KAT2A

KAT2A
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1F68, 1Z4R, 3D7C, 5H86, 5H84
Identifiers
Aliases	KAT2A , GCN5, GCN5L2, PCAF-b, hGCN5, lysine acetyltransferase 2A
External IDs	OMIM: 602301; MGI: 1343101; HomoloGene: 41343; GeneCards: KAT2A; OMA:KAT2A - orthologs
Gene location (Human) Chr. Chromosome 17 (human) [1] Band 17q21.2 Start 42,113,111 bp [1] End 42,121,367 bp [1]
Gene location (Mouse) Chr. Chromosome 11 (mouse) [2] Band 11 D|11 63.53 cM Start 100,595,572 bp [2] End 100,603,291 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right uterine tube left ovary right ovary right hemisphere of cerebellum right adrenal cortex right frontal lobe left uterine tube left adrenal cortex body of uterus canal of the cervix Top expressed in internal carotid artery external carotid artery otic placode tail of embryo otic vesicle saccule genital tubercle epiblast lacrimal gland hair follicle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity transcription coactivator activity N-acetyltransferase activity transcription factor binding histone deacetylase binding chromatin binding H3 histone acetyltransferase activity protein binding acetyltransferase activity histone acetyltransferase activity (H4-K12 specific) protein phosphatase binding acyltransferase activity histone acetyltransferase activity thiol-dependent deubiquitinase peptide-lysine-N-acetyltransferase activity histone succinyltransferase activity Cellular component transcription factor TFTC complex nucleoplasm histone acetyltransferase complex mitotic spindle extracellular space nucleus chromosome cytoplasm centrosome microtubule organizing center cytoskeleton oxoglutarate dehydrogenase complex Biological process positive regulation of transcription regulatory region DNA binding somitogenesis epigenetic maintenance of chromatin in transcription-competent conformation chromatin remodeling metencephalon development cellular response to nerve growth factor stimulus regulation of transcription, DNA-templated regulation of protein stability response to organic cyclic compound multicellular organism growth positive regulation of protein targeting to mitochondrion regulation of transcription by RNA polymerase II cardiac muscle cell differentiation cellular response to tumor necrosis factor histone H3-K14 acetylation positive regulation of cell projection organization in utero embryonic development transcription by RNA polymerase II transcription, DNA-templated nervous system development positive regulation of histone acetylation histone deubiquitination telencephalon development neural tube closure response to nutrient levels regulation of autophagy of mitochondrion histone acetylation histone H3 acetylation cell population proliferation viral process intracellular distribution of mitochondria histone H4-K12 acetylation alpha-tubulin acetylation midbrain development protein deubiquitination cytokine production heart development long-term memory internal peptidyl-lysine acetylation regulation of regulatory T cell differentiation positive regulation of transcription by RNA polymerase II negative regulation of centriole replication regulation of synaptic plasticity regulation of T cell activation limb development histone succinylation positive regulation of cardiac muscle cell differentiation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 2648 14534 Ensembl ENSG00000108773 ENSMUSG00000020918 UniProt Q92830 Q9JHD2 RefSeq (mRNA) NM_021078 NM_001376227 NM_001038010 NM_020004 RefSeq (protein) NP_066564 NP_001363156 NP_001033099 NP_064388 Location (UCSC) Chr 17: 42.11 – 42.12 Mb Chr 11: 100.6 – 100.6 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Histone acetyltransferase KAT2A is an enzyme that in humans is encoded by the KAT2A gene. ^{[5] [6]}

Interactions

GCN5L2 has been shown to interact with:

• DDB1, ^[7]
• Ku70, ^[8]
• Ku80, ^[8]
• TADA2L, ^{[8] [9]}
• TAF9, ^[7] and
• Transcription initiation protein SPT3 homolog. ^{[7] [10]}

References

1. GRCh38: Ensembl release 89: ENSG00000108773 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000020918 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Candau R, Moore PA, Wang L, Barlev N, Ying CY, Rosen CA, Berger SL (February 1996). "Identification of human proteins functionally conserved with the yeast putative adaptors ADA2 and GCN5". Mol Cell Biol. 16 (2): 593–602. doi:10.1128/mcb.16.2.593. PMC   231038 . PMID   8552087.
6. "Entrez Gene: GCN5L2 GCN5 general control of amino-acid synthesis 5-like 2 (yeast)".
7. Martinez E, Palhan VB, Tjernberg A, Lymar ES, Gamper AM, Kundu TK, Chait BT, Roeder RG (October 2001). "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 (20): 6782–95. doi:10.1128/MCB.21.20.6782-6795.2001. PMC   99856 . PMID   11564863.
8. Barlev NA, Poltoratsky V, Owen-Hughes T, Ying C, Liu L, Workman JL, Berger SL (March 1998). "Repression of GCN5 histone acetyltransferase activity via bromodomain-mediated binding and phosphorylation by the Ku-DNA-dependent protein kinase complex". Mol. Cell. Biol. 18 (3): 1349–58. doi:10.1128/mcb.18.3.1349. PMC   108848 . PMID   9488450.
9. Wang L, Mizzen C, Ying C, Candau R, Barlev N, Brownell J, Allis CD, Berger SL (January 1997). "Histone acetyltransferase activity is conserved between yeast and human GCN5 and is required for complementation of growth and transcriptional activation". Mol. Cell. Biol. 17 (1): 519–27. doi:10.1128/mcb.17.1.519. PMC   231776 . PMID   8972232.
10. Brand M, Moggs JG, Oulad-Abdelghani M, Lejeune F, Dilworth FJ, Stevenin J, Almouzni G, Tora L (June 2001). "UV-damaged DNA-binding protein in the TFTC complex links DNA damage recognition to nucleosome acetylation". EMBO J. 20 (12): 3187–96. doi:10.1093/emboj/20.12.3187. PMC   150203 . PMID   11406595.

Further reading

• Berry R, Stevens TJ, Walter NA, Wilcox AS, Rubano T, Hopkins JA, Weber J, Goold R, Soares MB, Sikela JM (1995). "Gene-based sequence-tagged-sites (STSs) as the basis for a human gene map". Nat. Genet. 10 (4): 415–23. doi:10.1038/ng0895-415. PMID   7670491. S2CID   22277955.
• Yang XJ, Ogryzko VV, Nishikawa J, Howard BH, Nakatani Y (1996). "A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A". Nature. 382 (6589): 319–24. Bibcode:1996Natur.382..319Y. doi:10.1038/382319a0. PMID   8684459. S2CID   4328685.
• Wang L, Mizzen C, Ying C, Candau R, Barlev N, Brownell J, Allis CD, Berger SL (1997). "Histone acetyltransferase activity is conserved between yeast and human GCN5 and is required for complementation of growth and transcriptional activation". Mol. Cell. Biol. 17 (1): 519–27. doi:10.1128/mcb.17.1.519. PMC   231776 . PMID   8972232.
• Carter KC, Wang L, Shell BK, Zamir I, Berger SL, Moore PA (1997). "The human transcriptional adaptor genes TADA2L and GCN5L2 colocalize to chromosome 17q12-q21 and display a similar tissue expression pattern". Genomics. 40 (3): 497–500. doi:10.1006/geno.1996.4605. PMID   9073520.
• Barlev NA, Poltoratsky V, Owen-Hughes T, Ying C, Liu L, Workman JL, Berger SL (1998). "Repression of GCN5 histone acetyltransferase activity via bromodomain-mediated binding and phosphorylation by the Ku-DNA-dependent protein kinase complex". Mol. Cell. Biol. 18 (3): 1349–58. doi:10.1128/mcb.18.3.1349. PMC   108848 . PMID   9488450.
• Smith ER, Belote JM, Schiltz RL, Yang XJ, Moore PA, Berger SL, Nakatani Y, Allis CD (1998). "Cloning of Drosophila GCN5: conserved features among metazoan GCN5 family members". Nucleic Acids Res. 26 (12): 2948–54. doi:10.1093/nar/26.12.2948. PMC   147644 . PMID   9611240.
• Randhawa GS, Bell DW, Testa JR, Feinberg AP (1998). "Identification and mapping of human histone acetylation modifier gene homologues". Genomics. 51 (2): 262–9. doi: 10.1006/geno.1998.5370 . PMID   9722949.
• Xu W, Edmondson DG, Roth SY (1998). "Mammalian GCN5 and P/CAF acetyltransferases have homologous amino-terminal domains important for recognition of nucleosomal substrates". Mol. Cell. Biol. 18 (10): 5659–69. doi:10.1128/MCB.18.10.5659. PMC   109152 . PMID   9742083.
• Brand M, Yamamoto K, Staub A, Tora L (1999). "Identification of TATA-binding protein-free TAFII-containing complex subunits suggests a role in nucleosome acetylation and signal transduction". J. Biol. Chem. 274 (26): 18285–9. doi: 10.1074/jbc.274.26.18285 . PMID   10373431.
• McMahon SB, Wood MA, Cole MD (2000). "The essential cofactor TRRAP recruits the histone acetyltransferase hGCN5 to c-Myc". Mol. Cell. Biol. 20 (2): 556–62. doi:10.1128/MCB.20.2.556-562.2000. PMC   85131 . PMID   10611234.
• Kurooka H, Honjo T (2000). "Functional interaction between the mouse notch1 intracellular region and histone acetyltransferases PCAF and GCN5". J. Biol. Chem. 275 (22): 17211–20. doi: 10.1074/jbc.M000909200 . PMID   10747963.
• Hudson BP, Martinez-Yamout MA, Dyson HJ, Wright PE (2000). "Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain". J. Mol. Biol. 304 (3): 355–70. doi:10.1006/jmbi.2000.4207. PMID   11090279.
• Col E, Caron C, Seigneurin-Berny D, Gracia J, Favier A, Khochbin S (2001). "The histone acetyltransferase, hGCN5, interacts with and acetylates the HIV transactivator, Tat". J. Biol. Chem. 276 (30): 28179–84. doi: 10.1074/jbc.M101385200 . PMID   11384967.
• Brand M, Moggs JG, Oulad-Abdelghani M, Lejeune F, Dilworth FJ, Stevenin J, Almouzni G, Tora L (2001). "UV-damaged DNA-binding protein in the TFTC complex links DNA damage recognition to nucleosome acetylation". EMBO J. 20 (12): 3187–96. doi:10.1093/emboj/20.12.3187. PMC   150203 . PMID   11406595.
• Gangloff YG, Pointud JC, Thuault S, Carré L, Romier C, Muratoglu S, Brand M, Tora L, Couderc JL, Davidson I (2001). "The TFIID components human TAF(II)140 and Drosophila BIP2 (TAF(II)155) are novel metazoan homologues of yeast TAF(II)47 containing a histone fold and a PHD finger". Mol. Cell. Biol. 21 (15): 5109–21. doi:10.1128/MCB.21.15.5109-5121.2001. PMC   87236 . PMID   11438666.
• Martinez E, Palhan VB, Tjernberg A, Lymar ES, Gamper AM, Kundu TK, Chait BT, Roeder RG (2001). "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 (20): 6782–95. doi:10.1128/MCB.21.20.6782-6795.2001. PMC   99856 . PMID   11564863.
• Yanagisawa J, Kitagawa H, Yanagida M, Wada O, Ogawa S, Nakagomi M, Oishi H, Yamamoto Y, Nagasawa H, McMahon SB, Cole MD, Tora L, Takahashi N, Kato S (2002). "Nuclear receptor function requires a TFTC-type histone acetyl transferase complex". Mol. Cell. 9 (3): 553–62. doi: 10.1016/S1097-2765(02)00478-1 . PMID   11931763. (Retracted, see doi:10.1016/j.molcel.2014.04.017, PMID   24932468,  Retraction Watch . If this is an intentional citation to a retracted paper, please replace {{ retracted |...}} with {{ retracted |...|intentional=yes}}.)
• Brès V, Kiernan R, Emiliani S, Benkirane M (2002). "Tat acetyl-acceptor lysines are important for human immunodeficiency virus type-1 replication". J. Biol. Chem. 277 (25): 22215–21. doi: 10.1074/jbc.M201895200 . PMID   11956210.
• Col E, Gilquin B, Caron C, Khochbin S (2002). "Tat-controlled protein acetylation". J. Biol. Chem. 277 (40): 37955–60. doi: 10.1074/jbc.M206694200 . PMID   12154097.

External links

• FactorBook GCN5