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Group by :Switch typeMotif classProteinEnzymePathway            Group Index    Colouring Info              Filtered: ELM:LIG_WW_1 (19 hits) x
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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
Amiloride-sensitive sodium channel subunit gammaAngiomotinDystroglycan
Latent membrane protein 2 (Epstein-Barr)Mothers against decapentaplegic homolog 3Receptor tyrosine-protein kinase erbB-4
Transcription factor AP-1 (Mus)Tumor protein p73


MotifStartEndSwitch TypeSwitch SubtypeSwitch DescriptionInformation

Amiloride-sensitive sodium channel subunit gamma - SCNN1G -  Homo sapiens
LIG_WW_1624627SpecificityDomain hidingPhosphorylation of Isoform Nedd4-2a of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L) by Serine/threonine-protein kinase Sgk1 (SGK1) induces binding to 14-3-3 protein eta (YWHAH). This inhibits (whether allosterically or sterically is not known) interactions of NEDD4L via its WW domains with the PY motif in Amiloride-sensitive sodium channel subunit gamma (SCNN1G) (ENaC). As a result, ENaC does not get degraded and ENaC-mediated Na+ currents increase.
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Angiomotin - AMOT -  Homo sapiens
LIG_WW_1239242BinaryPre‑translationalAlternative splicing removes the WW-binding motif of Angiomotin (AMOT), abrogating binding to Yorkie homolog (YAP1). The splice specific Isoform p130 of Angiomotin (AMOT) of AMOT works within the Hippo pathway to sequester the transcription coactivator YAP1 away at tight junction. In contrast Isoform p80 of Angiomotin (AMOT) of AMOT lacks WW-binding motif.
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LIG_WW_1239242BinaryPre‑translationalAlternative splicing removes the WW-binding motif of Angiomotin (AMOT), abrogating binding to WW domain-containing transcription regulator protein 1 (WWTR1). The splice specific Isoform p130 of Angiomotin (AMOT) of AMOT works within the Hippo pathway to sequester the transcription coactivator YAP1 away at tight junction. In contrast Isoform p80 of Angiomotin (AMOT) of AMOT lacks WW-binding motif.
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LIG_WW_1239242BinaryPre‑translationalAlternative splicing removes the WW-binding motif of Angiomotin (AMOT), abrogating binding to Yorkie homolog (YAP1). The splice specific Isoform p130 of Angiomotin (AMOT) of AMOT works within the Hippo pathway to sequester the transcription coactivator YAP1 away at tight junction. In contrast Isoform p80 of Angiomotin (AMOT) of AMOT lacks WW-binding motif.
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Dystroglycan - DAG1 -  Homo sapiens
LIG_WW_1889892SpecificityAltered binding specificityAdhesion-dependent phosphorylation of Y892 in Dystroglycan (DAG1) by Src kinase (Proto-oncogene tyrosine-protein kinase Src (SRC)) switches the specificity of DAG1 from the WW domain containing cytoskeletal linker Dystrophin (DMD) to the SH2 domain containing Tyrosine-protein kinase Fyn (FYN).
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LIG_WW_1889892SpecificityAltered binding specificityAdhesion-dependent phosphorylation of Y892 in Dystroglycan (DAG1) by c-Src (SRC) switches the specificity of DAG1 from WW domain containing proteins like Utrophin (UTRN) to SH2 domain containing proteins like Tyrosine-protein kinase CSK (CSK).
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LIG_WW_1889892SpecificityCompetitionThe WW-binding motif for Dystrophin (DMD) and the SH3-binding motif for Growth factor receptor-bound protein 2 (GRB2) on Dystroglycan (DAG1) overlap, making their interactions mutually exclusive and competitive.
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LIG_WW_1889892SpecificityCompetitionThe WW-binding motif for Dystrophin (DMD) and the SH3-binding motif for Growth factor receptor-bound protein 2 (GRB2) on Dystroglycan (DAG1) overlap, making their interactions mutually exclusive and competitive.
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Latent membrane protein 2 - LMP2 -  Epstein-Barr virus (strain B95-8)
LIG_WW_15760BinaryPre‑translationalAlternative splicing removes the WW-binding motif of Latent membrane protein 2 (LMP2), abrogating binding to E3 ubiquitin-protein ligase Itchy (Itch).
details
LIG_WW_198101BinaryPre‑translationalAlternative splicing removes the WW-binding motif of Latent membrane protein 2 (LMP2), abrogating binding to E3 ubiquitin-protein ligase Itchy (Itch).
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LIG_WW_15760BinaryPre‑translationalAlternative splicing removes the WW-binding motif of Latent membrane protein 2 (LMP2), abrogating binding to E3 ubiquitin-protein ligase Itchy (Itch).
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Mothers against decapentaplegic homolog 3 - SMAD3 -  Homo sapiens
LIG_WW_1181184SpecificityAltered binding specificityCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. See also switch details and switch details.
details
LIG_WW_1181184Avidity‑sensingCDK8/9 phosphorylates Mothers against decapentaplegic homolog 3 (SMAD3) at T179 and S208. Phosphorylation of T179 creates a binding site for the WW domain of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), while phosphorylation of S208 primes SMAD3 for phosphorylation of S204 by Glycogen synthase kinase-3 beta (GSK3B). The pS204-pS208 forms a binding site for the third WW domain of the E3 ubiquitin-protein ligase NEDD4-like (NEDD4L), whose second WW domain will displace the WW domain of PIN1 at the pT179-PY box site of SMAD3. This regulation couples SMAD3 activation to SMAD3 destruction in an ordered fashion. Dual phosphorylation of the two NEDD4L-binding sites mediates high-avidity binding of two WW domains of NEDD4L to SMAD3. See also switch details and switch details.
details

Receptor tyrosine-protein kinase erbB-4 - ERBB4 -  Homo sapiens
LIG_WW_110531056SpecificityAltered binding specificityPhosphorylation-dependent binding of Receptor tyrosine-protein kinase erbB-4 (ERBB4) to the SH2 domains of Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1) results in signaling activation, while binding to the WW domains of E3 ubiquitin-protein ligase Itchy homolog (ITCH) to unphopshorylated ERBB4 results in ubiquitylation, endocytosis and ultimately degradation of ERBB4.
details
LIG_WW_110531056BinaryPre‑translationalAlternative splicing removes the WW-binding motif of Receptor tyrosine-protein kinase erbB-4 (ERBB4), abrogating binding to E3 ubiquitin-protein ligase Itchy homolog (ITCH). The presence of a WW-binding motif mediates ERBB4 mono-ubiquitination and endocytosis by the WW domain-containing HECT-type E3 ubiquitin ligase ITCH.
details
LIG_WW_110531056BinaryPre‑translationalAlternative splicing removes the WW-binding motif of Receptor tyrosine-protein kinase erbB-4 (ERBB4), abrogating binding to E3 ubiquitin-protein ligase Itchy homolog (ITCH). The presence of a WW-binding motif mediates ERBB4 mono-ubiquitination and endocytosis by the WW domain-containing HECT-type E3 ubiquitin ligase ITCH.
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Transcription factor AP-1 - Jun -  Mus musculus
LIG_WW_1167170BinaryPhysicochemical compatibilityPhosphorylation of Y170 in the WW-binding motif of Transcription factor AP-1 (Jun) by Tyrosine-protein kinase ABL1 (Abl1) blocks binding to the E3 ubiquitin-protein ligase Itchy (Itch). As a result, Transcription factor AP-1 (Jun) is not ubiquitylated by E3 ubiquitin-protein ligase Itchy (Itch), and thus not targeted for proteasomal degradation. Regulation of transcriptional activity of Transcription factor AP-1 (Jun) by Tyrosine-protein kinase ABL1 (Abl1) required translocation of the kinase to the nucleus, which was triggered by T cell activation.
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Tumor protein p73 - TP73 -  Homo sapiens
LIG_WW_1484487SpecificityCompetitionThe transcriptional coactivator YAP1 and the ubiquitin ligase Itch competitively bind to the same WW-binding motif of p73. Binding of YAP1 prevents Itch-mediated ubiquitylation of p73, resulting in stabilisation, and increases trancriptional activity of p73.
details
LIG_WW_1484487SpecificityCompetitionThe transcriptional coactivator YAP1 and the ubiquitin ligase Itch competitively bind to the same WW-binding motif of p73. Binding of YAP1 prevents Itch-mediated ubiquitylation of p73, resulting in stabilisation, and increases trancriptional activity of p73.
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