Entry Database : PDB / ID : 7by1 Structure visualization Downloads & linksTitle Crystal structure of GCN5 PCAF N-terminal domain ComponentsHistone acetyltransferase KAT2A Details Keywords UNKNOWN FUNCTION / Ubiquitin ligaseFunction / homology Function and homology informationFunction Domain/homology Component
: / SAGA complex => GO:0000124 / : / : / : / B-WICH complex positively regulates rRNA expression / : / histone succinyltransferase activity / peptidyl-lysine glutarylation / histone glutaryltransferase activity ... : / SAGA complex => GO:0000124 / : / : / : / B-WICH complex positively regulates rRNA expression / : / histone succinyltransferase activity / peptidyl-lysine glutarylation / histone glutaryltransferase activity / metencephalon development / alpha-tubulin acetylation / : / regulation of cartilage development / : / positive regulation of cell projection organization / : / histone H4K12 acetyltransferase activity / NOTCH1 Intracellular Domain Regulates Transcription / RUNX3 regulates NOTCH signaling / positive regulation of cardiac muscle cell differentiation / Notch-HLH transcription pathway / regulation of bone development / regulation of stem cell population maintenance / regulation of regulatory T cell differentiation / negative regulation of centriole replication / oxoglutarate dehydrogenase complex / transcription factor TFTC complex / telencephalon development / internal peptidyl-lysine acetylation / histone H3 acetyltransferase activity / Ub-specific processing proteases / N-acetyltransferase activity / limb development / regulation of T cell activation / peptide-lysine-N-acetyltransferase activity / midbrain development / intracellular distribution of mitochondria / transcription factor binding / acetyltransferase activity / histone acetyltransferase complex / long-term memory / somitogenesis / histone acetyltransferase activity / histone acetyltransferase / positive regulation of gluconeogenesis / Transferases; Acyltransferases; Transferring groups other than aminoacyl groups / response to nutrient levels / cellular response to nerve growth factor stimulus / positive regulation of cytokine production / neural tube closure / regulation of synaptic plasticity / regulation of protein stability / multicellular organism growth / response to organic cyclic compound / mitotic spindle / histone deacetylase binding / cellular response to tumor necrosis factor / nervous system development / heart development / protein phosphatase binding / in utero embryonic development / cell population proliferation / transcription coactivator activity / centrosome / chromatin binding / chromatin / positive regulation of DNA-templated transcription / positive regulation of transcription by RNA polymerase II / nucleus Similarity search - Function PCAF, N-terminal / Histone acetyltransferase GCN5/PCAF / PCAF (P300/CBP-associated factor) N-terminal domain / Histone acetyltransferase GCN5 / Acetyltransferase (GNAT) family / Gcn5-related N-acetyltransferase (GNAT) domain profile. / GNAT domain / Acyl-CoA N-acyltransferase / Bromodomain, conserved site / Bromodomain signature. ... PCAF, N-terminal / Histone acetyltransferase GCN5/PCAF / PCAF (P300/CBP-associated factor) N-terminal domain / Histone acetyltransferase GCN5 / Acetyltransferase (GNAT) family / Gcn5-related N-acetyltransferase (GNAT) domain profile. / GNAT domain / Acyl-CoA N-acyltransferase / Bromodomain, conserved site / Bromodomain signature. / Bromodomain / Bromodomain profile. / bromo domain / Bromodomain / Bromodomain-like superfamily Similarity search - Domain/homologyBiological species Mus musculus (house mouse)Method X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution : 1.8 Å DetailsAuthors Hibi, R. / Toma-Fukai, S. / Shimizu, T. Funding support Japan, 1items Details Hide detailsOrganization Grant number Country Ministry of Education, Culture, Sports, Science and Technology (Japan) Japan
CitationJournal : J.Biol.Chem. / Year : 2020Title : Crystal structure of GCN5 PCAF N-terminal domain reveals atypical ubiquitin ligase structure.Authors : Toma-Fukai, S. / Hibi, R. / Naganuma, T. / Sakai, M. / Saijo, S. / Shimizu, N. / Matsumoto, M. / Shimizu, T. History Deposition Apr 21, 2020 Deposition site : PDBJ / Processing site : PDBJRevision 1.0 Aug 26, 2020 Provider : repository / Type : Initial releaseRevision 1.1 Sep 2, 2020 Group : Database references / Category : citation / citation_authorItem : _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed ... _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID / _citation_author.name Revision 1.2 Nov 11, 2020 Group : Database references / Category : citation / citation_authorItem : _citation.journal_volume / _citation.page_first ... _citation.journal_volume / _citation.page_first / _citation.page_last / _citation_author.identifier_ORCID / _citation_author.name Revision 1.3 Mar 27, 2024 Group : Data collection / Database references / Refinement descriptionCategory : chem_comp_atom / chem_comp_bond ... chem_comp_atom / chem_comp_bond / database_2 / struct_ncs_dom_lim Item : _database_2.pdbx_DOI / _database_2.pdbx_database_accession ... _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id
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