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Protein

Histone acetyltransferase KAT2B

Gene

Kat2b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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, 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.By similarity

Catalytic activityi

Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N6-acetyl-L-lysine.By similarity

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

Keywordsi

Molecular functionActivator, Acyltransferase, Transferase
Biological processBiological rhythms, Cell cycle, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-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-8936459. RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
R-MMU-8941856. RUNX3 regulates NOTCH signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase KAT2B (EC:2.3.1.48By similarity)
Alternative name(s):
Histone acetyltransferase PCAF1 Publication
Short name:
Histone acetylase PCAF1 Publication
Lysine acetyltransferase 2BCurated
P300/CBP-associated factor1 Publication
Short name:
P/CAF1 Publication
Gene namesi
Name:Kat2bImported
Synonyms:Pcaf1 Publication
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1343094. Kat2b.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Disruption phenotypei

No visible phenotype (PubMed:11017084).1 Publication

PTM / Processingi

Molecule processing

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

Proteomic databases

MaxQBiQ9JHD1.
PaxDbiQ9JHD1.
PRIDEiQ9JHD1.

PTM databases

iPTMnetiQ9JHD1.
PhosphoSitePlusiQ9JHD1.

Expressioni

Developmental stagei

Expression is low during embryogenesis and becomes up-regulated in some adult tissues including heart and skeletal muscle.1 Publication

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). Interacts with TBX5 (By similarity). Interacts with PLK4 (By similarity).By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Nr2c1Q505F13EBI-2325611,EBI-15617004

GO - Molecular functioni

Protein-protein interaction databases

BioGridi202042. 20 interactors.
DIPiDIP-29281N.
IntActiQ9JHD1. 3 interactors.
MINTiQ9JHD1.
STRINGi10090.ENSMUSP00000000724.

Structurei

Secondary structure

1813
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi707 – 722Combined sources16
Helixi727 – 729Combined sources3
Turni735 – 737Combined sources3
Helixi741 – 744Combined sources4
Helixi751 – 759Combined sources9
Helixi766 – 783Combined sources18
Helixi789 – 807Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5ML0X-ray1.64A705-813[»]
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

Sequence similaritiesi

Keywords - Domaini

Bromodomain

Phylogenomic databases

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

Family and domain databases

Gene3Di1.20.920.10. 1 hit.
InterProiView protein in InterPro
IPR016181. Acyl_CoA_acyltransferase.
IPR001487. Bromodomain.
IPR036427. Bromodomain-like_sf.
IPR018359. Bromodomain_CS.
IPR037800. GCN5.
IPR016376. GCN5/PCAF.
IPR000182. GNAT_dom.
IPR009464. PCAF_N.
PANTHERiPTHR22880:SF124. PTHR22880:SF124. 1 hit.
PfamiView protein in Pfam
PF00583. Acetyltransf_1. 1 hit.
PF00439. Bromodomain. 1 hit.
PF06466. PCAF_N. 1 hit.
PIRSFiPIRSF003048. Histone_acetylase_PCAF. 1 hit.
PRINTSiPR00503. BROMODOMAIN.
SMARTiView protein in SMART
SM00297. BROMO. 1 hit.
SUPFAMiSSF47370. SSF47370. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEiView protein in PROSITE
PS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS51186. GNAT. 1 hit.

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.

Similar proteinsi

Entry informationi

Entry nameiKAT2B_MOUSE
AccessioniPrimary (citable) accession number: Q9JHD1
Secondary accession number(s): Q3U142, Q640M9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: March 28, 2018
This is version 136 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome