Tag | Content |
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CPLM ID | CPLM-013578 |
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; Lysine N-methyltransferase 1D |
Gene Name | Ehmt1 |
Gene Synonyms/Alias | Euhmtase1; Glp; Kmt1d |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
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825 | DAVKYLIKAGAQVDP | ubiquitination | [1] |
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Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
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 735 764 ANK 1. REPEAT 770 799 ANK 2. REPEAT 803 832 ANK 3. REPEAT 836 866 ANK 4. REPEAT 870 899 ANK 5. REPEAT 903 932 ANK 6. REPEAT 936 965 ANK 7. REPEAT 969 1002 ANK 8. DOMAIN 1058 1121 Pre-SET. DOMAIN 1124 1241 SET. REGION 903 905 Histone H3K9me binding (By similarity). REGION 1134 1136 S-adenosyl-L-methionine binding (By REGION 1160 1179 Interaction with histone H3 (By REGION 1198 1199 S-adenosyl-L-methionine binding (By REGION 1240 1243 Interaction with histone H3 (By METAL 1060 1060 Zinc 1 (By similarity). METAL 1060 1060 Zinc 2 (By similarity). METAL 1062 1062 Zinc 1 (By similarity). METAL 1066 1066 Zinc 1 (By similarity). METAL 1066 1066 Zinc 3 (By similarity). METAL 1071 1071 Zinc 1 (By similarity). METAL 1073 1073 Zinc 2 (By similarity). METAL 1103 1103 Zinc 2 (By similarity). METAL 1103 1103 Zinc 3 (By similarity). METAL 1107 1107 Zinc 2 (By similarity). METAL 1109 1109 Zinc 3 (By similarity). METAL 1113 1113 Zinc 3 (By similarity). METAL 1201 1201 Zinc 4 (By similarity). METAL 1254 1254 Zinc 4 (By similarity). METAL 1256 1256 Zinc 4 (By similarity). METAL 1261 1261 Zinc 4 (By similarity). BINDING 1153 1153 Histone H3K9me (By similarity). BINDING 1171 1171 S-adenosyl-L-methionine (By similarity). BINDING 1255 1255 S-adenosyl-L-methionine; via amide |
Keyword | Alternative splicing; ANK repeat; Chromatin regulator; Chromosome; Complete proteome; Metal-binding; Methyltransferase; Nucleus; Reference proteome; Repeat; S-adenosyl-L-methionine; Transferase; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1296 AA |
Protein Sequence | MAAADAEQAV LAKQETKQDC CMKTELLRED TPMAADEGST EKQEGETPMA ADGETNGSCE 60 KSGDPSHLNA PKHTQENTRA SPQEGTNRVS RVAENGVSER DTEVGKQNHV TADDFMQTSV 120 IGSNGYFLNK PALQGQPLRT PNILTSSLPG HAAKTLPGGA SKCRTLSALP QTPTTAPTVP 180 GEGSADTEDR KPTASGTDVR VHRARKTMPK SILGLHAASK DHREVQDHKE PKEDINRNIS 240 ECGRQQLLPT FPALHQSLPQ NQCYMATTKS QTACLPFVLA AAVSRKKKRR MGTYSLVPKK 300 KTKVLKQRTV IEMFKSITHS TVGAKGEKAL DDSALHVNGE SLEMDSEDED SDELEDDEDH 360 GAEQAAAFPT EDSRTSKESM SETDRAAKMD GDSEEEQESP DTGEDEDGGD ESDLSSESSI 420 KKKFLKRRGK TDSPWIKPAR KRRRRSRKKP SSMLGSEACK SSPGSMEQAA LGDSAGYMEV 480 SLDSLDLRVR GILSSQTENE GLASGPDVLG TDGLQEVPLC SCRMETPKSR EISTLANNQC 540 MATESVDHEL GRCTNSVVKY ELMRPSNKAP LLVLCEDHRG RMVKHQCCPG CGYFCTAGNF 600 MECQPESSIS HRFHKDCASR VNNASYCPHC GEEASKAKEV TIAKADTTST VTLAPGQEKS 660 LAAEGRADTT TGSIAGAPED ERSQSTAPQA PECFDPAGPA GLVRPTSGLS QGPGKETLES 720 ALIALDSEKP KKLRFHPKQL YFSARQGELQ KVLLMLVDGI DPNFKMEHQS KRSPLHAAAE 780 AGHVDICHML VQAGANIDTC SEDQRTPLME AAENNHLDAV KYLIKAGAQV DPKDAEGSTC 840 LHLAAKKGHY DVVQYLLSNG QMDVNCQDDG GWTPMIWATE YKHVELVKLL LSKGSDINIR 900 DNEENICLHW AAFSGCVDIA EILLAAKCDL HAVNIHGDSP LHIAARENRY DCVVLFLSRD 960 SDVTLKNKEG ETPLQCASLS SQVWSALQMS KALRDSAPDK PVAVEKTVSR DIARGYERIP 1020 IPCVNAVDSE LCPTNYKYVS QNCVTSPMNI DRNITHLQYC VCVDDCSSST CMCGQLSMRC 1080 WYDKDGRLLP EFNMAEPPLI FECNHACSCW RNCRNRVVQN GLRARLQLYR TQDMGWGVRS 1140 LQDIPLGTFV CEYVGELISD SEADVREEDS YLFDLDNKDG EVYCIDARFY GNVSRFINHH 1200 CEPNLVPVRV FMSHQDLRFP RIAFFSTRLI QAGEQLGFDY GERFWDVKGK LFSCRCGSSK 1260 CRHSSAALAQ RQASAAQEPQ ENGLPDTSSA AAADPL 1296 |
Gene Ontology | GO:0005694; C:chromosome; IEA:UniProtKB-SubCell. GO:0005634; C:nucleus; IDA:UniProtKB. GO:0046976; F:histone methyltransferase activity (H3-K27 specific); IDA:UniProtKB. GO:0046974; F:histone methyltransferase activity (H3-K9 specific); IDA:UniProtKB. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0006306; P:DNA methylation; IDA:UniProtKB. GO:0009790; P:embryo development; IMP:UniProtKB. GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:MGI. GO:0018027; P:peptidyl-lysine dimethylation; IMP:UniProtKB. GO:0018026; P:peptidyl-lysine monomethylation; IMP:UniProtKB. |
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