KAT2A

KAT2A
ساختارهای موجود
PDB	جستجوی هم‌ساخت‌شناسی: PDBe RCSB
فهرست شناسه‌های PDB
	1F68, 1Z4R, 3D7C, 5H86, 5H84
معین‌کننده‌ها
نام‌های دیگر	KAT2A, GCN5, GCN5L2, PCAF-b, hGCN5, lysine acetyltransferase 2A
شناسه‌های بیرونی	OMIM: 602301 MGI: 1343101 HomoloGene: 41343 GeneCards: KAT2A
موقعیت ژن (موش)
کروموزوم	کروموزوم ۱۱ (موش)
پایان	100,603,291 bp
الگوی گسترش RNA
	More reference expression data
هستی‌شناسی ژن
عملکرد ملکولی	• transferase activity; • GO:0001105 transcription coactivator activity; • N-acetyltransferase activity; • transcription factor binding; • histone deacetylase binding; • chromatin binding; • H3 histone acetyltransferase activity; • GO:0001948، GO:0016582 پیوند پروتئینی; • 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;
ترکیبات سلولی	• transcription factor TFTC complex; • نوکلئوپلاسم; • histone acetyltransferase complex; • mitotic spindle; • extracellular space; • هسته یاخته; • کروموزوم; • سیتوپلاسم; • میان‌تن; • microtubule organizing center; • اسکلت سلولی; • oxoglutarate dehydrogenase complex;
فرایند زیستی	• 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; • GO:0009373 regulation of transcription, DNA-templated; • regulation of protein stability; • GO:1904578 response to organic cyclic compound; • multicellular organism growth; • positive regulation of protein targeting to mitochondrion; • GO:0044324، GO:0003256، GO:1901213، GO:0046019، GO:0046020، GO:1900094، GO:0061216، GO:0060994، GO:1902064، GO:0003258، GO:0072212 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; • جنین‌شناسی دستگاه عصبی مرکزی; • 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; • تکثیر سلولی; • GO:0022415 viral process; • intracellular distribution of mitochondria; • histone H4-K12 acetylation; • alpha-tubulin acetylation; • midbrain development; • protein deubiquitination; • GO:0032617 cytokine production; • heart development; • حافظه بلندمدت; • internal peptidyl-lysine acetylation; • regulation of regulatory T cell differentiation; • GO:0003257، GO:0010735، GO:1901228، GO:1900622، GO:1904488 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;
	منابع: آمیگو / کوئیک‌گو
هم‌ساخت‌شناسی
	2648
	14534
	ENSG00000108773
	ENSMUSG00000020918
	Q92830
	Q9JHD2
	NM_021078، NM_001376227 XM_006721818، NM_021078، NM_001376227
	NM_020004، XM_017314270، XM_017314271، XM_017314272، XM_017314273، NR_166132، NR_166133 NM_001038010، NM_020004، XM_017314270، XM_017314271، XM_017314272، XM_017314273، NR_166132، NR_166133
	XP_006721881، XP_016879937، NP_001363156 NP_066564، XP_006721881، XP_016879937، NP_001363156
	NP_064388، XP_017169759، XP_017169760، XP_017169761، XP_017169762 NP_001033099، NP_064388، XP_017169759، XP_017169760، XP_017169761، XP_017169762
	ویکی‌داده
مشاهده/ویرایش انسان	مشاهده/ویرایش موش

هیستون استیل‌ترانسفراز KAT2A آنزیمی است که در انسان توسط ژن KAT2A کدگذاری می شود.^[۴]^[۵]

فعل و انفعالات[ویرایش]

مشخص شده است که این آنزیم با پروتئین های زیر تعامل پروتئین-پروتئین دارد:

DDB1،^[۶]
Ku70،^[۷]
Ku80،^[۷]
TADA2L،^[۷]^[۸]
TAF9،^[۶] و
Transcription initiation protein SPT3 homolog.^[۶]^[۹]

منابع[ویرایش]

↑ ^۱٫۰ ^۱٫۱ ^۱٫۲ GRCm38: Ensembl release 89: ENSMUSG00000020918 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ 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.
↑ "Entrez Gene: GCN5L2 GCN5 general control of amino-acid synthesis 5-like 2 (yeast)".
↑ ^۶٫۰ ^۶٫۱ ^۶٫۲ 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.
↑ ^۷٫۰ ^۷٫۱ ^۷٫۲ 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.
↑ 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.
↑ 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.

جهت مطالعه[ویرایش]

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. 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.
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.

پیوند به بیرون[ویرایش]

GCN5 در دانشنامهٔ اجزای دی‌ان‌ای

[refGRCm38Ensembl-1] ۱٫۰ ^۱٫۱ ^۱٫۲ GRCm38: Ensembl release 89: ENSMUSG00000020918 - Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[3] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid8552087-4] 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.

[entrez-5] "Entrez Gene: GCN5L2 GCN5 general control of amino-acid synthesis 5-like 2 (yeast)".

[pmid11564863-6] ۶٫۰ ^۶٫۱ ^۶٫۲ 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.

[pmid9488450-7] ۷٫۰ ^۷٫۱ ^۷٫۲ 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.

[pmid8972232-8] 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.

[pmid11406595-9] 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.

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