KEGG   ENZYME: 2.1.1.356Help
Entry
EC 2.1.1.356                Enzyme                                 

Name
[histone H3]-lysine27 N-trimethyltransferase;
KMT6A (gene name);
KMT6B (gene name);
EZH1 (gene name);
EZH2 (gene name)
Class
Transferases;
Transferring one-carbon groups;
Methyltransferases
BRITE hierarchy
Sysname
S-adenosyl-L-methionine:[histone H3]-L-lysine27 N6-methyltransferase
Reaction(IUBMB)
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine27 = 3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27 (overall reaction);
(1a) S-adenosyl-L-methionine + a [histone H3]-L-lysine27 = S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine27;
(1b) S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine27 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine27;
(1c) S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine27 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
Reaction(KEGG)
Substrate
S-adenosyl-L-methionine [CPD:C00019];
[histone H3]-L-lysine27;
[histone H3]-N6-methyl-L-lysine27;
[histone H3]-N6,N6-dimethyl-L-lysine27
Product
S-adenosyl-L-homocysteine [CPD:C00021];
[histone H3]-N6,N6,N6-trimethyl-L-lysine27;
[histone H3]-N6-methyl-L-lysine27;
[histone H3]-N6,N6-dimethyl-L-lysine27
Comment
This entry describes enzymes that successively methylate the L-lysine27 residue of histone H3 (H3K27), ultimately generating a trimethylated form. These modifications influence the binding of chromatin-associated proteins. The methylation of lysine27 leads to transcriptional repression of the affected target genes. The enzyme associates with other proteins to form a complex that is essential for activity. The enzyme can also methylate some non-histone proteins.
History
EC 2.1.1.356 created 1976 as EC 2.1.1.43, modified 1982, modified 1983, part transferred 2019 to EC 2.1.1.356
Pathway
ec00310  Lysine degradation
ec01100  Metabolic pathways
Orthology
K11430  [histone H3]-lysine27 N-trimethyltransferase EZH2
K17451  [histone H3]-lysine27 N-trimethyltransferase EZH1
Genes
HSA: 2145(EZH1) 2146(EZH2)
PTR: 454697(EZH1) 745437(EZH2)
PPS: 100967877(EZH1) 100971244(EZH2)
GGO: 101126515(EZH1) 101147968(EZH2)
PON: 100171872(EZH1) 100447447(EZH2)
NLE: 100604860(EZH1)
MCC: 709075(EZH2) 711173(EZH1)
MCF: 102130547(EZH1)
CSAB: 103243395(EZH1)
RRO: 104680126(EZH1)
RBB: 108526767(EZH1)
CJC: 100411881(EZH1)
SBQ: 101038203(EZH1)
MMU: 14055(Ezh1) 14056(Ezh2)
MCAL: 110304611(Ezh1)
MPAH: 110331872(Ezh1)
RNO: 303547(Ezh1) 312299(Ezh2)
MUN: 110550881(Ezh1)
CGE: 100760595(Ezh1)
NGI: 103735912(Ezh1)
HGL: 101723063(Ezh1)
CCAN: 109687337(Ezh1)
OCU: 100351852(EZH1)
TUP: 102485788(EZH1)
CFA: 475511(EZH2) 480516(EZH1)
VVP: 112910738(EZH1)
AML: 100466177(EZH2) 100472619(EZH1)
UMR: 103672584(EZH1)
UAH: 113265406(EZH1)
ORO: 101379551(EZH1)
ELK: 111151338
FCA: 101087309(EZH2) 101099602(EZH1)
PTG: 102961028(EZH1)
PPAD: 109258535(EZH1)
AJU: 106972615(EZH1)
BTA: 509106(EZH2) 533087(EZH1)
BOM: 102276653(EZH1)
BIU: 109573994(EZH1)
BBUB: 102407322(EZH1)
CHX: 102189343(EZH1)
OAS: 101104765(EZH1)
SSC: 100518394(EZH1) 100625497(EZH2)
CFR: 102516907(EZH1)
CDK: 105090473(EZH1)
LVE: 103073364(EZH1)
OOR: 101285746(EZH1)
DLE: 111166246(EZH1)
PCAD: 102994197(EZH1)
ECB: 100051290(EZH2) 100052411(EZH1)
EPZ: 103550351(EZH1)
EAI: 106826432(EZH1)
MYB: 102259730(EZH1)
MYD: 102755313(EZH1)
MNA: 107528927(EZH1)
HAI: 109395755(EZH1)
DRO: 112298572(EZH1)
PALE: 102879627(EZH1)
RAY: 107513838(EZH1)
MJV: 108386069(EZH1)
LAV: 100673691(EZH1)
TMU: 101360468
MDO: 100010738(EZH1) 100013390(EZH2)
SHR: 100926678(EZH2) 100932535(EZH1)
PCW: 110198374(EZH1)
OAA: 100073485(EZH2) 100082851(EZH1)
GGA: 420023(EZH1) 420784(EZH2)
MGP: 100540374(EZH2) 100547448(EZH1)
CJO: 107325326(EZH1)
NMEL: 110388515(EZH1)
APLA: 101791765(EZH1)
ACYG: 106048025(EZH1)
TGU: 100226728(EZH2) 100227472(EZH1)
LSR: 110471820(EZH1)
SCAN: 103821570(EZH1)
GFR: 102035477(EZH1)
FAB: 101811414(EZH1)
PHI: 102103576(EZH1)
PMAJ: 107215126(EZH1)
CCAE: 111940096(EZH1)
CCW: 104697765(EZH1)
ETL: 114063607(EZH1)
FPG: 101915579(EZH1)
FCH: 102052374(EZH1)
CLV: 102097006(EZH1)
EGZ: 104134781(EZH1)
NNI: 104009878(EZH1)
ACUN: 113489070
PADL: 103919098(EZH1)
AAM: 106491114(EZH1)
ASN: 102383438(EZH1)
AMJ: 102566481(EZH1)
PSS: 102463087(EZH1)
CMY: 102934538(EZH1)
CPIC: 101934118(EZH1)
ACS: 100559669(ezh1) 100564989(ezh2)
PVT: 110080273(EZH1)
PBI: 103052924(EZH1)
PMUR: 107302416(EZH1)
TSR: 106554239(EZH1)
PMUA: 114581626(EZH1)
GJA: 107123351(EZH1)
XLA: 100381148(ezh2.S) 108701022(ezh1.L) 108702719(ezh1.S) 399174(ezh2.L)
XTR: 100493532(ezh1) 550047(ezh2)
NPR: 108796324(EZH1)
DRE: 664754(ezh1) 768133(ezh2)
IPU: 108279279(ezh1)
PHYP: 113528051(ezh1)
AMEX: 103044086(ezh1)
EEE: 113590056
TRU: 101068728(ezh2) 101070195(ezh1)
LCO: 104923910(ezh1)
NCC: 104944052
MZE: 101474304(ezh1)
ONL: 100695015(ezh1)
OLA: 100125823(ezh2) 101166385(ezh1)
XMA: 102228014(ezh1)
XCO: 114160264(ezh1)
PRET: 103468644(ezh1) 103469387
CVG: 107091776(ezh1)
NFU: 107378461(ezh1)
KMR: 108243802(ezh1)
ALIM: 106528219(ezh1)
AOCE: 111564547(ezh1)
CSEM: 103393149(ezh1)
POV: 109634330(ezh1)
LCF: 108900993(ezh1)
SDU: 111217595(ezh1)
SLAL: 111660565(ezh1)
HCQ: 109508596
BPEC: 110166859(ezh1)
MALB: 109964204(ezh1)
SALP: 111980227
ELS: 105013194(ezh1)
LCM: 102364190(EZH1)
CIN: 100177449
SPU: 585842
DME: Dmel_CG6502(E(z))
DER: 6546346
DPE: 6601386
DWI: 6646360
AAG: 5577466
AME: 552235
NVI: 100113526
TCA: 659759
API: 100168406
CEL: CELE_R06A4.7(mes-2)
CBR: CBG11099(Cbr-mes-2)
BMY: Bm1_55060
HMG: 100201207
ATH: AT1G02580(MEA) AT2G23380(CLF) AT4G02020(SWN)
GMX: 100809840
FVE: 101314790
CSV: 101210052
RCU: 8267339
SLY: 100134891(EZ1)
DOSA: Os03t0307800-01(Os03g0307800)
SBI: 8083989
ZMA: 541955(mez3)
 » show all
Taxonomy
Reference
1  [PMID:12351676]
  Authors
Cao R, Wang L, Wang H, Xia L, Erdjument-Bromage H, Tempst P, Jones RS, Zhang Y
  Title
Role of histone H3 lysine 27 methylation in Polycomb-group silencing.
  Journal
Science 298:1039-43 (2002)
  Sequence
[hsa:2146]
Reference
2  [PMID:12435631]
  Authors
Kuzmichev A, Nishioka K, Erdjument-Bromage H, Tempst P, Reinberg D
  Title
Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein.
  Journal
Genes Dev 16:2893-905 (2002)
  Sequence
[hsa:2146]
Reference
3  [PMID:15231737]
  Authors
Kirmizis A, Bartley SM, Kuzmichev A, Margueron R, Reinberg D, Green R, Farnham PJ
  Title
Silencing of human polycomb target genes is associated with methylation of histone H3 Lys 27.
  Journal
Genes Dev 18:1592-605 (2004)
  Sequence
[hsa:2146]
Reference
4  [PMID:17200670]
  Authors
Schlesinger Y, Straussman R, Keshet I, Farkash S, Hecht M, Zimmerman J, Eden E, Yakhini Z, Ben-Shushan E, Reubinoff BE, Bergman Y, Simon I, Cedar H
  Title
Polycomb-mediated methylation on Lys27 of histone H3 pre-marks genes for de novo  methylation in cancer.
  Journal
Nat Genet 39:232-6 (2007)
  Sequence
[hsa:2146]
Reference
5  [PMID:19026780]
  Authors
Shen X, Liu Y, Hsu YJ, Fujiwara Y, Kim J, Mao X, Yuan GC, Orkin SH
  Title
EZH1 mediates methylation on histone H3 lysine 27 and complements EZH2 in maintaining stem cell identity and executing pluripotency.
  Journal
Mol Cell 32:491-502 (2008)
  Sequence
[mmu:14055 14056]
Reference
6  [PMID:21317239]
  Authors
Ezhkova E, Lien WH, Stokes N, Pasolli HA, Silva JM, Fuchs E
  Title
EZH1 and EZH2 cogovern histone H3K27 trimethylation and are essential for hair follicle homeostasis and wound repair.
  Journal
Genes Dev 25:485-98 (2011)
  Sequence
[mmu:14055 14056]
Other DBs
ExplorEnz - The Enzyme Database: 2.1.1.356
IUBMB Enzyme Nomenclature: 2.1.1.356
ExPASy - ENZYME nomenclature database: 2.1.1.356
BRENDA, the Enzyme Database: 2.1.1.356

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