KMT5A

N-lysine methyltransferase KMT5A is an enzyme that in humans is encoded by the KMT5A gene. 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.

KMT5A
Available structures PDB 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, PR/SET07
External IDs	OMIM: 607240 MGI: 1915206 HomoloGene: 41372 GeneCards: KMT5A
EC number	2.1.1.354
Gene location (Human) Chr. Chromosome 12 (human) Band 12q24.31 Start 123,384,132 bp End 123,409,353 bp
Gene location (Mouse) Chr. Chromosome 5 (mouse) Band 5|5 F Start 124,577,993 bp End 124,600,371 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in sural nerve right coronary artery thoracic aorta ascending aorta Achilles tendon right lobe of thyroid gland body of pancreas popliteal artery left lobe of thyroid gland left uterine tube Top expressed in pyloric antrum lip knee joint yolk sac cumulus cell secondary oocyte lacrimal gland esophagus ascending aorta right ventricle More reference expression data BioGPS More reference expression data
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 by RNA polymerase II 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 regulation of signal transduction by p53 class mediator histone H4-K20 methylation chromatin organization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 387893 67956 Ensembl ENSG00000183955 ENSMUSG00000049327 UniProt Q9NQR1 Q2YDW7 RefSeq (mRNA) NM_020382 NM_001324504 NM_001324505 NM_001324506 NM_001367386 NM_001367388 NM_001367389 NM_030241 NM_001310723 NM_001310725 NM_001310727 RefSeq (protein) NP_001311433 NP_001311434 NP_001311435 NP_065115 NP_001354315 NP_001354317 NP_001354318 NP_001297652 NP_001297654 NP_001297656 NP_084517 NP_001392317 NP_001392319 Location (UCSC) Chr 12: 123.38 – 123.41 Mb Chr 5: 124.58 – 124.6 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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

Further reading

• 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. doi:10.1016/S0092-8674(00)81821-8. PMID 8980232. S2CID 18409257.
• 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. doi:10.1101/gad.1014902. PMC 186671. PMID 12208845.
• 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. doi:10.1093/emboj/cdf577. PMC 131074. PMID 12411495.
• 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" (PDF). Nature. 421 (6923): 652–6. Bibcode:2003Natur.421..652X. doi:10.1038/nature01378. PMID 12540855. S2CID 4423407.
• 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. doi:10.1101/gad.1315905. PMC 1151661. PMID 15933069.
• 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. doi:10.1074/jbc.M501691200. PMID 15964846.
• 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. doi:10.1016/j.molcel.2007.07.012. PMC 2693209. PMID 17707234.
• 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. PMID 28249161.