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Protein

Histone acetyltransferase KAT2B

Gene

KAT2B

Organism
Homo sapiens (Human)
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. Inhibits cell-cycle progression and counteracts the mitogenic activity of the adenoviral oncoprotein E1A. In case of HIV-1 infection, it is recruited by the viral protein Tat. Regulates Tat's transactivating activity and may help inducing chromatin remodeling of proviral genes. Acts as a circadian transcriptional coactivator which enhances the activity of the circadian transcriptional activators: NPAS2-ARNTL/BMAL1 and CLOCK-ARNTL/BMAL1 heterodimers.5 Publications

Catalytic activityi

Acetyl-CoA + [histone] = CoA + acetyl-[histone].1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei570 – 5701Proton donor/acceptor1 Publication

GO - Molecular functioni

  • acetyltransferase activity Source: UniProtKB
  • cyclin-dependent protein serine/threonine kinase inhibitor activity Source: UniProtKB
  • histone acetyltransferase activity Source: UniProtKB
  • histone deacetylase binding Source: UniProtKB
  • lysine N-acetyltransferase activity, acting on acetyl phosphate as donor Source: UniProtKB
  • protein complex binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • transcription coactivator activity Source: UniProtKB
  • transcription cofactor activity Source: UniProtKB
  • transcription factor binding Source: UniProtKB

GO - Biological processi

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

Keywords - Molecular functioni

Activator, Acyltransferase, Transferase

Keywords - Biological processi

Biological rhythms, Cell cycle, Host-virus interaction, Transcription, Transcription regulation

Enzyme and pathway databases

BRENDAi2.3.1.48. 2681.
ReactomeiREACT_118568. Pre-NOTCH Transcription and Translation.
REACT_118713. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_14835. Notch-HLH transcription pathway.
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_264245. HATs acetylate histones.
REACT_953. 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
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:8638. KAT2B.

Subcellular locationi

GO - Cellular componenti

  • A band Source: Ensembl
  • actomyosin Source: Ensembl
  • Ada2/Gcn5/Ada3 transcription activator complex Source: BHF-UCL
  • I band Source: Ensembl
  • kinetochore Source: Ensembl
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • PCAF complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi752 – 7521V → A: Reduced acetyl-lysine binding. 1 Publication
Mutagenesisi760 – 7601Y → A: Reduced acetyl-lysine binding. 1 Publication
Mutagenesisi802 – 8021Y → A: Reduced acetyl-lysine binding. 1 Publication
Mutagenesisi809 – 8091Y → A: Complete loss of acetyl-lysine binding. 1 Publication

Organism-specific databases

PharmGKBiPA162392705.

Polymorphism and mutation databases

BioMutaiKAT2B.
DMDMi83287776.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 832832Histone acetyltransferase KAT2BPRO_0000211208Add
BLAST

Proteomic databases

MaxQBiQ92831.
PaxDbiQ92831.
PRIDEiQ92831.

2D gel databases

REPRODUCTION-2DPAGEQ92831.

PTM databases

PhosphoSiteiQ92831.

Expressioni

Tissue specificityi

Ubiquitously expressed but most abundant in heart and skeletal muscle.1 Publication

Gene expression databases

BgeeiQ92831.
CleanExiHS_KAT2B.
GenevisibleiQ92831. HS.

Organism-specific databases

HPAiCAB004526.
HPA055839.

Interactioni

Subunit structurei

Interacts with SIRT1. Interacts (unsumoylated form) with NR2C1; the interaction promotes transactivation activity (By similarity). Interacts with EP300, CREBBP and DDX17. Interacts with NCOA1 and NCOA3. Component of a large chromatin remodeling complex, at least composed of MYSM1, KAT2B/PCAF, RBM10 and KIF11/TRIP5. Interacts with NR2C2 (hypophosphorylated and unsumoylated form); the interaction promotes the transactivation activity of NR2C2. Binds to HTLV-1 Tax. Interacts with and acetylates HIV-1 Tat. 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 E2F1; the interaction acetylates E2F1 augmenting its DNA-binding and transcriptional activity. Interacts with NPAS2, ARNTL/BMAL1 and CLOCK. Interacts with BCAS3. Interacts with CEBPB (PubMed:17301242).By similarity17 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P032553EBI-477430,EBI-2603114From a different organism.
P03255-23EBI-477430,EBI-6859460From a different organism.
BUB1BO6056614EBI-477430,EBI-1001438
CREBBPQ927934EBI-477430,EBI-81215
E7P031295EBI-477430,EBI-866453From a different organism.
EHMT2Q96KQ73EBI-477430,EBI-744366
EP300Q094722EBI-477430,EBI-447295
HIF1AQ166652EBI-477430,EBI-447269
His3:CG33854P022992EBI-477430,EBI-522090From a different organism.
His4:CG33909P840402EBI-477430,EBI-185028From a different organism.
SIRT1Q96EB63EBI-477430,EBI-1802965
SIRT2Q8IXJ64EBI-477430,EBI-477232
TAF9Q165943EBI-477430,EBI-712521
Tp63O88898-23EBI-477430,EBI-2338228From a different organism.
TWIST1Q156722EBI-477430,EBI-1797287
USF1P224155EBI-477430,EBI-1054489

Protein-protein interaction databases

BioGridi114375. 174 interactions.
DIPiDIP-29778N.
IntActiQ92831. 35 interactions.
MINTiMINT-150079.
STRINGi9606.ENSP00000263754.

Structurei

Secondary structure

1
832
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi494 – 4996Combined sources
Beta strandi503 – 5053Combined sources
Helixi509 – 52517Combined sources
Helixi531 – 5388Combined sources
Beta strandi543 – 5508Combined sources
Beta strandi553 – 56311Combined sources
Turni564 – 5674Combined sources
Beta strandi568 – 5769Combined sources
Helixi578 – 5803Combined sources
Beta strandi582 – 5843Combined sources
Helixi585 – 59915Combined sources
Beta strandi604 – 6096Combined sources
Turni611 – 6133Combined sources
Helixi614 – 6185Combined sources
Turni619 – 6213Combined sources
Beta strandi623 – 6253Combined sources
Helixi630 – 6334Combined sources
Beta strandi644 – 6496Combined sources
Helixi727 – 74115Combined sources
Beta strandi742 – 7443Combined sources
Helixi746 – 7483Combined sources
Helixi754 – 7563Combined sources
Beta strandi757 – 7593Combined sources
Helixi760 – 7634Combined sources
Beta strandi764 – 7663Combined sources
Helixi770 – 7789Combined sources
Helixi785 – 80218Combined sources
Beta strandi805 – 8073Combined sources
Helixi808 – 82619Combined sources
Beta strandi828 – 8303Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CM0X-ray2.30A/B493-658[»]
1JM4NMR-B719-832[»]
1N72NMR-A719-832[»]
1WUGNMR-A719-832[»]
1WUMNMR-A719-832[»]
1ZS5NMR-A719-832[»]
2RNWNMR-A719-832[»]
2RNXNMR-A719-832[»]
3GG3X-ray2.25A/B715-831[»]
4NSQX-ray2.31A/B/C/D493-658[»]
ProteinModelPortaliQ92831.
SMRiQ92831. Positions 493-653, 719-832.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92831.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini503 – 651149N-acetyltransferasePROSITE-ProRule annotationBy similarityAdd
BLAST
Domaini740 – 81071BromoPROSITE-ProRule annotationCuratedAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni574 – 5763Acetyl-CoA binding1 Publication
Regioni581 – 5877Acetyl-CoA binding1 Publication
Regioni612 – 6154Acetyl-CoA binding1 Publication

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.
InParanoidiQ92831.
KOiK06062.
OMAiKIMMWLV.
OrthoDBiEOG7ZKS9B.
PhylomeDBiQ92831.
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.

Q92831-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEAGGAGPG GCGAGAGAGA GPGALPPQPA ALPPAPPQGS PCAAAAGGSG
60 70 80 90 100
ACGPATAVAA AGTAEGPGGG GSARIAVKKA QLRSAPRAKK LEKLGVYSAC
110 120 130 140 150
KAEESCKCNG WKNPNPSPTP PRADLQQIIV SLTESCRSCS HALAAHVSHL
160 170 180 190 200
ENVSEEEMNR LLGIVLDVEY LFTCVHKEED ADTKQVYFYL FKLLRKSILQ
210 220 230 240 250
RGKPVVEGSL EKKPPFEKPS IEQGVNNFVQ YKFSHLPAKE RQTIVELAKM
260 270 280 290 300
FLNRINYWHL EAPSQRRLRS PNDDISGYKE NYTRWLCYCN VPQFCDSLPR
310 320 330 340 350
YETTQVFGRT LLRSVFTVMR RQLLEQARQE KDKLPLEKRT LILTHFPKFL
360 370 380 390 400
SMLEEEVYSQ NSPIWDQDFL SASSRTSQLG IQTVINPPPV AGTISYNSTS
410 420 430 440 450
SSLEQPNAGS SSPACKASSG LEANPGEKRK MTDSHVLEEA KKPRVMGDIP
460 470 480 490 500
MELINEVMST ITDPAAMLGP ETNFLSAHSA RDEAARLEER RGVIEFHVVG
510 520 530 540 550
NSLNQKPNKK ILMWLVGLQN VFSHQLPRMP KEYITRLVFD PKHKTLALIK
560 570 580 590 600
DGRVIGGICF RMFPSQGFTE IVFCAVTSNE QVKGYGTHLM NHLKEYHIKH
610 620 630 640 650
DILNFLTYAD EYAIGYFKKQ GFSKEIKIPK TKYVGYIKDY EGATLMGCEL
660 670 680 690 700
NPRIPYTEFS VIIKKQKEII KKLIERKQAQ IRKVYPGLSC FKDGVRQIPI
710 720 730 740 750
ESIPGIRETG WKPSGKEKSK EPRDPDQLYS TLKSILQQVK SHQSAWPFME
760 770 780 790 800
PVKRTEAPGY YEVIRFPMDL KTMSERLKNR YYVSKKLFMA DLQRVFTNCK
810 820 830
EYNPPESEYY KCANILEKFF FSKIKEAGLI DK
Length:832
Mass (Da):93,013
Last modified:May 10, 2005 - v3
Checksum:i72F516E8BC00CC0C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti804 – 8052PP → AA in AAC50890 (PubMed:8684459).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti386 – 3861N → S.
Corresponds to variant rs17006625 [ dbSNP | Ensembl ].
VAR_034372

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U57317 mRNA. Translation: AAC50890.2.
BC060823 mRNA. Translation: AAH60823.1.
BC070075 mRNA. Translation: AAH70075.1.
CCDSiCCDS2634.1.
PIRiS71788.
RefSeqiNP_003875.3. NM_003884.4.
UniGeneiHs.533055.

Genome annotation databases

EnsembliENST00000263754; ENSP00000263754; ENSG00000114166.
GeneIDi8850.
KEGGihsa:8850.
UCSCiuc003cbq.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U57317 mRNA. Translation: AAC50890.2.
BC060823 mRNA. Translation: AAH60823.1.
BC070075 mRNA. Translation: AAH70075.1.
CCDSiCCDS2634.1.
PIRiS71788.
RefSeqiNP_003875.3. NM_003884.4.
UniGeneiHs.533055.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CM0X-ray2.30A/B493-658[»]
1JM4NMR-B719-832[»]
1N72NMR-A719-832[»]
1WUGNMR-A719-832[»]
1WUMNMR-A719-832[»]
1ZS5NMR-A719-832[»]
2RNWNMR-A719-832[»]
2RNXNMR-A719-832[»]
3GG3X-ray2.25A/B715-831[»]
4NSQX-ray2.31A/B/C/D493-658[»]
ProteinModelPortaliQ92831.
SMRiQ92831. Positions 493-653, 719-832.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114375. 174 interactions.
DIPiDIP-29778N.
IntActiQ92831. 35 interactions.
MINTiMINT-150079.
STRINGi9606.ENSP00000263754.

Chemistry

BindingDBiQ92831.
ChEMBLiCHEMBL5500.
GuidetoPHARMACOLOGYi2737.

PTM databases

PhosphoSiteiQ92831.

Polymorphism and mutation databases

BioMutaiKAT2B.
DMDMi83287776.

2D gel databases

REPRODUCTION-2DPAGEQ92831.

Proteomic databases

MaxQBiQ92831.
PaxDbiQ92831.
PRIDEiQ92831.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263754; ENSP00000263754; ENSG00000114166.
GeneIDi8850.
KEGGihsa:8850.
UCSCiuc003cbq.3. human.

Organism-specific databases

CTDi8850.
GeneCardsiGC03P020081.
HGNCiHGNC:8638. KAT2B.
HPAiCAB004526.
HPA055839.
MIMi602303. gene.
neXtProtiNX_Q92831.
PharmGKBiPA162392705.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5076.
GeneTreeiENSGT00760000119099.
HOGENOMiHOG000007151.
InParanoidiQ92831.
KOiK06062.
OMAiKIMMWLV.
OrthoDBiEOG7ZKS9B.
PhylomeDBiQ92831.
TreeFamiTF105399.

Enzyme and pathway databases

BRENDAi2.3.1.48. 2681.
ReactomeiREACT_118568. Pre-NOTCH Transcription and Translation.
REACT_118713. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_14835. Notch-HLH transcription pathway.
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_264245. HATs acetylate histones.
REACT_953. RNA Polymerase I Transcription Initiation.

Miscellaneous databases

ChiTaRSiKAT2B. human.
EvolutionaryTraceiQ92831.
GeneWikiiPCAF.
GenomeRNAii8850.
NextBioi33221.
PROiQ92831.
SOURCEiSearch...

Gene expression databases

BgeeiQ92831.
CleanExiHS_KAT2B.
GenevisibleiQ92831. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A."
    Yang X.-J., Ogryzko V.V., Nishikawa J., Howard B.H., Nakatani Y.
    Nature 382:319-324(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, TISSUE SPECIFICITY, INTERACTION WITH EP300 AND CREBBP.
    Tissue: Liver.
  2. Nakatani Y.
    Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
    Tissue: Liver.
  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].
  4. "The transcriptional coactivators p300 and CBP are histone acetyltransferases."
    Ogryzko V.V., Schiltz R.L., Russanova V., Howard B.H., Nakatani Y.
    Cell 87:953-959(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME ACTIVITY.
  5. "TRAM-1, a novel 160-kDa thyroid hormone receptor activator molecule, exhibits distinct properties from steroid receptor coactivator-1."
    Takeshita A., Cardona G.R., Koibuchi N., Suen C.-S., Chin W.W.
    J. Biol. Chem. 272:27629-27634(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NCOA3.
  6. Cited for: INTERACTION WITH NCOA1.
  7. "Acetylation and modulation of erythroid Krueppel-like factor (EKLF) activity by interaction with histone acetyltransferases."
    Zhang W., Bieker J.J.
    Proc. Natl. Acad. Sci. U.S.A. 95:9855-9860(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KLF1, FUNCTION.
  8. Cited for: INTERACTION WITH E2F1, FUNCTION.
  9. "p300 and p300/cAMP-responsive element-binding protein associated factor interact with human T-cell lymphotropic virus type-1 Tax in a multi-histone acetyltransferase/activator-enhancer complex."
    Harrod R., Kuo Y.-L., Tang Y., Yao Y., Vassilev A., Nakatani Y., Giam C.-Z.
    J. Biol. Chem. 275:11852-11857(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HTLV-1 TAX.
  10. "Interaction of EVI1 with cAMP-responsive element-binding protein-binding protein (CBP) and p300/CBP-associated factor (P/CAF) results in reversible acetylation of EVI1 and in co-localization in nuclear speckles."
    Chakraborty S., Senyuk V., Sitailo S., Chi Y., Nucifora G.
    J. Biol. Chem. 276:44936-44943(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MECOM.
  11. "Differential acetylation of Tat coordinates its interaction with the co-activators cyclin T1 and PCAF."
    Bres V., Tagami H., Peloponese J.-M., Loret E., Jeang K.-T., Nakatani Y., Emiliani S., Benkirane M., Kiernan R.E.
    EMBO J. 21:6811-6819(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIV-1 TAT.
  12. "Histone acetyltransferase-dependent chromatin remodeling and the vascular clock."
    Curtis A.M., Seo S.B., Westgate E.J., Rudic R.D., Smyth E.M., Chakravarti D., FitzGerald G.A., McNamara P.
    J. Biol. Chem. 279:7091-7097(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NPAS2; ARNTL/BMAL1 AND CLOCK.
  13. "Site-specific acetylation of the fetal globin activator NF-E4 prevents its ubiquitination and regulates its interaction with the histone deacetylase, HDAC1."
    Zhao Q., Cumming H., Cerruti L., Cunningham J.M., Jane S.M.
    J. Biol. Chem. 279:41477-41486(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NFE4.
  14. "The transforming acidic coiled coil proteins interact with nuclear histone acetyltransferases."
    Gangisetty O., Lauffart B., Sondarva G.V., Chelsea D.M., Still I.H.
    Oncogene 23:2559-2563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TACC1; TACC2 AND TACC3.
  15. "Modulation of testicular receptor 4 activity by mitogen-activated protein kinase-mediated phosphorylation."
    Huq M.D., Gupta P., Tsai N.P., Wei L.N.
    Mol. Cell. Proteomics 5:2072-2082(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NR2C2.
  16. "Concerted activation of the Mdm2 promoter by p72 RNA helicase and the coactivators p300 and P/CAF."
    Shin S., Janknecht R.
    J. Cell. Biochem. 101:1252-1265(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DDX17.
  17. "Glucocorticoid-stimulated preadipocyte differentiation is mediated through acetylation of C/EBPbeta by GCN5."
    Wiper-Bergeron N., Salem H.A., Tomlinson J.J., Wu D., Hache R.J.
    Proc. Natl. Acad. Sci. U.S.A. 104:2703-2708(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CEBPB.
  18. "A histone H2A deubiquitinase complex coordinating histone acetylation and H1 dissociation in transcriptional regulation."
    Zhu P., Zhou W., Wang J., Puc J., Ohgi K.A., Erdjument-Bromage H., Tempst P., Glass C.K., Rosenfeld M.G.
    Mol. Cell 27:609-621(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A LARGE CHROMATIN REMODELING COMPLEX.
  19. "Estrogen induces expression of BCAS3, a novel estrogen receptor-alpha coactivator, through proline-, glutamic acid-, and leucine-rich protein-1 (PELP1)."
    Gururaj A.E., Peng S., Vadlamudi R.K., Kumar R.
    Mol. Endocrinol. 21:1847-1860(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BCAS3.
  20. "Acetylation stabilizes ATP-citrate lyase to promote lipid biosynthesis and tumor growth."
    Lin R., Tao R., Gao X., Li T., Zhou X., Guan K.L., Xiong Y., Lei Q.Y.
    Mol. Cell 51:506-518(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  21. "Crystal structure of the histone acetyltransferase domain of the human PCAF transcriptional regulator bound to coenzyme A."
    Clements A., Rojas J.R., Trievel R.C., Wang L., Berger S.L., Marmorstein R.
    EMBO J. 18:3521-3532(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 493-658 IN COMPLEX WITH COENZYME A, ACTIVE SITE.
  22. "Structure and ligand of a histone acetyltransferase bromodomain."
    Dhalluin C., Carlson J.E., Zeng L., He C., Aggarwal A.K., Zhou M.-M.
    Nature 399:491-496(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 715-832, MUTAGENESIS OF VAL-752; TYR-760; TYR-802 AND TYR-809.
    Tissue: Liver.
  23. "Structural basis of lysine-acetylated HIV-1 Tat recognition by PCAF bromodomain."
    Mujtaba S., He Y., Zeng L., Farooq A., Carlson J.E., Ott M., Verdin E., Zhou M.-M.
    Mol. Cell 9:575-586(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 719-832 IN COMPLEX WITH HIV-1 TAT.
  24. Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 715-831.

Entry informationi

Entry nameiKAT2B_HUMAN
AccessioniPrimary (citable) accession number: Q92831
Secondary accession number(s): Q6NSK1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: May 10, 2005
Last modified: June 24, 2015
This is version 167 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.