HTATIP

HIV-1 Tat interagujući protein, 60 kDa
HIV-1 Tat interagujući protein, 60 kDa
	PDB prikaz baziran na 2ou2.
Dostupne strukture
	2ou2
Identifikatori
Simboli	HTATIP; ESA1; HTATIP1; PLIP; TIP; TIP60; cPLA2
Vanjski ID	OMIM: 601409 MGI: 1932051 HomoloGene: 4657 GeneCards: HTATIP Gene
Ontologija gena
Molekularna funkcija	• hromatinsko vezivanje; • aktivnost transkripcionog koaktivatora; • aktivnost histonske acetiltransferaze; • proteinsko vezivanje; • vezivanje jona cinka; • aktivnost aciltransferaze; • aktivnost transferaze; • vezivanje metalnih jona; • vezivanje androgenskoh receptora;
Celularna komponenta	• hromatin; • nukleus; • kompleks NuA4 histon acetiltransferaze;
Biološki proces	• regulacija ćelijskog rasta; • popravka prekida dvostruke spirale; • hromatinsko formiranje ili razlaganje; • transkripcija; • transkripcija od RNK polimeraznog II promotera; • hromatinska modifikacija; • histonska acetilacija; • signalni put androgenskog receptora; • pozitivna regulacija transkripcije, DNK-zavisna;
Pregled RNK izražavanja
	podaci
Ortolozi
Vrsta	Čovek
Entrez	10524
Ensembl	ENSG00000172977
UniProt	Q92993
RefSeq (mRNA)	NM_006388
RefSeq (protein)	NP_006379
Lokacija (UCSC)	Chr 11:; 65.24 - 65.24 Mb
PubMed pretraga	[1]

HTATIP, histonska acetiltransferaza KAT5, je enzim koji je kod čoveka kodiran KAT5 genom.^[1]^[2]

Protein kodiran ovim genom pripada MYST familiji histonskih acetil transferaza (HAT). On je bio originalno izolovan kao HIV-1 TAT-interaktivni protein. HAT proteini učestvuju u regulaciji hromatinskog remodelovanja, transkripciji i drugim nuklearnim procesima putem acetilacije histona i nehistonskih proteina. Ovaj protein je histonska acetilaza koja učestvuje u DNK popravci i apoptozi, i za nju se smatra da ima ulogu u prenosu signala. Alternativno splajsovanje ovog gena rezultuje u višestrukim transkriptnim varijantama.^[2]

Interakcije

Za HTATIP je bilo pokazano da interaguje sa HDAC7A,^[3] FANCD2,^[4] CREB1,^[5] ETV6,^[6] Mdm2,^[7] Myc,^[8] BCL3,^[9] androgenskim receptorom,^[10] endotelinskim receptorom tipa A^[11] i PLA2G4A.^[12]

Reference

^ Kamine J, Elangovan B, Subramanian T, Coleman D, Chinnadurai G (1996). „Identification of a cellular protein that specifically interacts with the essential cysteine region of the HIV-1 Tat transactivator”. Virology. 216 (2): 357—66. PMID 8607265. doi:10.1006/viro.1996.0071.
^ ^а ^б „Entrez Gene: HTATIP HIV-1 Tat interacting protein, 60kDa”.
^ Xiao, Hui; Chung Jin; et al. (2003). „Tip60 is a co-repressor for STAT3”. J. Biol. Chem. United States. 278 (13): 11197—204. ISSN 0021-9258. PMID 12551922. doi:10.1074/jbc.M210816200.
^ Hejna, James; Holtorf Megan; et al. (2008). „Tip60 is required for DNA interstrand cross-link repair in the Fanconi anemia pathway”. J. Biol. Chem. United States. 283 (15): 9844—51. ISSN 0021-9258. PMC 2398728  . PMID 18263878. doi:10.1074/jbc.M709076200.
^ Gavaravarapu, S; Kamine J (2000). „Tip60 inhibits activation of CREB protein by protein kinase A”. Biochem. Biophys. Res. Commun. UNITED STATES. 269 (3): 758—66. ISSN 0006-291X. PMID 10720489. doi:10.1006/bbrc.2000.2358.
^ Nordentoft, Iver; Jørgensen Poul (2003). „The acetyltransferase 60 kDa trans-acting regulatory protein of HIV type 1-interacting protein (Tip60) interacts with the translocation E26 transforming-specific leukaemia gene (TEL) and functions as a transcriptional co-repressor”. Biochem. J. England. 374 (Pt 1): 165—73. ISSN 0264-6021. PMC 1223570  . PMID 12737628. doi:10.1042/BJ20030087.
^ Legube, Gaëlle; Linares Laetitia K; et al. (2002). „Tip60 is targeted to proteasome-mediated degradation by Mdm2 and accumulates after UV irradiation”. EMBO J. England. 21 (7): 1704—12. ISSN 0261-4189. PMC 125958  . PMID 11927554. doi:10.1093/emboj/21.7.1704.
^ Frank, Scott R; Parisi Tiziana; et al. (2003). „MYC recruits the TIP60 histone acetyltransferase complex to chromatin”. EMBO Rep. England. 4 (6): 575—80. ISSN 1469-221X. PMC 1319201  . PMID 12776177. doi:10.1038/sj.embor.embor861.
^ Dechend, R; Hirano F; et al. (1999). „The Bcl-3 oncoprotein acts as a bridging factor between NF-kappaB/Rel and nuclear co-regulators”. Oncogene. ENGLAND. 18 (22): 3316—23. ISSN 0950-9232. PMID 10362352. doi:10.1038/sj.onc.1202717.
^ Gaughan, Luke; Logan Ian R; et al. (2002). „Tip60 and histone deacetylase 1 regulate androgen receptor activity through changes to the acetylation status of the receptor”. J. Biol. Chem. United States. 277 (29): 25904—13. ISSN 0021-9258. PMID 11994312. doi:10.1074/jbc.M203423200.
^ Lee, H J; Chun M; Kandror K V (2001). „Tip60 and HDAC7 interact with the endothelin receptor a and may be involved in downstream signaling”. J. Biol. Chem. United States. 276 (20): 16597—600. ISSN 0021-9258. PMID 11262386. doi:10.1074/jbc.C000909200.
^ Sheridan, A M; Force T; et al. (2001). „PLIP, a novel splice variant of Tip60, interacts with group IV cytosolic phospholipase A(2), induces apoptosis, and potentiates prostaglandin production”. Mol. Cell. Biol. United States. 21 (14): 4470—81. ISSN 0270-7306. PMC 87107  . PMID 11416127. doi:10.1128/MCB.21.14.4470-4481.2001.

Literatura

Doyon Y, Côté J (2004). „The highly conserved and multifunctional NuA4 HAT complex.”. Curr. Opin. Genet. Dev. 14 (2): 147—54. PMID 15196461. doi:10.1016/j.gde.2004.02.009.
Sapountzi V, Logan IR, Robson CN (2006). „Cellular functions of TIP60.”. Int. J. Biochem. Cell Biol. 38 (9): 1496—509. PMID 16698308. doi:10.1016/j.biocel.2006.03.003.
Maruyama K, Sugano S (1994). „Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.”. Gene. 138 (1-2): 171—4. PMID 8125298. doi:10.1016/0378-1119(94)90802-8.
Suzuki Y; Yoshitomo-Nakagawa K; Maruyama K; et al. (1997). „Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.”. Gene. 200 (1-2): 149—56. PMID 9373149. doi:10.1016/S0378-1119(97)00411-3.
Yamamoto T, Horikoshi M (1998). „Novel substrate specificity of the histone acetyltransferase activity of HIV-1-Tat interactive protein Tip60.”. J. Biol. Chem. 272 (49): 30595—8. PMID 9388189. doi:10.1074/jbc.272.49.30595.
Kimura A, Horikoshi M (1999). „Tip60 acetylates six lysines of a specific class in core histones in vitro.”. Genes Cells. 3 (12): 789—800. PMID 10096020. doi:10.1046/j.1365-2443.1998.00229.x.
Dechend R; Hirano F; Lehmann K; et al. (1999). „The Bcl-3 oncoprotein acts as a bridging factor between NF-kappaB/Rel and nuclear co-regulators.”. Oncogene. 18 (22): 3316—23. PMID 10362352. doi:10.1038/sj.onc.1202717.
Brady ME; Ozanne DM; Gaughan L; et al. (1999). „Tip60 is a nuclear hormone receptor coactivator.”. J. Biol. Chem. 274 (25): 17599—604. PMID 10364196. doi:10.1074/jbc.274.25.17599.
Creaven M; Hans F; Mutskov V; et al. (1999). „Control of the histone-acetyltransferase activity of Tip60 by the HIV-1 transactivator protein, Tat.”. Biochemistry. 38 (27): 8826—30. PMID 10393559. doi:10.1021/bi9907274.
Sliva D; Zhu YX; Tsai S; et al. (1999). „Tip60 interacts with human interleukin-9 receptor alpha-chain.”. Biochem. Biophys. Res. Commun. 263 (1): 149—55. PMID 10486269. doi:10.1006/bbrc.1999.1083.
Gavaravarapu S, Kamine J (2000). „Tip60 inhibits activation of CREB protein by protein kinase A.”. Biochem. Biophys. Res. Commun. 269 (3): 758—66. PMID 10720489. doi:10.1006/bbrc.2000.2358.
Husi H; Ward MA; Choudhary JS; et al. (2000). „Proteomic analysis of NMDA receptor-adhesion protein signaling complexes.”. Nat. Neurosci. 3 (7): 661—9. PMID 10862698. doi:10.1038/76615.
Ikura T; Ogryzko VV; Grigoriev M; et al. (2000). „Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis.”. Cell. 102 (4): 463—73. PMID 10966108. doi:10.1016/S0092-8674(00)00051-9.
Ran Q, Pereira-Smith OM (2001). „Identification of an alternatively spliced form of the Tat interactive protein (Tip60), Tip60(beta).”. Gene. 258 (1-2): 141—6. PMID 11111051. doi:10.1016/S0378-1119(00)00410-8.
Lee HJ, Chun M, Kandror KV (2001). „Tip60 and HDAC7 interact with the endothelin receptor a and may be involved in downstream signaling.”. J. Biol. Chem. 276 (20): 16597—600. PMID 11262386. doi:10.1074/jbc.C000909200.
Hlubek F; Löhberg C; Meiler J; et al. (2001). „Tip60 is a cell-type-specific transcriptional regulator.”. J. Biochem. 129 (4): 635—41. PMID 11275565.
Sheridan AM; Force T; Yoon HJ; et al. (2001). „PLIP, a novel splice variant of Tip60, interacts with group IV cytosolic phospholipase A(2), induces apoptosis, and potentiates prostaglandin production.”. Mol. Cell. Biol. 21 (14): 4470—81. PMC 87107  . PMID 11416127. doi:10.1128/MCB.21.14.4470-4481.2001.
Cao X, Südhof TC (2001). „A transcriptionally [correction of transcriptively] active complex of APP with Fe65 and histone acetyltransferase Tip60.”. Science. 293 (5527): 115—20. PMID 11441186. doi:10.1126/science.1058783.
Legube G; Linares LK; Lemercier C; et al. (2002). „Tip60 is targeted to proteasome-mediated degradation by Mdm2 and accumulates after UV irradiation.”. EMBO J. 21 (7): 1704—12. PMC 125958  . PMID 11927554. doi:10.1093/emboj/21.7.1704.

[pmid8607265-1] Kamine J, Elangovan B, Subramanian T, Coleman D, Chinnadurai G (1996). „Identification of a cellular protein that specifically interacts with the essential cysteine region of the HIV-1 Tat transactivator”. Virology. 216 (2): 357—66. PMID 8607265. doi:10.1006/viro.1996.0071.

[entrez-2] а ^б „Entrez Gene: HTATIP HIV-1 Tat interacting protein, 60kDa”.

[pmid12551922-3] Xiao, Hui; Chung Jin; et al. (2003). „Tip60 is a co-repressor for STAT3”. J. Biol. Chem. United States. 278 (13): 11197—204. ISSN 0021-9258. PMID 12551922. doi:10.1074/jbc.M210816200.

[pmid18263878-4] Hejna, James; Holtorf Megan; et al. (2008). „Tip60 is required for DNA interstrand cross-link repair in the Fanconi anemia pathway”. J. Biol. Chem. United States. 283 (15): 9844—51. ISSN 0021-9258. PMC 2398728  . PMID 18263878. doi:10.1074/jbc.M709076200.

[pmid10720489-5] Gavaravarapu, S; Kamine J (2000). „Tip60 inhibits activation of CREB protein by protein kinase A”. Biochem. Biophys. Res. Commun. UNITED STATES. 269 (3): 758—66. ISSN 0006-291X. PMID 10720489. doi:10.1006/bbrc.2000.2358.

[pmid12737628-6] Nordentoft, Iver; Jørgensen Poul (2003). „The acetyltransferase 60 kDa trans-acting regulatory protein of HIV type 1-interacting protein (Tip60) interacts with the translocation E26 transforming-specific leukaemia gene (TEL) and functions as a transcriptional co-repressor”. Biochem. J. England. 374 (Pt 1): 165—73. ISSN 0264-6021. PMC 1223570  . PMID 12737628. doi:10.1042/BJ20030087.

[pmid11927554-7] Legube, Gaëlle; Linares Laetitia K; et al. (2002). „Tip60 is targeted to proteasome-mediated degradation by Mdm2 and accumulates after UV irradiation”. EMBO J. England. 21 (7): 1704—12. ISSN 0261-4189. PMC 125958  . PMID 11927554. doi:10.1093/emboj/21.7.1704.

[pmid12776177-8] Frank, Scott R; Parisi Tiziana; et al. (2003). „MYC recruits the TIP60 histone acetyltransferase complex to chromatin”. EMBO Rep. England. 4 (6): 575—80. ISSN 1469-221X. PMC 1319201  . PMID 12776177. doi:10.1038/sj.embor.embor861.

[pmid10362352-9] Dechend, R; Hirano F; et al. (1999). „The Bcl-3 oncoprotein acts as a bridging factor between NF-kappaB/Rel and nuclear co-regulators”. Oncogene. ENGLAND. 18 (22): 3316—23. ISSN 0950-9232. PMID 10362352. doi:10.1038/sj.onc.1202717.

[pmid11994312-10] Gaughan, Luke; Logan Ian R; et al. (2002). „Tip60 and histone deacetylase 1 regulate androgen receptor activity through changes to the acetylation status of the receptor”. J. Biol. Chem. United States. 277 (29): 25904—13. ISSN 0021-9258. PMID 11994312. doi:10.1074/jbc.M203423200.

[pmid11262386-11] Lee, H J; Chun M; Kandror K V (2001). „Tip60 and HDAC7 interact with the endothelin receptor a and may be involved in downstream signaling”. J. Biol. Chem. United States. 276 (20): 16597—600. ISSN 0021-9258. PMID 11262386. doi:10.1074/jbc.C000909200.

[pmid11416127-12] Sheridan, A M; Force T; et al. (2001). „PLIP, a novel splice variant of Tip60, interacts with group IV cytosolic phospholipase A(2), induces apoptosis, and potentiates prostaglandin production”. Mol. Cell. Biol. United States. 21 (14): 4470—81. ISSN 0270-7306. PMC 87107  . PMID 11416127. doi:10.1128/MCB.21.14.4470-4481.2001.

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