Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Histone acetyltransferase KAT2A

Gene

KAT2A

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. 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. Also acetylates non-histone proteins, such as CEBPB (PubMed:17301242). Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. 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.2 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei575Proton donor/acceptor1 Publication1

GO - Molecular functioni

  • chromatin binding Source: Ensembl
  • H3 histone acetyltransferase activity Source: BHF-UCL
  • histone acetyltransferase activity Source: UniProtKB
  • histone acetyltransferase activity (H4-K12 specific) Source: Ensembl
  • histone deacetylase binding Source: UniProtKB
  • transcription coactivator activity Source: UniProtKB
  • transcription factor binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Host-virus interaction, Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciZFISH:HS03151-MONOMER.
BRENDAi2.3.1.48. 2681.
ReactomeiR-HSA-1912408. Pre-NOTCH Transcription and Translation.
R-HSA-2122947. NOTCH1 Intracellular Domain Regulates Transcription.
R-HSA-2644606. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
R-HSA-2894862. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
R-HSA-3214847. HATs acetylate histones.
R-HSA-350054. Notch-HLH transcription pathway.
R-HSA-5250924. B-WICH complex positively regulates rRNA expression.
R-HSA-5689880. Ub-specific processing proteases.
R-HSA-73762. RNA Polymerase I Transcription Initiation.
SignaLinkiQ92830.
SIGNORiQ92830.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:4201. KAT2A.

Subcellular locationi

GO - Cellular componenti

  • Ada2/Gcn5/Ada3 transcription activator complex Source: BHF-UCL
  • extracellular space Source: UniProtKB
  • mitotic spindle Source: Ensembl
  • nuclear chromatin Source: Ensembl
  • nucleoplasm Source: Reactome
  • STAGA complex Source: UniProtKB
  • transcription factor TFTC complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi2648.
OpenTargetsiENSG00000108773.
PharmGKBiPA162392664.

Chemistry databases

ChEMBLiCHEMBL5501.

Polymorphism and mutation databases

BioMutaiKAT2A.
DMDMi209572743.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00002112022 – 837Histone acetyltransferase KAT2AAdd BLAST836

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ92830.
MaxQBiQ92830.
PaxDbiQ92830.
PeptideAtlasiQ92830.
PRIDEiQ92830.

PTM databases

iPTMnetiQ92830.
PhosphoSitePlusiQ92830.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000108773.
CleanExiHS_KAT2A.
ExpressionAtlasiQ92830. baseline and differential.
GenevisibleiQ92830. HS.

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. Component of the ADA2A-containing complex (ATAC), composed of KAT14, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1. In the complex, it probably interacts directly with KAT14, MBIP and WDR5. Interacts with PML (By similarity). Interacts with CEBPB (PubMed:17301242). Interacts with and acetylates HIV-1 Tat.By similarity1 Publication

Binary interactionsi

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

GO - Molecular functioni

  • histone deacetylase binding Source: UniProtKB
  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108918. 112 interactors.
DIPiDIP-28146N.
IntActiQ92830. 39 interactors.
MINTiMINT-199927.
STRINGi9606.ENSP00000225916.

Chemistry databases

BindingDBiQ92830.

Structurei

Secondary structure

1837
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi498 – 504Combined sources7
Helixi514 – 530Combined sources17
Helixi536 – 543Combined sources8
Beta strandi549 – 555Combined sources7
Beta strandi558 – 568Combined sources11
Turni569 – 572Combined sources4
Beta strandi573 – 581Combined sources9
Helixi583 – 585Combined sources3
Beta strandi587 – 589Combined sources3
Helixi590 – 604Combined sources15
Beta strandi609 – 614Combined sources6
Helixi616 – 618Combined sources3
Helixi619 – 624Combined sources6
Beta strandi627 – 629Combined sources3
Helixi635 – 638Combined sources4
Turni639 – 641Combined sources3
Beta strandi649 – 654Combined sources6
Helixi730 – 746Combined sources17
Helixi748 – 753Combined sources6
Turni759 – 761Combined sources3
Helixi765 – 768Combined sources4
Helixi775 – 783Combined sources9
Helixi790 – 807Combined sources18
Helixi813 – 831Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F68NMR-A730-832[»]
1Z4RX-ray1.74A497-662[»]
3D7CX-ray2.06A/B729-837[»]
5H84X-ray2.00A497-662[»]
5H86X-ray2.08A497-662[»]
ProteinModelPortaliQ92830.
SMRiQ92830.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92830.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini503 – 656N-acetyltransferasePROSITE-ProRule annotationAdd BLAST154
Domaini745 – 815BromoPROSITE-ProRule annotationAdd BLAST71

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni579 – 581Acetyl-CoA binding1 Publication3
Regioni586 – 592Acetyl-CoA binding1 Publication7
Regioni617 – 620Acetyl-CoA binding1 Publication4

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.
InParanoidiQ92830.
KOiK06062.
OMAiDYYEIIR.
OrthoDBiEOG091G03ZO.
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. AlignAdd to basket

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)DescriptionActionsGraphical viewLength
Sequence conflicti116E → G in AAC39769 (PubMed:8552087).Curated1
Sequence conflicti134M → I in AAC39769 (PubMed:8552087).Curated1
Sequence conflicti269K → E in AAC39769 (PubMed:8552087).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0005561 – 410Missing in isoform 2. CuratedAdd BLAST410

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
XP_016879937.1. XM_017024448.1.
UniGeneiHs.463045.

Genome annotation databases

EnsembliENST00000225916; ENSP00000225916; ENSG00000108773. [Q92830-1]
GeneIDi2648.
KEGGihsa:2648.
UCSCiuc002hyx.3. human. [Q92830-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
XP_016879937.1. XM_017024448.1.
UniGeneiHs.463045.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F68NMR-A730-832[»]
1Z4RX-ray1.74A497-662[»]
3D7CX-ray2.06A/B729-837[»]
5H84X-ray2.00A497-662[»]
5H86X-ray2.08A497-662[»]
ProteinModelPortaliQ92830.
SMRiQ92830.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108918. 112 interactors.
DIPiDIP-28146N.
IntActiQ92830. 39 interactors.
MINTiMINT-199927.
STRINGi9606.ENSP00000225916.

Chemistry databases

BindingDBiQ92830.
ChEMBLiCHEMBL5501.

PTM databases

iPTMnetiQ92830.
PhosphoSitePlusiQ92830.

Polymorphism and mutation databases

BioMutaiKAT2A.
DMDMi209572743.

Proteomic databases

EPDiQ92830.
MaxQBiQ92830.
PaxDbiQ92830.
PeptideAtlasiQ92830.
PRIDEiQ92830.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000225916; ENSP00000225916; ENSG00000108773. [Q92830-1]
GeneIDi2648.
KEGGihsa:2648.
UCSCiuc002hyx.3. human. [Q92830-1]

Organism-specific databases

CTDi2648.
DisGeNETi2648.
GeneCardsiKAT2A.
HGNCiHGNC:4201. KAT2A.
HPAiHPA048958.
MIMi602301. gene.
neXtProtiNX_Q92830.
OpenTargetsiENSG00000108773.
PharmGKBiPA162392664.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1472. Eukaryota.
COG5076. LUCA.
GeneTreeiENSGT00760000119099.
HOGENOMiHOG000007151.
InParanoidiQ92830.
KOiK06062.
OMAiDYYEIIR.
OrthoDBiEOG091G03ZO.
PhylomeDBiQ92830.
TreeFamiTF105399.

Enzyme and pathway databases

BioCyciZFISH:HS03151-MONOMER.
BRENDAi2.3.1.48. 2681.
ReactomeiR-HSA-1912408. Pre-NOTCH Transcription and Translation.
R-HSA-2122947. NOTCH1 Intracellular Domain Regulates Transcription.
R-HSA-2644606. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
R-HSA-2894862. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
R-HSA-3214847. HATs acetylate histones.
R-HSA-350054. Notch-HLH transcription pathway.
R-HSA-5250924. B-WICH complex positively regulates rRNA expression.
R-HSA-5689880. Ub-specific processing proteases.
R-HSA-73762. RNA Polymerase I Transcription Initiation.
SignaLinkiQ92830.
SIGNORiQ92830.

Miscellaneous databases

ChiTaRSiKAT2A. human.
EvolutionaryTraceiQ92830.
GeneWikiiGCN5L2.
GenomeRNAii2648.
PROiQ92830.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000108773.
CleanExiHS_KAT2A.
ExpressionAtlasiQ92830. baseline and differential.
GenevisibleiQ92830. 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]
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 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: November 2, 2016
This is version 184 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

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.