KEGG   ENZYME: 2.1.1.362Help
Entry
EC 2.1.1.362                Enzyme                                 

Name
[histone H4]-N-methyl-L-lysine20 N-methyltransferase;
KMT5B (gene name);
KMT5C (gene name);
SUV420H1 (gene name);
SUV420H2 (gene name)
Class
Transferases;
Transferring one-carbon groups;
Methyltransferases
BRITE hierarchy
Sysname
S-adenosyl-L-methionine:[histone H4]-N6-methyl-L-lysine20 N6-methyltransferase
Reaction(IUBMB)
S-adenosyl-L-methionine + a [histone H4]-N6-methyl-L-lysine20 = S-adenosyl-L-homocysteine + a [histone H4]-N6,N6-dimethyl-L-lysine20
Reaction(KEGG)
(other) R04866
Show
Substrate
S-adenosyl-L-methionine [CPD:C00019];
[histone H4]-N6-methyl-L-lysine20
Product
S-adenosyl-L-homocysteine [CPD:C00021];
[histone H4]-N6,N6-dimethyl-L-lysine20
Comment
This entry describes a group of enzymes that catalyse a single methylation of monomethylated lysine20 of histone H4 (H4K20m1, generated by EC 2.1.1.361, [histone H4]-lysine20 N-methyltransferase), forming the dimethylated form. This modification is broadly distributed across the genome and is likely important for general chromatin-mediated processes. The double-methylated form of lysine20 in histone H4 is the most abundant methylation state of this residue and is found on ~80% of all histone H4 molecules. Full activity of the enzyme requires that the lysine at position 9 of histone H3 is trimethylated.
History
EC 2.1.1.362 created 1976 as EC 2.1.1.43, modified 1982, modified 1983, part transferred 2019 to EC 2.1.1.362
Pathway
ec00310  Lysine degradation
ec01100  Metabolic pathways
Orthology
K11429  [histone H4]-N-methyl-L-lysine20 N-methyltransferase
Genes
HSA: 51111(KMT5B) 84787(KMT5C)
PTR: 451378(KMT5B) 735868(KMT5C)
PON: 100450271(KMT5B) 100450936(KMT5C)
MCC: 699963(KMT5C) 710481(KMT5B)
MMU: 225888(Kmt5b) 232811(Kmt5c)
RNO: 308345(Kmt5c) 361688(Kmt5b)
CFA: 483690(KMT5B) 484295(KMT5C)
AML: 100468595(KMT5B) 100478438(KMT5C)
BTA: 519777(KMT5C) 767828(KMT5B)
SSC: 100521358(KMT5B) 110261054(KMT5C)
ECB: 100053438(KMT5B) 100055743(KMT5C)
MDO: 100010281(KMT5B)
SHR: 100917457(KMT5B)
OAA: 100088070(KMT5B) 114814778(KMT5C)
GGA: 101748081(KMT5C) 425119(KMT5B)
MGP: 100547012(KMT5B)
TGU: 100222904(KMT5B) 115491558(KMT5C)
XLA: 108697809(kmt5c.S) 444204(kmt5b.S) 495826(kmt5b.L) 779432(kmt5c.L)
XTR: 100038141(kmt5b) 100145748(kmt5c)
DRE: 569041(kmt5c) 572849(kmt5b)
CIN: 100186975
SPU: 583266
DME: Dmel_CG13363(Hmt4-20)
AME: 411906
BIM: 100742553
HST: 105183369
CFO: 105255356
NVI: 100122935
TCA: 663776
CEL: CELE_C32D5.5(set-4)
CBR: CBG02629(Cbr-set-4)
BMY: Bm1_06250
HMG: 100207998
NCR: NCU08551
MGR: MGG_07393
ANI: AN6147.2
ANG: ANI_1_476104(An12g03880)
SPO: SPCC4B3.12(set9)
CNE: CNC03710
CNB: CNBC3500
MGL: MGL_1066
 » show all
Taxonomy
Reference
1  [PMID:15145825]
  Authors
Schotta G, Lachner M, Sarma K, Ebert A, Sengupta R, Reuter G, Reinberg D, Jenuwein T
  Title
A silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatin.
  Journal
Genes Dev 18:1251-62 (2004)
DOI:10.1101/gad.300704
  Sequence
Reference
2  [PMID:23345616]
  Authors
Jorgensen S, Schotta G, Sorensen CS
  Title
Histone H4 lysine 20 methylation: key player in epigenetic regulation of genomic  integrity.
  Journal
Nucleic Acids Res 41:2797-806 (2013)
Reference
3  [PMID:24396869]
  Authors
Wu H, Siarheyeva A, Zeng H, Lam R, Dong A, Wu XH, Li Y, Schapira M, Vedadi M, Min J
  Title
Crystal structures of the human histone H4K20 methyltransferases SUV420H1 and SUV420H2.
  Journal
FEBS Lett 587:3859-68 (2013)
  Sequence
[hsa:51111 84787]
Reference
4  [PMID:24049080]
  Authors
Southall SM, Cronin NB, Wilson JR
  Title
A novel route to product specificity in the Suv4-20 family of histone H4K20 methyltransferases.
  Journal
Nucleic Acids Res 42:661-71 (2014)
  Sequence
Reference
5  [PMID:27105552]
  Authors
Weirich S, Kudithipudi S, Jeltsch A
  Title
Specificity of the SUV4-20H1 and SUV4-20H2 protein lysine methyltransferases and  methylation of novel substrates.
  Journal
J Mol Biol 428:2344-2358 (2016)
Other DBs
ExplorEnz - The Enzyme Database: 2.1.1.362
IUBMB Enzyme Nomenclature: 2.1.1.362
ExPASy - ENZYME nomenclature database: 2.1.1.362
BRENDA, the Enzyme Database: 2.1.1.362

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