ID A0A452EQH7_CAPHI Unreviewed; 546 AA.
AC A0A452EQH7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 28-JAN-2026, entry version 36.
DE RecName: Full=Histone acetyltransferase KAT5 {ECO:0000256|ARBA:ARBA00073520};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
DE AltName: Full=60 kDa Tat-interactive protein {ECO:0000256|ARBA:ARBA00075576};
DE AltName: Full=Histone acetyltransferase HTATIP {ECO:0000256|ARBA:ARBA00078544};
DE AltName: Full=Lysine acetyltransferase 5 {ECO:0000256|ARBA:ARBA00081819};
DE AltName: Full=Protein 2-hydroxyisobutyryltransferase KAT5 {ECO:0000256|ARBA:ARBA00076578};
DE AltName: Full=Protein acetyltransferase KAT5 {ECO:0000256|ARBA:ARBA00076154};
DE AltName: Full=Protein crotonyltransferase KAT5 {ECO:0000256|ARBA:ARBA00078969};
DE AltName: Full=Protein lactyltransferase KAT5 {ECO:0000256|ARBA:ARBA00077013};
GN Name=KAT5 {ECO:0000313|Ensembl:ENSCHIP00000014439.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000014439.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000014439.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00010038959.1, ECO:0000313|Proteomes:UP000694566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Siddiki A.Z., Baten A., Billah M., Alam M.A.U., Shawrob K.S.M., Saha S.,
RA Chowdhury M., Rahman A.H., Stear M., Miah G., Das G.B., Hossain M.M.,
RA Kumkum M., Islam M.S., Mollah A.M., Ahsan A., Tusar F., Khan M.K.I.;
RT "Genome sequencing and reference-guided assembly of Black Bengal Goat
RT (Capra hircus).";
RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSCHIP00000014439.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAY-2025) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-butenoyl-CoA + L-lysyl-[protein] = N(6)-(2E)-butenoyl-L-
CC lysyl-[protein] + CoA + H(+); Xref=Rhea:RHEA:53908, Rhea:RHEA-
CC COMP:9752, Rhea:RHEA-COMP:13707, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57332,
CC ChEBI:CHEBI:137954; Evidence={ECO:0000256|ARBA:ARBA00047752};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53909;
CC Evidence={ECO:0000256|ARBA:ARBA00047752};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-lactoyl-CoA + L-lysyl-[protein] = N(6)-[(S)-lactoyl]-L-
CC lysyl-[protein] + CoA + H(+); Xref=Rhea:RHEA:61996, Rhea:RHEA-
CC COMP:9752, Rhea:RHEA-COMP:19466, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:231527,
CC ChEBI:CHEBI:231528; Evidence={ECO:0000256|ARBA:ARBA00047411};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61997;
CC Evidence={ECO:0000256|ARBA:ARBA00047411};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxyisobutanoyl-CoA + L-lysyl-[protein] = N(6)-(2-
CC hydroxyisobutanoyl)-L-lysyl-[protein] + CoA + H(+);
CC Xref=Rhea:RHEA:24180, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:15921,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:131780, ChEBI:CHEBI:144968;
CC Evidence={ECO:0000256|ARBA:ARBA00047557};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24181;
CC Evidence={ECO:0000256|ARBA:ARBA00047557};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[histone] + acetyl-CoA = N(6)-acetyl-L-lysyl-[histone]
CC + CoA + H(+); Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845, Rhea:RHEA-
CC COMP:11338, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC Evidence={ECO:0000256|ARBA:ARBA00048940};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993;
CC Evidence={ECO:0000256|ARBA:ARBA00048940};
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
CC {ECO:0000256|ARBA:ARBA00010107}.
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DR EMBL; LWLT01000026; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_017898875.1; XM_018043386.1.
DR AlphaFoldDB; A0A452EQH7; -.
DR SMR; A0A452EQH7; -.
DR STRING; 9925.ENSCHIP00000014439; -.
DR Ensembl; ENSCHIT00000022232.1; ENSCHIP00000014439.1; ENSCHIG00000015445.1.
DR Ensembl; ENSCHIT00010054468.1; ENSCHIP00010038959.1; ENSCHIG00010028467.1.
DR GeneID; 100861366; -.
DR KEGG; chx:100861366; -.
DR CTD; 10524; -.
DR GeneTree; ENSGT00940000162343; -.
DR OrthoDB; 787137at2759; -.
DR Proteomes; UP000291000; Chromosome 29.
DR Bgee; ENSCHIG00000015445; Expressed in rumen and 18 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0000776; C:kinetochore; IEA:Ensembl.
DR GO; GO:0097431; C:mitotic spindle pole; IEA:Ensembl.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0000786; C:nucleosome; IEA:Ensembl.
DR GO; GO:0032777; C:piccolo histone acetyltransferase complex; IEA:Ensembl.
DR GO; GO:0035861; C:site of double-strand break; IEA:Ensembl.
DR GO; GO:0000812; C:Swr1 complex; IEA:Ensembl.
DR GO; GO:0005667; C:transcription regulator complex; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0043999; F:histone H2AK5 acetyltransferase activity; IEA:Ensembl.
DR GO; GO:0046972; F:histone H4K16 acetyltransferase activity; IEA:Ensembl.
DR GO; GO:0140065; F:peptide butyryltransferase activity; IEA:Ensembl.
DR GO; GO:0140064; F:peptide crotonyltransferase activity; IEA:Ensembl.
DR GO; GO:0120300; F:peptide lactyltransferase (CoA-dependent) activity; IEA:Ensembl.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035973; P:aggrephagy; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; IEA:Ensembl.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IEA:Ensembl.
DR GO; GO:0042149; P:cellular response to glucose starvation; IEA:Ensembl.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; IEA:Ensembl.
DR GO; GO:0000729; P:DNA double-strand break processing; IEA:Ensembl.
DR GO; GO:0140861; P:DNA repair-dependent chromatin remodeling; IEA:Ensembl.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:Ensembl.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:Ensembl.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IEA:Ensembl.
DR GO; GO:1905691; P:lipid droplet disassembly; IEA:Ensembl.
DR GO; GO:0140694; P:membraneless organelle assembly; IEA:Ensembl.
DR GO; GO:2000042; P:negative regulation of double-strand break repair via homologous recombination; IEA:Ensembl.
DR GO; GO:0032703; P:negative regulation of interleukin-2 production; IEA:Ensembl.
DR GO; GO:0045662; P:negative regulation of myoblast differentiation; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0021915; P:neural tube development; IEA:Ensembl.
DR GO; GO:0022008; P:neurogenesis; IEA:Ensembl.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:Ensembl.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IEA:Ensembl.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IEA:Ensembl.
DR GO; GO:1905337; P:positive regulation of aggrephagy; IEA:Ensembl.
DR GO; GO:1902425; P:positive regulation of attachment of mitotic spindle microtubules to kinetochore; IEA:Ensembl.
DR GO; GO:0042753; P:positive regulation of circadian rhythm; IEA:Ensembl.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IEA:Ensembl.
DR GO; GO:0062033; P:positive regulation of mitotic sister chromatid segregation; IEA:Ensembl.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; IEA:Ensembl.
DR GO; GO:0045591; P:positive regulation of regulatory T cell differentiation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; IEA:Ensembl.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:1990166; P:protein localization to site of double-strand break; IEA:Ensembl.
DR GO; GO:0071211; P:protein targeting to vacuole involved in autophagy; IEA:Ensembl.
DR GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; IEA:Ensembl.
DR GO; GO:0010212; P:response to ionizing radiation; IEA:Ensembl.
DR GO; GO:0035092; P:sperm DNA condensation; IEA:Ensembl.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IEA:Ensembl.
DR CDD; cd18985; CBD_TIP60_like; 1.
DR CDD; cd04301; NAT_SF; 1.
DR FunFam; 1.10.10.10:FF:000022; Histone acetyltransferase; 1.
DR FunFam; 2.30.30.140:FF:000013; Histone acetyltransferase; 1.
DR FunFam; 3.30.60.60:FF:000001; Histone acetyltransferase; 1.
DR FunFam; 3.40.630.30:FF:000002; Histone acetyltransferase; 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; IPR050603; MYST_HAT.
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:SF219; 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 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000291000};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 260..537
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 436
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 546 AA; 61756 MW; 8550C5BF51E8C391 CRC64;
MAEVVSPVPG AGRREPGEVG RARGPPVADP GAALSPQGEI IEGCRLPVLR RNQDNEDEWP
LAEILSVKDI SGRKLFYVHY IDFNKRLDEW VTHERLDLKK IQFPKKEAKT PTKNGLPGSR
PGSPEREVPA SAQASGKTLP IPVQITLRFN LPKEREAIPG GEPDQPLSSS SCLQPNHRST
KRKVEVVSPA TPVPSETAPA SVFPQNGSAR RAVAAQPGRK RKSNCLGTDE DSQDSSDGIP
SAPRMTGSLV SDRSHDDIVT RMKNIECIEL GRHRLKPWYF SPYPQELTAL PVLYLCEFCL
KYGRSLKCLQ RHLTKCDLRH PPGNEIYRKG TISFFEIDGR KNKSYSQNLC LLAKCFLDHK
TLYYDTDPFL FYVMTEYDCK GFHIVGYFSK EKESTEDYNV ACILTLPPYQ RRGYGKLLIE
FSYELSKVEG KTGTPEKPLS DLGLLSYRSY WSQTILEILM GLKSESGERP QITINEISEI
TSIKKEDVIS TLQYLNLINY YKGQYILTLS EDIVDGHERA MLKRLLRIDS KCLHFTPKDW
SKRGKW
//
