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词条 SETD7
释义

  1. References

  2. Further reading

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

1. ^{{cite journal | vauthors = Nishioka K, Chuikov S, Sarma K, Erdjument-Bromage H, Allis CD, Tempst P, Reinberg D | 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 |date=Feb 2002 | pmid = 11850410 | pmc = 155346 | doi = 10.1101/gad.967202 }}
2. ^{{cite journal | vauthors = Wang H, Cao R, Xia L, Erdjument-Bromage H, Borchers C, Tempst P, Zhang Y | title = Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase | journal = Mol Cell | volume = 8 | issue = 6 | pages = 1207–17 |date=Jan 2002 | pmid = 11779497 | pmc = | doi =10.1016/S1097-2765(01)00405-1 }}
3. ^{{cite web | title = Entrez Gene: SETD7 SET domain containing (lysine methyltransferase) 7| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=80854| accessdate = }}

Further reading

{{refbegin | 2}}
  • {{cite journal |vauthors=Nagase T, Kikuno R, Hattori A, etal |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=10.1093/dnares/7.6.347 }}
  • {{cite journal |vauthors=Wilson JR, Jing C, Walker PA, etal |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=10.1016/S0092-8674(02)00964-9 }}
  • {{cite journal |vauthors=Jacobs SA, Harp JM, Devarakonda S, etal |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 |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |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 | pmc=139241 }}
  • {{cite journal |vauthors=Kwon T, Chang JH, Kwak E, etal |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 | pmc=140100 }}
  • {{cite journal |vauthors=Xiao B, Jing C, Wilson JR, etal |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 |vauthors=Wysocka J, Myers MP, Laherty CD, etal |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 | pmc=196026 }}
  • {{cite journal |vauthors=Kouskouti A, Scheer E, Staub A, etal |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=10.1016/S1097-2765(04)00182-0 }}
  • {{cite journal |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |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 | pmc=528928 }}
  • {{cite journal |vauthors=Chuikov S, Kurash JK, Wilson JR, etal |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 | vauthors=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 |vauthors=Hayakawa T, Ohtani Y, Hayakawa N, etal |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 }}
{{refend}}{{PDB Gallery|geneid=80854}}{{gene-4-stub}}
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