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Q92831

- KAT2B_HUMAN

UniProt

Q92831 - KAT2B_HUMAN

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Protein
Histone acetyltransferase KAT2B
Gene
KAT2B, PCAF
Organism
Homo sapiens (Human)
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. 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

GO - Molecular functioni

  1. acetyltransferase activity Source: UniProtKB
  2. cyclin-dependent protein serine/threonine kinase inhibitor activity Source: UniProtKB
  3. histone acetyltransferase activity Source: UniProtKB
  4. histone deacetylase binding Source: UniProtKB
  5. lysine N-acetyltransferase activity Source: UniProtKB
  6. protein binding Source: UniProtKB
  7. protein complex binding Source: UniProtKB
  8. protein kinase binding Source: UniProtKB
  9. transcription coactivator activity Source: UniProtKB
  10. transcription cofactor activity Source: UniProtKB
  11. transcription factor binding Source: UniProtKB

GO - Biological processi

  1. N-terminal peptidyl-lysine acetylation Source: UniProtKB
  2. Notch signaling pathway Source: Reactome
  3. cell cycle arrest Source: ProtInc
  4. cellular response to insulin stimulus Source: BHF-UCL
  5. chromatin organization Source: Reactome
  6. chromatin remodeling Source: UniProtKB
  7. gene expression Source: Reactome
  8. histone H3 acetylation Source: BHF-UCL
  9. internal peptidyl-lysine acetylation Source: UniProtKB
  10. negative regulation of cell proliferation Source: UniProtKB
  11. negative regulation of cyclin-dependent protein serine/threonine kinase activity Source: Ensembl
  12. peptidyl-lysine acetylation Source: BHF-UCL
  13. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  14. protein acetylation Source: ProtInc
  15. regulation of protein ADP-ribosylation Source: BHF-UCL
  16. rhythmic process Source: UniProtKB-KW
  17. transcription from RNA polymerase I promoter Source: Reactome
  18. transcription initiation from RNA polymerase I promoter Source: Reactome
  19. transcription initiation from RNA polymerase II promoter Source: Reactome
  20. 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

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_172610. 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)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:8638. KAT2B.

Subcellular locationi

Nucleus By similarity By similarity

GO - Cellular componenti

  1. A band Source: Ensembl
  2. Ada2/Gcn5/Ada3 transcription activator complex Source: BHF-UCL
  3. I band Source: Ensembl
  4. PCAF complex Source: UniProtKB
  5. actomyosin Source: Ensembl
  6. kinetochore Source: Ensembl
  7. nucleoplasm Source: Reactome
  8. nucleus 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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 832832Histone acetyltransferase KAT2B
PRO_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.
GenevestigatoriQ92831.

Organism-specific databases

HPAiCAB004526.

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.14 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P032553EBI-477430,EBI-2603114From a different organism.
P03255-23EBI-477430,EBI-6859460From a different organism.
BUB1BO6056613EBI-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. 136 interactions.
DIPiDIP-29778N.
IntActiQ92831. 35 interactions.
MINTiMINT-150079.
STRINGi9606.ENSP00000263754.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiQ92831.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini503 – 651149N-acetyltransferaseBy similarity
Add
BLAST
Domaini740 – 81071Bromo
Add
BLAST

Domaini

The bromodomain mediates binding to HIV-1 Tat.

Sequence similaritiesi

Contains 1 bromo domain.

Keywords - Domaini

Bromodomain

Phylogenomic databases

eggNOGiCOG5076.
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

MSEAGGAGPG GCGAGAGAGA GPGALPPQPA ALPPAPPQGS PCAAAAGGSG    50
ACGPATAVAA AGTAEGPGGG GSARIAVKKA QLRSAPRAKK LEKLGVYSAC 100
KAEESCKCNG WKNPNPSPTP PRADLQQIIV SLTESCRSCS HALAAHVSHL 150
ENVSEEEMNR LLGIVLDVEY LFTCVHKEED ADTKQVYFYL FKLLRKSILQ 200
RGKPVVEGSL EKKPPFEKPS IEQGVNNFVQ YKFSHLPAKE RQTIVELAKM 250
FLNRINYWHL EAPSQRRLRS PNDDISGYKE NYTRWLCYCN VPQFCDSLPR 300
YETTQVFGRT LLRSVFTVMR RQLLEQARQE KDKLPLEKRT LILTHFPKFL 350
SMLEEEVYSQ NSPIWDQDFL SASSRTSQLG IQTVINPPPV AGTISYNSTS 400
SSLEQPNAGS SSPACKASSG LEANPGEKRK MTDSHVLEEA KKPRVMGDIP 450
MELINEVMST ITDPAAMLGP ETNFLSAHSA RDEAARLEER RGVIEFHVVG 500
NSLNQKPNKK ILMWLVGLQN VFSHQLPRMP KEYITRLVFD PKHKTLALIK 550
DGRVIGGICF RMFPSQGFTE IVFCAVTSNE QVKGYGTHLM NHLKEYHIKH 600
DILNFLTYAD EYAIGYFKKQ GFSKEIKIPK TKYVGYIKDY EGATLMGCEL 650
NPRIPYTEFS VIIKKQKEII KKLIERKQAQ IRKVYPGLSC FKDGVRQIPI 700
ESIPGIRETG WKPSGKEKSK EPRDPDQLYS TLKSILQQVK SHQSAWPFME 750
PVKRTEAPGY YEVIRFPMDL KTMSERLKNR YYVSKKLFMA DLQRVFTNCK 800
EYNPPESEYY KCANILEKFF FSKIKEAGLI DK 832
Length:832
Mass (Da):93,013
Last modified:May 10, 2005 - v3
Checksum:i72F516E8BC00CC0C
GO

Natural variant

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti804 – 8052PP → AA in AAC50890. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Polymorphism databases

DMDMi83287776.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U57317 mRNA. Translation: AAC50890.2 .
BC060823 mRNA. Translation: AAH60823.1 .
BC070075 mRNA. Translation: AAH70075.1 .
CCDSi CCDS2634.1.
PIRi S71788.
RefSeqi NP_003875.3. NM_003884.4.
UniGenei Hs.533055.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CM0 X-ray 2.30 A/B 493-658 [» ]
1JM4 NMR - B 719-832 [» ]
1N72 NMR - A 719-832 [» ]
1WUG NMR - A 719-832 [» ]
1WUM NMR - A 719-832 [» ]
1ZS5 NMR - A 719-832 [» ]
2RNW NMR - A 719-832 [» ]
2RNX NMR - A 719-832 [» ]
3GG3 X-ray 2.25 A/B 715-831 [» ]
4NSQ X-ray 2.31 A/B/C/D 493-658 [» ]
ProteinModelPortali Q92831.
SMRi Q92831. Positions 493-653, 719-832.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114375. 136 interactions.
DIPi DIP-29778N.
IntActi Q92831. 35 interactions.
MINTi MINT-150079.
STRINGi 9606.ENSP00000263754.

Chemistry

BindingDBi Q92831.
ChEMBLi CHEMBL5500.
GuidetoPHARMACOLOGYi 2737.

PTM databases

PhosphoSitei Q92831.

Polymorphism databases

DMDMi 83287776.

2D gel databases

REPRODUCTION-2DPAGE Q92831.

Proteomic databases

MaxQBi Q92831.
PaxDbi Q92831.
PRIDEi Q92831.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000263754 ; ENSP00000263754 ; ENSG00000114166 .
GeneIDi 8850.
KEGGi hsa:8850.
UCSCi uc003cbq.3. human.

Organism-specific databases

CTDi 8850.
GeneCardsi GC03P020081.
HGNCi HGNC:8638. KAT2B.
HPAi CAB004526.
MIMi 602303. gene.
neXtProti NX_Q92831.
PharmGKBi PA162392705.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5076.
HOGENOMi HOG000007151.
InParanoidi Q92831.
KOi K06062.
OMAi KIMMWLV.
OrthoDBi EOG7ZKS9B.
PhylomeDBi Q92831.
TreeFami TF105399.

Enzyme and pathway databases

Reactomei REACT_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_172610. HATs acetylate histones.
REACT_953. RNA Polymerase I Transcription Initiation.

Miscellaneous databases

ChiTaRSi KAT2B. human.
EvolutionaryTracei Q92831.
GeneWikii PCAF.
GenomeRNAii 8850.
NextBioi 33221.
PROi Q92831.
SOURCEi Search...

Gene expression databases

Bgeei Q92831.
CleanExi HS_KAT2B.
Genevestigatori Q92831.

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. "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. "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.
  18. "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.
  19. "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.
  20. "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.
  21. 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: September 3, 2014
This is version 157 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

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