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K(lysine) acetyltransferase 5
Protein HTATIP PDB 2ou2.png
PDB rendering based on 2ou2.
Available structures
PDB Ortholog search: PDBe, RCSB
External IDs OMIM601409 MGI1932051 HomoloGene100661 IUPHAR: 2664 ChEMBL: 5750 GeneCards: KAT5 Gene
EC number
RNA expression pattern
PBB GE HTATIP 206689 x at tn.png
PBB GE HTATIP 209192 x at tn.png
PBB GE HTATIP 214258 x at tn.png
More reference expression data
Species Human Mouse
Entrez 10524 81601
Ensembl ENSG00000172977 ENSMUSG00000024926
UniProt Q92993 Q8CHK4
RefSeq (mRNA) NM_001206833 NM_001199247
RefSeq (protein) NP_001193762 NP_001186176
Location (UCSC) Chr 11:
65.48 – 65.49 Mb
Chr 19:
5.6 – 5.61 Mb
PubMed search [1] [2]

Histone acetyltransferase KAT5 is an enzyme that in humans is encoded by the KAT5 gene.[1][2]


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.[2]


HTATIP has been shown to interact with:


  1. ^ Kamine J, Elangovan B, Subramanian T, Coleman D, Chinnadurai G (May 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. 
  2. ^ a b "Entrez Gene: HTATIP HIV-1 Tat interacting protein, 60kDa". 
  3. ^ Gaughan L, Logan IR, Cook S, Neal DE, Robson CN (July 2002). "Tip60 and histone deacetylase 1 regulate androgen receptor activity through changes to the acetylation status of the receptor". J. Biol. Chem. 277 (29): 25904–13. doi:10.1074/jbc.M203423200. PMID 11994312. 
  4. ^ Dechend R, Hirano F, Lehmann K, Heissmeyer V, Ansieau S, Wulczyn FG, Scheidereit C, Leutz A (June 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. 
  5. ^ Gavaravarapu S, Kamine J (March 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. 
  6. ^ Nordentoft I, Jørgensen P (August 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. 374 (Pt 1): 165–73. doi:10.1042/BJ20030087. PMC 1223570. PMID 12737628. 
  7. ^ Lee HJ, Chun M, Kandror KV (May 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. 
  8. ^ Hejna J, Holtorf M, Hines J, Mathewson L, Hemphill A, Al-Dhalimy M, Olson SB, Moses RE (April 2008). "Tip60 is required for DNA interstrand cross-link repair in the Fanconi anemia pathway". J. Biol. Chem. 283 (15): 9844–51. doi:10.1074/jbc.M709076200. PMC 2398728. PMID 18263878. 
  9. ^ Xiao H, Chung J, Kao HY, Yang YC (March 2003). "Tip60 is a co-repressor for STAT3". J. Biol. Chem. 278 (13): 11197–204. doi:10.1074/jbc.M210816200. PMID 12551922. 
  10. ^ Legube G, Linares LK, Lemercier C, Scheffner M, Khochbin S, Trouche D (April 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. PMC 125958. PMID 11927554. 
  11. ^ Frank SR, Parisi T, Taubert S, Fernandez P, Fuchs M, Chan HM, Livingston DM, Amati B (June 2003). "MYC recruits the TIP60 histone acetyltransferase complex to chromatin". EMBO Rep. 4 (6): 575–80. doi:10.1038/sj.embor.embor861. PMC 1319201. PMID 12776177. 
  12. ^ Sheridan AM, Force T, Yoon HJ, O'Leary E, Choukroun G, Taheri MR, Bonventre JV (July 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. PMC 87107. PMID 11416127. 

Further reading[edit]