SETD7

SETD7

SET domain containing (lysine methyltransferase) 7, also known as SETD7, is a human gene.cite web | title = Entrez Gene: SETD7 SET domain containing (lysine methyltransferase) 7| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=80854| accessdate = ]

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References

Further reading

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*cite journal | author=Nagase T, Kikuno R, Hattori A, "et al." |title=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. |journal=DNA Res. |volume=7 |issue= 6 |pages= 347–55 |year= 2001 |pmid= 11214970 |doi=
*cite journal | author=Wang H, Cao R, Xia L, "et al." |title=Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase. |journal=Mol. Cell |volume=8 |issue= 6 |pages= 1207–17 |year= 2002 |pmid= 11779497 |doi=
*cite journal | author=Nishioka K, Chuikov S, Sarma K, "et al." |title=Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation. |journal=Genes Dev. |volume=16 |issue= 4 |pages= 479–89 |year= 2002 |pmid= 11850410 |doi= 10.1101/gad.967202
*cite journal | author=Wilson JR, Jing C, Walker PA, "et al." |title=Crystal structure and functional analysis of the histone methyltransferase SET7/9. |journal=Cell |volume=111 |issue= 1 |pages= 105–15 |year= 2002 |pmid= 12372304 |doi=
*cite journal | author=Jacobs SA, Harp JM, Devarakonda S, "et al." |title=The active site of the SET domain is constructed on a knot. |journal=Nat. Struct. Biol. |volume=9 |issue= 11 |pages= 833–8 |year= 2002 |pmid= 12389038 |doi= 10.1038/nsb861
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Kwon T, Chang JH, Kwak E, "et al." |title=Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet. |journal=EMBO J. |volume=22 |issue= 2 |pages= 292–303 |year= 2003 |pmid= 12514135 |doi= 10.1093/emboj/cdg025
*cite journal | author=Xiao B, Jing C, Wilson JR, "et al." |title=Structure and catalytic mechanism of the human histone methyltransferase SET7/9. |journal=Nature |volume=421 |issue= 6923 |pages= 652–6 |year= 2003 |pmid= 12540855 |doi= 10.1038/nature01378
*cite journal | author=Wysocka J, Myers MP, Laherty CD, "et al." |title=Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1. |journal=Genes Dev. |volume=17 |issue= 7 |pages= 896–911 |year= 2003 |pmid= 12670868 |doi= 10.1101/gad.252103
*cite journal | author=Kouskouti A, Scheer E, Staub A, "et al." |title=Gene-specific modulation of TAF10 function by SET9-mediated methylation. |journal=Mol. Cell |volume=14 |issue= 2 |pages= 175–82 |year= 2004 |pmid= 15099517 |doi=
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Chuikov S, Kurash JK, Wilson JR, "et al." |title=Regulation of p53 activity through lysine methylation. |journal=Nature |volume=432 |issue= 7015 |pages= 353–60 |year= 2004 |pmid= 15525938 |doi= 10.1038/nature03117
*cite journal | author=Couture JF, Collazo E, Hauk G, Trievel RC |title=Structural basis for the methylation site specificity of SET7/9. |journal=Nat. Struct. Mol. Biol. |volume=13 |issue= 2 |pages= 140–6 |year= 2006 |pmid= 16415881 |doi= 10.1038/nsmb1045
*cite journal | author=Hayakawa T, Ohtani Y, Hayakawa N, "et al." |title=RBP2 is an MRG15 complex component and down-regulates intragenic histone H3 lysine 4 methylation. |journal=Genes Cells |volume=12 |issue= 6 |pages= 811–26 |year= 2007 |pmid= 17573780 |doi= 10.1111/j.1365-2443.2007.01089.x

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