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Q9JHD1

- KAT2B_MOUSE

UniProt

Q9JHD1 - KAT2B_MOUSE

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Protein

Histone acetyltransferase KAT2B

Gene

Kat2b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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. Acts as a circadian transcriptional coactivator which enhances the activity of the circadian transcriptional activators: NPAS2-ARNTL/BMAL1 and CLOCK-ARNTL/BMAL1 heterodimers (By similarity).By similarity

Catalytic activityi

Acetyl-CoA + [histone] = CoA + acetyl-[histone].

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei551 – 5511Proton donor/acceptorBy similarity

GO - Molecular functioni

  1. cyclin-dependent protein serine/threonine kinase inhibitor activity Source: UniProtKB
  2. histone acetyltransferase activity Source: MGI
  3. lysine N-acetyltransferase activity, acting on acetyl phosphate as donor Source: UniProtKB
  4. protein kinase binding Source: UniProtKB
  5. transcription coactivator activity Source: MGI

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cellular response to insulin stimulus Source: Ensembl
  3. chromatin remodeling Source: UniProtKB
  4. histone acetylation Source: MGI
  5. histone H3-K9 acetylation Source: MGI
  6. internal peptidyl-lysine acetylation Source: UniProtKB
  7. negative regulation of cell proliferation Source: Ensembl
  8. negative regulation of cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB
  9. N-terminal peptidyl-lysine acetylation Source: Ensembl
  10. positive regulation of gluconeogenesis by positive regulation of transcription from RNA polymerase II promoter Source: MGI
  11. positive regulation of transcription, DNA-templated Source: MGI
  12. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  13. protein acetylation Source: MGI
  14. regulation of protein ADP-ribosylation Source: Ensembl
  15. regulation of transcription, DNA-templated Source: MGI
  16. rhythmic process Source: UniProtKB-KW
  17. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Acyltransferase, Transferase

Keywords - Biological processi

Biological rhythms, Cell cycle, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_196464. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_196516. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
REACT_196589. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_196591. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_223683. Notch-HLH transcription pathway.
REACT_226917. HATs acetylate histones.
REACT_235780. RNA Polymerase I Transcription Initiation.
REACT_268602. Pre-NOTCH Transcription and Translation.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Kat2b
Synonyms:Pcaf
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 17

Organism-specific databases

MGIiMGI:1343094. Kat2b.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. A band Source: MGI
  2. actomyosin Source: MGI
  3. Ada2/Gcn5/Ada3 transcription activator complex Source: MGI
  4. histone acetyltransferase complex Source: MGI
  5. I band Source: MGI
  6. kinetochore Source: MGI
  7. nucleoplasm Source: Reactome
  8. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 813813Histone acetyltransferase KAT2BPRO_0000322986Add
BLAST

Proteomic databases

PaxDbiQ9JHD1.
PRIDEiQ9JHD1.

Expressioni

Gene expression databases

BgeeiQ9JHD1.
ExpressionAtlasiQ9JHD1. baseline and differential.
GenevestigatoriQ9JHD1.

Interactioni

Subunit structurei

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.By similarity2 Publications

Protein-protein interaction databases

BioGridi202042. 15 interactions.
DIPiDIP-29281N.
IntActiQ9JHD1. 2 interactions.
MINTiMINT-7984938.

Structurei

3D structure databases

ProteinModelPortaliQ9JHD1.
SMRiQ9JHD1. Positions 474-633, 706-812.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini484 – 632149N-acetyltransferasePROSITE-ProRule annotationAdd
BLAST
Domaini721 – 79171BromoPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni555 – 5573Acetyl-CoA bindingBy similarity
Regioni562 – 5687Acetyl-CoA bindingBy similarity
Regioni593 – 5964Acetyl-CoA bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi48 – 536Poly-Gly

Domaini

The bromodomain mediates binding to HIV-1 Tat.

Sequence similaritiesi

Contains 1 bromo domain.PROSITE-ProRule annotation
Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

Keywords - Domaini

Bromodomain

Phylogenomic databases

eggNOGiCOG5076.
GeneTreeiENSGT00760000119099.
HOGENOMiHOG000007151.
InParanoidiQ9JHD1.
KOiK06062.
OMAiKIMMWLV.
OrthoDBiEOG7ZKS9B.
PhylomeDBiQ9JHD1.
TreeFamiTF105399.

Family and domain databases

Gene3Di1.20.920.10. 1 hit.
3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR000182. GNAT_dom.
IPR016376. Hist_acetylase_PCAF.
IPR009464. PCAF_N.
[Graphical view]
PfamiPF13508. Acetyltransf_7. 1 hit.
PF00439. Bromodomain. 1 hit.
PF06466. PCAF_N. 1 hit.
[Graphical view]
PIRSFiPIRSF003048. Histone_acetylase_PCAF. 1 hit.
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00297. BROMO. 1 hit.
[Graphical view]
SUPFAMiSSF47370. SSF47370. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEiPS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS51186. GNAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9JHD1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAEAGGAGSP ALPPAPPHGS PRTLATAAGS SASCGPATAV AAAGTAEGPG
60 70 80 90 100
GGGSARIAVK KAQLRSAPRA KKLEKLGVYS ACKAEESCKC NGWKNPNPSP
110 120 130 140 150
TPPRGDLQQI IVSLTESCRS CSHALAAHVS HLENVSEEEM DRLLGIVLDV
160 170 180 190 200
EYLFTCVHKE EDADTKQVYF YLFKLLRKSI LQRGKPVVEG SLEKKPPFEK
210 220 230 240 250
PSIEQGVNNF VQYKFSHLPS KERQTTIELA KMFLNRINYW HLEAPSQRRL
260 270 280 290 300
RSPNDDISGY KENYTRWLCY CNVPQFCDSL PRYETTKVFG RTLLRSVFTI
310 320 330 340 350
MRRQLLEQAR QEKDKLPLEK RTLILTHFPK FLSMLEEEVY SQNSPIWDQD
360 370 380 390 400
FLSASSRTSP LGIQTVISPP VTGTALFSSN STSHEQINGG RTSPGCRGSS
410 420 430 440 450
GLEANPGEKR KMNNSHAPEE AKRSRVMGDI PVELINEVMS TITDPAGMLG
460 470 480 490 500
PETNFLSAHS ARDEAARLEE RRGVIEFHVV GNSLNQKPNK KILMWLVGLQ
510 520 530 540 550
NVFSHQLPRM PKEYITRLVF DPKHKTLALI KDGRVIGGIC FRMFPSQGFT
560 570 580 590 600
EIVFCAVTSN EQVKGYGTHL MNHLKEYHIK HEILNFLTYA DEYAIGYFKK
610 620 630 640 650
QGFSKEIKIP KTKYVGYIKD YEGATLMGCE LNPQIPYTEF SVIIKKQKEI
660 670 680 690 700
IKKLIERKQA QIRKVYPGLS CFKDGVRQIP IESIPGIRET GWKPSGKEKS
710 720 730 740 750
KEPKDPEQLY STLKNILQQV KNHPNAWPFM EPVKRTEAPG YYEVIRFPMD
760 770 780 790 800
LKTMSERLRN RYYVSKKLFM ADLQRVFTNC KEYNPPESEY YKCASILEKF
810
FFSKIKEAGL IDK
Length:813
Mass (Da):91,769
Last modified:March 18, 2008 - v2
Checksum:i38E52F326794F523
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti293 – 2942LL → FV in AAF70498. (PubMed:9742083)Curated
Sequence conflicti319 – 3191E → G in BAE33658. (PubMed:16141072)Curated
Sequence conflicti459 – 4591H → L in AAF70498. (PubMed:9742083)Curated
Sequence conflicti548 – 5481G → A in AAF70498. (PubMed:9742083)Curated
Sequence conflicti554 – 5541F → L in AAF70498. (PubMed:9742083)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF254442 mRNA. Translation: AAF70498.1.
AK156290 mRNA. Translation: BAE33658.1.
BC082581 mRNA. Translation: AAH82581.1.
BC145896 mRNA. Translation: AAI45897.1.
CCDSiCCDS28880.1.
RefSeqiNP_064389.2. NM_020005.4.
UniGeneiMm.255025.

Genome annotation databases

EnsembliENSMUST00000000724; ENSMUSP00000000724; ENSMUSG00000000708.
GeneIDi18519.
KEGGimmu:18519.
UCSCiuc008czp.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF254442 mRNA. Translation: AAF70498.1 .
AK156290 mRNA. Translation: BAE33658.1 .
BC082581 mRNA. Translation: AAH82581.1 .
BC145896 mRNA. Translation: AAI45897.1 .
CCDSi CCDS28880.1.
RefSeqi NP_064389.2. NM_020005.4.
UniGenei Mm.255025.

3D structure databases

ProteinModelPortali Q9JHD1.
SMRi Q9JHD1. Positions 474-633, 706-812.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202042. 15 interactions.
DIPi DIP-29281N.
IntActi Q9JHD1. 2 interactions.
MINTi MINT-7984938.

Proteomic databases

PaxDbi Q9JHD1.
PRIDEi Q9JHD1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000000724 ; ENSMUSP00000000724 ; ENSMUSG00000000708 .
GeneIDi 18519.
KEGGi mmu:18519.
UCSCi uc008czp.2. mouse.

Organism-specific databases

CTDi 8850.
MGIi MGI:1343094. Kat2b.

Phylogenomic databases

eggNOGi COG5076.
GeneTreei ENSGT00760000119099.
HOGENOMi HOG000007151.
InParanoidi Q9JHD1.
KOi K06062.
OMAi KIMMWLV.
OrthoDBi EOG7ZKS9B.
PhylomeDBi Q9JHD1.
TreeFami TF105399.

Enzyme and pathway databases

Reactomei REACT_196464. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_196516. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
REACT_196589. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_196591. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_223683. Notch-HLH transcription pathway.
REACT_226917. HATs acetylate histones.
REACT_235780. RNA Polymerase I Transcription Initiation.
REACT_268602. Pre-NOTCH Transcription and Translation.

Miscellaneous databases

ChiTaRSi Kat2b. mouse.
NextBioi 294272.
PROi Q9JHD1.
SOURCEi Search...

Gene expression databases

Bgeei Q9JHD1.
ExpressionAtlasi Q9JHD1. baseline and differential.
Genevestigatori Q9JHD1.

Family and domain databases

Gene3Di 1.20.920.10. 1 hit.
3.40.630.30. 1 hit.
InterProi IPR016181. Acyl_CoA_acyltransferase.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR000182. GNAT_dom.
IPR016376. Hist_acetylase_PCAF.
IPR009464. PCAF_N.
[Graphical view ]
Pfami PF13508. Acetyltransf_7. 1 hit.
PF00439. Bromodomain. 1 hit.
PF06466. PCAF_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF003048. Histone_acetylase_PCAF. 1 hit.
PRINTSi PR00503. BROMODOMAIN.
SMARTi SM00297. BROMO. 1 hit.
[Graphical view ]
SUPFAMi SSF47370. SSF47370. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEi PS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS51186. GNAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NR2C1.
  5. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NR2C1.

Entry informationi

Entry nameiKAT2B_MOUSE
AccessioniPrimary (citable) accession number: Q9JHD1
Secondary accession number(s): Q3U142, Q640M9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: November 26, 2014
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3