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KAT2A_DANRE
ID   KAT2A_DANRE             Reviewed;         795 AA.
AC   A0A0R4IXF6; A0A0R4IN10; Q1L672;
DT   28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2016, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=Histone acetyltransferase KAT2A {ECO:0000250|UniProtKB:Q92830};
DE            EC=2.3.1.48 {ECO:0000250|UniProtKB:Q92830};
DE   AltName: Full=Histone glutaryltransferase KAT2A {ECO:0000305};
DE            EC=2.3.1.- {ECO:0000250|UniProtKB:Q92830};
DE   AltName: Full=Histone succinyltransferase KAT2A {ECO:0000250|UniProtKB:Q92830};
DE            EC=2.3.1.- {ECO:0000250|UniProtKB:Q92830};
DE   AltName: Full=Lysine acetyltransferase 2A {ECO:0000303|PubMed:29174768};
GN   Name=kat2a {ECO:0000303|PubMed:29174768,
GN   ECO:0000312|ZFIN:ZDB-GENE-080403-11};
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   NUCLEOTIDE SEQUENCE [MRNA] OF 526-715.
RX   PubMed=17997606; DOI=10.1371/journal.pgen.0030188;
RA   Bertrand S., Thisse B., Tavares R., Sachs L., Chaumot A., Bardet P.-L.,
RA   Escriva H., Duffraisse M., Marchand O., Safi R., Thisse C., Laudet V.;
RT   "Unexpected novel relational links uncovered by extensive developmental
RT   profiling of nuclear receptor expression.";
RL   PLoS Genet. 3:E188-E188(2007).
RN   [3]
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   [4]
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: Protein lysine acyltransferase that can act as a
CC       acetyltransferase, glutaryltransferase or succinyltransferase,
CC       depending on the context (By similarity). Acts as a histone lysine
CC       succinyltransferase: catalyzes succinylation of histone H3 on 'Lys-79'
CC       (H3K79succ), with a maximum frequency around the transcription start
CC       sites of genes (By similarity). Succinylation of histones gives a
CC       specific tag for epigenetic transcription activation (By similarity).
CC       Association with the 2-oxoglutarate dehydrogenase complex, which
CC       provides succinyl-CoA, is required for histone succinylation (By
CC       similarity). In different complexes, functions either as an
CC       acetyltransferase (HAT) or as a succinyltransferase: in the SAGA and
CC       ATAC complexes, acts as a histone acetyltransferase (By similarity).
CC       Has significant histone acetyltransferase activity with core histones,
CC       but not with nucleosome core particles (By similarity). Acetylation of
CC       histones gives a specific tag for epigenetic transcription activation
CC       (By similarity). Also acetylates non-histone proteins, such as tbx5
CC       (PubMed:29174768). Involved in heart and limb development by mediating
CC       acetylation of tbx5 (PubMed:29174768). Together with kat2b, 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). Also acts as a histone glutaryltransferase:
CC       catalyzes glutarylation of histone H4 on 'Lys-91' (H4K91glu), a mark
CC       that destabilizes nucleosomes by promoting dissociation of the H2A-H2B
CC       dimers from nucleosomes (By similarity). {ECO:0000250|UniProtKB:Q92830,
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:Q92830};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L-
CC         lysyl-[histone]; Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845,
CC         Rhea:RHEA-COMP:11338, 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:Q92830};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993;
CC         Evidence={ECO:0000250|UniProtKB:Q92830};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[protein] + succinyl-CoA = CoA + H(+) + N(6)-succinyl-
CC         L-lysyl-[protein]; Xref=Rhea:RHEA:16261, Rhea:RHEA-COMP:9752,
CC         Rhea:RHEA-COMP:11877, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:87830;
CC         Evidence={ECO:0000250|UniProtKB:Q92830};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutaryl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-glutaryl-
CC         L-lysyl-[protein]; Xref=Rhea:RHEA:18009, Rhea:RHEA-COMP:9752,
CC         Rhea:RHEA-COMP:11875, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57378, ChEBI:CHEBI:87828;
CC         Evidence={ECO:0000250|UniProtKB:Q92830};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18010;
CC         Evidence={ECO:0000250|UniProtKB:Q92830};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92830}.
CC       Chromosome {ECO:0000250|UniProtKB:Q92830}. Cytoplasm, cytoskeleton,
CC       microtubule organizing center, centrosome
CC       {ECO:0000250|UniProtKB:Q92830}.
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. By 40-48 hpf, expression remains strongly expressed in
CC       the head region but is reduced throughout the rest of the embryo
CC       (PubMed:30424580). Expressed in the heart and tail regions throughout
CC       developmental stages (PubMed:29174768). {ECO:0000269|PubMed:29174768,
CC       ECO:0000269|PubMed:30424580}.
CC   -!- DOMAIN: Loop3 is required for substrate specificity and adopts
CC       different structural conformations in succinyl-CoA-bound and acetyl-
CC       CoA-bound forms. Tyr-603 has an important role in the selective binding
CC       of succinyl-CoA over acetyl-CoA. {ECO:0000250|UniProtKB:Q92830}.
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; BX005093; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; FO818663; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DQ017634; AAY85289.1; -; mRNA.
DR   RefSeq; XP_009297593.1; XM_009299318.2.
DR   AlphaFoldDB; A0A0R4IXF6; -.
DR   SMR; A0A0R4IXF6; -.
DR   STRING; 7955.ENSDARP00000011795; -.
DR   PaxDb; A0A0R4IXF6; -.
DR   Ensembl; ENSDART00000157682; ENSDARP00000141597; ENSDARG00000104734.
DR   GeneID; 555517; -.
DR   KEGG; dre:555517; -.
DR   CTD; 2648; -.
DR   ZFIN; ZDB-GENE-080403-11; kat2a.
DR   eggNOG; KOG1472; Eukaryota.
DR   GeneTree; ENSGT00940000158799; -.
DR   OMA; NHLKDYS; -.
DR   OrthoDB; 349249at2759; -.
DR   Reactome; R-DRE-5250924; B-WICH complex positively regulates rRNA expression.
DR   Reactome; R-DRE-5689880; Ub-specific processing proteases.
DR   Reactome; R-DRE-8941856; RUNX3 regulates NOTCH signaling.
DR   PRO; PR:A0A0R4IXF6; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 3.
DR   Bgee; ENSDARG00000104734; Expressed in blastula and 28 other tissues.
DR   ExpressionAtlas; A0A0R4IXF6; baseline.
DR   GO; GO:0140672; C:ATAC complex; IBA:GO_Central.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0000123; C:histone acetyltransferase complex; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR   GO; GO:0010484; F:H3 histone acetyltransferase activity; IBA:GO_Central.
DR   GO; GO:0004402; F:histone acetyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0106229; F:histone glutaryltransferase activity; ISS:UniProtKB.
DR   GO; GO:0106078; F:histone succinyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR   GO; GO:0060349; P:bone morphogenesis; IMP:ZFIN.
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; ISS:UniProtKB.
DR   GO; GO:0044154; P:histone H3-K14 acetylation; IBA:GO_Central.
DR   GO; GO:0106077; P:histone succinylation; ISS:UniProtKB.
DR   GO; GO:0018393; P:internal peptidyl-lysine acetylation; ISS:UniProtKB.
DR   GO; GO:0060173; P:limb development; IMP:UniProtKB.
DR   GO; GO:0007616; P:long-term memory; ISS:UniProtKB.
DR   GO; GO:0106227; P:peptidyl-lysine glutarylation; ISS:UniProtKB.
DR   GO; GO:0001819; P:positive regulation of cytokine production; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; 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:0045589; P:regulation of regulatory T cell differentiation; ISS:UniProtKB.
DR   GO; GO:0048167; P:regulation of synaptic plasticity; ISS:UniProtKB.
DR   GO; GO:0050863; P:regulation of T cell activation; ISS:UniProtKB.
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   Acyltransferase; Bromodomain; Chromosome; Cytoplasm; Cytoskeleton; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation; Transferase.
FT   CHAIN           1..795
FT                   /note="Histone acetyltransferase KAT2A"
FT                   /id="PRO_0000443447"
FT   DOMAIN          461..614
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   DOMAIN          703..773
FT                   /note="Bromo"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          597..606
FT                   /note="Loop 3"
FT                   /evidence="ECO:0000250|UniProtKB:Q92830"
FT   COMPBIAS        8..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        533
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q92830"
FT   BINDING         537..539
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q92830"
FT   BINDING         537..539
FT                   /ligand="succinyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57292"
FT                   /evidence="ECO:0000250|UniProtKB:Q92830"
FT   BINDING         544..550
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q92830"
FT   BINDING         544..550
FT                   /ligand="succinyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57292"
FT                   /evidence="ECO:0000250|UniProtKB:Q92830"
FT   BINDING         575
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q92830"
FT   BINDING         575
FT                   /ligand="succinyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57292"
FT                   /evidence="ECO:0000250|UniProtKB:Q92830"
FT   CONFLICT        712..713
FT                   /note="ME -> LH (in Ref. 2; AAY85289)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   795 AA;  90624 MW;  F2081631E5391B92 CRC64;
     MADPAAQSSA QPRLQQAQSS GPTGSNSNPG AGSSDPARPG LSQQQWSSQK KAQVRSFPRA
     KKLEKLGVFS SCKANDACKC NGWKNPNPPT AARMELQQQA ASLTETCRSC GHSLAEHVSH
     LENVSEEEIN RLLGMVVDVE NLFMSVHKEE DTDTKQVYFY LFKLLRKCIL QMGKPVVEGS
     LGSPPFEKPN IEQGVLNFVQ YKFSHLAPKE RQTMYELSKM FLLCLNYWKL ETPSQFRQRA
     QKEDAAAYKV DYTRWLCYCH VPQSNDSLPR YETCQVFGRS LLKSIFTVTR RQLLEKFRVE
     KDKLPPEKRT LILTHFPKFL SMLEEEIYGE NSPIWEADFT MPASEGTQLG HQTVLSPVSI
     SGSPHSKGSS ASALGVTGLD VASSEPTIGE KRKLPEALTL EDAKRIRVMG DIPMELVNEV
     MKTITDPAAM LGPETSLLSA NAARDETARL EERRGIIEFH VIGNSLSQKS NKKILMWLVG
     LQNVFSHQLP RMPKEYITRL VFDPKHKTLA LIKDGRVIGG ICFRMFPTQG FTEIVFCAVT
     SNEQVKGYGT HLMNHLKEYH IKHGILYFLT YADEYAIGYF KKQGFSKDIK VPKSRYLGYI
     KDYEGATLME CELNPRIPYT ELSHIIKRQK EIIKKLIERK QNQIRKVYPG LTCFKEGVRQ
     IPVESIPGIR ETGWKPSAKE KSKELKDPDL LYNMLKNLLA QIKTHPDAWP FMEPVKKSEA
     PDYYEVIRFP IDLKTMTERL KNRYYVTKKL FIADLQRVIT NCREYNPPDS EYCKSANTLE
     KFFYFKLKEA GLIDK
 
 
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