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Histone acetyltransferase KAT2B (EC 2 3 1 48) (Histone acetyltransferase PCAF) (Histone acetylase PCAF) (Lysine acetyltransferase 2B) (P300/CBP-associated factor) (P/CAF)

 KAT2B_DANRE             Reviewed;         796 AA.
Q1LUC3;
28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
30-MAY-2006, sequence version 1.
12-SEP-2018, entry version 99.
RecName: Full=Histone acetyltransferase KAT2B {ECO:0000250|UniProtKB:Q92831};
EC=2.3.1.48 {ECO:0000250|UniProtKB:Q92831};
AltName: Full=Histone acetyltransferase PCAF {ECO:0000250|UniProtKB:Q92831};
Short=Histone acetylase PCAF {ECO:0000250|UniProtKB:Q92831};
AltName: Full=Lysine acetyltransferase 2B {ECO:0000250|UniProtKB:Q92831};
AltName: Full=P300/CBP-associated factor {ECO:0000250|UniProtKB:Q92831};
Short=P/CAF {ECO:0000250|UniProtKB:Q92831};
Name=kat2b {ECO:0000312|ZFIN:ZDB-GENE-060503-207};
Danio rerio (Zebrafish) (Brachydanio rerio).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
Cyprinidae; Danio.
NCBI_TaxID=7955;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Tuebingen;
PubMed=23594743; DOI=10.1038/nature12111;
Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C.,
Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G.,
Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B.,
Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S.,
Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C.,
Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H.,
Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C.,
Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
Humphries M., Sycamore N., Barker D., Saunders D., Wallis J.,
Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S.,
Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R.,
Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R.,
Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R.,
Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A.,
Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S.,
Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J.,
Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
Stemple D.L.;
"The zebrafish reference genome sequence and its relationship to the
human genome.";
Nature 496:498-503(2013).
[2]
FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=29174768; DOI=10.1016/j.yjmcc.2017.11.013;
Ghosh T.K., Aparicio-Sanchez J.J., Buxton S., Ketley A., Mohamed T.,
Rutland C.S., Loughna S., Brook J.D.;
"Acetylation of TBX5 by KAT2B and KAT2A regulates heart and limb
development.";
J. Mol. Cell. Cardiol. 114:185-198(2017).
-!- FUNCTION: Functions as a histone acetyltransferase (HAT) to
promote transcriptional activation (By similarity). Has
significant histone acetyltransferase activity with core histones
(H3 and H4), and also with nucleosome core particles (By
similarity). Also acetylates non-histone proteins
(PubMed:29174768). Involved in heart and limb development by
mediating acetylation of tbx5 (PubMed:29174768).
{ECO:0000250|UniProtKB:Q92831, ECO:0000269|PubMed:29174768}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + [protein]-L-lysine = CoA +
[protein]-N(6)-acetyl-L-lysine. {ECO:0000250|UniProtKB:Q92831}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92831}.
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
{ECO:0000250|UniProtKB:Q92831}. Note=Mainly localizes to the
nucleus. Also localizes to centrosomes in late G1 and around the
G1/S transition, coinciding with the onset of centriole formation.
{ECO:0000250|UniProtKB:Q92831}.
-!- DEVELOPMENTAL STAGE: Expressed in the heart and tail regions
throughout developmental stages. {ECO:0000269|PubMed:29174768}.
-!- DISRUPTION PHENOTYPE: Morpholino knockdown of kat2a and kat2b
leads to impaired heart and limb development. Abnormal fin
development is also observed. {ECO:0000269|PubMed:29174768}.
-!- SIMILARITY: Belongs to the acetyltransferase family. GCN5
subfamily. {ECO:0000305}.
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EMBL; BX950869; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX957344; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; NP_001038499.1; NM_001045034.1.
UniGene; Dr.97337; -.
ProteinModelPortal; Q1LUC3; -.
STRING; 7955.ENSDARP00000085190; -.
PaxDb; Q1LUC3; -.
Ensembl; ENSDART00000090757; ENSDARP00000085190; ENSDARG00000062634.
GeneID; 563942; -.
KEGG; dre:563942; -.
CTD; 8850; -.
ZFIN; ZDB-GENE-060503-207; kat2b.
eggNOG; KOG1472; Eukaryota.
eggNOG; COG5076; LUCA.
GeneTree; ENSGT00920000149009; -.
HOGENOM; HOG000007151; -.
HOVERGEN; HBG051710; -.
InParanoid; Q1LUC3; -.
KO; K06062; -.
OMA; QVIRFPM; -.
OrthoDB; EOG091G03ZO; -.
PhylomeDB; Q1LUC3; -.
TreeFam; TF105399; -.
PRO; PR:Q1LUC3; -.
Proteomes; UP000000437; Chromosome 19.
Bgee; ENSDARG00000062634; Expressed in 17 organ(s), highest expression level in heart.
GO; GO:0005813; C:centrosome; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; ISS:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0007507; P:heart development; IMP:UniProtKB.
GO; GO:0018393; P:internal peptidyl-lysine acetylation; ISS:UniProtKB.
GO; GO:0060173; P:limb development; IMP:UniProtKB.
GO; GO:0046600; P:negative regulation of centriole replication; ISS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.20.920.10; -; 1.
InterPro; IPR016181; Acyl_CoA_acyltransferase.
InterPro; IPR001487; Bromodomain.
InterPro; IPR036427; Bromodomain-like_sf.
InterPro; IPR018359; Bromodomain_CS.
InterPro; IPR037800; GCN5.
InterPro; IPR016376; GCN5/PCAF.
InterPro; IPR000182; GNAT_dom.
InterPro; IPR009464; PCAF_N.
PANTHER; PTHR22880:SF124; PTHR22880:SF124; 1.
Pfam; PF00583; Acetyltransf_1; 1.
Pfam; PF00439; Bromodomain; 1.
Pfam; PF06466; PCAF_N; 1.
PIRSF; PIRSF003048; Histone_acetylase_PCAF; 1.
PRINTS; PR00503; BROMODOMAIN.
SMART; SM00297; BROMO; 1.
SUPFAM; SSF47370; SSF47370; 1.
SUPFAM; SSF55729; SSF55729; 1.
PROSITE; PS00633; BROMODOMAIN_1; 1.
PROSITE; PS50014; BROMODOMAIN_2; 1.
PROSITE; PS51186; GNAT; 1.
2: Evidence at transcript level;
Activator; Acyltransferase; Biological rhythms; Bromodomain;
Cell cycle; Complete proteome; Cytoplasm; Cytoskeleton; Nucleus;
Reference proteome; Transcription; Transcription regulation;
Transferase.
CHAIN 1 796 Histone acetyltransferase KAT2B.
/FTId=PRO_0000443448.
DOMAIN 469 617 N-acetyltransferase.
{ECO:0000255|PROSITE-ProRule:PRU00532}.
DOMAIN 704 774 Bromo. {ECO:0000255|PROSITE-
ProRule:PRU00035}.
REGION 540 542 Acetyl-CoA binding.
{ECO:0000250|UniProtKB:Q92830}.
REGION 547 553 Acetyl-CoA binding.
{ECO:0000250|UniProtKB:Q92830}.
REGION 578 581 Acetyl-CoA binding.
{ECO:0000250|UniProtKB:Q92830}.
ACT_SITE 536 536 Proton donor/acceptor.
{ECO:0000250|UniProtKB:Q92830}.
SEQUENCE 796 AA; 90026 MW; B1B321F4A513B9E5 CRC64;
MSESTGIPQG SPAVGAAGSA PAAPGVGGTE CSGAAVGSAR IAVKKAQLRS SPRPKKLEKL
GVYSSCKAEG ACKCNGWKSQ NPPPTPPPPT PPRAEQPTAV SLMEPCRSCS HALGDHVTHL
ENVSEEEMNR LLGIVLDVEY LYTCVHKEED PDTKQVYFSL FKLLRKCILQ MGRPVVEALE
SPPFEKPSIE QGVNNFVQYK FSHLPSKERQ TIVELAKMFL NQINYWQLET PSQKRQRAPD
DDVAGYKVNY TRWLCYCNVP QFCDSLPRYE ATQIFGRIFL RSVFTIMRKQ LLEQARQEKD
KLPPEKRTLI LTHFPKFLSM LEEEVYSHNS PIWSENFMIG LSGGQIPTVV SAPPVNRSLY
YSSSPAPVEL AGGGSVSPAR KTASVLEPNP GGEKRKPAEP LSHEDSKRPR VVGDIPMELI
NEVMSTITDP TAMLGPETSL LSAHSARDEA ARLEERRGVI EFHVIGNSLN QKPNKKILMW
LVGLQNVFSH QLPRMPKEYI TRLVFDPKHK TLSLIKDGRV IGGICFRMFP TQGFTEIVFC
AVTSNEQVKG YGTHLMNHLK EYHIKHEILN FLTYADEYAI GYFKKQGFSK DIKVPKSKYV
GYIKDYEGAT LMGCELNPCI PYTEFSVIIK KQKEIIKKLI ERKQAQIRKV YPGLSCFKEG
VRQIAIESIP GIRETGWKPL GKSKELKDPD QLYSTLKNIL TQVKSHPNAW PFMEPVKKNE
APGYYQVIRF PMDLKTMSER LKSRYYTTRK LFMADMQRIF TNCREYNPPE SEYYKCANLL
EKFFYTKIKE AGLIDK


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