KAT2B_DANRE
ID KAT2B_DANRE Reviewed; 796 AA.
AC Q1LUC3;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Histone acetyltransferase KAT2B {ECO:0000250|UniProtKB:Q92831};
DE EC=2.3.1.48 {ECO:0000250|UniProtKB:Q92831};
DE AltName: Full=Histone acetyltransferase PCAF {ECO:0000250|UniProtKB:Q92831};
DE Short=Histone acetylase PCAF {ECO:0000250|UniProtKB:Q92831};
DE AltName: Full=Lysine acetyltransferase 2B {ECO:0000250|UniProtKB:Q92831};
DE AltName: Full=P300/CBP-associated factor {ECO:0000250|UniProtKB:Q92831};
DE Short=P/CAF {ECO:0000250|UniProtKB:Q92831};
DE AltName: Full=Spermidine acetyltransferase KAT2B;
DE EC=2.3.1.57 {ECO:0000250|UniProtKB:Q92831};
GN Name=kat2b {ECO:0000312|ZFIN:ZDB-GENE-060503-207};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=29174768; DOI=10.1016/j.yjmcc.2017.11.013;
RA Ghosh T.K., Aparicio-Sanchez J.J., Buxton S., Ketley A., Mohamed T.,
RA Rutland C.S., Loughna S., Brook J.D.;
RT "Acetylation of TBX5 by KAT2B and KAT2A regulates heart and limb
RT development.";
RL J. Mol. Cell. Cardiol. 114:185-198(2017).
RN [3]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=30424580; DOI=10.3390/jdb6040027;
RA Sen R., Pezoa S.A., Carpio Shull L., Hernandez-Lagunas L., Niswander L.A.,
RA Artinger K.B.;
RT "Kat2a and Kat2b acetyltransferase activity regulates craniofacial
RT cartilage and bone differentiation in zebrafish and mice.";
RL J. Dev. Biol. 6:0-0(2018).
CC -!- FUNCTION: Functions as a histone acetyltransferase (HAT) to promote
CC transcriptional activation (By similarity). Has significant histone
CC acetyltransferase activity with core histones (H3 and H4), and also
CC with nucleosome core particles (By similarity). Also acetylates non-
CC histone proteins (PubMed:29174768). Involved in heart and limb
CC development by mediating acetylation of tbx5 (PubMed:29174768). Also
CC acetylates spermidine (By similarity). Together with kat2a, required
CC for growth and differentiation of craniofacial cartilage and bone by
CC regulating acetylation of histone H3 at 'Lys-9' (H3K9ac)
CC (PubMed:30424580). {ECO:0000250|UniProtKB:Q92831,
CC ECO:0000269|PubMed:29174768, ECO:0000269|PubMed:30424580}.
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:Q92831};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + spermidine = CoA + H(+) + N(8)-acetylspermidine;
CC Xref=Rhea:RHEA:28270, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57834, ChEBI:CHEBI:58535; EC=2.3.1.57;
CC Evidence={ECO:0000250|UniProtKB:Q92831};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92831}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q92831}. Note=Mainly localizes to the nucleus.
CC Also localizes to centrosomes in late G1 and around the G1/S
CC transition, coinciding with the onset of centriole formation.
CC {ECO:0000250|UniProtKB:Q92831}.
CC -!- DEVELOPMENTAL STAGE: Widely expressed throughout the anterior head
CC region, including the central nervous system, the eye and branchial
CC arches at 24 hours post fertilization (hpf). Expressed strongly in the
CC brain region, with expression extending posteriorly in the spinal cord.
CC By 40-48 hpf, expression remains strongly expressed in the head region
CC but is reduced throughout the rest of the embryo (PubMed:30424580).
CC Expressed in the heart and tail regions throughout developmental stages
CC (PubMed:29174768). {ECO:0000269|PubMed:29174768,
CC ECO:0000269|PubMed:30424580}.
CC -!- DISRUPTION PHENOTYPE: Craniofacial cartilage and bone defects,
CC characterized by shortening and hypoplastic nature of the cartilage
CC elements and disruption of the posterior ceratobranchial cartilages
CC (PubMed:30424580). Morpholino knockdown of kat2a and kat2b leads to
CC impaired heart and limb development. Abnormal fin development is also
CC observed (PubMed:29174768). {ECO:0000269|PubMed:29174768,
CC ECO:0000269|PubMed:30424580}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. GCN5 subfamily.
CC {ECO:0000305}.
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DR EMBL; BX950869; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX957344; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001038499.1; NM_001045034.1.
DR AlphaFoldDB; Q1LUC3; -.
DR SMR; Q1LUC3; -.
DR STRING; 7955.ENSDARP00000085190; -.
DR PaxDb; Q1LUC3; -.
DR Ensembl; ENSDART00000090757; ENSDARP00000085190; ENSDARG00000062634.
DR GeneID; 563942; -.
DR KEGG; dre:563942; -.
DR CTD; 8850; -.
DR ZFIN; ZDB-GENE-060503-207; kat2b.
DR eggNOG; KOG1472; Eukaryota.
DR GeneTree; ENSGT00940000154995; -.
DR HOGENOM; CLU_015901_0_0_1; -.
DR InParanoid; Q1LUC3; -.
DR OMA; DFAIGYF; -.
DR OrthoDB; 349249at2759; -.
DR PhylomeDB; Q1LUC3; -.
DR TreeFam; TF105399; -.
DR Reactome; R-DRE-2032785; YAP1- and WWTR1 (TAZ)-stimulated gene expression.
DR Reactome; R-DRE-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-DRE-5689901; Metalloprotease DUBs.
DR Reactome; R-DRE-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-DRE-8941856; RUNX3 regulates NOTCH signaling.
DR Reactome; R-DRE-9018519; Estrogen-dependent gene expression.
DR Reactome; R-DRE-9617629; Regulation of FOXO transcriptional activity by acetylation.
DR PRO; PR:Q1LUC3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 19.
DR Bgee; ENSDARG00000062634; Expressed in retina and 23 other tissues.
DR GO; GO:0140672; C:ATAC complex; IBA:GO_Central.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0004145; F:diamine N-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0010484; F:H3 histone acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0060349; P:bone morphogenesis; IMP:ZFIN.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0007507; P:heart development; IMP:UniProtKB.
DR GO; GO:0016573; P:histone acetylation; IMP:UniProtKB.
DR GO; GO:0043966; P:histone H3 acetylation; IBA:GO_Central.
DR GO; GO:0018393; P:internal peptidyl-lysine acetylation; ISS:UniProtKB.
DR GO; GO:0060173; P:limb development; IMP:UniProtKB.
DR GO; GO:0046600; P:negative regulation of centriole replication; ISS:UniProtKB.
DR GO; GO:2000233; P:negative regulation of rRNA processing; ISS:UniProtKB.
DR GO; GO:1902425; P:positive regulation of attachment of mitotic spindle microtubules to kinetochore; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006473; P:protein acetylation; ISS:UniProtKB.
DR GO; GO:1903010; P:regulation of bone development; IMP:UniProtKB.
DR GO; GO:0061035; P:regulation of cartilage development; IMP:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR Gene3D; 1.20.920.10; -; 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; IPR016376; GCN5/PCAF.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR009464; PCAF_N.
DR PANTHER; PTHR45750; PTHR45750; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF06466; PCAF_N; 1.
DR PIRSF; PIRSF003048; Histone_acetylase_PCAF; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 2: Evidence at transcript level;
KW Activator; Acyltransferase; Biological rhythms; Bromodomain; Cell cycle;
KW Cytoplasm; Cytoskeleton; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..796
FT /note="Histone acetyltransferase KAT2B"
FT /id="PRO_0000443448"
FT DOMAIN 469..617
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT DOMAIN 704..774
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..95
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 536
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT BINDING 540..542
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT BINDING 547..553
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT BINDING 578..581
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
SQ 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
