| 释义 |
- References
- Further reading
{{Infobox_gene}}N-lysine methyltransferase KMT5A is an enzyme that in humans is encoded by the KMT5A gene.[1][2][3][4] The enzyme is a histone methyltransferase, SET domain-containing and lysine-specific. The enzyme transfers one methyl group to histone H4 lysine residue at position 20. S-Adenosyl methionine (SAM) is both the cofactor and the methyl group donor. The lysine residue is converted to N6-methyllysine residue. This histone modification is often abbreviated H4K20me1: - H4 - type of histone
- K - symbol of lysine
- 20 - position of the lysine residue modified
- me - abbreviation for methyl group
- 1 - number of methyl groups transferred
References 1. ^{{cite journal | vauthors = Couture JF, Collazo E, Brunzelle JS, Trievel RC | title = Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase | journal = Genes & Development | volume = 19 | issue = 12 | pages = 1455–65 | date = June 2005 | pmid = 15933070 | pmc = 1151662 | doi = 10.1101/gad.1318405 }}
2. ^{{cite journal | vauthors = Nishioka K, Rice JC, Sarma K, Erdjument-Bromage H, Werner J, Wang Y, Chuikov S, Valenzuela P, Tempst P, Steward R, Lis JT, Allis CD, Reinberg D | title = PR-Set7 is a nucleosome-specific methyltransferase that modifies lysine 20 of histone H4 and is associated with silent chromatin | journal = Molecular Cell | volume = 9 | issue = 6 | pages = 1201–13 | date = June 2002 | pmid = 12086618 | pmc = | doi = 10.1016/S1097-2765(02)00548-8 }}
3. ^{{cite journal | vauthors = Fang J, Feng Q, Ketel CS, Wang H, Cao R, Xia L, Erdjument-Bromage H, Tempst P, Simon JA, Zhang Y | title = Purification and functional characterization of SET8, a nucleosomal histone H4-lysine 20-specific methyltransferase | journal = Current Biology | volume = 12 | issue = 13 | pages = 1086–99 | date = July 2002 | pmid = 12121615 | pmc = | doi = 10.1016/S0960-9822(02)00924-7 }}
4. ^{{cite web | title = Entrez Gene: KMT5A lysine methyltransferase 5A [ Homo sapiens (human) ]| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=387893| accessdate = }}
Further reading {{refbegin|33em}}{{PBB_Further_reading
| citations =- {{cite journal | vauthors = Mizzen CA, Yang XJ, Kokubo T, Brownell JE, Bannister AJ, Owen-Hughes T, Workman J, Wang L, Berger SL, Kouzarides T, Nakatani Y, Allis CD | title = The TAF(II)250 subunit of TFIID has histone acetyltransferase activity | journal = Cell | volume = 87 | issue = 7 | pages = 1261–70 | date = December 1996 | pmid = 8980232 | doi = 10.1016/S0092-8674(00)81821-8 }}
- {{cite journal | vauthors = Rice JC, Nishioka K, Sarma K, Steward R, Reinberg D, Allis CD | title = Mitotic-specific methylation of histone H4 Lys 20 follows increased PR-Set7 expression and its localization to mitotic chromosomes | journal = Genes & Development | volume = 16 | issue = 17 | pages = 2225–30 | date = September 2002 | pmid = 12208845 | pmc = 186671 | doi = 10.1101/gad.1014902 }}
- {{cite journal | vauthors = Schlisio S, Halperin T, Vidal M, Nevins JR | title = Interaction of YY1 with E2Fs, mediated by RYBP, provides a mechanism for specificity of E2F function | journal = The EMBO Journal | volume = 21 | issue = 21 | pages = 5775–86 | date = November 2002 | pmid = 12411495 | pmc = 131074 | doi = 10.1093/emboj/cdf577 }}
- {{cite journal | vauthors = Xiao B, Jing C, Wilson JR, Walker PA, Vasisht N, Kelly G, Howell S, Taylor IA, Blackburn GM, Gamblin SJ | title = Structure and catalytic mechanism of the human histone methyltransferase SET7/9 | journal = Nature | volume = 421 | issue = 6923 | pages = 652–6 | date = February 2003 | pmid = 12540855 | doi = 10.1038/nature01378 }}
- {{cite journal | vauthors = Xiao B, Jing C, Kelly G, Walker PA, Muskett FW, Frenkiel TA, Martin SR, Sarma K, Reinberg D, Gamblin SJ, Wilson JR | title = Specificity and mechanism of the histone methyltransferase Pr-Set7 | journal = Genes & Development | volume = 19 | issue = 12 | pages = 1444–54 | date = June 2005 | pmid = 15933069 | pmc = 1151661 | doi = 10.1101/gad.1315905 }}
- {{cite journal | vauthors = Yin Y, Liu C, Tsai SN, Zhou B, Ngai SM, Zhu G | title = SET8 recognizes the sequence RHRK20VLRDN within the N terminus of histone H4 and mono-methylates lysine 20 | journal = The Journal of Biological Chemistry | volume = 280 | issue = 34 | pages = 30025–31 | date = August 2005 | pmid = 15964846 | doi = 10.1074/jbc.M501691200 }}
- {{cite journal | vauthors = Shi X, Kachirskaia I, Yamaguchi H, West LE, Wen H, Wang EW, Dutta S, Appella E, Gozani O | title = Modulation of p53 function by SET8-mediated methylation at lysine 382 | journal = Molecular Cell | volume = 27 | issue = 4 | pages = 636–46 | date = August 2007 | pmid = 17707234 | pmc = 2693209 | doi = 10.1016/j.molcel.2007.07.012 }}
- {{cite journal | vauthors = Tanaka H, Takebayashi SI, Sakamoto A, Igata T, Nakatsu Y, Saitoh N, Hino S, Nakao M | title = The SETD8/PR-Set7 Methyltransferase Functions as a Barrier to Prevent Senescence-Associated Metabolic Remodeling | journal = Cell Reports | volume = 18 | issue = 9 | pages = 2148–2161 | date = February 2017 | pmid = 28249161| pmc = | doi = 10.1016/j.celrep.2017.02.021 }}
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