KAT5

K(lysine) acetyltransferase 5

PDB rendering based on 2ou2.
Identifiers
Symbols KAT5; ESA1; HTATIP; HTATIP1; PLIP; TIP; TIP60; cPLA2
External IDs OMIM: 601409 MGI: 1932051 HomoloGene: 100661 GeneCards: KAT5 Gene
EC number 2.3.1.48
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez 10524 81601
Ensembl ENSG00000172977 ENSMUSG00000024926
UniProt Q92993 Q3UJQ1
RefSeq (mRNA) NM_001206833.1 NM_178637
RefSeq (protein) NP_001193762.1 NP_848752
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]

Contents

Function

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]

Interactions

HTATIP has been shown to interact with HDAC7A,[3] FANCD2,[4] CREB1,[5] ETV6,[6] Mdm2,[7] Myc,[8] BCL3,[9] Androgen receptor,[10] Endothelin receptor type A[11] and PLA2G4A.[12]

References

  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". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10524. 
  3. ^ Xiao, Hui; Chung Jin, Kao Hung-Ying, Yang Yu-Chung (Mar. 2003). "Tip60 is a co-repressor for STAT3". J. Biol. Chem. (United States) 278 (13): 11197–204. doi:10.1074/jbc.M210816200. ISSN 0021-9258. PMID 12551922. 
  4. ^ Hejna, James; Holtorf Megan, Hines Jennie, Mathewson Lauren, Hemphill Aaron, Al-Dhalimy Muhsen, Olson Susan B, Moses Robb E (Apr. 2008). "Tip60 is required for DNA interstrand cross-link repair in the Fanconi anemia pathway". J. Biol. Chem. (United States) 283 (15): 9844–51. doi:10.1074/jbc.M709076200. ISSN 0021-9258. PMC 2398728. PMID 18263878. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2398728. 
  5. ^ Gavaravarapu, S; Kamine J (Mar. 2000). "Tip60 inhibits activation of CREB protein by protein kinase A". Biochem. Biophys. Res. Commun. (UNITED STATES) 269 (3): 758–66. doi:10.1006/bbrc.2000.2358. ISSN 0006-291X. PMID 10720489. 
  6. ^ Nordentoft, Iver; Jørgensen Poul (Aug. 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. doi:10.1042/BJ20030087. ISSN 0264-6021. PMC 1223570. PMID 12737628. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1223570. 
  7. ^ Legube, Gaëlle; Linares Laetitia K, Lemercier Claudie, Scheffner Martin, Khochbin Saadi, Trouche Didier (Apr. 2002). "Tip60 is targeted to proteasome-mediated degradation by Mdm2 and accumulates after UV irradiation". EMBO J. (England) 21 (7): 1704–12. doi:10.1093/emboj/21.7.1704. ISSN 0261-4189. PMC 125958. PMID 11927554. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=125958. 
  8. ^ Frank, Scott R; Parisi Tiziana, Taubert Stefan, Fernandez Paula, Fuchs Miriam, Chan Ho-Man, Livingston David M, Amati Bruno (Jun. 2003). "MYC recruits the TIP60 histone acetyltransferase complex to chromatin". EMBO Rep. (England) 4 (6): 575–80. doi:10.1038/sj.embor.embor861. ISSN 1469-221X. PMC 1319201. PMID 12776177. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1319201. 
  9. ^ Dechend, R; Hirano F, Lehmann K, Heissmeyer V, Ansieau S, Wulczyn F G, Scheidereit C, Leutz A (Jun. 1999). "The Bcl-3 oncoprotein acts as a bridging factor between NF-kappaB/Rel and nuclear co-regulators". Oncogene (ENGLAND) 18 (22): 3316–23. doi:10.1038/sj.onc.1202717. ISSN 0950-9232. PMID 10362352. 
  10. ^ Gaughan, Luke; Logan Ian R, Cook Susan, Neal David E, Robson Craig N (Jul. 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. doi:10.1074/jbc.M203423200. ISSN 0021-9258. PMID 11994312. 
  11. ^ Lee, H J; Chun M, Kandror K V (May. 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. doi:10.1074/jbc.C000909200. ISSN 0021-9258. PMID 11262386. 
  12. ^ Sheridan, A M; Force T, Yoon H J, O'Leary E, Choukroun G, Taheri M R, Bonventre J V (Jul. 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. doi:10.1128/MCB.21.14.4470-4481.2001. ISSN 0270-7306. PMC 87107. PMID 11416127. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=87107. 


Further reading