CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019413
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Histone-lysine N-methyltransferase EHMT2 
Protein Synonyms/Alias
 Euchromatic histone-lysine N-methyltransferase 2; HLA-B-associated transcript 8; Histone H3-K9 methyltransferase 3; H3-K9-HMTase 3; Lysine N-methyltransferase 1C; Protein G9a 
Gene Name
 EHMT2 
Gene Synonyms/Alias
 BAT8; C6orf30; G9A; KMT1C; NG36 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
185PKVHRARKTMSKPGNmethylation[1, 2]
882ANPELRNKEGDTAWDubiquitination[3]
1047LQLYRTAKMGWGVRAubiquitination[4]
Reference
 [1] Protein lysine methyltransferase G9a acts on non-histone targets.
 Rathert P, Dhayalan A, Murakami M, Zhang X, Tamas R, Jurkowska R, Komatsu Y, Shinkai Y, Cheng X, Jeltsch A.
 Nat Chem Biol. 2008 Jun;4(6):344-6. [PMID: 18438403]
 [2] Update on activities at the Universal Protein Resource (UniProt) in 2013.
 e="String">UniProt Consortium.
 Nucleic Acids Res. 2013 Jan;41(Database issue):D43-7. [PMID: 23161681]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473
Functional Description
 Histone methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting HP1 proteins to methylated histones. Also mediates monomethylation of 'Lys-56' of histone H3 (H3K56me1) in G1 phase, leading to promote interaction between histone H3 and PCNA and regulating DNA replication. Also weakly methylates 'Lys-27' of histone H3 (H3K27me). Also required for DNA methylation, the histone methyltransferase activity is not required for DNA methylation, suggesting that these 2 activities function independently. Probably targeted to histone H3 by different DNA-binding proteins like E2F6, MGA, MAX and/or DP1. May also methylate histone H1. In addition to the histone methyltransferase activity, also methylates non-histone proteins: mediates dimethylation of 'Lys- 373' of p53/TP53. Also methylates CDYL, WIZ, ACIN1, DNMT1, HDAC1, ERCC6, KLF12 and itself. 
Sequence Annotation
 REPEAT 649 678 ANK 1.
 REPEAT 684 713 ANK 2.
 REPEAT 717 746 ANK 3.
 REPEAT 750 780 ANK 4.
 REPEAT 784 813 ANK 5.
 REPEAT 817 846 ANK 6.
 REPEAT 850 879 ANK 7.
 DOMAIN 972 1035 Pre-SET.
 DOMAIN 1038 1155 SET.
 DOMAIN 1164 1180 Post-SET.
 REGION 817 819 Histone H3K9me binding (By similarity).
 REGION 1048 1050 S-adenosyl-L-methionine binding.
 REGION 1074 1093 Interaction with histone H3 (By
 REGION 1112 1113 S-adenosyl-L-methionine binding.
 REGION 1154 1157 Interaction with histone H3 (By
 METAL 974 974 Zinc 1.
 METAL 974 974 Zinc 2.
 METAL 976 976 Zinc 1.
 METAL 980 980 Zinc 1.
 METAL 980 980 Zinc 3.
 METAL 985 985 Zinc 1.
 METAL 987 987 Zinc 2.
 METAL 1017 1017 Zinc 2.
 METAL 1017 1017 Zinc 3.
 METAL 1021 1021 Zinc 2.
 METAL 1023 1023 Zinc 3.
 METAL 1027 1027 Zinc 3.
 METAL 1115 1115 Zinc 4.
 METAL 1168 1168 Zinc 4.
 METAL 1170 1170 Zinc 4.
 METAL 1175 1175 Zinc 4.
 BINDING 1067 1067 Histone H3K9me (By similarity).
 BINDING 1085 1085 S-adenosyl-L-methionine.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 140 140 Phosphoserine.
 MOD_RES 173 173 Phosphoserine.
 MOD_RES 185 185 N6,N6,N6-trimethyllysine; by EHMT2;
 MOD_RES 185 185 N6,N6-dimethyllysine; by EHMT2;
 MOD_RES 232 232 Phosphoserine.
 MOD_RES 246 246 Phosphoserine.
 MOD_RES 413 413 Phosphoserine.
 MOD_RES 555 555 Phosphothreonine (By similarity).
 MOD_RES 569 569 Phosphoserine.
 MOD_RES 1204 1204 Phosphoserine.
 MOD_RES 1210 1210 Phosphothreonine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; ANK repeat; Chromatin regulator; Chromosome; Complete proteome; Metal-binding; Methylation; Methyltransferase; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; S-adenosyl-L-methionine; Transferase; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1210 AA 
Protein Sequence
MAAAAGAAAA AAAEGEAPAE MGALLLEKET RGATERVHGS LGDTPRSEET LPKATPDSLE 60
PAGPSSPASV TVTVGDEGAD TPVGATPLIG DESENLEGDG DLRGGRILLG HATKSFPSSP 120
SKGGSCPSRA KMSMTGAGKS PPSVQSLAMR LLSMPGAQGA AAAGSEPPPA TTSPEGQPKV 180
HRARKTMSKP GNGQPPVPEK RPPEIQHFRM SDDVHSLGKV TSDLAKRRKL NSGGGLSEEL 240
GSARRSGEVT LTKGDPGSLE EWETVVGDDF SLYYDSYSVD ERVDSDSKSE VEALTEQLSE 300
EEEEEEEEEE EEEEEEEEEE EEEDEESGNQ SDRSGSSGRR KAKKKWRKDS PWVKPSRKRR 360
KREPPRAKEP RGVNGVGSSG PSEYMEVPLG SLELPSEGTL SPNHAGVSND TSSLETERGF 420
EELPLCSCRM EAPKIDRISE RAGHKCMATE SVDGELSGCN AAILKRETMR PSSRVALMVL 480
CETHRARMVK HHCCPGCGYF CTAGTFLECH PDFRVAHRFH KACVSQLNGM VFCPHCGEDA 540
SEAQEVTIPR GDGVTPPAGT AAPAPPPLSQ DVPGRADTSQ PSARMRGHGE PRRPPCDPLA 600
DTIDSSGPSL TLPNGGCLSA VGLPLGPGRE ALEKALVIQE SERRKKLRFH PRQLYLSVKQ 660
GELQKVILML LDNLDPNFQS DQQSKRTPLH AAAQKGSVEI CHVLLQAGAN INAVDKQQRT 720
PLMEAVVNNH LEVARYMVQR GGCVYSKEED GSTCLHHAAK IGNLEMVSLL LSTGQVDVNA 780
QDSGGWTPII WAAEHKHIEV IRMLLTRGAD VTLTDNEENI CLHWASFTGS AAIAEVLLNA 840
RCDLHAVNYH GDTPLHIAAR ESYHDCVLLF LSRGANPELR NKEGDTAWDL TPERSDVWFA 900
LQLNRKLRLG VGNRAIRTEK IICRDVARGY ENVPIPCVNG VDGEPCPEDY KYISENCETS 960
TMNIDRNITH LQHCTCVDDC SSSNCLCGQL SIRCWYDKDG RLLQEFNKIE PPLIFECNQA 1020
CSCWRNCKNR VVQSGIKVRL QLYRTAKMGW GVRALQTIPQ GTFICEYVGE LISDAEADVR 1080
EDDSYLFDLD NKDGEVYCID ARYYGNISRF INHLCDPNII PVRVFMLHQD LRFPRIAFFS 1140
SRDIRTGEEL GFDYGDRFWD IKSKYFTCQC GSEKCKHSAE AIALEQSRLA RLDPHPELLP 1200
ELGSLPPVNT 1210 
Gene Ontology
 GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; ISS:UniProtKB.
 GO:0046976; F:histone methyltransferase activity (H3-K27 specific); ISS:UniProtKB.
 GO:0046974; F:histone methyltransferase activity (H3-K9 specific); ISS:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006306; P:DNA methylation; ISS:UniProtKB.
 GO:0010424; P:DNA methylation on cytosine within a CG sequence; IEA:Compara.
 GO:0009566; P:fertilization; IEA:Compara.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Compara.
 GO:0035265; P:organ growth; IEA:Compara.
 GO:0018027; P:peptidyl-lysine dimethylation; IDA:UniProtKB.
 GO:0006275; P:regulation of DNA replication; IMP:UniProtKB.
 GO:0007286; P:spermatid development; IEA:Compara.
 GO:0007130; P:synaptonemal complex assembly; IEA:Compara. 
Interpro
 IPR002110; Ankyrin_rpt.
 IPR020683; Ankyrin_rpt-contain_dom.
 IPR003616; Post-SET_dom.
 IPR007728; Pre-SET_dom.
 IPR003606; Pre-SET_Zn-bd_sub.
 IPR001214; SET_dom. 
Pfam
 PF00023; Ank
 PF05033; Pre-SET
 PF00856; SET 
SMART
 SM00248; ANK
 SM00508; PostSET
 SM00468; PreSET
 SM00317; SET 
PROSITE
 PS50297; ANK_REP_REGION
 PS50088; ANK_REPEAT
 PS50868; POST_SET
 PS50867; PRE_SET
 PS50280; SET 
PRINTS
 PR01415; ANKYRIN.