Enzyme

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ID:2.1.1.43
Description:Histone-lysine N-methyltransferase.
Alternative Name: Protein-lysine N-methyltransferase.
Protein methyltransferase II.
Protein methylase III.
Protein methylase 3.
Cath: 1.10.10.1700; 1.10.1740.10; 1.10.1740.100; 1.10.260.170; 1.10.260.60; 1.10.30.10; 1.10.8.850; 1.20.5.4240; 3.30.160.60; 3.30.40.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.1.1.43
BRENDA Enzyme Link: BRENDA 2.1.1.43
KEGG Enzyme Link: KEGG2.1.1.43
BioCyc Enzyme Link: BioCyc 2.1.1.43
ExPASy Enzyme Link: ExPASy2.1.1.43
EC2PDB Enzyme Link: EC2PDB 2.1.1.43
ExplorEnz Enzyme Link: ExplorEnz 2.1.1.43
PRIAM enzyme-specific profiles Link: PRIAM 2.1.1.43
IntEnz Enzyme Link: IntEnz 2.1.1.43
MEDLINE Enzyme Link: MEDLINE 2.1.1.43
MSA:

2.1.1.43;

Phylogenetic Tree:

2.1.1.43;

Uniprot:
M-CSA:
RHEA:10024 L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine
RULE(radius=1) [*:1]-[NH2;+0:2].[*:3]-[S+;H0:4](-[*:5])-[CH3;+0:6]>>[*:1]-[NH;+0:2]-[CH3;+0:6].[*:3]-[S;H0;+0:4]-[*:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Solubilization and partial purification of protein methylase 3 from calf thymus nuclei.Paik WK, Kim S1970 Nov 255484460
Partial purification and characterization of a protein lysine methyltransferase from plasmodia of Physarum polycephalum.Venkatesan M, McManus IR1979 Nov 27391266
Structure of human SMYD2 protein reveals the basis of p53 tumor suppressor methylation.Wang L, Li L, Zhang H, Luo X, Dai J, Zhou S, Gu J, Zhu J, Atadja P, Lu C, Li E, Zhao K2011 Nov 421880715
The structure of NSD1 reveals an autoregulatory mechanism underlying histone H3K36 methylation.Qiao Q, Li Y, Chen Z, Wang M, Reinberg D, Xu RM2011 Mar 1121196496
Structural biology of human H3K9 methyltransferases.Wu H, Min J, Lunin VV, Antoshenko T, Dombrovski L, Zeng H, Allali-Hassani A, Campagna-Slater V, Vedadi M, Arrowsmith CH, Plotnikov AN, Schapira M2010 Jan 1120084102
Structural basis for the requirement of additional factors for MLL1 SET domain activity and recognition of epigenetic marks.Southall SM, Wong PS, Odho Z, Roe SM, Wilson JR2009 Jan 3019187761
Dynamic histone H3 methylation during gene induction: HYPB/Setd2 mediates all H3K36 trimethylation.Edmunds JW, Mahadevan LC, Clayton AL2008 Jan 2318157086
PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4 methyltransferase complex.Cho YW, Hong T, Hong S, Guo H, Yu H, Kim D, Guszczynski T, Dressler GR, Copeland TD, Kalkum M, Ge K2007 Jul 1317500065
Identification of the MLL2 complex as a coactivator for estrogen receptor alpha.Mo R, Rao SM, Zhu YJ2006 Jun 916603732
Structural basis for the methylation site specificity of SET7/9.Couture JF, Collazo E, Hauk G, Trievel RC2006 Feb16415881
The SET domain protein Metnase mediates foreign DNA integration and links integration to nonhomologous end-joining repair.Lee SH, Oshige M, Durant ST, Rasila KK, Williamson EA, Ramsey H, Kwan L, Nickoloff JA, Hromas R2005 Dec 1316332963
Histone methyltransferases G9a and GLP form heteromeric complexes and are both crucial for methylation of euchromatin at H3-K9.Tachibana M, Ueda J, Fukuda M, Takeda N, Ohta T, Iwanari H, Sakihama T, Kodama T, Hamakubo T, Shinkai Y2005 Apr 115774718
ASH1, a Drosophila trithorax group protein, is required for methylation of lysine 4 residues on histone H3.Byrd KN, Shearn A2003 Sep 3013679578
ALL-1 is a histone methyltransferase that assembles a supercomplex of proteins involved in transcriptional regulation.Nakamura T, Mori T, Tada S, Krajewski W, Rozovskaia T, Wassell R, Dubois G, Mazo A, Croce CM, Canaani E2002 Nov12453419
Drosophila enhancer of Zeste/ESC complexes have a histone H3 methyltransferase activity that marks chromosomal Polycomb sites.Czermin B, Melfi R, McCabe D, Seitz V, Imhof A, Pirrotta V2002 Oct 1812408863
Purification and functional characterization of SET8, a nucleosomal histone H4-lysine 20-specific methyltransferase.Fang J, Feng Q, Ketel CS, Wang H, Cao R, Xia L, Erdjument-Bromage H, Tempst P, Simon JA, Zhang Y2002 Jul 912121615
PR-Set7 is a nucleosome-specific methyltransferase that modifies lysine 20 of histone H4 and is associated with silent chromatin.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 D2002 Jun12086618
A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells.Ogawa H, Ishiguro K, Gaubatz S, Livingston DM, Nakatani Y2002 May 1012004135
Set domain-containing protein, G9a, is a novel lysine-preferring mammalian histone methyltransferase with hyperactivity and specific selectivity to lysines 9 and 27 of histone H3.Tachibana M, Sugimoto K, Fukushima T, Shinkai Y2001 Jul 611316813
Regulation of chromatin structure by site-specific histone H3 methyltransferases.Rea S, Eisenhaber F, O'Carroll D, Strahl BD, Sun ZW, Schmid M, Opravil S, Mechtler K, Ponting CP, Allis CD, Jenuwein T2000 Aug 1010949293