ID   KAT2B_MOUSE             Reviewed;         813 AA.
AC   Q9JHD1; Q3U142; Q640M9;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   25-JAN-2012, entry version 74.
DE   RecName: Full=Histone acetyltransferase KAT2B;
DE            EC=2.3.1.48;
DE   AltName: Full=Histone acetyltransferase PCAF;
DE            Short=Histone acetylase PCAF;
DE   AltName: Full=Lysine acetyltransferase 2B;
DE   AltName: Full=P300/CBP-associated factor;
DE            Short=P/CAF;
GN   Name=Kat2b; Synonyms=Pcaf;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=98414582; PubMed=9742083;
RA   Xu W., Edmondson D.G., Roth S.Y.;
RT   "Mammalian GCN5 and P/CAF acetyltransferases have homologous amino-
RT   terminal domains important for recognition of nucleosomal
RT   substrates.";
RL   Mol. Cell. Biol. 18:5659-5669(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD; TISSUE=Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   INTERACTION WITH NR2C1.
RX   PubMed=17187077; DOI=10.1038/nsmb1185;
RA   Park S.W., Hu X., Gupta P., Lin Y.P., Ha S.G., Wei L.N.;
RT   "SUMOylation of Tr2 orphan receptor involves Pml and fine-tunes Oct4
RT   expression in stem cells.";
RL   Nat. Struct. Mol. Biol. 14:68-75(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   INTERACTION WITH NR2C1.
RX   PubMed=18682553; DOI=10.1073/pnas.0710561105;
RA   Gupta P., Ho P.C., Huq M.M., Ha S.G., Park S.W., Khan A.A., Tsai N.P.,
RA   Wei L.N.;
RT   "Retinoic acid-stimulated sequential phosphorylation, PML recruitment,
RT   and SUMOylation of nuclear receptor TR2 to suppress Oct4 expression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:11424-11429(2008).
CC   -!- FUNCTION: Functions as a histone acetyltransferase (HAT) to
CC       promote transcriptional activation. Has significant histone
CC       acetyltransferase activity with core histones (H3 and H4), and
CC       also with nucleosome core particles (By similarity).
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + [histone] = CoA + acetyl-
CC       [histone].
CC   -!- SUBUNIT: Interacts with SIRT1. Interacts with EP300 and CREBBP.
CC       Component of a large chromatin remodeling complex, at least
CC       composed of MYSM1, KAT2B/PCAF, RBM10 and KIF11/TRIP5. Interacts
CC       with KLF1; the interaction does not acetylate KLF1 and there is no
CC       enhancement of its transactivational activity. Interacts with
CC       NFE4. Interacts with MECOM. Interacts with NR2C2
CC       (hypophosphorylated and unsumoylated form); the interaction
CC       promotes the transactivation activity of NR2C2 (By similarity).
CC       Interacts with NFE4. Interacts with MECOM. Interacts with E2F1;
CC       the interaction acetylates E2F1 augmenting its DNA-binding and
CC       transcriptional activity (By similarity). Interacts (unsumoylated
CC       form) with NR2C1; the interaction promotes transactivation
CC       activity.
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- DOMAIN: The bromodomain mediates binding to HIV-1 Tat.
CC   -!- SIMILARITY: Belongs to the GCN5 family.
CC   -!- SIMILARITY: Contains 1 bromo domain.
CC   -!- SIMILARITY: Contains 1 N-acetyltransferase domain.
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DR   EMBL; AF254442; AAF70498.1; -; mRNA.
DR   EMBL; AK156290; BAE33658.1; -; mRNA.
DR   EMBL; BC082581; AAH82581.1; -; mRNA.
DR   EMBL; BC145896; AAI45897.1; -; mRNA.
DR   IPI; IPI00471164; -.
DR   RefSeq; NP_064389.2; NM_020005.4.
DR   UniGene; Mm.255025; -.
DR   UniGene; Mm.483572; -.
DR   HSSP; Q92831; 1CM0.
DR   ProteinModelPortal; Q9JHD1; -.
DR   SMR; Q9JHD1; 474-633, 706-812.
DR   DIP; DIP-29281N; -.
DR   MINT; MINT-6166901; -.
DR   STRING; Q9JHD1; -.
DR   PRIDE; Q9JHD1; -.
DR   Ensembl; ENSMUST00000000724; ENSMUSP00000000724; ENSMUSG00000000708.
DR   GeneID; 18519; -.
DR   KEGG; mmu:18519; -.
DR   CTD; 8850; -.
DR   MGI; MGI:1343094; Kat2b.
DR   eggNOG; roNOG10302; -.
DR   GeneTree; ENSGT00430000030976; -.
DR   InParanoid; Q9JHD1; -.
DR   OMA; YSACKAE; -.
DR   OrthoDB; EOG4F1X2G; -.
DR   NextBio; 294272; -.
DR   ArrayExpress; Q9JHD1; -.
DR   Bgee; Q9JHD1; -.
DR   Genevestigator; Q9JHD1; -.
DR   GO; GO:0031672; C:A band; IDA:MGI.
DR   GO; GO:0042641; C:actomyosin; IDA:MGI.
DR   GO; GO:0016585; C:chromatin remodeling complex; ISS:UniProtKB.
DR   GO; GO:0031674; C:I band; IDA:MGI.
DR   GO; GO:0000776; C:kinetochore; IDA:MGI.
DR   GO; GO:0004861; F:cyclin-dependent protein kinase inhibitor activity; IDA:UniProtKB.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IDA:MGI.
DR   GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR   GO; GO:0003713; F:transcription coactivator activity; IDA:MGI.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0045736; P:negative regulation of cyclin-dependent protein kinase activity; IDA:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IGI:MGI.
DR   GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR   InterPro; IPR000182; AcTrfase_GCN5-related_dom.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   InterPro; IPR016376; Hist_acetylase_PCAF.
DR   InterPro; IPR009464; PCAF_N.
DR   Gene3D; G3DSA:3.40.630.30; Acyl_CoA_acyltransferase; 1.
DR   Gene3D; G3DSA:1.20.920.10; Bromodomain; 1.
DR   KO; K06062; -.
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; SSF55729; Acyl_CoA_acyltransferase; 1.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Acyltransferase; Bromodomain; Cell cycle;
KW   Complete proteome; Nucleus; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation; Transferase.
FT   CHAIN         1    813       Histone acetyltransferase KAT2B.
FT                                /FTId=PRO_0000322986.
FT   DOMAIN      484    632       N-acetyltransferase.
FT   DOMAIN      721    791       Bromo.
FT   COMPBIAS     48     53       Poly-Gly.
FT   MOD_RES      20     20       Phosphoserine.
FT   MOD_RES     710    710       Phosphotyrosine (By similarity).
FT   MOD_RES     714    714       N6-acetyllysine (By similarity).
FT   CONFLICT    293    294       LL -> FV (in Ref. 1; AAF70498).
FT   CONFLICT    319    319       E -> G (in Ref. 2; BAE33658).
FT   CONFLICT    459    459       H -> L (in Ref. 1; AAF70498).
FT   CONFLICT    548    548       G -> A (in Ref. 1; AAF70498).
FT   CONFLICT    554    554       F -> L (in Ref. 1; AAF70498).
SQ   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
//