HTATIP

HTATIP

HIV-1 Tat interacting protein, 60kDa, also known as HTATIP, is a human gene.cite web | title = Entrez Gene: HTATIP HIV-1 Tat interacting protein, 60kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10524| accessdate = ]

PBB_Summary
section_title =
summary_text = The protein encoded by this gene belongs to the MYST family of histone acetyl transferases (HATs) and was originally isolated as an HIV-1 TAT-interactive protein. HATs play important roles in regulating chromatin remodeling, transcription and other nuclear processes by acetylating histone and nonhistone proteins. This protein is a histone acetylase that has a role in DNA repair and apoptosis and is thought to play an important role in signal transduction. Alternative splicing of this gene results in multiple transcript variants.cite web | title = Entrez Gene: HTATIP HIV-1 Tat interacting protein, 60kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10524| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Doyon Y, Côté J |title=The highly conserved and multifunctional NuA4 HAT complex. |journal=Curr. Opin. Genet. Dev. |volume=14 |issue= 2 |pages= 147–54 |year= 2004 |pmid= 15196461 |doi= 10.1016/j.gde.2004.02.009
*cite journal | author=Sapountzi V, Logan IR, Robson CN |title=Cellular functions of TIP60. |journal=Int. J. Biochem. Cell Biol. |volume=38 |issue= 9 |pages= 1496–509 |year= 2006 |pmid= 16698308 |doi= 10.1016/j.biocel.2006.03.003
*cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=
*cite journal | author=Kamine J, Elangovan B, Subramanian T, "et al." |title=Identification of a cellular protein that specifically interacts with the essential cysteine region of the HIV-1 Tat transactivator. |journal=Virology |volume=216 |issue= 2 |pages= 357–66 |year= 1996 |pmid= 8607265 |doi= 10.1006/viro.1996.0071
*cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, "et al." |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=
*cite journal | author=Yamamoto T, Horikoshi M |title=Novel substrate specificity of the histone acetyltransferase activity of HIV-1-Tat interactive protein Tip60. |journal=J. Biol. Chem. |volume=272 |issue= 49 |pages= 30595–8 |year= 1998 |pmid= 9388189 |doi=
*cite journal | author=Kimura A, Horikoshi M |title=Tip60 acetylates six lysines of a specific class in core histones in vitro. |journal=Genes Cells |volume=3 |issue= 12 |pages= 789–800 |year= 1999 |pmid= 10096020 |doi=
*cite journal | author=Dechend R, Hirano F, Lehmann K, "et al." |title=The Bcl-3 oncoprotein acts as a bridging factor between NF-kappaB/Rel and nuclear co-regulators. |journal=Oncogene |volume=18 |issue= 22 |pages= 3316–23 |year= 1999 |pmid= 10362352 |doi= 10.1038/sj.onc.1202717
*cite journal | author=Brady ME, Ozanne DM, Gaughan L, "et al." |title=Tip60 is a nuclear hormone receptor coactivator. |journal=J. Biol. Chem. |volume=274 |issue= 25 |pages= 17599–604 |year= 1999 |pmid= 10364196 |doi=
*cite journal | author=Creaven M, Hans F, Mutskov V, "et al." |title=Control of the histone-acetyltransferase activity of Tip60 by the HIV-1 transactivator protein, Tat. |journal=Biochemistry |volume=38 |issue= 27 |pages= 8826–30 |year= 1999 |pmid= 10393559 |doi= 10.1021/bi9907274
*cite journal | author=Sliva D, Zhu YX, Tsai S, "et al." |title=Tip60 interacts with human interleukin-9 receptor alpha-chain. |journal=Biochem. Biophys. Res. Commun. |volume=263 |issue= 1 |pages= 149–55 |year= 1999 |pmid= 10486269 |doi= 10.1006/bbrc.1999.1083
*cite journal | author=Gavaravarapu S, Kamine J |title=Tip60 inhibits activation of CREB protein by protein kinase A. |journal=Biochem. Biophys. Res. Commun. |volume=269 |issue= 3 |pages= 758–66 |year= 2000 |pmid= 10720489 |doi= 10.1006/bbrc.2000.2358
*cite journal | author=Husi H, Ward MA, Choudhary JS, "et al." |title=Proteomic analysis of NMDA receptor-adhesion protein signaling complexes. |journal=Nat. Neurosci. |volume=3 |issue= 7 |pages= 661–9 |year= 2000 |pmid= 10862698 |doi= 10.1038/76615
*cite journal | author=Ikura T, Ogryzko VV, Grigoriev M, "et al." |title=Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis. |journal=Cell |volume=102 |issue= 4 |pages= 463–73 |year= 2000 |pmid= 10966108 |doi=
*cite journal | author=Ran Q, Pereira-Smith OM |title=Identification of an alternatively spliced form of the Tat interactive protein (Tip60), Tip60(beta). |journal=Gene |volume=258 |issue= 1-2 |pages= 141–6 |year= 2001 |pmid= 11111051 |doi=
*cite journal | author=Lee HJ, Chun M, Kandror KV |title=Tip60 and HDAC7 interact with the endothelin receptor a and may be involved in downstream signaling. |journal=J. Biol. Chem. |volume=276 |issue= 20 |pages= 16597–600 |year= 2001 |pmid= 11262386 |doi= 10.1074/jbc.C000909200
*cite journal | author=Hlubek F, Löhberg C, Meiler J, "et al." |title=Tip60 is a cell-type-specific transcriptional regulator. |journal=J. Biochem. |volume=129 |issue= 4 |pages= 635–41 |year= 2001 |pmid= 11275565 |doi=
*cite journal | author=Sheridan AM, Force T, Yoon HJ, "et al." |title=PLIP, a novel splice variant of Tip60, interacts with group IV cytosolic phospholipase A(2), induces apoptosis, and potentiates prostaglandin production. |journal=Mol. Cell. Biol. |volume=21 |issue= 14 |pages= 4470–81 |year= 2001 |pmid= 11416127 |doi= 10.1128/MCB.21.14.4470-4481.2001
*cite journal | author=Cao X, Südhof TC |title=A transcriptionally [correction of transcriptively] active complex of APP with Fe65 and histone acetyltransferase Tip60. |journal=Science |volume=293 |issue= 5527 |pages= 115–20 |year= 2001 |pmid= 11441186 |doi= 10.1126/science.1058783
*cite journal | author=Legube G, Linares LK, Lemercier C, "et al." |title=Tip60 is targeted to proteasome-mediated degradation by Mdm2 and accumulates after UV irradiation. |journal=EMBO J. |volume=21 |issue= 7 |pages= 1704–12 |year= 2002 |pmid= 11927554 |doi= 10.1093/emboj/21.7.1704

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