Q9JHD1 (KAT2B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone acetyltransferase KAT2B
EC=2.3.1.48

Alternative name(s):
Histone acetyltransferase PCAF
Short name=Histone acetylase PCAF
Lysine acetyltransferase 2B
P300/CBP-associated factor
Short name=P/CAF

Gene names

Name:	Kat2b
Synonyms:	Pcaf

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	813 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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 By similarity.
Catalytic activity	Acetyl-CoA + [histone] = CoA + acetyl-[histone].
Subunit structure	Interacts with SIRT1. Interacts with EP300 and CREBBP. 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 By similarity. Interacts with NFE4. Interacts with MECOM. Interacts with E2F1; the interaction acetylates E2F1 augmenting its DNA-binding and transcriptional activity By similarity. Interacts (unsumoylated form) with NR2C1; the interaction promotes transactivation activity. Ref.4 Ref.6
Subcellular location	Nucleus By similarity.
Domain	The bromodomain mediates binding to HIV-1 Tat.
Sequence similarities	Belongs to the GCN5 family. Contains 1 bromo domain. Contains 1 N-acetyltransferase domain.

Ontologies

Keywords
Biological process	Cell cycle Transcription Transcription regulation
Cellular component	Nucleus
Domain	Bromodomain
Molecular function	Acyltransferase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of cyclin-dependent protein kinase activity Inferred from direct assay. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Inferred from genetic interaction. Source: MGI transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	A band Inferred from direct assay. Source: MGI I band Inferred from direct assay. Source: MGI actomyosin Inferred from direct assay. Source: MGI chromatin remodeling complex Inferred from sequence or structural similarity. Source: UniProtKB kinetochore Inferred from direct assay. Source: MGI
Molecular function	cyclin-dependent protein kinase inhibitor activity Inferred from direct assay. Source: UniProtKB histone acetyltransferase activity Inferred from direct assay Ref.1. Source: MGI protein kinase binding Inferred from physical interaction. Source: UniProtKB transcription coactivator activity Inferred from direct assay. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 813	813	Histone acetyltransferase KAT2B		PRO_0000322986
Regions
	Domain	484 – 632	149	N-acetyltransferase
	Domain	721 – 791	71	Bromo
	Compositional bias	48 – 53	6	Poly-Gly
Amino acid modifications
	Modified residue	20	1	Phosphoserine Ref.5
	Modified residue	710	1	Phosphotyrosine By similarity
	Modified residue	714	1	N6-acetyllysine By similarity
Experimental info
	Sequence conflict	293 – 294	2	LL → FV in AAF70498. Ref.1
	Sequence conflict	319	1	E → G in BAE33658. Ref.2
	Sequence conflict	459	1	H → L in AAF70498. Ref.1
	Sequence conflict	548	1	G → A in AAF70498. Ref.1
	Sequence conflict	554	1	F → L in AAF70498. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9JHD1 [UniParc]. Last modified March 18, 2008. Version 2. Checksum: 38E52F326794F523	FASTA	813	91,769
	10 20 30 40 50 60 MAEAGGAGSP ALPPAPPHGS PRTLATAAGS SASCGPATAV AAAGTAEGPG GGGSARIAVK 70 80 90 100 110 120 KAQLRSAPRA KKLEKLGVYS ACKAEESCKC NGWKNPNPSP TPPRGDLQQI IVSLTESCRS 130 140 150 160 170 180 CSHALAAHVS HLENVSEEEM DRLLGIVLDV EYLFTCVHKE EDADTKQVYF YLFKLLRKSI 190 200 210 220 230 240 LQRGKPVVEG SLEKKPPFEK PSIEQGVNNF VQYKFSHLPS KERQTTIELA KMFLNRINYW 250 260 270 280 290 300 HLEAPSQRRL RSPNDDISGY KENYTRWLCY CNVPQFCDSL PRYETTKVFG RTLLRSVFTI 310 320 330 340 350 360 MRRQLLEQAR QEKDKLPLEK RTLILTHFPK FLSMLEEEVY SQNSPIWDQD FLSASSRTSP 370 380 390 400 410 420 LGIQTVISPP VTGTALFSSN STSHEQINGG RTSPGCRGSS GLEANPGEKR KMNNSHAPEE 430 440 450 460 470 480 AKRSRVMGDI PVELINEVMS TITDPAGMLG PETNFLSAHS ARDEAARLEE RRGVIEFHVV 490 500 510 520 530 540 GNSLNQKPNK KILMWLVGLQ NVFSHQLPRM PKEYITRLVF DPKHKTLALI KDGRVIGGIC 550 560 570 580 590 600 FRMFPSQGFT EIVFCAVTSN EQVKGYGTHL MNHLKEYHIK HEILNFLTYA DEYAIGYFKK 610 620 630 640 650 660 QGFSKEIKIP KTKYVGYIKD YEGATLMGCE LNPQIPYTEF SVIIKKQKEI IKKLIERKQA 670 680 690 700 710 720 QIRKVYPGLS CFKDGVRQIP IESIPGIRET GWKPSGKEKS KEPKDPEQLY STLKNILQQV 730 740 750 760 770 780 KNHPNAWPFM EPVKRTEAPG YYEVIRFPMD LKTMSERLRN RYYVSKKLFM ADLQRVFTNC 790 800 810 KEYNPPESEY YKCASILEKF FFSKIKEAGL IDK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mammalian GCN5 and P/CAF acetyltransferases have homologous amino-terminal domains important for recognition of nucleosomal substrates." Xu W., Edmondson D.G., Roth S.Y. Mol. Cell. Biol. 18:5659-5669(1998) [PubMed: 9742083] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The transcriptional landscape of the mammalian genome." 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. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: NOD. Tissue: Spleen.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Brain and Eye.
[4]	"SUMOylation of Tr2 orphan receptor involves Pml and fine-tunes Oct4 expression in stem cells." Park S.W., Hu X., Gupta P., Lin Y.P., Ha S.G., Wei L.N. Nat. Struct. Mol. Biol. 14:68-75(2007) [PubMed: 17187077] [Abstract] Cited for: INTERACTION WITH NR2C1.
[5]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, MASS SPECTROMETRY. Tissue: Liver.
[6]	"Retinoic acid-stimulated sequential phosphorylation, PML recruitment, and SUMOylation of nuclear receptor TR2 to suppress Oct4 expression." Gupta P., Ho P.C., Huq M.M., Ha S.G., Park S.W., Khan A.A., Tsai N.P., Wei L.N. Proc. Natl. Acad. Sci. U.S.A. 105:11424-11429(2008) [PubMed: 18682553] [Abstract] Cited for: INTERACTION WITH NR2C1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF254442 mRNA. Translation: AAF70498.1. AK156290 mRNA. Translation: BAE33658.1. BC082581 mRNA. Translation: AAH82581.1. BC145896 mRNA. Translation: AAI45897.1.
IPI	IPI00471164.
RefSeq	NP_064389.2. NM_020005.4.
UniGene	Mm.255025. Mm.483572.
3D structure databases
HSSP	HSSP built from PDB template 1CM0 based on UniProtKB Q92831.
ProteinModelPortal	Q9JHD1.
SMR	Q9JHD1. Positions 474-633, 706-812.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-29281N.
MINT	MINT-6166901.
STRING	Q9JHD1.
Proteomic databases
PRIDE	Q9JHD1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000000724; ENSMUSP00000000724; ENSMUSG00000000708.
GeneID	18519.
KEGG	mmu:18519.
Organism-specific databases
CTD	8850.
MGI	MGI:1343094. Kat2b.
Phylogenomic databases
eggNOG	roNOG10302.
GeneTree	ENSGT00430000030976.
InParanoid	Q9JHD1.
OMA	YSACKAE.
OrthoDB	EOG4F1X2G.
Gene expression databases
ArrayExpress	Q9JHD1.
Bgee	Q9JHD1.
Genevestigator	Q9JHD1.
Family and domain databases
InterPro	IPR000182. AcTrfase_GCN5-related_dom. IPR016181. Acyl_CoA_acyltransferase. IPR001487. Bromodomain. IPR018359. Bromodomain_CS. IPR016376. Hist_acetylase_PCAF. IPR009464. PCAF_N. [Graphical view]
Gene3D	G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit. G3DSA:1.20.920.10. Bromodomain. 1 hit.
KO	K06062.
Pfam	PF00583. Acetyltransf_1. 1 hit. PF00439. Bromodomain. 1 hit. PF06466. PCAF_N. 1 hit. [Graphical view]
PIRSF	PIRSF003048. Histone_acetylase_PCAF. 1 hit.
PRINTS	PR00503. BROMODOMAIN.
SMART	SM00297. BROMO. 1 hit. [Graphical view]
SUPFAM	SSF55729. Acyl_CoA_acyltransferase. 1 hit. SSF47370. Bromodomain. 1 hit.
PROSITE	PS00633. BROMODOMAIN_1. 1 hit. PS50014. BROMODOMAIN_2. 1 hit. PS51186. GNAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	294272.
SOURCE	Search...

Entry information

Entry name

KAT2B_MOUSE

Accession

Primary (citable) accession number: Q9JHD1
Secondary accession number(s): Q3U142, Q640M9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	March 18, 2008
Last modified:	January 25, 2012
This is version 74 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program