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Histone acetyltransferase KAT2A (EC 2.3.1.48) (General control of amino acid synthesis protein 5-like 2) (Histone acetyltransferase GCN5) (HsGCN5) (Lysine acetyltransferase 2A) (STAF97)

 KAT2A_HUMAN             Reviewed;         837 AA.
Q92830; Q8N1A2; Q9UCW1;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
14-OCT-2008, sequence version 3.
30-AUG-2017, entry version 190.
RecName: Full=Histone acetyltransferase KAT2A;
EC=2.3.1.48;
AltName: Full=General control of amino acid synthesis protein 5-like 2;
AltName: Full=Histone acetyltransferase GCN5;
Short=HsGCN5;
AltName: Full=Lysine acetyltransferase 2A;
AltName: Full=STAF97;
Name=KAT2A; Synonyms=GCN5, GCN5L2, HGCN5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), AND CHARACTERIZATION.
TISSUE=Testis;
PubMed=8552087; DOI=10.1128/MCB.16.2.593;
Candau R., Moore P.A., Wang L., Barlev N., Ying C.Y., Rosen C.A.,
Berger S.L.;
"Identification of human proteins functionally conserved with the
yeast putative adaptors ADA2 and GCN5.";
Mol. Cell. Biol. 16:593-602(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND ALTERNATIVE SPLICING.
TISSUE=Liver;
PubMed=9611240; DOI=10.1093/nar/26.12.2948;
Smith E.R., Belote J.M., Schlitz R.L., Yang X.-J., Moore P.A.,
Berger S.L., Nakatani Y., Allis C.D.;
"Cloning of Drosophila GCN5: conserved features among metazoan GCN5
family members.";
Nucleic Acids Res. 26:2948-2954(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye, Skin, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 362-837 (ISOFORM 1).
TISSUE=Brain;
PubMed=8684459; DOI=10.1038/382319a0;
Yang X.-J., Ogryzko V.V., Nishikawa J., Howard B.H., Nakatani Y.;
"A p300/CBP-associated factor that competes with the adenoviral
oncoprotein E1A.";
Nature 382:319-324(1996).
[6]
SUBCELLULAR LOCATION, IDENTIFICATION IN THE STAGA COMPLEX WITH SUPT3H;
KIAA0764; TAF5L; TAF6L; TRRAP; TADA3L; TAF10; TAF12 AND TAF9, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=11564863; DOI=10.1128/MCB.21.20.6782-6795.2001;
Martinez E., Palhan V.B., Tjernberg A., Lymar E.S., Gamper A.M.,
Kundu T.K., Chait B.T., Roeder R.G.;
"Human STAGA complex is a chromatin-acetylating transcription
coactivator that interacts with pre-mRNA splicing and DNA damage-
binding factors in vivo.";
Mol. Cell. Biol. 21:6782-6795(2001).
[7]
IDENTIFICATION IN THE TFTC-HAT COMPLEX WITH TAF5L; TAF6L; TADA3L;
SUPT3H; TAF2; TAF4; TAF5; TRRAP AND TAF10.
PubMed=10373431; DOI=10.1074/jbc.274.26.18285;
Brand M., Yamamoto K., Staub A., Tora L.;
"Identification of TATA-binding protein-free TAFII-containing complex
subunits suggests a role in nucleosome acetylation and signal
transduction.";
J. Biol. Chem. 274:18285-18289(1999).
[8]
INTERACTION WITH TRRAP.
PubMed=10611234; DOI=10.1128/MCB.20.2.556-562.2000;
McMahon S.B., Wood M.A., Cole M.D.;
"The essential cofactor TRRAP recruits the histone acetyltransferase
hGCN5 to c-Myc.";
Mol. Cell. Biol. 20:556-562(2000).
[9]
INTERACTION WITH HIV-1 TAT.
PubMed=11384967; DOI=10.1074/jbc.M101385200;
Col E., Caron C., Seigneurin-Berny D., Gracia J., Favier A.,
Khochbin S.;
"The histone acetyltransferase, hGCN5, interacts with and acetylates
the HIV transactivator, Tat.";
J. Biol. Chem. 276:28179-28184(2001).
[10]
INTERACTION WITH TAF3.
PubMed=11438666; DOI=10.1128/MCB.21.15.5109-5121.2001;
Gangloff Y.G., Pointud J.-C., Thuault S., Carre L., Romier C.,
Muratoglu S., Brand M., Tora L., Couderc J.-L., Davidson I.;
"The TFIID components human TAFII140 and Drosophila BIP2 (TAFII155)
are novel metazoan homologues of yeast TAFII47 containing a histone
fold and a PHD finger.";
Mol. Cell. Biol. 21:5109-5121(2001).
[11]
INTERACTION WITH TACC1; TACC2 AND TACC3.
PubMed=14767476; DOI=10.1038/sj.onc.1207424;
Gangisetty O., Lauffart B., Sondarva G.V., Chelsea D.M., Still I.H.;
"The transforming acidic coiled coil proteins interact with nuclear
histone acetyltransferases.";
Oncogene 23:2559-2563(2004).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
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.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[13]
FUNCTION, AND INTERACTION WITH CEBPB.
PubMed=17301242; DOI=10.1073/pnas.0607378104;
Wiper-Bergeron N., Salem H.A., Tomlinson J.J., Wu D., Hache R.J.;
"Glucocorticoid-stimulated preadipocyte differentiation is mediated
through acetylation of C/EBPbeta by GCN5.";
Proc. Natl. Acad. Sci. U.S.A. 104:2703-2708(2007).
[14]
IDENTIFICATION IN STAGA COMPLEX.
PubMed=18206972; DOI=10.1016/j.molcel.2007.12.011;
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.;
"A TFTC/STAGA module mediates histone H2A and H2B deubiquitination,
coactivates nuclear receptors, and counteracts heterochromatin
silencing.";
Mol. Cell 29:92-101(2008).
[15]
FUNCTION, AND IDENTIFICATION IN ATAC COMPLEX.
PubMed=19103755; DOI=10.1128/MCB.01599-08;
Guelman S., Kozuka K., Mao Y., Pham V., Solloway M.J., Wang J., Wu J.,
Lill J.R., Zha J.;
"The double-histone-acetyltransferase complex ATAC is essential for
mammalian development.";
Mol. Cell. Biol. 29:1176-1188(2009).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[17]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-728; LYS-759 AND LYS-791,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[18]
STRUCTURE BY NMR OF 730-832.
PubMed=11090279; DOI=10.1006/jmbi.2000.4207;
Hudson B.P., Martinez-Yamout M.A., Dyson H.J., Wright P.E.;
"Solution structure and acetyl-lysine binding activity of the GCN5
bromodomain.";
J. Mol. Biol. 304:355-370(2000).
[19]
X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 497-662 IN COMPLEX WITH
ACETYL-COA, AND ACTIVE SITE.
PubMed=17410582; DOI=10.1002/prot.21407;
Schuetz A., Bernstein G., Dong A., Antoshenko T., Wu H., Loppnau P.,
Bochkarev A., Plotnikov A.N.;
"Crystal structure of a binary complex between human GCN5 histone
acetyltransferase domain and acetyl coenzyme A.";
Proteins 68:403-407(2007).
[20]
X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) OF 729-837.
PubMed=22464331; DOI=10.1016/j.cell.2012.02.013;
Filippakopoulos P., Picaud S., Mangos M., Keates T., Lambert J.P.,
Barsyte-Lovejoy D., Felletar I., Volkmer R., Muller S., Pawson T.,
Gingras A.C., Arrowsmith C.H., Knapp S.;
"Histone recognition and large-scale structural analysis of the human
bromodomain family.";
Cell 149:214-231(2012).
-!- FUNCTION: 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. {ECO:0000269|PubMed:17301242,
ECO:0000269|PubMed:19103755}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + [protein]-L-lysine = CoA +
[protein]-N(6)-acetyl-L-lysine.
-!- SUBUNIT: 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. {ECO:0000250|UniProtKB:Q9JHD2,
ECO:0000269|PubMed:17301242}.
-!- INTERACTION:
O75717:WDHD1; NbExp=5; IntAct=EBI-477622, EBI-3951691;
Q8IYH5:ZZZ3; NbExp=2; IntAct=EBI-477622, EBI-2795524;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11564863}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=GCN5-L;
IsoId=Q92830-1; Sequence=Displayed;
Name=2; Synonyms=GCN5-S;
IsoId=Q92830-2; Sequence=VSP_000556;
-!- TISSUE SPECIFICITY: Expressed in all tissues tested, with most
abundant expression in ovary.
-!- SIMILARITY: Belongs to the acetyltransferase family. GCN5
subfamily. {ECO:0000305}.
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EMBL; AF029777; AAC39769.1; -; mRNA.
EMBL; CH471152; EAW60803.1; -; Genomic_DNA.
EMBL; BC032743; AAH32743.1; -; mRNA.
EMBL; BC039907; AAH39907.1; -; mRNA.
EMBL; BC105977; AAI05978.1; -; mRNA.
EMBL; U57316; AAC50641.1; -; Genomic_DNA.
CCDS; CCDS11417.1; -. [Q92830-1]
PIR; S71789; S71789.
RefSeq; NP_066564.2; NM_021078.2. [Q92830-1]
RefSeq; XP_016879937.1; XM_017024448.1.
UniGene; Hs.463045; -.
PDB; 1F68; NMR; -; A=730-832.
PDB; 1Z4R; X-ray; 1.74 A; A=497-662.
PDB; 3D7C; X-ray; 2.06 A; A/B=729-837.
PDB; 5H84; X-ray; 2.00 A; A=497-662.
PDB; 5H86; X-ray; 2.08 A; A=497-662.
PDBsum; 1F68; -.
PDBsum; 1Z4R; -.
PDBsum; 3D7C; -.
PDBsum; 5H84; -.
PDBsum; 5H86; -.
ProteinModelPortal; Q92830; -.
SMR; Q92830; -.
BioGrid; 108918; 114.
DIP; DIP-28146N; -.
IntAct; Q92830; 39.
MINT; MINT-199927; -.
STRING; 9606.ENSP00000225916; -.
BindingDB; Q92830; -.
ChEMBL; CHEMBL5501; -.
DrugBank; DB01992; Coenzyme A.
iPTMnet; Q92830; -.
PhosphoSitePlus; Q92830; -.
BioMuta; KAT2A; -.
DMDM; 209572743; -.
EPD; Q92830; -.
MaxQB; Q92830; -.
PaxDb; Q92830; -.
PeptideAtlas; Q92830; -.
PRIDE; Q92830; -.
Ensembl; ENST00000225916; ENSP00000225916; ENSG00000108773. [Q92830-1]
GeneID; 2648; -.
KEGG; hsa:2648; -.
UCSC; uc002hyx.3; human. [Q92830-1]
CTD; 2648; -.
DisGeNET; 2648; -.
GeneCards; KAT2A; -.
HGNC; HGNC:4201; KAT2A.
HPA; HPA048958; -.
MIM; 602301; gene.
neXtProt; NX_Q92830; -.
OpenTargets; ENSG00000108773; -.
PharmGKB; PA162392664; -.
eggNOG; KOG1472; Eukaryota.
eggNOG; COG5076; LUCA.
GeneTree; ENSGT00760000119099; -.
HOGENOM; HOG000007151; -.
InParanoid; Q92830; -.
KO; K06062; -.
OMA; NHLKDYS; -.
OrthoDB; EOG091G03ZO; -.
PhylomeDB; Q92830; -.
TreeFam; TF105399; -.
BRENDA; 2.3.1.48; 2681.
Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation.
Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
Reactome; R-HSA-3214847; HATs acetylate histones.
Reactome; R-HSA-350054; Notch-HLH transcription pathway.
Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
Reactome; R-HSA-8941856; RUNX3 regulates NOTCH signaling.
SignaLink; Q92830; -.
SIGNOR; Q92830; -.
ChiTaRS; KAT2A; human.
EvolutionaryTrace; Q92830; -.
GeneWiki; GCN5L2; -.
GenomeRNAi; 2648; -.
PRO; PR:Q92830; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000108773; -.
CleanEx; HS_KAT2A; -.
ExpressionAtlas; Q92830; baseline and differential.
Genevisible; Q92830; HS.
GO; GO:0005671; C:Ada2/Gcn5/Ada3 transcription activator complex; IDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0072686; C:mitotic spindle; IEA:Ensembl.
GO; GO:0000790; C:nuclear chromatin; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0030914; C:STAGA complex; IDA:UniProtKB.
GO; GO:0033276; C:transcription factor TFTC complex; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0010484; F:H3 histone acetyltransferase activity; IDA:BHF-UCL.
GO; GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB.
GO; GO:0043997; F:histone acetyltransferase activity (H4-K12 specific); IEA:Ensembl.
GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; TAS:Reactome.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0071929; P:alpha-tubulin acetylation; IEA:Ensembl.
GO; GO:0055007; P:cardiac muscle cell differentiation; IEA:Ensembl.
GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEA:Ensembl.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
GO; GO:0006338; P:chromatin remodeling; TAS:ProtInc.
GO; GO:0016578; P:histone deubiquitination; IDA:UniProtKB.
GO; GO:0043966; P:histone H3 acetylation; IDA:UniProtKB.
GO; GO:0044154; P:histone H3-K14 acetylation; IEA:Ensembl.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0048312; P:intracellular distribution of mitochondria; IEA:Ensembl.
GO; GO:0022037; P:metencephalon development; IEA:Ensembl.
GO; GO:0030901; P:midbrain development; IEA:Ensembl.
GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
GO; GO:0031346; P:positive regulation of cell projection organization; IEA:Ensembl.
GO; GO:0045815; P:positive regulation of gene expression, epigenetic; TAS:Reactome.
GO; GO:0035948; P:positive regulation of gluconeogenesis by positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0035066; P:positive regulation of histone acetylation; IEA:Ensembl.
GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; IMP:ParkinsonsUK-UCL.
GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; IEA:Ensembl.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:1903146; P:regulation of mitophagy; IMP:ParkinsonsUK-UCL.
GO; GO:0031647; P:regulation of protein stability; IMP:MGI.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
GO; GO:0021537; P:telencephalon development; IEA:Ensembl.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 1.20.920.10; -; 1.
InterPro; IPR016181; Acyl_CoA_acyltransferase.
InterPro; IPR001487; Bromodomain.
InterPro; IPR018359; Bromodomain_CS.
InterPro; IPR016376; GCN5/PCAF.
InterPro; IPR000182; GNAT_dom.
InterPro; IPR009464; PCAF_N.
Pfam; PF00583; Acetyltransf_1; 1.
Pfam; PF00439; Bromodomain; 1.
Pfam; PF06466; PCAF_N; 1.
PIRSF; PIRSF003048; Histone_acetylase_PCAF; 1.
PRINTS; PR00503; BROMODOMAIN.
SMART; SM00297; BROMO; 1.
SUPFAM; SSF47370; SSF47370; 1.
SUPFAM; SSF55729; SSF55729; 1.
PROSITE; PS00633; BROMODOMAIN_1; 1.
PROSITE; PS50014; BROMODOMAIN_2; 1.
PROSITE; PS51186; GNAT; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Acyltransferase; Alternative splicing;
Bromodomain; Complete proteome; Host-virus interaction;
Isopeptide bond; Nucleus; Reference proteome; Transcription;
Transcription regulation; Transferase; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 837 Histone acetyltransferase KAT2A.
/FTId=PRO_0000211202.
DOMAIN 503 656 N-acetyltransferase.
{ECO:0000255|PROSITE-ProRule:PRU00532}.
DOMAIN 745 815 Bromo. {ECO:0000255|PROSITE-
ProRule:PRU00035}.
REGION 579 581 Acetyl-CoA binding.
{ECO:0000269|PubMed:17410582}.
REGION 586 592 Acetyl-CoA binding.
{ECO:0000269|PubMed:17410582}.
REGION 617 620 Acetyl-CoA binding.
{ECO:0000269|PubMed:17410582}.
ACT_SITE 575 575 Proton donor/acceptor.
{ECO:0000303|PubMed:17410582}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22814378}.
CROSSLNK 728 728 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 759 759 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 791 791 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 410 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_000556.
CONFLICT 116 116 E -> G (in Ref. 1; AAC39769).
{ECO:0000305}.
CONFLICT 134 134 M -> I (in Ref. 1; AAC39769).
{ECO:0000305}.
CONFLICT 269 269 K -> E (in Ref. 1; AAC39769).
{ECO:0000305}.
STRAND 498 504 {ECO:0000244|PDB:1Z4R}.
HELIX 514 530 {ECO:0000244|PDB:1Z4R}.
HELIX 536 543 {ECO:0000244|PDB:1Z4R}.
STRAND 549 555 {ECO:0000244|PDB:1Z4R}.
STRAND 558 568 {ECO:0000244|PDB:1Z4R}.
TURN 569 572 {ECO:0000244|PDB:1Z4R}.
STRAND 573 581 {ECO:0000244|PDB:1Z4R}.
HELIX 583 585 {ECO:0000244|PDB:1Z4R}.
STRAND 587 589 {ECO:0000244|PDB:1Z4R}.
HELIX 590 604 {ECO:0000244|PDB:1Z4R}.
STRAND 609 614 {ECO:0000244|PDB:1Z4R}.
HELIX 616 618 {ECO:0000244|PDB:1Z4R}.
HELIX 619 624 {ECO:0000244|PDB:1Z4R}.
STRAND 627 629 {ECO:0000244|PDB:1Z4R}.
HELIX 635 638 {ECO:0000244|PDB:1Z4R}.
TURN 639 641 {ECO:0000244|PDB:1Z4R}.
STRAND 649 654 {ECO:0000244|PDB:1Z4R}.
HELIX 730 746 {ECO:0000244|PDB:3D7C}.
HELIX 748 753 {ECO:0000244|PDB:3D7C}.
TURN 759 761 {ECO:0000244|PDB:3D7C}.
HELIX 765 768 {ECO:0000244|PDB:3D7C}.
HELIX 775 783 {ECO:0000244|PDB:3D7C}.
HELIX 790 807 {ECO:0000244|PDB:3D7C}.
HELIX 813 831 {ECO:0000244|PDB:3D7C}.
SEQUENCE 837 AA; 93926 MW; 728CC8ACF08600EA CRC64;
MAEPSQAPTP APAAQPRPLQ SPAPAPTPTP APSPASAPIP TPTPAPAPAP AAAPAGSTGT
GGPGVGSGGA GSGGDPARPG LSQQQRASQR KAQVRGLPRA KKLEKLGVFS ACKANETCKC
NGWKNPKPPT APRMDLQQPA ANLSELCRSC EHPLADHVSH LENVSEDEIN RLLGMVVDVE
NLFMSVHKEE DTDTKQVYFY LFKLLRKCIL QMTRPVVEGS LGSPPFEKPN IEQGVLNFVQ
YKFSHLAPRE RQTMFELSKM FLLCLNYWKL ETPAQFRQRS QAEDVATYKV NYTRWLCYCH
VPQSCDSLPR YETTHVFGRS LLRSIFTVTR RQLLEKFRVE KDKLVPEKRT LILTHFPKFL
SMLEEEIYGA NSPIWESGFT MPPSEGTQLV PRPASVSAAV VPSTPIFSPS MGGGSNSSLS
LDSAGAEPMP GEKRTLPENL TLEDAKRLRV MGDIPMELVN EVMLTITDPA AMLGPETSLL
SANAARDETA RLEERRGIIE FHVIGNSLTP KANRRVLLWL VGLQNVFSHQ LPRMPKEYIA
RLVFDPKHKT LALIKDGRVI GGICFRMFPT QGFTEIVFCA VTSNEQVKGY GTHLMNHLKE
YHIKHNILYF LTYADEYAIG YFKKQGFSKD IKVPKSRYLG YIKDYEGATL MECELNPRIP
YTELSHIIKK QKEIIKKLIE RKQAQIRKVY PGLSCFKEGV RQIPVESVPG IRETGWKPLG
KEKGKELKDP DQLYTTLKNL LAQIKSHPSA WPFMEPVKKS EAPDYYEVIR FPIDLKTMTE
RLRSRYYVTR KLFVADLQRV IANCREYNPP DSEYCRCASA LEKFFYFKLK EGGLIDK


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