ID G1T541_RABIT Unreviewed; 795 AA.
AC G1T541;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Histone acetyltransferase {ECO:0000256|PIRNR:PIRNR003048};
DE EC=2.3.1.48 {ECO:0000256|PIRNR:PIRNR003048};
GN Name=KAT2A {ECO:0000313|Ensembl:ENSOCUP00000011435.3};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000011435.3, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000011435.3, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000011435.3,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000011435.3}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000011435.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|PIRNR:PIRNR003048};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR003048}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. GCN5 subfamily.
CC {ECO:0000256|ARBA:ARBA00008607, ECO:0000256|PIRNR:PIRNR003048}.
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DR EMBL; AAGW02039747; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02039748; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1T541; -.
DR SMR; G1T541; -.
DR STRING; 9986.ENSOCUP00000011435; -.
DR PaxDb; 9986-ENSOCUP00000011435; -.
DR Ensembl; ENSOCUT00000013287.3; ENSOCUP00000011435.3; ENSOCUG00000013285.3.
DR eggNOG; KOG1472; Eukaryota.
DR GeneTree; ENSGT00940000158799; -.
DR HOGENOM; CLU_015901_0_0_1; -.
DR InParanoid; G1T541; -.
DR TreeFam; TF105399; -.
DR Proteomes; UP000001811; Chromosome 19.
DR Bgee; ENSOCUG00000013285; Expressed in uterus and 15 other cell types or tissues.
DR GO; GO:0140672; C:ATAC complex; IEA:Ensembl.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0072686; C:mitotic spindle; IEA:Ensembl.
DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:Ensembl.
DR GO; GO:0000124; C:SAGA complex; IEA:Ensembl.
DR GO; GO:0033276; C:transcription factor TFTC 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:0042826; F:histone deacetylase binding; IEA:Ensembl.
DR GO; GO:0106229; F:histone glutaryltransferase activity; IEA:Ensembl.
DR GO; GO:0043993; F:histone H3K18 acetyltransferase activity; IEA:Ensembl.
DR GO; GO:0043992; F:histone H3K9 acetyltransferase activity; IEA:Ensembl.
DR GO; GO:0043997; F:histone H4K12 acetyltransferase activity; IEA:Ensembl.
DR GO; GO:0106078; F:histone succinyltransferase activity; IEA:Ensembl.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
DR GO; GO:0048144; P:fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0006094; P:gluconeogenesis; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0007616; P:long-term memory; IEA:Ensembl.
DR GO; GO:0022037; P:metencephalon development; IEA:Ensembl.
DR GO; GO:0030901; P:midbrain development; IEA:Ensembl.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:0046600; P:negative regulation of centriole replication; IEA:Ensembl.
DR GO; GO:0045721; P:negative regulation of gluconeogenesis; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
DR GO; GO:0001819; P:positive regulation of cytokine production; IEA:Ensembl.
DR GO; GO:0045722; P:positive regulation of gluconeogenesis; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:1903010; P:regulation of bone development; IEA:Ensembl.
DR GO; GO:0061035; P:regulation of cartilage development; IEA:Ensembl.
DR GO; GO:0051302; P:regulation of cell division; IEA:Ensembl.
DR GO; GO:0045995; P:regulation of embryonic development; IEA:Ensembl.
DR GO; GO:0031647; P:regulation of protein stability; IEA:Ensembl.
DR GO; GO:0045589; P:regulation of regulatory T cell differentiation; IEA:Ensembl.
DR GO; GO:2000036; P:regulation of stem cell population maintenance; IEA:Ensembl.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IEA:Ensembl.
DR GO; GO:0090043; P:regulation of tubulin deacetylation; IEA:Ensembl.
DR GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
DR GO; GO:0021537; P:telencephalon development; IEA:Ensembl.
DR CDD; cd04301; NAT_SF; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR037800; GCN5.
DR InterPro; IPR016376; GCN5/PCAF.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR009464; PCAF_N.
DR PANTHER; PTHR45750; GH11602P; 1.
DR PANTHER; PTHR45750:SF1; HISTONE ACETYLTRANSFERASE KAT2A; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF06466; PCAF_N; 1.
DR PIRSF; PIRSF003048; Histone_acetylase_PCAF; 2.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|PIRNR:PIRNR003048};
KW Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR003048};
KW Reference proteome {ECO:0000313|Proteomes:UP000001811};
KW Transcription {ECO:0000256|PIRNR:PIRNR003048};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR003048};
KW Transferase {ECO:0000256|PIRNR:PIRNR003048}.
FT DOMAIN 503..656
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT DOMAIN 725..773
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..51
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 575
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR003048-1"
FT BINDING 579..581
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|PIRSR:PIRSR003048-2"
FT BINDING 586..592
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|PIRSR:PIRSR003048-2"
FT BINDING 617..620
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|PIRSR:PIRSR003048-2"
SQ SEQUENCE 795 AA; 89037 MW; 12E454A2FDC9DFE7 CRC64;
MAEPSQAPAP VPAAQPRPLQ SPAPTPTPTP APSPASAPTP APTPAPAPAP AAAPAGSTGT
GGPGVGSGGT GSGGDPARPG LSQQQRASQR KAQVRGLPRA KKLEKLGVFS ACKANETCKC
NGWKNPKPPT APRMDLQQPA ANLSELCRSC EHPLADHVSH LENVSEDEIN RLLGMVVDVE
NLFMSVHKEE DTDTKQVYFY LFKLLRKCIL QMTRPVVEGS LGSPPFEKPN IEQGVLNFVQ
YKFSHLAPRE RQTMFELSKM FLLCLNYWKL ETPAQFRQRS QSEDVATYKV NYTRWLCYCH
VPQSCDSLPR YETTHVFGRS LLRSIFTVTR RQLLEKFRVE KDKLVPEKRT LILTHFPKFL
SMLEEEIYGA NSPIWESGFT MPPSEGTQLG PRPATVSAAV VPSAPIFSPT MGGGSNSSLS
LDSAGAEPMP GEKRKLPENL TLEDAKRLRV MGDIPMELVN EVMLTITDPA AMLGPETSLL
SANAARDETA RLEERRGIIE FHVIGNSLTP KANRRVLLWL VGLQNVFSHQ LPRMPKEYIA
RLVFDPKHKT LALIKDGRVI GGICFRMFPT QGFTEIVFCA VTSNEQVKGY GTHLMNHLKE
YHIKHNILYF LTYADEYAIG YFKKQGFSKD IKVPKSRYLG YIKDYEGATL MECELNPRIP
YTELSHIIKK QKEIIKKLIE RKQAQIRKVY PGLSCFKEGV RQIPVESVPG IRETGWKPLG
KEKGEVIRFP IDLKTMTERL RSRYYVTRKL FVADLQRVIA NCREYNPPDS EYCRCASALE
KFFYFKLKEG GLIDK
//
