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Protein

Histone acetyltransferase KAT2B

Gene

Kat2b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei551Proton donor/acceptorBy similarity1

GO - Molecular functioni

  • acetyltransferase activity Source: Reactome
  • chromatin binding Source: UniProtKB
  • cyclin-dependent protein serine/threonine kinase inhibitor activity Source: UniProtKB
  • histone acetyltransferase activity Source: MGI
  • histone deacetylase binding Source: MGI
  • lysine N-acetyltransferase activity, acting on acetyl phosphate as donor Source: UniProtKB
  • protein complex binding Source: MGI
  • protein kinase binding Source: UniProtKB
  • RNA polymerase II regulatory region sequence-specific DNA binding Source: MGI
  • transcription coactivator activity Source: MGI
  • transcription cofactor activity Source: MGI
  • transcription factor binding Source: MGI

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • cellular response to insulin stimulus Source: MGI
  • chromatin remodeling Source: UniProtKB
  • histone acetylation Source: MGI
  • histone H3 acetylation Source: MGI
  • histone H3-K9 acetylation Source: MGI
  • internal peptidyl-lysine acetylation Source: UniProtKB
  • negative regulation of cell proliferation Source: MGI
  • negative regulation of cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB
  • Notch signaling pathway Source: Reactome
  • N-terminal peptidyl-lysine acetylation Source: MGI
  • peptidyl-lysine acetylation Source: MGI
  • positive regulation of gluconeogenesis by positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • positive regulation of transcription, DNA-templated Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • protein acetylation Source: MGI
  • regulation of protein ADP-ribosylation Source: MGI
  • regulation of transcription, DNA-templated Source: MGI
  • rhythmic process Source: UniProtKB-KW
  • transcription initiation from RNA polymerase I promoter Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Activator, Acyltransferase, Transferase

Keywords - Biological processi

Biological rhythms, Cell cycle, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-MMU-1912408. Pre-NOTCH Transcription and Translation.
R-MMU-2032785. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
R-MMU-2122947. NOTCH1 Intracellular Domain Regulates Transcription.
R-MMU-350054. Notch-HLH transcription pathway.
R-MMU-5250924. B-WICH complex positively regulates rRNA expression.
R-MMU-5689901. Metalloprotease DUBs.
R-MMU-73762. RNA Polymerase I Transcription Initiation.

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
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1343094. Kat2b.

Subcellular locationi

GO - Cellular componenti

  • A band Source: MGI
  • actomyosin Source: MGI
  • Ada2/Gcn5/Ada3 transcription activator complex Source: MGI
  • histone acetyltransferase complex Source: MGI
  • I band Source: MGI
  • kinetochore Source: MGI
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003229861 – 813Histone acetyltransferase KAT2BAdd BLAST813

Proteomic databases

PaxDbiQ9JHD1.
PRIDEiQ9JHD1.

PTM databases

iPTMnetiQ9JHD1.
PhosphoSitePlusiQ9JHD1.

Expressioni

Gene expression databases

BgeeiENSMUSG00000000708.
ExpressionAtlasiQ9JHD1. baseline and differential.
GenevisibleiQ9JHD1. MM.

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. Interacts with CEBPB (By similarity). Interacts with NR4A3 (PubMed:12709428).By similarity3 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi202042. 20 interactors.
DIPiDIP-29281N.
IntActiQ9JHD1. 1 interactor.
MINTiMINT-7984938.
STRINGi10090.ENSMUSP00000000724.

Structurei

3D structure databases

ProteinModelPortaliQ9JHD1.
SMRiQ9JHD1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini484 – 632N-acetyltransferasePROSITE-ProRule annotationAdd BLAST149
Domaini721 – 791BromoPROSITE-ProRule annotationAdd BLAST71

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni555 – 557Acetyl-CoA bindingBy similarity3
Regioni562 – 568Acetyl-CoA bindingBy similarity7
Regioni593 – 596Acetyl-CoA bindingBy similarity4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi48 – 53Poly-Gly6

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

eggNOGiKOG1472. Eukaryota.
COG5076. LUCA.
GeneTreeiENSGT00760000119099.
HOGENOMiHOG000007151.
InParanoidiQ9JHD1.
KOiK06062.
OMAiHIAHLDN.
OrthoDBiEOG091G03ZO.
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]
PfamiPF00583. Acetyltransf_1. 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)DescriptionActionsGraphical viewLength
Sequence conflicti293 – 294LL → FV in AAF70498 (PubMed:9742083).Curated2
Sequence conflicti319E → G in BAE33658 (PubMed:16141072).Curated1
Sequence conflicti459H → L in AAF70498 (PubMed:9742083).Curated1
Sequence conflicti548G → A in AAF70498 (PubMed:9742083).Curated1
Sequence conflicti554F → L in AAF70498 (PubMed:9742083).Curated1

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.
CCDSiCCDS28880.1.
RefSeqiNP_064389.2. NM_020005.4.
UniGeneiMm.255025.

3D structure databases

ProteinModelPortaliQ9JHD1.
SMRiQ9JHD1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202042. 20 interactors.
DIPiDIP-29281N.
IntActiQ9JHD1. 1 interactor.
MINTiMINT-7984938.
STRINGi10090.ENSMUSP00000000724.

PTM databases

iPTMnetiQ9JHD1.
PhosphoSitePlusiQ9JHD1.

Proteomic databases

PaxDbiQ9JHD1.
PRIDEiQ9JHD1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi8850.
MGIiMGI:1343094. Kat2b.

Phylogenomic databases

eggNOGiKOG1472. Eukaryota.
COG5076. LUCA.
GeneTreeiENSGT00760000119099.
HOGENOMiHOG000007151.
InParanoidiQ9JHD1.
KOiK06062.
OMAiHIAHLDN.
OrthoDBiEOG091G03ZO.
PhylomeDBiQ9JHD1.
TreeFamiTF105399.

Enzyme and pathway databases

ReactomeiR-MMU-1912408. Pre-NOTCH Transcription and Translation.
R-MMU-2032785. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
R-MMU-2122947. NOTCH1 Intracellular Domain Regulates Transcription.
R-MMU-350054. Notch-HLH transcription pathway.
R-MMU-5250924. B-WICH complex positively regulates rRNA expression.
R-MMU-5689901. Metalloprotease DUBs.
R-MMU-73762. RNA Polymerase I Transcription Initiation.

Miscellaneous databases

ChiTaRSiKat2b. mouse.
PROiQ9JHD1.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000000708.
ExpressionAtlasiQ9JHD1. baseline and differential.
GenevisibleiQ9JHD1. MM.

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]
PfamiPF00583. Acetyltransf_1. 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]
ProtoNetiSearch...

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 30, 2016
This is version 124 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.