{"metadata":{"accession":"PF07039","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR010750","hierarchy":null,"name":{"name":"SGF29 tudor-like domain","short":"SGF29_Tudor"},"description":[{"text":"<p>SAGA-associated factor 29 (SGF29) is involved in transcriptional regulation as a chromatin reader component of some histone acetyltransferase (HAT) SAGA-type complexes like the TFTC-HAT, ATAC or STAGA complexes [[cite:PUB00053704],[cite:PUB00088833],[cite:PUB00099984],[cite:PUB00058697],[cite:PUB00099985]]. It specifically recognises and binds methylated 'Lys-4' of histone H3 (H3K4me), with a preference for the trimethylated form (H3K4me3). It also may be involved in MYC-mediated oncogenic transformation [[cite:PUB00053704]]. This entry represents the two tandem tudor-like domains found at the C-terminal of yeast and human SGF29 proteins and the plant homologues.  Each of them has a negatively-charged pocket capable of binding H3A1  and an aromatic cage for the recognition of H3K4me2/3 residues [[cite:PUB00099984],[cite:PUB00058697]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00088833":{"PMID":20850016,"ISBN":null,"volume":"142","issue":"6","year":2010,"title":"Quantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers.","URL":null,"raw_pages":"967-80","medline_journal":"Cell","ISO_journal":"Cell","authors":["Vermeulen M","Eberl HC","Matarese F","Marks H","Denissov S","Butter F","Lee KK","Olsen JV","Hyman AA","Stunnenberg HG","Mann M."],"DOI_URL":"https://doi.org/10.1016/j.cell.2010.08.020"},"PUB00099984":{"PMID":26421618,"ISBN":null,"volume":"10","issue":"9","year":2015,"title":"The Role of Electrostatic Interactions in Binding of Histone H3K4me2/3 to the Sgf29 Tandem Tudor Domain.","URL":null,"raw_pages":"e0139205","medline_journal":"PLoS One","ISO_journal":"PLoS One","authors":["Pieters BJ","Meulenbroeks E","Belle R","Mecinovic J."],"DOI_URL":null},"PUB00053704":{"PMID":19103755,"ISBN":null,"volume":"29","issue":"5","year":2009,"title":"The double-histone-acetyltransferase complex ATAC is essential for mammalian development.","URL":null,"raw_pages":"1176-88","medline_journal":"Mol Cell Biol","ISO_journal":"Mol. Cell. Biol.","authors":["Guelman S","Kozuka K","Mao Y","Pham V","Solloway MJ","Wang J","Wu J","Lill JR","Zha J."],"DOI_URL":"http://dx.doi.org/10.1128/MCB.01599-08"},"PUB00099985":{"PMID":26578293,"ISBN":null,"volume":"6","issue":null,"year":2015,"title":"Chemical basis for the recognition of trimethyllysine by epigenetic reader proteins.","URL":null,"raw_pages":"8911","medline_journal":"Nat Commun","ISO_journal":"Nat Commun","authors":["Kamps JJ","Huang J","Poater J","Xu C","Pieters BJ","Dong A","Min J","Sherman W","Beuming T","Matthias Bickelhaupt F","Li H","Mecinovic J."],"DOI_URL":null},"PUB00058697":{"PMID":21685874,"ISBN":null,"volume":"30","issue":"14","year":2011,"title":"Sgf29 binds histone H3K4me2/3 and is required for SAGA complex recruitment and histone H3 acetylation.","URL":null,"raw_pages":"2829-42","medline_journal":"EMBO J","ISO_journal":"EMBO J.","authors":["Bian C","Xu C","Ruan J","Lee KK","Burke TL","Tempel W","Barsyte D","Li J","Wu M","Zhou BO","Fleharty BE","Paulson A","Allali-Hassani A","Zhou JQ","Mer G","Grant PA","Workman JL","Zang J","Min J."],"DOI_URL":"http://dx.doi.org/10.1038/emboj.2011.193"}},"set_info":{"accession":"CL0010","name":"SH3"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":78,"interactions":0,"matches":3994,"pathways":0,"proteins":3982,"proteomes":2817,"sets":1,"structural_models":{"alphafold":3328},"structures":11,"taxa":7563},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":95,"alignment:full":2907},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"3mew","name":"Crystal structure of Novel Tudor domain-containing protein SGF29"}}}