SETD7 explained

Histone-lysine N-methyltransferase SETD7 is an enzyme that in humans is encoded by the SETD7 gene.^{[1] [2] [3]}

Further reading

• Nagase T, Kikuno R, Hattori A, etal . Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro . DNA Res. . 7 . 6 . 347–55 . 2001 . 11214970 . 10.1093/dnares/7.6.347 . free .
• Wilson JR, Jing C, Walker PA, etal . Crystal structure and functional analysis of the histone methyltransferase SET7/9 . Cell . 111 . 1 . 105–15 . 2002 . 12372304 . 10.1016/S0092-8674(02)00964-9 . 14727763 . free .
• Jacobs SA, Harp JM, Devarakonda S, etal . The active site of the SET domain is constructed on a knot . Nat. Struct. Biol. . 9 . 11 . 833–8 . 2002 . 12389038 . 10.1038/nsb861 . 28718612 .
• Strausberg RL, Feingold EA, Grouse LH, etal . 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 . 2003 . 12477932 . 10.1073/pnas.242603899 . 139241 . 2002PNAS...9916899M . free .
• Kwon T, Chang JH, Kwak E, etal . Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9–AdoMet . EMBO J. . 22 . 2 . 292–303 . 2003 . 12514135 . 10.1093/emboj/cdg025 . 140100 .
• Xiao B, Jing C, Wilson JR, etal . Structure and catalytic mechanism of the human histone methyltransferase SET7/9 . Nature . 421 . 6923 . 652–6 . 2003 . 12540855 . 10.1038/nature01378 . 2003Natur.421..652X . 4423407 .
• Wysocka J, Myers MP, Laherty CD, etal . Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1 . Genes Dev. . 17 . 7 . 896–911 . 2003 . 12670868 . 10.1101/gad.252103 . 196026 .
• Kouskouti A, Scheer E, Staub A, etal . Gene-specific modulation of TAF10 function by SET9-mediated methylation . Mol. Cell . 14 . 2 . 175–82 . 2004 . 15099517 . 10.1016/S1097-2765(04)00182-0 . 10.1.1.320.8454 .
• Gerhard DS, Wagner L, Feingold EA, etal . The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) . Genome Res. . 14 . 10B . 2121–7 . 2004 . 15489334 . 10.1101/gr.2596504 . 528928 .
• Chuikov S, Kurash JK, Wilson JR, etal . Regulation of p53 activity through lysine methylation . Nature . 432 . 7015 . 353–60 . 2004 . 15525938 . 10.1038/nature03117 . 2004Natur.432..353C . 4398310 .
• Couture JF, Collazo E, Hauk G, Trievel RC . Structural basis for the methylation site specificity of SET7/9 . Nat. Struct. Mol. Biol. . 13 . 2 . 140–6 . 2006 . 16415881 . 10.1038/nsmb1045 . 38483056 .
• Hayakawa T, Ohtani Y, Hayakawa N, etal . RBP2 is an MRG15 complex component and down-regulates intragenic histone H3 lysine 4 methylation . Genes Cells . 12 . 6 . 811–26 . 2007 . 17573780 . 10.1111/j.1365-2443.2007.01089.x . 10003129 . free .

Notes and References

1. Nishioka K, Chuikov S, Sarma K, Erdjument-Bromage H, Allis CD, Tempst P, Reinberg D . Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation . Genes Dev . 16 . 4 . 479–89 . Feb 2002 . 11850410 . 155346 . 10.1101/gad.967202 .
2. Wang H, Cao R, Xia L, Erdjument-Bromage H, Borchers C, Tempst P, Zhang Y . Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase . Mol Cell . 8 . 6 . 1207–17 . Jan 2002 . 11779497 . 10.1016/S1097-2765(01)00405-1 . 37879139 . free .
3. Web site: SETD7 SET domain containing 7, histone lysine methyltransferase [Homo sapiens (human) ]].