ID TIP60_CAEEL Reviewed; 458 AA. AC Q9TYU5; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 155. DE RecName: Full=Histone acetyltransferase Tip60 homolog; DE EC=2.3.1.48 {ECO:0000250|UniProtKB:Q92993}; DE AltName: Full=Myst family histone acetyltransferase-like protein 1 {ECO:0000303|PubMed:15068795}; GN Name=mys-1 {ECO:0000303|PubMed:15068795, ECO:0000312|WormBase:VC5.4}; GN ORFNames=VC5.4; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. RX PubMed=15068795; DOI=10.1016/s1534-5807(04)00065-6; RA Ceol C.J., Horvitz H.R.; RT "A new class of C. elegans synMuv genes implicates a Tip60/NuA4-like HAT RT complex as a negative regulator of Ras signaling."; RL Dev. Cell 6:563-576(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for investigating RT biology."; RL Science 282:2012-2018(1998). RN [3] RP FUNCTION. RX PubMed=20181741; DOI=10.1242/dev.042812; RA Shibata Y., Takeshita H., Sasakawa N., Sawa H.; RT "Double bromodomain protein BET-1 and MYST HATs establish and maintain RT stable cell fates in C. elegans."; RL Development 137:1045-1053(2010). CC -!- FUNCTION: Probable catalytic subunit of the Tip60 chromatin-remodeling CC complex. May acetylate nucleosomal histone H4 and H2A CC (PubMed:15068795). Acts in the determination of vulval and distal tip CC cell (DTC) precursor cell fates (PubMed:15068795, PubMed:20181741). CC {ECO:0000269|PubMed:15068795, ECO:0000269|PubMed:20181741}. CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L- CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; CC Evidence={ECO:0000250|UniProtKB:Q92993}; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92993}. CC -!- PTM: Autoacetylation at Lys-268 is required for binding histones with CC high affinity and for proper function. {ECO:0000250|UniProtKB:Q9H7Z6}. CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY551963; AAS65427.1; -; mRNA. DR EMBL; FO081233; CCD70078.1; -; Genomic_DNA. DR PIR; T33814; T33814. DR RefSeq; NP_504796.1; NM_072395.3. DR AlphaFoldDB; Q9TYU5; -. DR SMR; Q9TYU5; -. DR BioGRID; 44141; 37. DR IntAct; Q9TYU5; 18. DR STRING; 6239.VC5.4.1; -. DR EPD; Q9TYU5; -. DR PaxDb; 6239-VC5-4-1; -. DR PeptideAtlas; Q9TYU5; -. DR EnsemblMetazoa; VC5.4.1; VC5.4.1; WBGene00007029. DR GeneID; 179096; -. DR KEGG; cel:CELE_VC5.4; -. DR UCSC; VC5.4; c. elegans. DR AGR; WB:WBGene00007029; -. DR WormBase; VC5.4; CE21225; WBGene00007029; mys-1. DR eggNOG; KOG2747; Eukaryota. DR GeneTree; ENSGT00940000163054; -. DR HOGENOM; CLU_011815_2_0_1; -. DR InParanoid; Q9TYU5; -. DR OMA; RIRNVEC; -. DR OrthoDB; 118560at2759; -. DR PhylomeDB; Q9TYU5; -. DR Reactome; R-CEL-201722; Formation of the beta-catenin:TCF transactivating complex. DR Reactome; R-CEL-9018519; Estrogen-dependent gene expression. DR SignaLink; Q9TYU5; -. DR PRO; PR:Q9TYU5; -. DR Proteomes; UP000001940; Chromosome V. DR Bgee; WBGene00007029; Expressed in embryo and 4 other cell types or tissues. DR GO; GO:0072487; C:MSL complex; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0046972; F:histone H4K16 acetyltransferase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central. DR GO; GO:0001708; P:cell fate specification; IMP:WormBase. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR GO; GO:0009996; P:negative regulation of cell fate specification; IMP:UniProtKB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IGI:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0071168; P:protein localization to chromatin; IGI:WormBase. DR CDD; cd18642; CBD_MOF_like; 1. DR CDD; cd04301; NAT_SF; 1. DR Gene3D; 2.30.30.140; -; 1. DR Gene3D; 3.40.630.30; -; 1. DR Gene3D; 3.30.60.60; N-acetyl transferase-like; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR016197; Chromo-like_dom_sf. DR InterPro; IPR000953; Chromo/chromo_shadow_dom. DR InterPro; IPR002717; HAT_MYST-type. DR InterPro; IPR025995; Tudor-knot. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR040706; Zf-MYST. DR PANTHER; PTHR10615; HISTONE ACETYLTRANSFERASE; 1. DR PANTHER; PTHR10615:SF161; HISTONE ACETYLTRANSFERASE KAT5; 1. DR Pfam; PF01853; MOZ_SAS; 1. DR Pfam; PF11717; Tudor-knot; 1. DR Pfam; PF17772; zf-MYST; 1. DR SMART; SM00298; CHROMO; 1. DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1. DR SUPFAM; SSF54160; Chromo domain-like; 1. DR PROSITE; PS51726; MYST_HAT; 1. PE 2: Evidence at transcript level; KW Acetylation; Acyltransferase; Chromatin regulator; Developmental protein; KW DNA damage; DNA repair; Metal-binding; Nucleus; Reference proteome; KW Transcription; Transcription regulation; Transferase; Zinc; Zinc-finger. FT CHAIN 1..458 FT /note="Histone acetyltransferase Tip60 homolog" FT /id="PRO_0000245807" FT DOMAIN 30..86 FT /note="Tudor-knot" FT /evidence="ECO:0000255" FT DOMAIN 168..446 FT /note="MYST-type HAT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063" FT ZN_FING 201..226 FT /note="C2HC MYST-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063" FT REGION 1..24 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 94..123 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 344 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6" FT BINDING 311..313 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6" FT BINDING 318..324 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6" FT BINDING 348 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6" FT BINDING 357 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6" FT MOD_RES 268 FT /note="N6-acetyllysine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6" SQ SEQUENCE 458 AA; 53143 MW; 19D7727E5B47D10B CRC64; MTEPKKEIIE DENHGISKKI PTDPRQYEKV TEGCRLLVMM ASQEEERWAE VISRCRAANG SIKFYVHYID CNRRLDEWVQ SDRLNLASCE LPKKGGKKGA HLREENRDSN ENEGKKSGRK RKIPLLPMDD LKAESVDPLQ AISTMTSGST PSLRGSMSMV GHSEDAMTRI RNVECIELGR SRIQPWYFAP YPQQLTSLDC IYICEFCLKY LKSKTCLKRH MEKCAMCHPP GNQIYSHDKL SFFEIDGRKN KSYAQNLCLL AKLFLDHKTL YYDTDPFLFY VLTEEDEKGH HIVGYFSKEK ESAEEYNVAC ILVLPPFQKK GYGSLLIEFS YELSKIEQKT GSPEKPLSDL GLLSYRSYWS MAIMKELFAF KRRHPGEDIT VQDISQSTSI KREDVVSTLQ QLDLYKYYKG SYIIVISDEK RQVYEKRIEA AKKKTRINPA ALQWRPKEYG KKRAQIMF //