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Database: UniProt
Entry: A0A0D9RBQ9_CHLSB
LinkDB: A0A0D9RBQ9_CHLSB
Original site: A0A0D9RBQ9_CHLSB 
ID   A0A0D9RBQ9_CHLSB        Unreviewed;       675 AA.
AC   A0A0D9RBQ9;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE            EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN   Name=KAT2B {ECO:0000313|Ensembl:ENSCSAP00000006048.1};
OS   Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000006048.1, ECO:0000313|Proteomes:UP000029965};
RN   [1] {ECO:0000313|Ensembl:ENSCSAP00000006048.1, ECO:0000313|Proteomes:UP000029965}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCSAP00000006048.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. GCN5 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008607}.
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DR   EMBL; AQIB01076453; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A0D9RBQ9; -.
DR   STRING; 60711.ENSCSAP00000006048; -.
DR   Ensembl; ENSCSAT00000007882.1; ENSCSAP00000006048.1; ENSCSAG00000009803.1.
DR   eggNOG; KOG1472; Eukaryota.
DR   GeneTree; ENSGT00940000154995; -.
DR   OMA; DFAIGYF; -.
DR   Proteomes; UP000029965; Chromosome 15.
DR   Bgee; ENSCSAG00000009803; Expressed in blood and 7 other cell types or tissues.
DR   GO; GO:0031672; C:A band; IEA:Ensembl.
DR   GO; GO:0042641; C:actomyosin; IEA:Ensembl.
DR   GO; GO:0140672; C:ATAC complex; IEA:Ensembl.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0031674; C:I band; IEA:Ensembl.
DR   GO; GO:0000776; C:kinetochore; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0004861; F:cyclin-dependent protein serine/threonine kinase inhibitor activity; 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:0043992; F:histone H3K9 acetyltransferase activity; IEA:Ensembl.
DR   GO; GO:0004468; F:lysine N-acetyltransferase activity, acting on acetyl phosphate as donor; IEA:Ensembl.
DR   GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR   GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:Ensembl.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0046600; P:negative regulation of centriole replication; IEA:Ensembl.
DR   GO; GO:2000233; P:negative regulation of rRNA processing; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:1902425; P:positive regulation of attachment of mitotic spindle microtubules to kinetochore; IEA:Ensembl.
DR   GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IEA:Ensembl.
DR   GO; GO:0045722; P:positive regulation of gluconeogenesis; IEA:Ensembl.
DR   GO; GO:0045821; P:positive regulation of glycolytic process; IEA:Ensembl.
DR   GO; GO:0000432; P:positive regulation of transcription from RNA polymerase II promoter by glucose; IEA:Ensembl.
DR   CDD; cd05509; Bromo_gcn5_like; 1.
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; IPR018359; Bromodomain_CS.
DR   InterPro; IPR037800; GCN5.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR009464; PCAF_N.
DR   PANTHER; PTHR45750; GH11602P; 1.
DR   PANTHER; PTHR45750:SF2; HISTONE ACETYLTRANSFERASE KAT2B; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF06466; PCAF_N; 1.
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; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
KW   Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW   ProRule:PRU00035}; Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          346..494
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
FT   DOMAIN          583..653
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   REGION          239..281
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          549..568
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        239..261
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        554..568
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   675 AA;  78009 MW;  B6B1692E91600302 CRC64;
     MNRLLGIVLD VEYLFTCVHK EEDADTKQVY FYLFKLLRKS ILQRGKPVVE GSLEKKPPFE
     KPSIEQGVNN FVQYKFSHLP AKERQTIVEL AKMFLNRINY WHLEAPSQRR LRSPNDDISG
     YKENYTRWLC YCNVPQFCDS LPRYETTQVF GRTLLRSVFT VMRRQLLEQA RQEKDKLPLE
     KRTLILTHFP KFLSMLEEEV YSQNSPIWDQ DFLSASSRTS QLGIQTVISP PPVAGTISYN
     STSSSLEQSN AGSSSPACKA SSGLEANPGE KRKMTDSHVL EEAKRPRVMG DIPMELINEV
     MSTITDPAAM LGPETNFLSA HSARDEAARL EERRGVIEFH VVGNSLNQKP NKKILMWLVG
     LQNVFSHQLP RMPKEYITRL VFDPKHKTLA LIKDGRVIGG ICFRMFPSQG FTEIVFCAVT
     SNEQVKGYGT HLMNHLKEYH IKHDILNFLT YADEYAIGYF KKQGFSKEIK IPKTKYVGYI
     KDYEGATLMG CELNPRIPYT EFSVIIKKQK EIIKKLIERK QAQIRKVYPG LSCFKDGVRQ
     IPIESIPGIR ETGWKPSGKE KSKEPRDPDQ LYSTLKSILQ QVKSHQSAWP FMEPVKRTEA
     PGYYEVIRFP MDLKTMSERL KNRYYVSKKL FMADLQRVFT NCKEYNPPES EYYKCANILE
     KFFFSKIKEA GLIDK
//
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