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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_MOUSE             Reviewed;         813 AA.
Q9JHD1; Q3U142; Q640M9;
18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
18-MAR-2008, sequence version 2.
12-SEP-2018, entry version 141.
RecName: Full=Histone acetyltransferase KAT2B;
EC=2.3.1.48 {ECO:0000250|UniProtKB:Q92831};
AltName: Full=Histone acetyltransferase PCAF {ECO:0000303|PubMed:11017084};
Short=Histone acetylase PCAF {ECO:0000303|PubMed:11017084};
AltName: Full=Lysine acetyltransferase 2B {ECO:0000305};
AltName: Full=P300/CBP-associated factor {ECO:0000303|PubMed:11017084};
Short=P/CAF {ECO:0000303|PubMed:11017084};
Name=Kat2b {ECO:0000312|MGI:MGI:1343094};
Synonyms=Pcaf {ECO:0000303|PubMed:11017084};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9742083; DOI=10.1128/MCB.18.10.5659;
Xu W., Edmondson D.G., Roth S.Y.;
"Mammalian GCN5 and P/CAF acetyltransferases have homologous amino-
terminal domains important for recognition of nucleosomal
substrates.";
Mol. Cell. Biol. 18:5659-5669(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=NOD; TISSUE=Spleen;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INTERACTION WITH NR4A3.
PubMed=12709428; DOI=10.1074/jbc.M300088200;
Wansa K.D., Harris J.M., Yan G., Ordentlich P., Muscat G.E.;
"The AF-1 domain of the orphan nuclear receptor NOR-1 mediates trans-
activation, coactivator recruitment, and activation by the purine
anti-metabolite 6-mercaptopurine.";
J. Biol. Chem. 278:24776-24790(2003).
[5]
INTERACTION WITH NR2C1.
PubMed=17187077; DOI=10.1038/nsmb1185;
Park S.W., Hu X., Gupta P., Lin Y.P., Ha S.G., Wei L.N.;
"SUMOylation of Tr2 orphan receptor involves Pml and fine-tunes Oct4
expression in stem cells.";
Nat. Struct. Mol. Biol. 14:68-75(2007).
[6]
INTERACTION WITH NR2C1.
PubMed=18682553; DOI=10.1073/pnas.0710561105;
Gupta P., Ho P.C., Huq M.M., Ha S.G., Park S.W., Khan A.A., Tsai N.P.,
Wei L.N.;
"Retinoic acid-stimulated sequential phosphorylation, PML recruitment,
and SUMOylation of nuclear receptor TR2 to suppress Oct4 expression.";
Proc. Natl. Acad. Sci. U.S.A. 105:11424-11429(2008).
[7]
DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=11017084; DOI=10.1038/79973;
Xu W., Edmondson D.G., Evrard Y.A., Wakamiya M., Behringer R.R.,
Roth S.Y.;
"Loss of Gcn5l2 leads to increased apoptosis and mesodermal defects
during mouse development.";
Nat. Genet. 26:229-232(2000).
-!- FUNCTION: Functions as a histone acetyltransferase (HAT) to
promote transcriptional activation. Has significant histone
acetyltransferase activity with core histones (H3 and H4), and
also with nucleosome core particles. Also acetylates non-histone
proteins, such as ACLY, PLK4 and TBX5. Inhibits cell-cycle
progression and counteracts the mitogenic activity of the
adenoviral oncoprotein E1A. Acts as a circadian transcriptional
coactivator which enhances the activity of the circadian
transcriptional activators: NPAS2-ARNTL/BMAL1 and CLOCK-
ARNTL/BMAL1 heterodimers. Involved in heart and limb development
by mediating acetylation of TBX5, acetylation regulating
nucleocytoplasmic shuttling of TBX5. Acts as a negative regulator
of centrosome amplification by mediating acetylation of PLK4.
{ECO:0000250|UniProtKB:Q92831}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + [protein]-L-lysine = CoA +
[protein]-N(6)-acetyl-L-lysine. {ECO:0000250|UniProtKB:Q92831}.
-!- SUBUNIT: Interacts with BCAS3. Interacts with SIRT1. Interacts
with EP300, CREBBP and DDX17. Component of a large chromatin
remodeling complex, at least composed of MYSM1, KAT2B/PCAF, RBM10
and KIF11/TRIP5. Interacts with KLF1; the interaction does not
acetylate KLF1 and there is no enhancement of its
transactivational activity. Interacts with NFE4. Interacts with
MECOM. Interacts with NR2C2 (hypophosphorylated and unsumoylated
form); the interaction promotes the transactivation activity of
NR2C2. Interacts with NFE4. Interacts with MECOM. Interacts with
E2F1; the interaction acetylates E2F1 augmenting its DNA-binding
and transcriptional activity. Interacts with NPAS2, ARNTL/BMAL1
and CLOCK (By similarity). Interacts (unsumoylated form) with
NR2C1; the interaction promotes transactivation activity.
Interacts with CEBPB (By similarity). Interacts with NR4A3
(PubMed:12709428). Interacts with TBX5 (By similarity). Interacts
with PLK4 (By similarity). {ECO:0000250|UniProtKB:Q92831,
ECO:0000269|PubMed:12709428, ECO:0000269|PubMed:17187077,
ECO:0000269|PubMed:18682553}.
-!- INTERACTION:
Q505F1:Nr2c1; NbExp=3; IntAct=EBI-2325611, EBI-15617004;
-!- 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: Expression is low during embryogenesis and
becomes up-regulated in some adult tissues including heart and
skeletal muscle. {ECO:0000269|PubMed:11017084}.
-!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:11017084).
{ECO:0000269|PubMed:11017084}.
-!- SIMILARITY: Belongs to the acetyltransferase family. GCN5
subfamily. {ECO:0000305}.
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EMBL; AF254442; AAF70498.1; -; mRNA.
EMBL; AK156290; BAE33658.1; -; mRNA.
EMBL; BC082581; AAH82581.1; -; mRNA.
EMBL; BC145896; AAI45897.1; -; mRNA.
CCDS; CCDS28880.1; -.
RefSeq; NP_064389.2; NM_020005.4.
UniGene; Mm.255025; -.
PDB; 5ML0; X-ray; 1.64 A; A=705-813.
PDBsum; 5ML0; -.
ProteinModelPortal; Q9JHD1; -.
SMR; Q9JHD1; -.
BioGrid; 202042; 20.
ComplexPortal; CPX-1024; PCAF histone acetylase complex.
ComplexPortal; CPX-1029; PCAF-containing ATAC complex.
DIP; DIP-29281N; -.
IntAct; Q9JHD1; 3.
MINT; Q9JHD1; -.
STRING; 10090.ENSMUSP00000000724; -.
iPTMnet; Q9JHD1; -.
PhosphoSitePlus; Q9JHD1; -.
MaxQB; Q9JHD1; -.
PaxDb; Q9JHD1; -.
PRIDE; Q9JHD1; -.
Ensembl; ENSMUST00000000724; ENSMUSP00000000724; ENSMUSG00000000708.
GeneID; 18519; -.
KEGG; mmu:18519; -.
UCSC; uc008czp.2; mouse.
CTD; 8850; -.
MGI; MGI:1343094; Kat2b.
eggNOG; KOG1472; Eukaryota.
eggNOG; COG5076; LUCA.
GeneTree; ENSGT00920000149009; -.
HOGENOM; HOG000007151; -.
InParanoid; Q9JHD1; -.
KO; K06062; -.
OMA; QVIRFPM; -.
OrthoDB; EOG091G03ZO; -.
PhylomeDB; Q9JHD1; -.
TreeFam; TF105399; -.
Reactome; R-MMU-2032785; YAP1- and WWTR1 (TAZ)-stimulated gene expression.
Reactome; R-MMU-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
Reactome; R-MMU-350054; Notch-HLH transcription pathway.
Reactome; R-MMU-5250924; B-WICH complex positively regulates rRNA expression.
Reactome; R-MMU-5689901; Metalloprotease DUBs.
Reactome; R-MMU-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
Reactome; R-MMU-8941856; RUNX3 regulates NOTCH signaling.
Reactome; R-MMU-9018519; Estrogen-dependent gene expression.
ChiTaRS; Kat2b; mouse.
PRO; PR:Q9JHD1; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000000708; Expressed in 296 organ(s), highest expression level in stria vascularis of cochlear duct.
ExpressionAtlas; Q9JHD1; baseline and differential.
Genevisible; Q9JHD1; MM.
GO; GO:0031672; C:A band; IDA:MGI.
GO; GO:0042641; C:actomyosin; IDA:MGI.
GO; GO:0005671; C:Ada2/Gcn5/Ada3 transcription activator complex; IDA:MGI.
GO; GO:0005813; C:centrosome; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0000123; C:histone acetyltransferase complex; IDA:MGI.
GO; GO:0031674; C:I band; IDA:MGI.
GO; GO:0000776; C:kinetochore; IDA:MGI.
GO; GO:0000790; C:nuclear chromatin; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0016407; F:acetyltransferase activity; EXP:Reactome.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0004861; F:cyclin-dependent protein serine/threonine kinase inhibitor activity; IDA:UniProtKB.
GO; GO:0004402; F:histone acetyltransferase activity; IDA:MGI.
GO; GO:0035035; F:histone acetyltransferase binding; ISO:MGI.
GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
GO; GO:0004468; F:lysine N-acetyltransferase activity, acting on acetyl phosphate as donor; IDA:UniProtKB.
GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:MGI.
GO; GO:0003713; F:transcription coactivator activity; IDA:MGI.
GO; GO:0003712; F:transcription coregulator activity; ISO:MGI.
GO; GO:0008134; F:transcription factor binding; ISO:MGI.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0032869; P:cellular response to insulin stimulus; ISO:MGI.
GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
GO; GO:0007507; P:heart development; ISS:UniProtKB.
GO; GO:0016573; P:histone acetylation; IDA:MGI.
GO; GO:0043966; P:histone H3 acetylation; ISO:MGI.
GO; GO:0043970; P:histone H3-K9 acetylation; IGI:MGI.
GO; GO:0018393; P:internal peptidyl-lysine acetylation; IMP:UniProtKB.
GO; GO:0060173; P:limb development; ISS:UniProtKB.
GO; GO:0018076; P:N-terminal peptidyl-lysine acetylation; ISO:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; ISO:MGI.
GO; GO:0046600; P:negative regulation of centriole replication; ISS:UniProtKB.
GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0018394; P:peptidyl-lysine acetylation; ISO:MGI.
GO; GO:0097755; P:positive regulation of blood vessel diameter; ISO:MGI.
GO; GO:0035563; P:positive regulation of chromatin binding; ISO:MGI.
GO; GO:0035948; P:positive regulation of gluconeogenesis by positive regulation of transcription from RNA polymerase II promoter; IGI:MGI.
GO; GO:0071442; P:positive regulation of histone H3-K14 acetylation; ISO:MGI.
GO; GO:2000617; P:positive regulation of histone H3-K9 acetylation; ISO:MGI.
GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0006473; P:protein acetylation; ISO:MGI.
GO; GO:0010835; P:regulation of protein ADP-ribosylation; ISO:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:MGI.
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.
1: Evidence at protein level;
3D-structure; Activator; Acyltransferase; Biological rhythms;
Bromodomain; Cell cycle; Complete proteome; Cytoplasm; Cytoskeleton;
Nucleus; Reference proteome; Transcription; Transcription regulation;
Transferase.
CHAIN 1 813 Histone acetyltransferase KAT2B.
/FTId=PRO_0000322986.
DOMAIN 484 632 N-acetyltransferase.
{ECO:0000255|PROSITE-ProRule:PRU00532}.
DOMAIN 721 791 Bromo. {ECO:0000255|PROSITE-
ProRule:PRU00035}.
REGION 555 557 Acetyl-CoA binding.
{ECO:0000250|UniProtKB:Q92830}.
REGION 562 568 Acetyl-CoA binding.
{ECO:0000250|UniProtKB:Q92830}.
REGION 593 596 Acetyl-CoA binding.
{ECO:0000250|UniProtKB:Q92830}.
COMPBIAS 48 53 Poly-Gly.
ACT_SITE 551 551 Proton donor/acceptor.
{ECO:0000250|UniProtKB:Q92830}.
CONFLICT 293 294 LL -> FV (in Ref. 1; AAF70498).
{ECO:0000305}.
CONFLICT 319 319 E -> G (in Ref. 2; BAE33658).
{ECO:0000305}.
CONFLICT 459 459 H -> L (in Ref. 1; AAF70498).
{ECO:0000305}.
CONFLICT 548 548 G -> A (in Ref. 1; AAF70498).
{ECO:0000305}.
CONFLICT 554 554 F -> L (in Ref. 1; AAF70498).
{ECO:0000305}.
HELIX 707 722 {ECO:0000244|PDB:5ML0}.
HELIX 727 729 {ECO:0000244|PDB:5ML0}.
TURN 735 737 {ECO:0000244|PDB:5ML0}.
HELIX 741 744 {ECO:0000244|PDB:5ML0}.
HELIX 751 759 {ECO:0000244|PDB:5ML0}.
HELIX 766 783 {ECO:0000244|PDB:5ML0}.
HELIX 789 807 {ECO:0000244|PDB:5ML0}.
SEQUENCE 813 AA; 91769 MW; 38E52F326794F523 CRC64;
MAEAGGAGSP ALPPAPPHGS PRTLATAAGS SASCGPATAV AAAGTAEGPG GGGSARIAVK
KAQLRSAPRA KKLEKLGVYS ACKAEESCKC NGWKNPNPSP TPPRGDLQQI IVSLTESCRS
CSHALAAHVS HLENVSEEEM DRLLGIVLDV EYLFTCVHKE EDADTKQVYF YLFKLLRKSI
LQRGKPVVEG SLEKKPPFEK PSIEQGVNNF VQYKFSHLPS KERQTTIELA KMFLNRINYW
HLEAPSQRRL RSPNDDISGY KENYTRWLCY CNVPQFCDSL PRYETTKVFG RTLLRSVFTI
MRRQLLEQAR QEKDKLPLEK RTLILTHFPK FLSMLEEEVY SQNSPIWDQD FLSASSRTSP
LGIQTVISPP VTGTALFSSN STSHEQINGG RTSPGCRGSS GLEANPGEKR KMNNSHAPEE
AKRSRVMGDI PVELINEVMS TITDPAGMLG PETNFLSAHS ARDEAARLEE RRGVIEFHVV
GNSLNQKPNK KILMWLVGLQ NVFSHQLPRM PKEYITRLVF DPKHKTLALI KDGRVIGGIC
FRMFPSQGFT EIVFCAVTSN EQVKGYGTHL MNHLKEYHIK HEILNFLTYA DEYAIGYFKK
QGFSKEIKIP KTKYVGYIKD YEGATLMGCE LNPQIPYTEF SVIIKKQKEI IKKLIERKQA
QIRKVYPGLS CFKDGVRQIP IESIPGIRET GWKPSGKEKS KEPKDPEQLY STLKNILQQV
KNHPNAWPFM EPVKRTEAPG YYEVIRFPMD LKTMSERLRN RYYVSKKLFM ADLQRVFTNC
KEYNPPESEY YKCASILEKF FFSKIKEAGL IDK


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