TIP60_CAEEL
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 03-AUG-2022, entry version 146.
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}.
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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; Q9TYU5; -.
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 CTD; 179096; -.
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; 629545at2759; -.
DR PhylomeDB; Q9TYU5; -.
DR Reactome; R-CEL-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-CEL-5693548; Sensing of DNA Double Strand Breaks.
DR Reactome; R-CEL-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-CEL-5693607; Processing of DNA double-strand break ends.
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 tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004402; F:histone acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; 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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
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 transcription, DNA-templated; 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 Gene3D; 1.10.10.10; -; 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 Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF11717; Tudor-knot; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SMART; SM00298; CHROMO; 1.
DR SUPFAM; SSF54160; SSF54160; 1.
DR SUPFAM; SSF55729; SSF55729; 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
