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Q92830

- KAT2A_HUMAN

UniProt

Q92830 - KAT2A_HUMAN

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Protein

Histone acetyltransferase KAT2A

Gene

KAT2A

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. Acetylation of histones gives a specific tag for epigenetic transcription activation. Has significant histone acetyltransferase activity with core histones, but not with nucleosome core particles. 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. Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei575 – 5751Proton donor/acceptor1 Publication

GO - Molecular functioni

  1. chromatin binding Source: Ensembl
  2. H3 histone acetyltransferase activity Source: BHF-UCL
  3. histone acetyltransferase activity Source: UniProtKB
  4. histone acetyltransferase activity (H4-K12 specific) Source: Ensembl
  5. histone deacetylase binding Source: UniProtKB
  6. transcription coactivator activity Source: UniProtKB

GO - Biological processi

  1. cell proliferation Source: Ensembl
  2. chromatin organization Source: Reactome
  3. chromatin remodeling Source: ProtInc
  4. histone deubiquitination Source: UniProtKB
  5. histone H3 acetylation Source: UniProtKB
  6. histone H3-K14 acetylation Source: Ensembl
  7. in utero embryonic development Source: Ensembl
  8. metencephalon development Source: Ensembl
  9. midbrain development Source: Ensembl
  10. multicellular organism growth Source: Ensembl
  11. neural tube closure Source: Ensembl
  12. positive regulation of gluconeogenesis Source: Ensembl
  13. regulation of protein stability Source: MGI
  14. regulation of transcription from RNA polymerase II promoter Source: ProtInc
  15. somitogenesis Source: Ensembl
  16. telencephalon development Source: Ensembl
  17. transcription from RNA polymerase II promoter Source: ProtInc
  18. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Host-virus interaction, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_118568. Pre-NOTCH Transcription and Translation.
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.
SignaLinkiQ92830.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase KAT2A (EC:2.3.1.48)
Alternative name(s):
General control of amino acid synthesis protein 5-like 2
Histone acetyltransferase GCN5
Short name:
HsGCN5
Lysine acetyltransferase 2A
STAF97
Gene namesi
Name:KAT2A
Synonyms:GCN5, GCN5L2, HGCN5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:4201. KAT2A.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. Ada2/Gcn5/Ada3 transcription activator complex Source: BHF-UCL
  2. extracellular space Source: UniProt
  3. mitotic spindle Source: Ensembl
  4. nucleoplasm Source: Reactome
  5. STAGA complex Source: UniProtKB
  6. transcription factor TFTC complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162392664.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 837836Histone acetyltransferase KAT2APRO_0000211202Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ92830.
PaxDbiQ92830.
PRIDEiQ92830.

PTM databases

PhosphoSiteiQ92830.

Expressioni

Tissue specificityi

Expressed in all tissues tested, with most abundant expression in ovary.

Gene expression databases

BgeeiQ92830.
CleanExiHS_KAT2A.
ExpressionAtlasiQ92830. baseline and differential.
GenevestigatoriQ92830.

Organism-specific databases

HPAiHPA048958.

Interactioni

Subunit structurei

Interacts with EP300, CREBBP and ADA2. Component of the TFTC-HAT complex, at least composed of TAF5L, TAF6L, TAF3, TADA3L, SUPT3H/SPT3, TAF2/TAFII150, TAF4/TAFII135, TAF5/TAFII100, KAT2A/GCN5L2, TAF10 and TRRAP. Interacts with TRRAP. Component of the STAGA transcription coactivator-HAT complex, at least composed of SUPT3H, KAT2A, SUPT7L, TAF5L, TAF6L, TADA3L, TAD1L, TAF10, TAF12, TRRAP and TAF9. The STAGA core complex is associated with a subcomplex required for histone deubiquitination composed of ATXN7L3, ENY2 and USP22. Interacts with and acetylates HIV-1 Tat. Component of the ADA2A-containing complex (ATAC), composed of CSRP2BP, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1. In the complex, it probably interacts directly with CSRP2BP, MBIP and WDR5. Interacts with PML (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
WDHD1O757175EBI-477622,EBI-3951691
ZZZ3Q8IYH52EBI-477622,EBI-2795524

Protein-protein interaction databases

BioGridi108918. 105 interactions.
DIPiDIP-28146N.
IntActiQ92830. 36 interactions.
MINTiMINT-199927.
STRINGi9606.ENSP00000225916.

Structurei

Secondary structure

1
837
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi498 – 5047
Helixi514 – 53017
Helixi536 – 5438
Beta strandi549 – 5557
Beta strandi558 – 56811
Turni569 – 5724
Beta strandi573 – 5819
Helixi583 – 5853
Beta strandi587 – 5893
Helixi590 – 60415
Beta strandi609 – 6146
Helixi616 – 6183
Helixi619 – 6246
Beta strandi627 – 6293
Helixi635 – 6384
Turni639 – 6413
Beta strandi649 – 6546
Helixi730 – 74617
Helixi748 – 7536
Turni759 – 7613
Helixi765 – 7684
Helixi775 – 7839
Helixi790 – 80718
Helixi813 – 83119

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F68NMR-A730-832[»]
1Z4RX-ray1.74A497-662[»]
3D7CX-ray2.06A/B729-837[»]
ProteinModelPortaliQ92830.
SMRiQ92830. Positions 497-658, 730-835.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92830.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini503 – 656154N-acetyltransferasePROSITE-ProRule annotationAdd
BLAST
Domaini745 – 81571BromoPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni579 – 5813Acetyl-CoA binding1 Publication
Regioni586 – 5927Acetyl-CoA binding1 Publication
Regioni617 – 6204Acetyl-CoA binding1 Publication

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.
InParanoidiQ92830.
KOiK06062.
OMAiNSPIWES.
PhylomeDBiQ92830.
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]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q92830-1) [UniParc]FASTAAdd to Basket

Also known as: GCN5-L

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAEPSQAPTP APAAQPRPLQ SPAPAPTPTP APSPASAPIP TPTPAPAPAP
60 70 80 90 100
AAAPAGSTGT GGPGVGSGGA GSGGDPARPG LSQQQRASQR KAQVRGLPRA
110 120 130 140 150
KKLEKLGVFS ACKANETCKC NGWKNPKPPT APRMDLQQPA ANLSELCRSC
160 170 180 190 200
EHPLADHVSH LENVSEDEIN RLLGMVVDVE NLFMSVHKEE DTDTKQVYFY
210 220 230 240 250
LFKLLRKCIL QMTRPVVEGS LGSPPFEKPN IEQGVLNFVQ YKFSHLAPRE
260 270 280 290 300
RQTMFELSKM FLLCLNYWKL ETPAQFRQRS QAEDVATYKV NYTRWLCYCH
310 320 330 340 350
VPQSCDSLPR YETTHVFGRS LLRSIFTVTR RQLLEKFRVE KDKLVPEKRT
360 370 380 390 400
LILTHFPKFL SMLEEEIYGA NSPIWESGFT MPPSEGTQLV PRPASVSAAV
410 420 430 440 450
VPSTPIFSPS MGGGSNSSLS LDSAGAEPMP GEKRTLPENL TLEDAKRLRV
460 470 480 490 500
MGDIPMELVN EVMLTITDPA AMLGPETSLL SANAARDETA RLEERRGIIE
510 520 530 540 550
FHVIGNSLTP KANRRVLLWL VGLQNVFSHQ LPRMPKEYIA RLVFDPKHKT
560 570 580 590 600
LALIKDGRVI GGICFRMFPT QGFTEIVFCA VTSNEQVKGY GTHLMNHLKE
610 620 630 640 650
YHIKHNILYF LTYADEYAIG YFKKQGFSKD IKVPKSRYLG YIKDYEGATL
660 670 680 690 700
MECELNPRIP YTELSHIIKK QKEIIKKLIE RKQAQIRKVY PGLSCFKEGV
710 720 730 740 750
RQIPVESVPG IRETGWKPLG KEKGKELKDP DQLYTTLKNL LAQIKSHPSA
760 770 780 790 800
WPFMEPVKKS EAPDYYEVIR FPIDLKTMTE RLRSRYYVTR KLFVADLQRV
810 820 830
IANCREYNPP DSEYCRCASA LEKFFYFKLK EGGLIDK
Length:837
Mass (Da):93,926
Last modified:October 14, 2008 - v3
Checksum:i728CC8ACF08600EA
GO
Isoform 2 (identifier: Q92830-2) [UniParc]FASTAAdd to Basket

Also known as: GCN5-S

The sequence of this isoform differs from the canonical sequence as follows:
     1-410: Missing.

Show »
Length:427
Mass (Da):48,921
Checksum:iA6EAE20DB0B49ADC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti116 – 1161E → G in AAC39769. (PubMed:8552087)Curated
Sequence conflicti134 – 1341M → I in AAC39769. (PubMed:8552087)Curated
Sequence conflicti269 – 2691K → E in AAC39769. (PubMed:8552087)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 410410Missing in isoform 2. CuratedVSP_000556Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF029777 mRNA. Translation: AAC39769.1.
CH471152 Genomic DNA. Translation: EAW60803.1.
BC032743 mRNA. Translation: AAH32743.1.
BC039907 mRNA. Translation: AAH39907.1.
BC105977 mRNA. Translation: AAI05978.1.
U57316 Genomic DNA. Translation: AAC50641.1.
CCDSiCCDS11417.1. [Q92830-1]
PIRiS71789.
RefSeqiNP_066564.2. NM_021078.2. [Q92830-1]
UniGeneiHs.463045.

Genome annotation databases

EnsembliENST00000225916; ENSP00000225916; ENSG00000108773. [Q92830-1]
GeneIDi2648.
KEGGihsa:2648.
UCSCiuc002hyx.2. human. [Q92830-1]

Polymorphism databases

DMDMi209572743.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF029777 mRNA. Translation: AAC39769.1 .
CH471152 Genomic DNA. Translation: EAW60803.1 .
BC032743 mRNA. Translation: AAH32743.1 .
BC039907 mRNA. Translation: AAH39907.1 .
BC105977 mRNA. Translation: AAI05978.1 .
U57316 Genomic DNA. Translation: AAC50641.1 .
CCDSi CCDS11417.1. [Q92830-1 ]
PIRi S71789.
RefSeqi NP_066564.2. NM_021078.2. [Q92830-1 ]
UniGenei Hs.463045.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1F68 NMR - A 730-832 [» ]
1Z4R X-ray 1.74 A 497-662 [» ]
3D7C X-ray 2.06 A/B 729-837 [» ]
ProteinModelPortali Q92830.
SMRi Q92830. Positions 497-658, 730-835.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108918. 105 interactions.
DIPi DIP-28146N.
IntActi Q92830. 36 interactions.
MINTi MINT-199927.
STRINGi 9606.ENSP00000225916.

Chemistry

ChEMBLi CHEMBL5501.

PTM databases

PhosphoSitei Q92830.

Polymorphism databases

DMDMi 209572743.

Proteomic databases

MaxQBi Q92830.
PaxDbi Q92830.
PRIDEi Q92830.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000225916 ; ENSP00000225916 ; ENSG00000108773 . [Q92830-1 ]
GeneIDi 2648.
KEGGi hsa:2648.
UCSCi uc002hyx.2. human. [Q92830-1 ]

Organism-specific databases

CTDi 2648.
GeneCardsi GC17M040265.
HGNCi HGNC:4201. KAT2A.
HPAi HPA048958.
MIMi 602301. gene.
neXtProti NX_Q92830.
PharmGKBi PA162392664.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5076.
GeneTreei ENSGT00760000119099.
HOGENOMi HOG000007151.
InParanoidi Q92830.
KOi K06062.
OMAi NSPIWES.
PhylomeDBi Q92830.
TreeFami TF105399.

Enzyme and pathway databases

Reactomei REACT_118568. Pre-NOTCH Transcription and Translation.
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.
SignaLinki Q92830.

Miscellaneous databases

ChiTaRSi KAT2A. human.
EvolutionaryTracei Q92830.
GeneWikii GCN5L2.
GenomeRNAii 2648.
NextBioi 10450.
PROi Q92830.
SOURCEi Search...

Gene expression databases

Bgeei Q92830.
CleanExi HS_KAT2A.
ExpressionAtlasi Q92830. baseline and differential.
Genevestigatori Q92830.

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 PF00583. Acetyltransf_1. 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. "Identification of human proteins functionally conserved with the yeast putative adaptors ADA2 and GCN5."
    Candau R., Moore P.A., Wang L., Barlev N., Ying C.Y., Rosen C.A., Berger S.L.
    Mol. Cell. Biol. 16:593-602(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), CHARACTERIZATION.
    Tissue: Testis.
  2. "Cloning of Drosophila GCN5: conserved features among metazoan GCN5 family members."
    Smith E.R., Belote J.M., Schlitz R.L., Yang X.-J., Moore P.A., Berger S.L., Nakatani Y., Allis C.D.
    Nucleic Acids Res. 26:2948-2954(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ALTERNATIVE SPLICING.
    Tissue: Liver.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
    Tissue: Eye, Skin and Testis.
  5. "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 [GENOMIC DNA] OF 362-837 (ISOFORM 1).
    Tissue: Brain.
  6. "Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo."
    Martinez E., Palhan V.B., Tjernberg A., Lymar E.S., Gamper A.M., Kundu T.K., Chait B.T., Roeder R.G.
    Mol. Cell. Biol. 21:6782-6795(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, IDENTIFICATION IN THE STAGA COMPLEX WITH SUPT3H; KIAA0764; TAF5L; TAF6L; TRRAP; TADA3L; TAF10; TAF12 AND TAF9, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "Identification of TATA-binding protein-free TAFII-containing complex subunits suggests a role in nucleosome acetylation and signal transduction."
    Brand M., Yamamoto K., Staub A., Tora L.
    J. Biol. Chem. 274:18285-18289(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE TFTC-HAT COMPLEX WITH TAF5L; TAF6L; TADA3L; SUPT3H; TAF2; TAF4; TAF5; TRRAP AND TAF10.
  8. "The essential cofactor TRRAP recruits the histone acetyltransferase hGCN5 to c-Myc."
    McMahon S.B., Wood M.A., Cole M.D.
    Mol. Cell. Biol. 20:556-562(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRRAP.
  9. "The histone acetyltransferase, hGCN5, interacts with and acetylates the HIV transactivator, Tat."
    Col E., Caron C., Seigneurin-Berny D., Gracia J., Favier A., Khochbin S.
    J. Biol. Chem. 276:28179-28184(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIV-1 TAT.
  10. "The TFIID components human TAFII140 and Drosophila BIP2 (TAFII155) are novel metazoan homologues of yeast TAFII47 containing a histone fold and a PHD finger."
    Gangloff Y.G., Pointud J.-C., Thuault S., Carre L., Romier C., Muratoglu S., Brand M., Tora L., Couderc J.-L., Davidson I.
    Mol. Cell. Biol. 21:5109-5121(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TAF3.
  11. "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.
  12. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "A TFTC/STAGA module mediates histone H2A and H2B deubiquitination, coactivates nuclear receptors, and counteracts heterochromatin silencing."
    Zhao Y., Lang G., Ito S., Bonnet J., Metzger E., Sawatsubashi S., Suzuki E., Le Guezennec X., Stunnenberg H.G., Krasnov A., Georgieva S.G., Schuele R., Takeyama K., Kato S., Tora L., Devys D.
    Mol. Cell 29:92-101(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN STAGA COMPLEX.
  14. "The double-histone-acetyltransferase complex ATAC is essential for mammalian development."
    Guelman S., Kozuka K., Mao Y., Pham V., Solloway M.J., Wang J., Wu J., Lill J.R., Zha J.
    Mol. Cell. Biol. 29:1176-1188(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN ATAC COMPLEX.
  15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  16. "Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain."
    Hudson B.P., Martinez-Yamout M.A., Dyson H.J., Wright P.E.
    J. Mol. Biol. 304:355-370(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 730-832.
  17. "Crystal structure of a binary complex between human GCN5 histone acetyltransferase domain and acetyl coenzyme A."
    Schuetz A., Bernstein G., Dong A., Antoshenko T., Wu H., Loppnau P., Bochkarev A., Plotnikov A.N.
    Proteins 68:403-407(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 497-662 IN COMPLEX WITH ACETYL-COA, ACTIVE SITE.
  18. Cited for: X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) OF 729-837.

Entry informationi

Entry nameiKAT2A_HUMAN
AccessioniPrimary (citable) accession number: Q92830
Secondary accession number(s): Q8N1A2, Q9UCW1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: October 14, 2008
Last modified: October 29, 2014
This is version 162 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 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3