HTATIP

HIV-1 Tat interacting protein, 60kDa
PDB rendering based on 2ou2.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 2ou2​
Identifiers
Symbols	HTATIP ; ESA1; HTATIP1; PLIP; TIP; TIP60; cPLA2
External IDs	Template:OMIM5 Template:MGI HomoloGene: 4657
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

HIV-1 Tat interacting protein, 60kDa, also known as HTATIP, is a human gene.

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.

Further reading

• Doyon Y, Côté J (2004). "The highly conserved and multifunctional NuA4 HAT complex". Curr. Opin. Genet. Dev. 14 (2): 147–54. doi:10.1016/j.gde.2004.02.009. PMID 15196461.
• Sapountzi V, Logan IR, Robson CN (2006). "Cellular functions of TIP60". Int. J. Biochem. Cell Biol. 38 (9): 1496–509. doi:10.1016/j.biocel.2006.03.003. PMID 16698308.CS1 maint: Multiple names: authors list (link)
• 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.
• Kamine J, Elangovan B, Subramanian T; et al. (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. doi:10.1006/viro.1996.0071. PMID 8607265.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.
• 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.
• 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. doi:10.1038/sj.onc.1202717. PMID 10362352.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. doi:10.1021/bi9907274. PMID 10393559.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. doi:10.1006/bbrc.1999.1083. PMID 10486269.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Gavaravarapu S, Kamine J (2000). "Tip60 inhibits activation of CREB protein by protein kinase A.". Biochem. Biophys. Res. Commun. 269 (3): 758–66. doi:10.1006/bbrc.2000.2358. PMID 10720489.
• Husi H, Ward MA, Choudhary JS; et al. (2000). "Proteomic analysis of NMDA receptor-adhesion protein signaling complexes". Nat. Neurosci. 3 (7): 661–9. doi:10.1038/76615. PMID 10862698.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.
• 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. doi:10.1074/jbc.C000909200. PMID 11262386.CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. doi:10.1128/MCB.21.14.4470-4481.2001. PMID 11416127.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. doi:10.1126/science.1058783. PMID 11441186.
• 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. doi:10.1093/emboj/21.7.1704. PMID 11927554.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)