a critical role and where Isoform Synaptojanin-145 of Synaptojanin-1 (SYNJ1) is by far the major synaptojanin isoform. Isoform Synaptojanin-145 of Synaptojanin-1 (SYNJ1) may be recruited early to clathrin-coated pits of synapses, either indirectly by adaptors that bind clathrin and AP-2, such as Amphiphysin (AMPH), or by interactions of endophilin family dimers with synaptic vesicle cargo, such as the vesicular glutamate transport.
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SYNJ1_HUMANLIG_EH_114031407Alternative splicing removes the EH-binding motif of Synaptojanin-1 (SYNJ1), abrogating binding to Epidermal growth factor receptor substrate 15 (EPS15). Isoform Synaptojanin-170 of Synaptojanin-1 (SYNJ1) is associated with clathrin-mediated endocytosis as a negative regulator of coat-membrane interaction. This isoform is virtually absent from mature neuronal synapses, where clathrin-mediated endocytosis plays a critical role and where Isoform Synaptojanin-145 of Synaptojanin-1 (SYNJ1) is by far the major synaptojanin isoform. Isoform Synaptojanin-145 of Synaptojanin-1 (SYNJ1) may be recruited early to clathrin-coated pits of synapses, either indirectly by adaptors that bind clathrin and AP-2, such as Amphiphysin (AMPH), or by interactions of endophilin family dimers with synaptic vesicle cargo, such as the vesicular glutamate receptor transport.
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SYNJ1_HUMANLIG_EH_114141418Alternative splicing removes the EH-binding motif of Synaptojanin-1 (SYNJ1), abrogating binding to Epidermal growth factor receptor substrate 15 (EPS15). Isoform Synaptojanin-170 of Synaptojanin-1 (SYNJ1) is associated with clathrin-mediated endocytosis as a negative regulator of coat-membrane interaction. This isoform is virtually absent from mature neuronal synapses, where clathrin-mediated endocytosis plays a critical role and where Isoform Synaptojanin-145 of Synaptojanin-1 (SYNJ1) is by far the major synaptojanin isoform. Isoform Synaptojanin-145 of Synaptojanin-1 (SYNJ1) may be recruited early to clathrin-coated pits of synapses, either indirectly by adaptors that bind clathrin and AP-2, such as Amphiphysin (AMPH), or by interactions of endophilin family dimers with synaptic vesicle cargo, such as the vesicular glutamate receptor transport.
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PAXI_HUMANLIG_SH2_IB118121Alternative splicing removes the SH2-binding motif of Paxillin (PXN), abrogating binding to Ras GTPase-activating protein 1 (RASA1).
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5HT4R_MOUSELIG_PDZ_Class_1382387Alternative splicing removes the PDZ-binding motif of Isoform 5-HT4(A) of 5-hydroxytryptamine receptor 4 (Htr4), abrogating binding to Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (Slc9a3r1). Isoform 5-HT4(A) of 5-hydroxytryptamine receptor 4 (Htr4) interacts specifically with a protein complex including Slc9a3r1 and Ezrin (Ezr) that might participate in its targeting to specialised subcellular regions, such as microvilli.
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ERBB4_HUMANLIG_SH2_IIA10561059Alternative splicing removes the SH2-binding motif of Receptor tyrosine-protein kinase erbB-4 (ERBB4), abrogating binding to Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1). The SH2-binding motif overlaps with a WW-binding motif. Binding of these motifs is regulated in a phosphorylation-dependent manner, ensuring ERBB4 is either endocytosed or stabilised.
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ERBB4_HUMANLIG_WW_110531056Alternative 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.
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AMOT_HUMANLIG_WW_1239242Alternative 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.
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PKHM2_HUMANLIG_TPR_Kinesin_1236240Alternative splicing removes the Kinesin Light Chain-binding motif of Pleckstrin homology domain-containing family M member 2 (PLEKHM2), abrogating binding to Kinesin light chain 2 (KLC2). Pleckstrin homology domain-containing family M member 2 (PLEKHM2) contains kinesin light chain (KLC) binding WD motifs (second motif at 205-210), and these are required for kinesin-1 recruitment and the peripheral movement of lysosomes. ADP-ribosylation factor-like protein 8B (ARL8B) and PLEKHM2 act together to recruit kinesin-1 to lysosomes and hence direct their movement toward microtubule plus ends. A splice variant of PLEKHM2 that lacks a light chain binding motif does not stimulate movement, suggesting fine-tuning by alternative splicing.
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PML_HUMANLIG_SUMO_SBM_1556566Alternative splicing removes the Sumoylation interacting motif (SIM) of Protein PML (PML), abrogating binding to Small ubiquitin-related modifier 1 (SUMO1) in Isoform TRIM19epsilon of Protein PML (PML). Isoforms lacking the SIM were resistant to As2O3-induced PML degradation.
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NFAC1_HUMANMOD_SUMO701704Alternative splicing removes the Sumoylation motif (SIM) of Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1), preventing the sumolyation of Isoform A-alpha of Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1). Both the Isoform C-alpha of Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1) and Isoform A-alpha of Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1) exert a differential effect upon IL-2 expression. However, the longer isoform, Isoform C-alpha of Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1), has a sumoylation motif and is therefore negatively regulated in a sumolyation-dependent manner.
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NFAC1_HUMANMOD_SUMO913916Alternative splicing removes the Sumoylation motif (SIM) of Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1), preventing the sumolyation of Isoform A-alpha of Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1). Both the Isoform C-alpha of Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1) and Isoform A-alpha of Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1) exert a differential effect upon IL-2 expression. However, the longer isoform, Isoform C-alpha of Nuclear factor of activated T-cells, cytoplasmic 1 (NFATC1), has a sumoylation motif and is therefore negatively regulated in a sumolyation-dependent manner.
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Type: Cumulative Subtype: Rheostatic
Rheostatic switches gradually alter the affinity of a motif for a single binding partner by addition of multiple PTMs that additively contribute to this modulation. Additional modifications can either strengthen or weaken an interaction.
P53_HUMANLIG_PH_Tfb15056Multisite 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).
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EGFR_HUMANLIG_TKB10691074While 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).
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SPY2_HUMANLIG_TKB5560While phosphorylation of Y55 induces binding, additional phosphorylation of T56 in the TKB-binding motif of Protein sprouty homolog 2 (SPRY2) lowers its binding affinity for E3 ubiquitin-protein ligase CBL (CBL).
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XRCC1_HUMANLIG_FHA_2517
521
523
527
Two 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.
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A4_HUMANLIG_SH2_GRB2757760While 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.
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ITB3_HUMANLIG_PTB_Phospho_1779785While 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.
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APC_HUMANLIG_SxIP_EBH_128012811Phosphorylation 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).
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P53_HUMANLIG_TAZ21925Multisite 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).
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DAXX_HUMANLIG_SUMO_SBM_1734740Multisite 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).
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MK67I_HUMANLIG_FHA_2238244Phosphorylation 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
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SMAD3_HUMANLIG_WW_Nedd4L203210CDK8/9 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.
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Type: Uncategorised Subtype: Uncategorised
Switches that have unique regulatory mechanisms. As more instances accumulate these switches may be worthy of a novel switch type
PPAL_HUMANTRG_ENDOCYTIC_2413416Phosphorylation 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.
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WASP_HUMANLIG_GBD_WASP_1466476Phosphorylation 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).
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WASL_HUMANLIG_GBD_WASP_1467477Phosphorylation of Neural Wiskott-Aldrich syndrome protein (WASL) at Y256 destabilises the auto-inhibitory intramolecular interaction of Neural Wiskott-Aldrich syndrome protein (WASL).
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PML_HUMANMOD_SUMO159162Sumoylation of K160 induces binding to the Protein PML (PML) protein. SUMO-modified forms of PML are essential for the recruitment of Protein PML (PML) to PML nuclear bodies.
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DAXX_HUMANLIG_SUMO_SBM_1733740Sumoylation of K160 induces binding to the Protein PML (PML) protein. SUMO-modified forms of PML are essential for the recruitment of Death domain-associated protein 6 (DAXX) to PML nuclear bodies.
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PML_HUMANMOD_SUMO159162Sumoylation of K160 induces binding to the Protein PML (PML) protein. SUMO-modified forms of PML are essential for the recruitment of Death domain-associated protein 6 (DAXX) to PML nuclear bodies.
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DAXX_HUMANLIG_SUMO_SBM_1733740Sumoylation of K160 induces binding to the Protein PML (PML) protein. SUMO-modified forms of PML are essential for the recruitment of Death domain-associated protein 6 (DAXX) to PML nuclear bodies.
details

Type: Specificity Subtype: Altered binding specificity
The balance of the competition for overlapping or adjacent, mutually exclusive interaction interfaces is tipped in favor of one of the interactors by PTM-dependent modulation of the intrinsic affinity of a binding region. Multiple, successive PTMs allow sequential switching of different binding partners in an ordered manner by step-wise alteration of binding specificity.
ITB3_HUMANLIG_PTB_Apo_2767774Phosphorylation 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.
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ITB3_HUMANLIG_PTB_Phospho_1767773Phosphorylation 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.
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CCNE1_HUMANMOD_GSK3_1377384Phosphorylation 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.
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CCNE1_HUMANDEG_SCF_FBW7_1378384Phosphorylation 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.
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SMAD3_HUMANDOC_WW_Pin1_4176181CDK8/9 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
SMAD3_HUMANMOD_GSK3_1201208CDK8/9 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
SMAD3_HUMANLIG_WW_Nedd4L203210CDK8/9 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
SMAD3_HUMANLIG_WW_1181184CDK8/9 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.
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CTLA4_MOUSETRG_ENDOCYTIC_2201204Dephosphorylation 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.
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CTLA4_MOUSELIG_SH2_STAT5201204Dephosphorylation 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.
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DAG1_HUMANLIG_WW_1889892Adhesion-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).
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DAG1_HUMANLIG_SH2_SRC892895Adhesion-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).
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FGD1_HUMANMOD_GSK3_1280287Phosphorylation 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.
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FGD1_HUMANDEG_SCF_TRCP1_1282287Phosphorylation 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.
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FGD3_HUMANMOD_GSK3_17784Phosphorylation 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.
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FGD3_HUMANMOD_GSK3_17380Phosphorylation 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.
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FGD3_HUMANDEG_SCF_TRCP1_17580Phosphorylation 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.
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MK67I_HUMANMOD_CDK235241Phosphorylation 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).
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MK67I_HUMANMOD_GSK3_1231238Phosphorylation 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).
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MK67I_HUMANMOD_GSK3_1227234Phosphorylation 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).
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MK67I_HUMANLIG_FHA_2238244Phosphorylation 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).
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MYC_HUMANMOD_ProDKin_15965Phosphorylation 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.
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MYC_HUMANMOD_GSK3_15562Phosphorylation 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.
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MYC_HUMANDEG_SCF_FBW7_15562Phosphorylation 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.
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JUN_HUMANMOD_GSK3_1236243Transcription 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.
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JUN_HUMANDEG_SCF_FBW7_1236243Transcription 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.
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CD3E_HUMANLIG_SH3_5184188Phosphorylation 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).
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CD3E_HUMANLIG_TYR_ITAM185202Phosphorylation 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).
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ITB2_HUMANLIG_Filamin753763Phosphorylation 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)).
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ITB2_HUMANLIG_14-3-3_3755760Phosphorylation 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)).
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DAG1_HUMANLIG_WW_1889892Adhesion-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).
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DAG1_HUMANLIG_SH2_SRC892895Adhesion-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).
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ERBB4_HUMANLIG_WW_110531056Phosphorylation-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.
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ERBB4_HUMANLIG_SH2_STAT510561059Phosphorylation-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.
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ATX1_HUMANLIG_ULM_U2AF65_1770775Phosphorylation 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.
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ATX1_HUMANLIG_14-3-3_1772777Phosphorylation 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.
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A4_HUMANLIG_PTB_Apo_2756763Phosphorylation 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).
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A4_HUMANLIG_SH2_GRB2757760Phosphorylation 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).
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ITB3_HUMANLIG_PTB_Apo_2779786Phosphorylation 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).
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ITB3_HUMANLIG_PTB_Phospho_1779785Phosphorylation 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).
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CCNE1_HUMANMOD_GSK3_1392399Phosphorylation 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.
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CCNE1_HUMANDEG_SCF_FBW7_1393399Phosphorylation 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.
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SRBP1_HUMANMOD_GSK3_1422430Phosphorylation 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.
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SRBP1_HUMANDEG_SCF_FBW7_1425430Phosphorylation 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.
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CTNB1_HUMANMOD_GSK3_13441Phosphorylation 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.
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CTNB1_HUMANMOD_GSK3_13037Phosphorylation 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.
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CTNB1_HUMANDEG_SCF_TRCP1_13237Phosphorylation 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.
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SNAI1_HUMANMOD_GSK3_193100Phosphorylation 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.
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SNAI1_HUMANDEG_SCF_TRCP1_195100Phosphorylation 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.
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YAP1_HUMANMOD_LATS_1376382Phosphorylation of Yorkie homolog (YAP1) at S381 by Serine/threonine-protein kinase LATS1 (LATS1) (a key regulator of the Hippo Pathway) primes the sequence for phosphorylation by Casein kinase I isoform epsilon (CSNK1E) at S384 and S387. This targets YAP1 to the SCF ubiqutin ligase complex, F-box/WD repeat-containing protein 1A (BTRC), which marks is YAP1 for subsequent degradation by the proteasomal system. N.B. Serine/threonine-protein kinase LATS2 (LATS2) can replace LATS1 and Casein kinase I isoform delta (CSNK1D) can replace CSNK1E
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YAP1_HUMANMOD_CK1_1381387Phosphorylation of Yorkie homolog (YAP1) at S381 by Serine/threonine-protein kinase LATS1 (LATS1) (a key regulator of the Hippo Pathway) primes the sequence for phosphorylation by Casein kinase I isoform epsilon (CSNK1E) at S384 and S387. This targets YAP1 to the SCF ubiqutin ligase complex, F-box/WD repeat-containing protein 1A (BTRC), which marks is YAP1 for subsequent degradation by the proteasomal system. N.B. Serine/threonine-protein kinase LATS2 (LATS2) can replace LATS1 and Casein kinase I isoform delta (CSNK1D) can replace CSNK1E
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YAP1_HUMANMOD_CK1_1384390Phosphorylation of Yorkie homolog (YAP1) at S381 by Serine/threonine-protein kinase LATS1 (LATS1) (a key regulator of the Hippo Pathway) primes the sequence for phosphorylation by Casein kinase I isoform epsilon (CSNK1E) at S384 and S387. This targets YAP1 to the SCF ubiqutin ligase complex, F-box/WD repeat-containing protein 1A (BTRC), which marks is YAP1 for subsequent degradation by the proteasomal system. N.B. Serine/threonine-protein kinase LATS2 (LATS2) can replace LATS1 and Casein kinase I isoform delta (CSNK1D) can replace CSNK1E
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YAP1_HUMANDEG_SCF_TRCP1_2383387Phosphorylation of Yorkie homolog (YAP1) at S381 by Serine/threonine-protein kinase LATS1 (LATS1) (a key regulator of the Hippo Pathway) primes the sequence for phosphorylation by Casein kinase I isoform epsilon (CSNK1E) at S384 and S387. This targets YAP1 to the SCF ubiqutin ligase complex, F-box/WD repeat-containing protein 1A (BTRC), which marks is YAP1 for subsequent degradation by the proteasomal system. N.B. Serine/threonine-protein kinase LATS2 (LATS2) can replace LATS1 and Casein kinase I isoform delta (CSNK1D) can replace CSNK1E
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DAXX_HUMANLIG_SUMO_SBM_1733740Acetylation of K33 in the SUMO2 inhibits binding to the Death domain-associated protein 6 (DAXX) protein see switch details. SUMO-modified forms of Protein PML (PML) are essential for the recruitment of Small ubiquitin-related modifier 2 (SUMO2) to PML nuclear bodies. The acetylated versions of SUMO1/2 failed to trigger recruitment of Small ubiquitin-related modifier 2 (SUMO2) into the nuclear bodies. An additional interaction is also possible upon acetylation with the Bromodomain of Histone acetyltransferase p300 (EP300) shown to bind the acetylated version of SUMO2. This does not occur with acetylated SUMO1. Acetylation is countered by Histone deacetylase family, HD type 1 subfamily.
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SUMO2_HUMANLIG_BROMO3333Acetylation of K33 in the SUMO2 inhibits binding to the Death domain-associated protein 6 (DAXX) protein see switch details. SUMO-modified forms of Protein PML (PML) are essential for the recruitment of Small ubiquitin-related modifier 2 (SUMO2) to PML nuclear bodies. The acetylated versions of SUMO1/2 failed to trigger recruitment of Small ubiquitin-related modifier 2 (SUMO2) into the nuclear bodies. An additional interaction is also possible upon acetylation with the Bromodomain of Histone acetyltransferase p300 (EP300) shown to bind the acetylated version of SUMO2. This does not occur with acetylated SUMO1. Acetylation is countered by Histone deacetylase family, HD type 1 subfamily.
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Type: Binary Subtype: Allostery
The binding properties of a motif or a motif-binding domain are modulated indirectly by allosteric effects resulting from PTM or effector binding at a site that is distinct from the actual interaction interface.
TGON3_RATTRG_ENDOCYTIC_2350353Binding of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate to the AP-2 complex alpha, beta and mu subunits exposes a binding site on the AP-2 complex subunit mu (Ap2m1) subunit for recruitment of Trans-Golgi network integral membrane protein TGN38 (Ttgn1) via an endocytosis motif.
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CD3E_HUMANLIG_SH3_5184188Ligand binding to the T cell receptor complex TCR-CD3 results in a conformational change that exposes an SH3-binding motif in T-cell surface glycoprotein CD3 epsilon chain (CD3E), resulting in recruitment of Cytoplasmic protein NCK2 (NCK2), involved in T cell activation.
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PDC6I_HUMANLIG_ALG2801810Binding of calcium(2+) to Programmed cell death protein 6 (PDCD6) opens a hydrophobic pocket on Programmed cell death protein 6 (PDCD6) that is required for binding of Programmed cell death 6-interacting protein (PDCD6IP).
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CDC20_HUMANLIG_MAD2129137Binding of Mad1-bound Closed (C-) Mitotic spindle assembly checkpoint protein MAD2A (MAD2L1) to Open (O-) Mitotic spindle assembly checkpoint protein MAD2A (MAD2L1) switches conformation of the latter to the C conformation, making the binding site for Cell division cycle protein 20 homolog (CDC20) available. This sequesters Cell division cycle protein 20 homolog (CDC20) to the spindle assembly checkpoint and prevents onset of anaphase.
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ARRB1_HUMANTRG_AP2beta_CARGO_1385395Binding of Beta-arrestin-1 (ARRB1) to ligand-induced, phosphorylated GPCRs results in a conformational change that makes the AP2-beta interaction motif in Beta-arrestin-1 (ARRB1) accessible for binding to AP-2 complex subunit beta (AP2B1), which mediates internalization of the GPCR.
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CD4_HUMANTRG_LysEnd_APsAcLL_1434439Binding of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate to the AP-2 complex alpha, beta and mu subunits exposes a binding site on the AP-2 complex subunit sigma (AP2S1) subunit for recruitment of T-cell surface glycoprotein CD4 (CD4) via an endocytosis motif.
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CTNB1_HUMANLIG_PDZ_Class_1776781Binding of Ezrin (EZR) via its FERM domain to the EB domain of Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (SLC9A3R1) results in allosteric coupling to the second PDZ domain of Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (SLC9A3R1), which results in relief of the intramolecular interaction with the PDZ binding ligand, thereby increasing the affinity of the PDZ domain for other ligands, including Catenin beta-1 (CTNNB1).
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RECO_BOVINMOD_NMyristoyl17Binding of calcium(2+) to Recoverin (RCVRN) results in a conformational change in Recoverin that makes the myristoyl moiety available for binding to the membrane.
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KAPCA_HUMANMOD_NMyristoyl17Phosphorylation of cAMP-dependent protein kinase catalytic subunit alpha (PRKACA) at S11 shifts the conformational equilibrium to the myristoyl-out conformation, making the myristoyl moiety available for interaction with the membrane.
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EGFR_HUMANTRG_ENDOCYTIC_29981001Binding of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate to the AP-2 complex alpha, beta and mu subunits exposes a binding site on the AP-2 complex subunit mu (AP2M1) subunit for recruitment of Epidermal growth factor receptor (EGFR) via an endocytosis motif.
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TFR1_HUMANTRG_ENDOCYTIC_22023Binding of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate to the AP-2 complex alpha, beta and mu subunits exposes a binding site on the AP-2 complex subunit mu (AP2M1) subunit for recruitment of Transferrin receptor protein 1 (TFRC) via an endocytosis motif.
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ENV_HTLV2TRG_ENDOCYTIC_2477480Binding of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate to the AP-2 complex alpha, beta and mu subunits exposes a binding site on the AP-2 complex subunit mu (AP2M1) subunit for recruitment of Envelope glycoprotein gp63 (env) via an endocytosis motif.
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VGLG_VSIVATRG_ENDOCYTIC_2501504Binding of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate to the AP-2 complex alpha, beta and mu subunits exposes a binding site on the AP-2 complex subunit mu (AP2M1) subunit for recruitment of Glycoprotein G (G) via an endocytosis motif.
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ENV_HV1H2TRG_ENDOCYTIC_2712715Binding of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate to the AP-2 complex alpha, beta and mu subunits exposes a binding site on the AP-2 complex subunit mu (AP2M1) subunit for recruitment of Envelope glycoprotein gp160 (env) via an endocytosis motif.
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ENV_SIVMKTRG_ENDOCYTIC_2723726Binding of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate to the AP-2 complex alpha, beta and mu subunits exposes a binding site on the AP-2 complex subunit mu (AP2M1) subunit for recruitment of Envelope glycoprotein gp160 (env) via an endocytosis motif.
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ASGR1_HUMANTRG_ENDOCYTIC_258Binding of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate to the AP-2 complex alpha, beta and mu subunits exposes a binding site on the AP-2 complex subunit mu (AP2M1) subunit for recruitment of Asialoglycoprotein receptor 1 (ASGR1) via an endocytosis motif.
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LAMP1_HUMANTRG_ENDOCYTIC_2414417Binding of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate to the AP-2 complex alpha, beta and mu subunits exposes a binding site on the AP-2 complex subunit mu (AP2M1) subunit for recruitment of Lysosome-associated membrane glycoprotein 1 (LAMP1) via an endocytosis motif.
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CTLA4_HUMANTRG_ENDOCYTIC_2201204Binding of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate to the AP-2 complex alpha, beta and mu subunits exposes a binding site on the AP-2 complex subunit mu (AP2M1) subunit for recruitment of Cytotoxic T-lymphocyte protein 4 (CTLA4) via an endocytosis motif.
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L1CAM_HUMANTRG_ENDOCYTIC_211761179Binding of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate to the AP-2 complex alpha, beta and mu subunits exposes a binding site on the AP-2 complex subunit mu (AP2M1) subunit for recruitment of Neural cell adhesion molecule L1 (L1CAM) via an endocytosis motif.
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ENV_BLVTRG_ENDOCYTIC_2487490Binding of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate to the AP-2 complex alpha, beta and mu subunits exposes a binding site on the AP-2 complex subunit mu (AP2M1) subunit for recruitment of Envelope glycoprotein (env) via an endocytosis motif.
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GE_VZVOTRG_ENDOCYTIC_2582585Binding of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate to the AP-2 complex alpha, beta and mu subunits exposes a binding site on the AP-2 complex subunit mu (AP2M1) subunit for recruitment of Envelope glycoprotein E (gE) via an endocytosis motif.
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NPC1_HUMANTRG_LysEnd_APsAcLL_112711276Binding of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate to the AP-2 complex alpha, beta and mu subunits exposes a binding site on the AP-2 complex subunit sigma (AP2S1) subunit for recruitment of Niemann-Pick C1 protein (NPC1) via an endocytosis motif.
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HG2A_HUMANTRG_LysEnd_APsAcLL_11924Binding of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate to the AP-2 complex alpha, beta and mu subunits exposes a binding site on the AP-2 complex subunit sigma (AP2S1) subunit for recruitment of HLA class II histocompatibility antigen gamma chain (CD74) via an endocytosis motif.
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CD3D_MOUSETRG_LysEnd_APsAcLL_1138143Binding of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate to the AP-2 complex alpha, beta and mu subunits exposes a binding site on the AP-2 complex subunit sigma (Ap2s1) subunit for recruitment of T-cell surface glycoprotein CD3 delta chain (Cd3d) via an endocytosis motif.
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NEF_HV1H2TRG_LysEnd_APsAcLL_1160165Binding of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate to the AP-2 complex alpha, beta and mu subunits exposes a binding site on the AP-2 complex subunit sigma (AP2S1) subunit for recruitment of Nef protein (nef) via an endocytosis motif.
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NEF_HV1B8TRG_LysEnd_APsAcLL_1159164Binding of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate to the AP-2 complex alpha, beta and mu subunits exposes a binding site on the AP-2 complex subunit sigma (AP2S1) subunit for recruitment of Protein Nef (nef) via an endocytosis motif.
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CD3G_MOUSETRG_LysEnd_APsAcLL_1149154Binding of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate to the AP-2 complex alpha, beta and mu subunits exposes a binding site on the AP-2 complex subunit sigma (Ap2s1) subunit for recruitment of T-cell surface glycoprotein CD3 gamma chain (Cd3g) via an endocytosis motif.
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CD44_HUMANTRG_LysEnd_APsAcLL_1708713Binding of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate to the AP-2 complex alpha, beta and mu subunits exposes a binding site on the AP-2 complex subunit sigma (AP2S1) subunit for recruitment of CD44 antigen (CD44) via an endocytosis motif.
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OPRD_HUMANTRG_LysEnd_APsAcLL_1241246Binding of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate to the AP-2 complex alpha, beta and mu subunits exposes a binding site on the AP-2 complex subunit sigma (AP2S1) subunit for recruitment of Delta-type opioid receptor (OPRD1) via an endocytosis motif.
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BCAM_HUMANTRG_LysEnd_APsAcLL_1604609Binding of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate to the AP-2 complex alpha, beta and mu subunits exposes a binding site on the AP-2 complex subunit sigma (AP2S1) subunit for recruitment of Basal cell adhesion molecule (BCAM) via an endocytosis motif.
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ENV_BLVTRG_LysEnd_APsAcLL_1463468Binding of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate to the AP-2 complex alpha, beta and mu subunits exposes a binding site on the AP-2 complex subunit sigma (AP2S1) subunit for recruitment of Envelope glycoprotein (env) via an endocytosis motif.
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BACE1_HUMANTRG_LysEnd_APsAcLL_1495500Binding of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate to the AP-2 complex alpha, beta and mu subunits exposes a binding site on the AP-2 complex subunit sigma (AP2S1) subunit for recruitment of Beta-secretase 1 (BACE1) via an endocytosis motif.
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ATP7A_HUMANTRG_LysEnd_APsAcLL_114831488Binding of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate to the AP-2 complex alpha, beta and mu subunits exposes a binding site on the AP-2 complex subunit sigma (AP2S1) subunit for recruitment of Copper-transporting ATPase 1 (ATP7A) via an endocytosis motif.
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NCOR1_HUMANLIG_CORNRBOX20512059Binding of the all-trans-retinoic acid ligand to the nuclear Retinoic acid receptor alpha (RARA) makes the binding site for the CORNRBOX motif of Nuclear receptor corepressor 1 (NCOR1) inaccessible.
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NCOR1_HUMANLIG_CORNRBOX22632271Binding of the all-trans-retinoic acid ligand to the nuclear Retinoic acid receptor alpha (RARA) makes the binding site for the CORNRBOX motif of Nuclear receptor corepressor 1 (NCOR1) inaccessible.
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NCOR2_HUMANLIG_CORNRBOX21432151Binding of the leukotriene D4 ligand to the nuclear Peroxisome proliferator-activated receptor alpha (PPARA) makes the binding site for the CORNRBOX motif of Nuclear receptor corepressor 2 (NCOR2) inaccessible.
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NCOR2_HUMANLIG_CORNRBOX23502358Binding of the leukotriene D4 ligand to the nuclear Peroxisome proliferator-activated receptor alpha (PPARA) makes the binding site for the CORNRBOX motif of Nuclear receptor corepressor 2 (NCOR2) inaccessible.
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NRIP1_HUMANLIG_NRBOX132138Binding of the estrogen ligand to the nuclear Estrogen receptor (ESR1) makes the binding site for the NRBOX motif of Nuclear receptor-interacting protein 1 (NRIP1) accessible.
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NRIP1_HUMANLIG_NRBOX184190Binding of the estrogen ligand to the nuclear Estrogen receptor (ESR1) makes the binding site for the NRBOX motif of Nuclear receptor-interacting protein 1 (NRIP1) accessible.
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NRIP1_HUMANLIG_NRBOX2026Binding of the estrogen ligand to the nuclear Estrogen receptor (ESR1) makes the binding site for the NRBOX motif of Nuclear receptor-interacting protein 1 (NRIP1) accessible.
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NRIP1_HUMANLIG_NRBOX265271Binding of the estrogen ligand to the nuclear Estrogen receptor (ESR1) makes the binding site for the NRBOX motif of Nuclear receptor-interacting protein 1 (NRIP1) accessible.
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NRIP1_HUMANLIG_NRBOX379385Binding of the estrogen ligand to the nuclear Estrogen receptor (ESR1) makes the binding site for the NRBOX motif of Nuclear receptor-interacting protein 1 (NRIP1) accessible.
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NRIP1_HUMANLIG_NRBOX499505Binding of the estrogen ligand to the nuclear Estrogen receptor (ESR1) makes the binding site for the NRBOX motif of Nuclear receptor-interacting protein 1 (NRIP1) accessible.
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NRIP1_HUMANLIG_NRBOX500506Binding of the estrogen ligand to the nuclear Estrogen receptor (ESR1) makes the binding site for the NRBOX motif of Nuclear receptor-interacting protein 1 (NRIP1) accessible.
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NRIP1_HUMANLIG_NRBOX712718Binding of the estrogen ligand to the nuclear Estrogen receptor (ESR1) makes the binding site for the NRBOX motif of Nuclear receptor-interacting protein 1 (NRIP1) accessible.
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NRIP1_HUMANLIG_NRBOX818824Binding of the estrogen ligand to the nuclear Estrogen receptor (ESR1) makes the binding site for the NRBOX motif of Nuclear receptor-interacting protein 1 (NRIP1) accessible.
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NRIP1_HUMANLIG_NRBOX935941Binding of the estrogen ligand to the nuclear Estrogen receptor (ESR1) makes the binding site for the NRBOX motif of Nuclear receptor-interacting protein 1 (NRIP1) accessible.
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NCOA2_HUMANLIG_NRBOX640646Binding of the glucocorticoid ligand to the nuclear Glucocorticoid receptor (NR3C1) makes the binding site for the NRBOX motif of Nuclear receptor coactivator 2 (NCOA2) accessible.
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NCOA2_HUMANLIG_NRBOX689695Binding of the glucocorticoid ligand to the nuclear Glucocorticoid receptor (NR3C1) makes the binding site for the NRBOX motif of Nuclear receptor coactivator 2 (NCOA2) accessible.
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NCOA2_HUMANLIG_NRBOX744750Binding of the glucocorticoid ligand to the nuclear Glucocorticoid receptor (NR3C1) makes the binding site for the NRBOX motif of Nuclear receptor coactivator 2 (NCOA2) accessible.
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MED1_HUMANLIG_NRBOX603609Binding of the 3,3',5-triiodo-L-thyronine ligand to the nuclear Thyroid hormone receptor alpha (THRA) makes the binding site for the NRBOX motif of Mediator of RNA polymerase II transcription subunit 1 (MED1) accessible.
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MED1_HUMANLIG_NRBOX644650Binding of the 3,3',5-triiodo-L-thyronine ligand to the nuclear Thyroid hormone receptor alpha (THRA) makes the binding site for the NRBOX motif of Mediator of RNA polymerase II transcription subunit 1 (MED1) accessible.
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NCOA6_MOUSELIG_NRBOX14941500Binding of the 15-deoxy-Delta(12,14)-prostaglandin J2 ligand to the nuclear Peroxisome proliferator-activated receptor gamma (Pparg) makes the binding site for the NRBOX motif of Nuclear receptor coactivator 6 (Ncoa6) accessible.
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WASP_HUMANLIG_GBD_WASP_1466476Binding of Cell division control protein 42 homolog (CDC42) to Wiskott-Aldrich syndrome protein (WAS) allosterically relieves an auto-inhibitory intramolecular interaction in Wiskott-Aldrich syndrome protein (WAS), which becomes active.
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WASP_HUMANLIG_GBD_WASP_1466476Binding of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate to Wiskott-Aldrich syndrome protein (WAS) allosterically relieves an auto-inhibitory intramolecular interaction in Wiskott-Aldrich syndrome protein (WAS), which becomes active.
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WASL_HUMANLIG_GBD_WASP_1467477Binding of Cell division control protein 42 homolog (CDC42) to Neural Wiskott-Aldrich syndrome protein (WASL) allosterically relieves an auto-inhibitory intramolecular interaction in Neural Wiskott-Aldrich syndrome protein (WASL), which becomes active.
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WASL_HUMANLIG_GBD_WASP_1467477Binding of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate to Neural Wiskott-Aldrich syndrome protein (WASL) allosterically relieves an auto-inhibitory intramolecular interaction in Neural Wiskott-Aldrich syndrome protein (WASL), which becomes active.
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S61A1_CANFALIG_IQ1331Binding of calcium(2+) to Calmodulin (Calm1) exposes a binding site on Calmodulin (Calm1) for the Calmodulin-binding IQ motif of Protein transport protein Sec61 subunit alpha isoform 1 (SEC61A1), an interaction that results in closure of the protein-conducting channel located in the ER.
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S61A1_CANFALIG_IQ1331Binding of calcium(2+) to Calmodulin (Calm1) exposes a binding site on Calmodulin (Calm1) for the Calmodulin-binding IQ motif of Protein transport protein Sec61 subunit alpha isoform 1 (SEC61A1), an interaction that results in closure of the protein-conducting channel located in the ER.
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Type: Pre‑assembly Subtype: Composite binding site formation
The formation of a complex results in the generation of a continuous motif-binding site that spans more than one component of this complex. Neither complex subunit on its own contains a functional binding domain for the motif, and interaction of the motif only occurs in the context of the active, fully assembled complex.
EDIL3_HUMANLIG_RGD9698Binding of EGF-like repeat and discoidin I-like domain-containing protein 3 (EDIL3) to integrin receptors depends on pre-assembly of Integrin alpha-V (ITGAV)-Integrin beta-3 (ITGB3) heterodimers, since association of the integrin alpha and beta subunits results in the formation of a composite binding site for the RGD motif in the ligand.
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DISG_TRIABLIG_RGD5153Binding of Disintegrin albolabrin to integrin receptors depends on pre-assembly of Integrin alpha-IIb (ITGA2B)-Integrin beta-3 (ITGB3) heterodimers, since association of the integrin alpha and beta subunits results in the formation of a composite binding site for the RGD motif in the ligand.
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FINC_HUMANLIG_RGD15241526Binding of Fibronectin (FN1) to integrin receptors depends on pre-assembly of Integrin alpha-V (ITGAV)-Integrin beta-3 (ITGB3) heterodimers, since association of the integrin alpha and beta subunits results in the formation of a composite binding site for the RGD motif in the ligand.
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POLG_FMDVOLIG_RGD869871Binding of Genome polyprotein to integrin receptors depends on pre-assembly of Integrin alpha-V (ITGAV)-Integrin beta-3 (ITGB3) heterodimers, since association of the integrin alpha and beta subunits results in the formation of a composite binding site for the RGD motif in the ligand.
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VTNC_HUMANLIG_RGD6466Binding of Vitronectin (VTN) to integrin receptors depends on pre-assembly of Integrin alpha-V (ITGAV)-Integrin beta-3 (ITGB3) heterodimers, since association of the integrin alpha and beta subunits results in the formation of a composite binding site for the RGD motif in the ligand.
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VWF_HUMANLIG_RGD25072509Binding of von Willebrand factor (VWF) to integrin receptors depends on pre-assembly of Integrin alpha-V (ITGAV)-Integrin beta-3 (ITGB3) heterodimers, since association of the integrin alpha and beta subunits results in the formation of a composite binding site for the RGD motif in the ligand.
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OSTP_HUMANLIG_RGD159161Binding of EGF-like repeat and discoidin I-like domain-containing protein 3 (EDIL3) to integrin receptors depends on pre-assembly of Integrin alpha-V (ITGAV)-Integrin beta-3 (ITGB3) heterodimers, since association of the integrin alpha and beta subunits results in the formation of a composite binding site for the RGD motif in the ligand.
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FINC_MOUSELIG_RGD16141616Binding of Fibronectin (Fn1) to integrin receptors depends on pre-assembly of Integrin alpha-5 (Itga5)-Integrin beta-1 (Itgb1) heterodimers, since association of the integrin alpha and beta subunits results in the formation of a composite binding site for the RGD motif in the ligand.
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VME1_TRIELLIG_RGD459461Binding of Zinc metalloproteinase/disintegrin to integrin receptors depends on pre-assembly of Integrin alpha-IIb (ITGA2B)-Integrin beta-3 (ITGB3) heterodimers, since association of the integrin alpha and beta subunits results in the formation of a composite binding site for the RGD motif in the ligand.
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DISB_TRIGALIG_RGD5153Binding of Disintegrin trigramin-beta-2 to integrin receptors depends on pre-assembly of Integrin alpha-IIb (ITGA2B)-Integrin beta-3 (ITGB3) heterodimers, since association of the integrin alpha and beta subunits results in the formation of a composite binding site for the RGD motif in the ligand.
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POLG_CXA9LIG_RGD858860Binding of Genome polyprotein to integrin receptors depends on pre-assembly of Integrin alpha-V (ITGAV)-Integrin beta-6 (ITGB6) heterodimers, since association of the integrin alpha and beta subunits results in the formation of a composite binding site for the RGD motif in the ligand.
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VTNC_MOUSELIG_RGD6466Binding of Vitronectin (Vtn) to integrin receptors depends on pre-assembly of Integrin alpha-V (Itgav)-Integrin beta-3 (Itgb3) heterodimers, since association of the integrin alpha and beta subunits results in the formation of a composite binding site for the RGD motif in the ligand.
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POLG_HPE1HLIG_RGD764766Binding of Genome polyprotein to integrin receptors depends on pre-assembly of Integrin alpha-V (ITGAV)-Integrin beta-6 (ITGB6) heterodimers, since association of the integrin alpha and beta subunits results in the formation of a composite binding site for the RGD motif in the ligand.
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FINC_HUMANLIG_Integrin_isoDGR_1263265Binding of Fibronectin (FN1) to integrin receptors depends on pre-assembly of Integrin alpha-V (ITGAV)-Integrin beta-3 (ITGB3) heterodimers, since association of the integrin alpha and beta subunits results in the formation of a composite binding site for the RGD motif in the ligand.
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CDN1B_HUMANMOD_CDK_1184190Binding 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.
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CDN1B_HUMANDEG_SCF_SKP2-CKS1_1183190Binding 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.
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CDN1C_HUMANMOD_CDK_1307313Binding 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).
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CDN1C_HUMANDEG_SCF_SKP2-CKS1_1306313Binding 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).
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CDN1C_MOUSEMOD_CDK_1339345Binding 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).
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CDN1C_MOUSEDEG_SCF_SKP2-CKS1_1338345Binding 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).
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IAA7_ARATHDEG_SCF_TIR1_18293Binding of Auxin-responsive protein IAA7 (IAA7) to Protein TRANSPORT INHIBITOR RESPONSE 1 (TIR1), an F-box substrate recognition subunit of the SCF E3 ubiquitin ligase, depends on binding of the plant hormone auxin to TIR1, as this pre-assembled complex provides a composite binding site for the degron motif in IAA7. Subsequent ubiquitylation of IAA7 by the SCF targets this transcriptional repressor for proteasomal degradation, a pre-requisite for the transcriptional response to auxin.
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IAA17_ARATHDEG_SCF_TIR1_18293Binding of Auxin-responsive protein IAA17 (IAA17) to Protein TRANSPORT INHIBITOR RESPONSE 1 (TIR1), an F-box substrate recognition subunit of the SCF E3 ubiquitin ligase, depends on binding of the plant hormone auxin to TIR1, as this pre-assembled complex provides a composite binding site for the degron motif in IAA17. Subsequent ubiquitylation of IAA17 by the SCF targets this transcriptional repressor for proteasomal degradation, a pre-requisite for the transcriptional response to auxin.
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IAA1_ARATHDEG_SCF_TIR1_15566Binding of Auxin-responsive protein IAA1 (IAA1) to Protein TRANSPORT INHIBITOR RESPONSE 1 (TIR1), an F-box substrate recognition subunit of the SCF E3 ubiquitin ligase, depends on binding of the plant hormone auxin to TIR1, as this pre-assembled complex provides a composite binding site for the degron motif in IAA1. Subsequent ubiquitylation of IAA1 by the SCF targets this transcriptional repressor for proteasomal degradation, a pre-requisite for the transcriptional response to auxin.
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IAA28_ARATHDEG_SCF_TIR1_14859Binding of Auxin-responsive protein IAA28 (IAA28) to Protein TRANSPORT INHIBITOR RESPONSE 1 (TIR1), an F-box substrate recognition subunit of the SCF E3 ubiquitin ligase, depends on binding of the plant hormone auxin to TIR1, as this pre-assembled complex provides a composite binding site for the degron motif in IAA28. Subsequent ubiquitylation of IAA28 by the SCF targets this transcriptional repressor for proteasomal degradation, a pre-requisite for the transcriptional response to auxin.
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IAA12_ARATHDEG_SCF_TIR1_16980Binding of Auxin-responsive protein IAA12 (IAA12) to Protein TRANSPORT INHIBITOR RESPONSE 1 (TIR1), an F-box substrate recognition subunit of the SCF E3 ubiquitin ligase, depends on binding of the plant hormone auxin to TIR1, as this pre-assembled complex provides a composite binding site for the degron motif in IAA12. Subsequent ubiquitylation of IAA12 by the SCF targets this transcriptional repressor for proteasomal degradation, a pre-requisite for the transcriptional response to auxin.
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IAA3_ARATHDEG_SCF_TIR1_16475Binding of Auxin-responsive protein IAA3 (IAA3) to Protein TRANSPORT INHIBITOR RESPONSE 1 (TIR1), an F-box substrate recognition subunit of the SCF E3 ubiquitin ligase, depends on binding of the plant hormone auxin to TIR1, as this pre-assembled complex provides a composite binding site for the degron motif in IAA3. Subsequent ubiquitylation of IAA3 by the SCF targets this transcriptional repressor for proteasomal degradation, a pre-requisite for the transcriptional response to auxin.
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TIF6B_ARATHDEG_SCF_COI1_1303320Binding of Protein TIFY 6B (TIFY6B) to Coronatine-insensitive protein 1 (COI1), an F-box substrate recognition subunit of the SCF E3 ubiquitin ligase, depends on binding of the plant hormone jasmonate to COI1, as this pre-assembled complex provides a composite binding site for the degron motif in TIFY6B. Subsequent ubiquitylation of TIFY6B by the SCF targets this transcriptional repressor for proteasomal degradation, a pre-requisite for the transcriptional response to jasmonate.
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TI10A_ARATHDEG_SCF_COI1_1203220Binding of Protein TIFY 10A (TIFY10A) to Coronatine-insensitive protein 1 (COI1), an F-box substrate recognition subunit of the SCF E3 ubiquitin ligase, depends on binding of the plant hormone jasmonate to COI1, as this pre-assembled complex provides a composite binding site for the degron motif in TIFY10A. Subsequent ubiquitylation of TIFY10A by the SCF targets this transcriptional repressor for proteasomal degradation, a pre-requisite for the transcriptional response to jasmonate.
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TIF7_ARATHDEG_SCF_COI1_1221238Binding of Protein TIFY 7 (TIFY7) to Coronatine-insensitive protein 1 (COI1), an F-box substrate recognition subunit of the SCF E3 ubiquitin ligase, depends on binding of the plant hormone jasmonate to COI1, as this pre-assembled complex provides a composite binding site for the degron motif in TIFY7. Subsequent ubiquitylation of TIFY7 by the SCF targets this transcriptional repressor for proteasomal degradation, a pre-requisite for the transcriptional response to jasmonate.
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TI10B_ARATHDEG_SCF_COI1_1205222Binding of Protein TIFY 10B (TIFY10B) to Coronatine-insensitive protein 1 (COI1), an F-box substrate recognition subunit of the SCF E3 ubiquitin ligase, depends on binding of the plant hormone jasmonate to COI1, as this pre-assembled complex provides a composite binding site for the degron motif in TIFY10B. Subsequent ubiquitylation of TIFY10B by the SCF targets this transcriptional repressor for proteasomal degradation, a pre-requisite for the transcriptional response to jasmonate.
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A7XXZ0_SOLLCDEG_SCF_COI1_1199216Binding of LOC100134911 to Coi1, an F-box substrate recognition subunit of the SCF E3 ubiquitin ligase, depends on binding of the plant hormone jasmonate to COI1, as this pre-assembled complex provides a composite binding site for the degron motif in the JAZ protein. Subsequent ubiquitylation of the JAZ protein by the SCF targets this transcriptional repressor for proteasomal degradation, a pre-requisite for the transcriptional response to jasmonate.
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B2XVS2_SOLLCDEG_SCF_COI1_1251268Binding of to Coi1, an F-box substrate recognition subunit of the SCF E3 ubiquitin ligase, depends on binding of the plant hormone jasmonate to COI1, as this pre-assembled complex provides a composite binding site for the degron motif in the JAZ protein. Subsequent ubiquitylation of the JAZ protein by the SCF targets this transcriptional repressor for proteasomal degradation, a pre-requisite for the transcriptional response to jasmonate.
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