Tag | Content |
---|
CPLM ID | CPLM-021544 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Histone-lysine N-methyltransferase EHMT1 |
Protein Synonyms/Alias | Euchromatic histone-lysine N-methyltransferase 1; Eu-HMTase1; G9a-like protein 1; GLP; GLP1; Histone H3-K9 methyltransferase 5; H3-K9-HMTase 5; Lysine N-methyltransferase 1D |
Gene Name | EHMT1 |
Gene Synonyms/Alias | EUHMTASE1; GLP; KIAA1876; KMT1D |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
---|
827 | EAVKYLIKAGALVDP | ubiquitination | [1] |
|
Reference | [1] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition. Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA. Mol Cell Proteomics. 2012 May;11(5):148-59. [ PMID: 22505724] |
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 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. During G0 phase, it probably contributes to silencing of MYC- and E2F-responsive genes, suggesting a role in G0/G1 transition in cell cycle. In addition to the histone methyltransferase activity, also methylates non- histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53. |
Sequence Annotation | REPEAT 737 766 ANK 1. REPEAT 772 801 ANK 2. REPEAT 805 834 ANK 3. REPEAT 838 868 ANK 4. REPEAT 872 901 ANK 5. REPEAT 905 934 ANK 6. REPEAT 938 967 ANK 7. REPEAT 971 1004 ANK 8. DOMAIN 1060 1123 Pre-SET. DOMAIN 1126 1243 SET. REGION 905 907 Histone H3K9me binding. REGION 1136 1138 S-adenosyl-L-methionine binding. REGION 1162 1181 Interaction with histone H3. REGION 1200 1201 S-adenosyl-L-methionine binding. REGION 1242 1245 Interaction with histone H3. METAL 1062 1062 Zinc 1. METAL 1062 1062 Zinc 2. METAL 1064 1064 Zinc 1. METAL 1068 1068 Zinc 1. METAL 1068 1068 Zinc 3. METAL 1073 1073 Zinc 1. METAL 1075 1075 Zinc 2. METAL 1105 1105 Zinc 2. METAL 1105 1105 Zinc 3. METAL 1109 1109 Zinc 2. METAL 1111 1111 Zinc 3. METAL 1115 1115 Zinc 3. METAL 1203 1203 Zinc 4. METAL 1256 1256 Zinc 4. METAL 1258 1258 Zinc 4. METAL 1263 1263 Zinc 4. BINDING 1155 1155 Histone H3K9me. BINDING 1173 1173 S-adenosyl-L-methionine. BINDING 1257 1257 S-adenosyl-L-methionine; via amide |
Keyword | 3D-structure; Alternative splicing; ANK repeat; Chromatin regulator; Chromosome; Complete proteome; Disease mutation; Mental retardation; Metal-binding; Methyltransferase; Nucleus; Polymorphism; Reference proteome; Repeat; S-adenosyl-L-methionine; Transferase; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1298 AA |
Protein Sequence | MAAADAEAVP ARGEPQQDCC VKTELLGEET PMAADEGSAE KQAGEAHMAA DGETNGSCEN 60 SDASSHANAA KHTQDSARVN PQDGTNTLTR IAENGVSERD SEAAKQNHVT ADDFVQTSVI 120 GSNGYILNKP ALQAQPLRTT STLASSLPGH AAKTLPGGAG KGRTPSAFPQ TPAAPPATLG 180 EGSADTEDRK LPAPGADVKV HRARKTMPKS VVGLHAASKD PREVREARDH KEPKEEINKN 240 ISDFGRQQLL PPFPSLHQSL PQNQCYMATT KSQTACLPFV LAAAVSRKKK RRMGTYSLVP 300 KKKTKVLKQR TVIEMFKSIT HSTVGSKGEK DLGASSLHVN GESLEMDSDE DDSEELEEDD 360 GHGAEQAAAF PTEDSRTSKE SMSEADRAQK MDGESEEEQE SVDTGEEEEG GDESDLSSES 420 SIKKKFLKRK GKTDSPWIKP ARKRRRRSRK KPSGALGSES YKSSAGSAEQ TAPGDSTGYM 480 EVSLDSLDLR VKGILSSQAE GLANGPDVLE TDGLQEVPLC SCRMETPKSR EITTLANNQC 540 MATESVDHEL GRCTNSVVKY ELMRPSNKAP LLVLCEDHRG RMVKHQCCPG CGYFCTAGNF 600 MECQPESSIS HRFHKDCASR VNNASYCPHC GEESSKAKEV TIAKADTTST VTPVPGQEKG 660 SALEGRADTT TGSAAGPPLS EDDKLQGAAS HVPEGFDPTG PAGLGRPTPG LSQGPGKETL 720 ESALIALDSE KPKKLRFHPK QLYFSARQGE LQKVLLMLVD GIDPNFKMEH QNKRSPLHAA 780 AEAGHVDICH MLVQAGANID TCSEDQRTPL MEAAENNHLE AVKYLIKAGA LVDPKDAEGS 840 TCLHLAAKKG HYEVVQYLLS NGQMDVNCQD DGGWTPMIWA TEYKHVDLVK LLLSKGSDIN 900 IRDNEENICL HWAAFSGCVD IAEILLAAKC DLHAVNIHGD SPLHIAAREN RYDCVVLFLS 960 RDSDVTLKNK EGETPLQCAS LNSQVWSALQ MSKALQDSAP DRPSPVERIV SRDIARGYER 1020 IPIPCVNAVD SEPCPSNYKY VSQNCVTSPM NIDRNITHLQ YCVCIDDCSS SNCMCGQLSM 1080 RCWYDKDGRL LPEFNMAEPP LIFECNHACS CWRNCRNRVV QNGLRARLQL YRTRDMGWGV 1140 RSLQDIPPGT FVCEYVGELI SDSEADVREE DSYLFDLDNK ISSA 1184 |
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:0009790; P:embryo development; ISS:UniProtKB. GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Compara. GO:0045892; P:negative regulation of transcription, DNA-dependent; ISS:UniProtKB. GO:0018027; P:peptidyl-lysine dimethylation; IDA:UniProtKB. GO:0018026; P:peptidyl-lysine monomethylation; ISS:UniProtKB. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |