HTATIP

From Wikipedia, the free encyclopedia

HIV-1 Tat interacting protein, 60kDa

PDB rendering based on 2ou2.

Available structures: 2ou2

Identifiers

Symbol(s)

HTATIP; ESA1; HTATIP1; PLIP; TIP; TIP60; cPLA2

External IDs

OMIM: 601409 MGI: 1932051 HomoloGene: 4657

Gene ontology
Molecular Function:	• chromatin binding • transcription coactivator activity • histone acetyltransferase activity • protein binding • zinc ion binding • acyltransferase activity • transferase activity • metal ion binding • androgen receptor binding
Cellular Component:	• chromatin • nucleus • NuA4 histone acetyltransferase complex
Biological Process:	• regulation of cell growth • double-strand break repair • chromatin assembly or disassembly • transcription • transcription from RNA polymerase II promoter • chromatin modification • histone acetylation • androgen receptor signaling pathway • positive regulation of transcription, DNA-dependent

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_006388 (mRNA)
NP_006379 (protein)

NM_178637 (mRNA)
NP_848752 (protein)

Location

Chr 11: 65.24 - 65.24 Mb

Chr 19: 5.6 - 5.61 Mb

Pubmed search

[1]

[2]

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

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: HTATIP HIV-1 Tat interacting protein, 60kDa.

[edit] 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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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. doi:10.1128/MCB.21.14.4470-4481.2001. PMID 11416127.
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.