Entry Database : PDB / ID : 2kxq Structure visualization Downloads & linksTitle Solution Structure of Smurf2 WW2 and WW3 bound to Smad7 PY motif containing peptide ComponentsE3 ubiquitin-protein ligase SMURF2 Smad7 PY motif containing peptide DetailsKeywords PROTEIN BINDING / WW / PY motif / Smurf2 / TGF-beta / modular bindingFunction / homology Function and homology informationFunction Domain/homology Component
positive regulation of chondrocyte hypertrophy / negative regulation of T-helper 17 type immune response / negative regulation of chondrocyte proliferation / negative regulation of T cell cytokine production / heteromeric SMAD protein complex / regulation of ventricular cardiac muscle cell membrane depolarization / negative regulation of T-helper 17 cell differentiation / regulation of transforming growth factor beta receptor signaling pathway / positive regulation of cell-cell adhesion / response to laminar fluid shear stress ... positive regulation of chondrocyte hypertrophy / negative regulation of T-helper 17 type immune response / negative regulation of chondrocyte proliferation / negative regulation of T cell cytokine production / heteromeric SMAD protein complex / regulation of ventricular cardiac muscle cell membrane depolarization / negative regulation of T-helper 17 cell differentiation / regulation of transforming growth factor beta receptor signaling pathway / positive regulation of cell-cell adhesion / response to laminar fluid shear stress / positive regulation of trophoblast cell migration / regulation of epithelial to mesenchymal transition / activin receptor binding / negative regulation of transcription by competitive promoter binding / negative regulation of ubiquitin-protein transferase activity / Signaling by BMP / type I transforming growth factor beta receptor binding / SMAD protein signal transduction / negative regulation of activin receptor signaling pathway / adherens junction assembly / HECT-type E3 ubiquitin transferase / protein-containing complex localization / negative regulation of epithelial to mesenchymal transition / I-SMAD binding / negative regulation of ossification / transcription regulator inhibitor activity / Wnt signaling pathway, planar cell polarity pathway / ventricular cardiac muscle tissue morphogenesis / artery morphogenesis / ureteric bud development / ventricular septum morphogenesis / negative regulation of SMAD protein signal transduction / negative regulation of peptidyl-threonine phosphorylation / SMAD binding / negative regulation of peptidyl-serine phosphorylation / negative regulation of BMP signaling pathway / regulation of cardiac muscle contraction / ubiquitin-like ligase-substrate adaptor activity / anatomical structure morphogenesis / ubiquitin ligase complex / negative regulation of protein ubiquitination / cellular response to transforming growth factor beta stimulus / collagen binding / transforming growth factor beta receptor signaling pathway / Downregulation of TGF-beta receptor signaling / negative regulation of cell migration / Asymmetric localization of PCP proteins / cellular response to leukemia inhibitory factor / Degradation of AXIN / Downregulation of SMAD2/3:SMAD4 transcriptional activity / SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription / negative regulation of transforming growth factor beta receptor signaling pathway / Hedgehog 'on' state / Regulation of RUNX3 expression and activity / fibrillar center / beta-catenin binding / ubiquitin-protein transferase activity / transcription corepressor activity / UCH proteinases / Interferon gamma signaling / ubiquitin protein ligase activity / positive regulation of canonical Wnt signaling pathway / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / Antigen processing: Ubiquitination & Proteasome degradation / ubiquitin-dependent protein catabolic process / proteasome-mediated ubiquitin-dependent protein catabolic process / cell differentiation / protein stabilization / Ub-specific processing proteases / protein ubiquitination / nuclear speck / membrane raft / negative regulation of DNA-templated transcription / centrosome / ubiquitin protein ligase binding / chromatin / regulation of transcription by RNA polymerase II / negative regulation of transcription by RNA polymerase II / protein-containing complex / nucleoplasm / identical protein binding / nucleus / metal ion binding / plasma membrane / cytosol / cytoplasm Similarity search - Function MAD homology, MH1 / Dwarfin / SMAD MH1 domain superfamily / MAD homology domain 1 (MH1) profile. / SMAD domain, Dwarfin-type / MH2 domain / MAD homology domain 2 (MH2) profile. / Domain B in dwarfin family proteins / MAD homology 1, Dwarfin-type / MH1 domain ... MAD homology, MH1 / Dwarfin / SMAD MH1 domain superfamily / MAD homology domain 1 (MH1) profile. / SMAD domain, Dwarfin-type / MH2 domain / MAD homology domain 2 (MH2) profile. / Domain B in dwarfin family proteins / MAD homology 1, Dwarfin-type / MH1 domain / Domain A in dwarfin family proteins / Ubiquitin Ligase Nedd4; Chain: W; - #10 / E3 ubiquitin-protein ligase, SMURF1 type / SMAD-like domain superfamily / Ubiquitin Ligase Nedd4; Chain: W; / : / HECT domain / HECT, E3 ligase catalytic domain / HECT-domain (ubiquitin-transferase) / HECT domain profile. / Domain Homologous to E6-AP Carboxyl Terminus with / C2 domain / Protein kinase C conserved region 2 (CalB) / SMAD/FHA domain superfamily / WW domain / WW/rsp5/WWP domain signature. / C2 domain / C2 domain profile. / WW domain superfamily / WW/rsp5/WWP domain profile. / Domain with 2 conserved Trp (W) residues / WW domain / Single Sheet / C2 domain superfamily / Mainly Beta Similarity search - Domain/homologyBiological species Homo sapiens (human)Method SOLUTION NMR DetailsAuthors Chong, A. / Lin, H. / Wrana, J. / Forman-Kay, J.D. CitationJournal : Proc.Natl.Acad.Sci.USA / Year : 2010Title : Coupling of tandem Smad ubiquitination regulatory factor (Smurf) WW domains modulates target specificity.Authors : Chong, P.A. / Lin, H. / Wrana, J.L. / Forman-Kay, J.D. History Deposition May 11, 2010 Deposition site : BMRB / Processing site : RCSBRevision 1.0 Oct 13, 2010 Provider : repository / Type : Initial releaseRevision 1.1 Jul 13, 2011 Group : Version format complianceRevision 1.2 Jun 20, 2012 Group : Database referencesRevision 1.3 May 1, 2024 Group : Data collection / Database referencesCategory : chem_comp_atom / chem_comp_bond ... chem_comp_atom / chem_comp_bond / database_2 / struct_ref_seq_dif Item : _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details
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