SETD8

From Wikipedia, the free encyclopedia


SET domain containing (lysine methyltransferase) 8
PDB rendering based on 1zkk.
Available structures: 1zkk, 2bqz
Identifiers
Symbol(s) SETD8; PR-Set7; SET07; SET8
External IDs OMIM: 607240 MGI: 1915206 HomoloGene: 41372
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 387893 67956
Ensembl ENSG00000183955 ENSMUSG00000049327
Uniprot Q9NQR1 Q2YDW7
Refseq NM_020382 (mRNA)
NP_065115 (protein)		 NM_030241 (mRNA)
NP_084517 (protein)
Location Chr 12: 122.43 - 122.46 Mb Chr 5: 124.7 - 124.72 Mb
Pubmed search [1] [2]

SET domain containing (lysine methyltransferase) 8, also known as SETD8, is a human gene.[1]


[edit] References

  1. ^ Entrez Gene: SETD8 SET domain containing (lysine methyltransferase) 8.

[edit] Further reading

  • Mizzen CA, Yang XJ, Kokubo T, et al. (1997). "The TAF(II)250 subunit of TFIID has histone acetyltransferase activity.". Cell 87 (7): 1261–70. PMID 8980232. 
  • Nishioka K, Rice JC, Sarma K, et al. (2002). "PR-Set7 is a nucleosome-specific methyltransferase that modifies lysine 20 of histone H4 and is associated with silent chromatin.". Mol. Cell 9 (6): 1201–13. PMID 12086618. 
  • Fang J, Feng Q, Ketel CS, et al. (2003). "Purification and functional characterization of SET8, a nucleosomal histone H4-lysine 20-specific methyltransferase.". Curr. Biol. 12 (13): 1086–99. PMID 12121615. 
  • Rice JC, Nishioka K, Sarma K, et al. (2002). "Mitotic-specific methylation of histone H4 Lys 20 follows increased PR-Set7 expression and its localization to mitotic chromosomes.". Genes Dev. 16 (17): 2225–30. doi:10.1101/gad.1014902. PMID 12208845. 
  • Schlisio S, Halperin T, Vidal M, Nevins JR (2002). "Interaction of YY1 with E2Fs, mediated by RYBP, provides a mechanism for specificity of E2F function.". EMBO J. 21 (21): 5775–86. PMID 12411495. 
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932. 
  • Xiao B, Jing C, Wilson JR, et al. (2003). "Structure and catalytic mechanism of the human histone methyltransferase SET7/9.". Nature 421 (6923): 652–6. doi:10.1038/nature01378. PMID 12540855. 
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334. 
  • Xiao B, Jing C, Kelly G, et al. (2005). "Specificity and mechanism of the histone methyltransferase Pr-Set7.". Genes Dev. 19 (12): 1444–54. doi:10.1101/gad.1315905. PMID 15933069. 
  • Couture JF, Collazo E, Brunzelle JS, Trievel RC (2005). "Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase.". Genes Dev. 19 (12): 1455–65. doi:10.1101/gad.1318405. PMID 15933070. 
  • Yin Y, Liu C, Tsai SN, et al. (2005). "SET8 recognizes the sequence RHRK20VLRDN within the N terminus of histone H4 and mono-methylates lysine 20.". J. Biol. Chem. 280 (34): 30025–31. doi:10.1074/jbc.M501691200. PMID 15964846. 
  • Shi X, Kachirskaia I, Yamaguchi H, et al. (2007). "Modulation of p53 function by SET8-mediated methylation at lysine 382.". Mol. Cell 27 (4): 636–46. doi:10.1016/j.molcel.2007.07.012. PMID 17707234. 
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