KMT5A

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1ZKK, 2BQZ, 3F9W, 3F9X, 3F9Y, 3F9Z, 4IJ8, 5HQ2

Identifiers

Aliases

KMT5A, PR-Set7, SET07, SET8, SETD8, lysine methyltransferase 5A

External IDs

MGI: 1915206 HomoloGene: 41372 GeneCards: KMT5A

EC number

2.1.1.43

Gene ontology
Molecular function	• protein-lysine N-methyltransferase activity • methyltransferase activity • transcription corepressor activity • p53 binding • protein binding • transferase activity • lysine N-methyltransferase activity • histone-lysine N-methyltransferase activity • histone methyltransferase activity (H4-K20 specific)
Cellular component	• nucleus • nucleoplasm • chromosome • cytosol
Biological process	• methylation • regulation of transcription, DNA-templated • peptidyl-lysine monomethylation • cell cycle • negative regulation of transcription from RNA polymerase II promoter • negative regulation of transcription, DNA-templated • cell division • transcription, DNA-templated • regulation of DNA damage response, signal transduction by p53 class mediator • histone lysine methylation • covalent chromatin modification • regulation of signal transduction by p53 class mediator • histone H4-K20 methylation
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


387893


67956

Ensembl


ENSG00000183955


ENSMUSG00000049327

UniProt


Q9NQR1


Q2YDW7

RefSeq (mRNA)


NM_020382 NM_001324504 NM_001324505 NM_001324506


NM_030241 NM_001310723 NM_001310725 NM_001310727

RefSeq (protein)


NP_001311433 NP_001311434 NP_001311435 NP_065115


NP_001297652 NP_001297654 NP_001297656 NP_084517

Location (UCSC)

Chr 12: 123.38 – 123.41 Mb

Chr 5: 124.44 – 124.46 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

N-lysine methyltransferase KMT5A is an enzyme that in humans is encoded by the KMT5A gene.^[3]^[4]^[5]^[6] 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.

Leftmost: side chain of lysine. Next: N⁶-methyllysine side chain.

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

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Couture JF, Collazo E, Brunzelle JS, Trievel RC (June 2005). "Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase". Genes & Development. 19 (12): 1455–65. PMC 1151662 . PMID 15933070. doi:10.1101/gad.1318405.
↑ 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 (June 2002). "PR-Set7 is a nucleosome-specific methyltransferase that modifies lysine 20 of histone H4 and is associated with silent chromatin". Molecular Cell. 9 (6): 1201–13. PMID 12086618. doi:10.1016/S1097-2765(02)00548-8.
↑ Fang J, Feng Q, Ketel CS, Wang H, Cao R, Xia L, Erdjument-Bromage H, Tempst P, Simon JA, Zhang Y (July 2002). "Purification and functional characterization of SET8, a nucleosomal histone H4-lysine 20-specific methyltransferase". Current Biology. 12 (13): 1086–99. PMID 12121615. doi:10.1016/S0960-9822(02)00924-7.
↑ "Entrez Gene: KMT5A lysine methyltransferase 5A [ Homo sapiens (human) ]".

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 (December 1996). "The TAF(II)250 subunit of TFIID has histone acetyltransferase activity". Cell. 87 (7): 1261–70. PMID 8980232. doi:10.1016/S0092-8674(00)81821-8.
Rice JC, Nishioka K, Sarma K, Steward R, Reinberg D, Allis CD (September 2002). "Mitotic-specific methylation of histone H4 Lys 20 follows increased PR-Set7 expression and its localization to mitotic chromosomes". Genes & Development. 16 (17): 2225–30. PMC 186671 . PMID 12208845. doi:10.1101/gad.1014902.
Schlisio S, Halperin T, Vidal M, Nevins JR (November 2002). "Interaction of YY1 with E2Fs, mediated by RYBP, provides a mechanism for specificity of E2F function". The EMBO Journal. 21 (21): 5775–86. PMC 131074 . PMID 12411495. doi:10.1093/emboj/cdf577.
Xiao B, Jing C, Wilson JR, Walker PA, Vasisht N, Kelly G, Howell S, Taylor IA, Blackburn GM, Gamblin SJ (February 2003). "Structure and catalytic mechanism of the human histone methyltransferase SET7/9". Nature. 421 (6923): 652–6. PMID 12540855. doi:10.1038/nature01378.
Xiao B, Jing C, Kelly G, Walker PA, Muskett FW, Frenkiel TA, Martin SR, Sarma K, Reinberg D, Gamblin SJ, Wilson JR (June 2005). "Specificity and mechanism of the histone methyltransferase Pr-Set7". Genes & Development. 19 (12): 1444–54. PMC 1151661 . PMID 15933069. doi:10.1101/gad.1315905.
Yin Y, Liu C, Tsai SN, Zhou B, Ngai SM, Zhu G (August 2005). "SET8 recognizes the sequence RHRK20VLRDN within the N terminus of histone H4 and mono-methylates lysine 20". The Journal of Biological Chemistry. 280 (34): 30025–31. PMID 15964846. doi:10.1074/jbc.M501691200.
Shi X, Kachirskaia I, Yamaguchi H, West LE, Wen H, Wang EW, Dutta S, Appella E, Gozani O (August 2007). "Modulation of p53 function by SET8-mediated methylation at lysine 382". Molecular Cell. 27 (4): 636–46. PMC 2693209 . PMID 17707234. doi:10.1016/j.molcel.2007.07.012.
Tanaka H, Takebayashi SI, Sakamoto A, Igata T, Nakatsu Y, Saitoh N, Hino S, Nakao M (February 2017). "The SETD8/PR-Set7 Methyltransferase Functions as a Barrier to Prevent Senescence-Associated Metabolic Remodeling". Cell Reports. 18 (9): 2148–2161. doi:10.1016/j.celrep.2017.02.021.

PDB gallery

1zkk: Crystal structure of hSET8 in ternary complex with H4 peptide (16-24) and AdoHcy

2bqz: CRYSTAL STRUCTURE OF A TERNARY COMPLEX OF THE HUMAN HISTONE METHYLTRANSFERASE PR-SET7 (ALSO KNOWN AS SET8)

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KMT5A

References

Further reading