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Overview

Uniprot IDQ9H9B1
Protein NameHistone-lysine N-methyltransferase EHMT1
Gene NameEHMT1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
199 PAPGADVKVHRARKT
219 VGLHAASKDPREVRE
231 VREARDHKEPKEEIN
239 EPKEEINKNISDFGR
317 RTVIEMFKSITHSTV
327 THSTVGSKGEKDLGA
439 KTDSPWIKPARKRRR
450 KRRRRSRKKPSGALG
568 ELMRPSNKAPLLVLC

Function

Histone methyltransferase that specifically mono-, di- and trimethylates 'Lys-9' of histone H3 (H3K9me1, H3K9me2 and H3K9me3, respectively) in euchromatin (PubMed:12004135). H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting HP1 proteins to methylated histones (PubMed:12004135). Also weakly methylates 'Lys-27' of histone H3 (H3K27me) (PubMed:12004135). Also required for DNA methylation, the histone methyltransferase activity is not required for DNA methylation, suggesting that these 2 activities function independently (By similarity). Probably targeted to histone H3 by different DNA-binding proteins like E2F6, MGA, MAX and/or DP1 (PubMed:12004135). During G0 phase, it probably contributes to silencing of MYC- and E2F-responsive genes, suggesting a role in G0/G1 transition in cell cycle (PubMed:12004135). Involved in the differentiation of myoblastic precursors into brown adipose cells: following recruitment to chromatin by PRDM16, mediates formation of H3K9me2 and H3K9me3, inhibiting the expression of white adipose-selective genes (By similarity). Also involved in the differentiation of beige adipocytes from white adipose cells following recruitment by PRDM16 (By similarity). EHMT1 also promotes protein stabilization of PRDM16, by preventing PRDM16 ubiquitination and degradation (By similarity). In addition to the histone methyltransferase activity, also methylates non-histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53 (PubMed:20118233). Represses the expression of mitochondrial function-related genes, perhaps by occupying their promoter regions, working in concert with probable chromatin reader BAZ2B (By similarity)

Protein Sequence

10 MAAADAEAVP 20 ARGEPQQDCC 30 VKTELLGEET 40 PMAADEGSAE 50 KQAGEAHMAA 60 DGETNGSCEN 70 SDASSHANAA 80 KHTQDSARVN 90 PQDGTNTLTR 100 IAENGVSERD 110 SEAAKQNHVT 120 ADDFVQTSVI 130 GSNGYILNKP 140 ALQAQPLRTT 150 STLASSLPGH 160 AAKTLPGGAG 170 KGRTPSAFPQ 180 TPAAPPATLG 190 EGSADTEDRK 200 LPAPGADVKV 210 HRARKTMPKS 220 VVGLHAASKD 230 PREVREARDH 240 KEPKEEINKN 250 ISDFGRQQLL 260 PPFPSLHQSL 270 PQNQCYMATT 280 KSQTACLPFV 290 LAAAVSRKKK 300 RRMGTYSLVP 310 KKKTKVLKQR 320 TVIEMFKSIT 330 HSTVGSKGEK 340 DLGASSLHVN 350 GESLEMDSDE 360 DDSEELEEDD 370 GHGAEQAAAF 380 PTEDSRTSKE 390 SMSEADRAQK 400 MDGESEEEQE 410 SVDTGEEEEG 420 GDESDLSSES 430 SIKKKFLKRK 440 GKTDSPWIKP 450 ARKRRRRSRK 460 KPSGALGSES 470 YKSSAGSAEQ 480 TAPGDSTGYM 490 EVSLDSLDLR 500 VKGILSSQAE 510 GLANGPDVLE 520 TDGLQEVPLC 530 SCRMETPKSR 540 EITTLANNQC 550 MATESVDHEL 560 GRCTNSVVKY 570 ELMRPSNKAP 580 LLVLCEDHRG 590 RMVKHQCCPG 600 CGYFCTAGNF 610 MECQPESSIS 620 HRFHKDCASR 630 VNNASYCPHC 640 GEESSKAKEV 650 TIAKADTTST 660 VTPVPGQEKG 670 SALEGRADTT 680 TGSAAGPPLS 690 EDDKLQGAAS 700 HVPEGFDPTG 710 PAGLGRPTPG 720 LSQGPGKETL 730 ESALIALDSE 740 KPKKLRFHPK 750 QLYFSARQGE 760 LQKVLLMLVD 770 GIDPNFKMEH 780 QNKRSPLHAA 790 AEAGHVDICH 800 MLVQAGANID 810 TCSEDQRTPL 820 MEAAENNHLE 830 AVKYLIKAGA 840 LVDPKDAEGS 850 TCLHLAAKKG 860 HYEVVQYLLS 870 NGQMDVNCQD 880 DGGWTPMIWA 890 TEYKHVDLVK 900 LLLSKGSDIN 910 IRDNEENICL 920 HWAAFSGCVD 930 IAEILLAAKC 940 DLHAVNIHGD 950 SPLHIAAREN 960 RYDCVVLFLS 970 RDSDVTLKNK 980 EGETPLQCAS 990 LNSQVWSALQ 1000 MSKALQDSAP 1010 DRPSPVERIV 1020 SRDIARGYER 1030 IPIPCVNAVD 1040 SEPCPSNYKY 1050 VSQNCVTSPM 1060 NIDRNITHLQ 1070 YCVCIDDCSS 1080 SNCMCGQLSM 1090 RCWYDKDGRL 1100 LPEFNMAEPP 1110 LIFECNHACS 1120 CWRNCRNRVV 1130 QNGLRARLQL 1140 YRTRDMGWGV 1150 RSLQDIPPGT 1160 FVCEYVGELI 1170 SDSEADVREE 1180 DSYLFDLDNK 1190 DGEVYCIDAR 1200 FYGNVSRFIN 1210 HHCEPNLVPV 1220 RVFMAHQDLR 1230 FPRIAFFSTR 1240 LIEAGEQLGF 1250 DYGERFWDIK 1260 GKLFSCRCGS 1270 PKCRHSSAAL 1280 AQRQASAAQE 1290 AQEDGLPDTS SAAAADPL

Gene Ontology

Classification GO ID Description
Biological Process GO:0018027 peptidyl-lysine dimethylation
Biological Process GO:0018026 peptidyl-lysine monomethylation
Biological Process GO:0120162 positive regulation of cold-induced thermogenesis
Biological Process GO:0050821 protein stabilization
Biological Process GO:0045995 regulation of embryonic development
Biological Process GO:0060992 response to fungicide
Cellular Component GO:0000785 chromatin
Cellular Component GO:0016604 nuclear body
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0070742 C2H2 zinc finger domain binding
Molecular Function GO:0046976 histone H3K27 methyltransferase activity
Molecular Function GO:0140942 histone H3K9 dimethyltransferase activity
Molecular Function GO:0046974 histone H3K9 methyltransferase activity
Molecular Function GO:0140948 histone H3K9 monomethyltransferase activity
Molecular Function GO:0140949 histone H3K9 trimethyltransferase activity
Molecular Function GO:0140947 histone H3K9me2 methyltransferase activity
Molecular Function GO:0008168 methyltransferase activity
Molecular Function GO:0002039 p53 binding
Molecular Function GO:0016279 protein-lysine N-methyltransferase activity
Molecular Function GO:0001222 transcription corepressor binding
Molecular Function GO:0008270 zinc ion binding
Biological Process GO:0160274 beige fat cell differentiation
Biological Process GO:0050873 brown fat cell differentiation
Biological Process GO:0006325 chromatin organization
Biological Process GO:0006346 DNA methylation-dependent constitutive heterochromatin formation
Biological Process GO:0040029 epigenetic regulation of gene expression
Biological Process GO:0140718 facultative heterochromatin formation
Biological Process GO:0045892 negative regulation of DNA-templated transcription
Biological Process GO:0051148 negative regulation of muscle cell differentiation
Biological Process GO:0000122 negative regulation of transcription by RNA polymerase II
Biological Process GO:0160275 negative regulation of white fat cell differentiation

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[3] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[4] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[5] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.