Search Results

Overview

Uniprot IDQ96KQ7
Protein NameHistone-lysine N-methyltransferase EHMT2
Gene NameEHMT2
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
131 GSCPSRAKMSMTGAG
179 TSPEGQPKVHRARKT
219 DDVHSLGKVTSDLAK
226 KVTSDLAKRRKLNSG
229 SDLAKRRKLNSGGGL
348 KAKKKWRKDSPWVKP

Function

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 (PubMed:11316813, PubMed:20084102). 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 (PubMed:22387026). Also weakly methylates 'Lys-27' of histone H3 (H3K27me) (PubMed:11316813). 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. Also able to mono- and dimethylate histone H1-4 at 'Lys-26' (H1.4K26me1 and H1.4K26me2, respectively) (PubMed:19144645). In addition to the histone methyltransferase activity, also methylates non-histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53 (PubMed:20118233). Also methylates CDYL, WIZ, ACIN1, DNMT1, HDAC1, ERCC6, KLF12 and itself (PubMed:18438403)

Protein Sequence

10 MAAAAGAAAA 20 AAAEGEAPAE 30 MGALLLEKET 40 RGATERVHGS 50 LGDTPRSEET 60 LPKATPDSLE 70 PAGPSSPASV 80 TVTVGDEGAD 90 TPVGATPLIG 100 DESENLEGDG 110 DLRGGRILLG 120 HATKSFPSSP 130 SKGGSCPSRA 140 KMSMTGAGKS 150 PPSVQSLAMR 160 LLSMPGAQGA 170 AAAGSEPPPA 180 TTSPEGQPKV 190 HRARKTMSKP 200 GNGQPPVPEK 210 RPPEIQHFRM 220 SDDVHSLGKV 230 TSDLAKRRKL 240 NSGGGLSEEL 250 GSARRSGEVT 260 LTKGDPGSLE 270 EWETVVGDDF 280 SLYYDSYSVD 290 ERVDSDSKSE 300 VEALTEQLSE 310 EEEEEEEEEE 320 EEEEEEEEEE 330 EEEDEESGNQ 340 SDRSGSSGRR 350 KAKKKWRKDS 360 PWVKPSRKRR 370 KREPPRAKEP 380 RGVNGVGSSG 390 PSEYMEVPLG 400 SLELPSEGTL 410 SPNHAGVSND 420 TSSLETERGF 430 EELPLCSCRM 440 EAPKIDRISE 450 RAGHKCMATE 460 SVDGELSGCN 470 AAILKRETMR 480 PSSRVALMVL 490 CETHRARMVK 500 HHCCPGCGYF 510 CTAGTFLECH 520 PDFRVAHRFH 530 KACVSQLNGM 540 VFCPHCGEDA 550 SEAQEVTIPR 560 GDGVTPPAGT 570 AAPAPPPLSQ 580 DVPGRADTSQ 590 PSARMRGHGE 600 PRRPPCDPLA 610 DTIDSSGPSL 620 TLPNGGCLSA 630 VGLPLGPGRE 640 ALEKALVIQE 650 SERRKKLRFH 660 PRQLYLSVKQ 670 GELQKVILML 680 LDNLDPNFQS 690 DQQSKRTPLH 700 AAAQKGSVEI 710 CHVLLQAGAN 720 INAVDKQQRT 730 PLMEAVVNNH 740 LEVARYMVQR 750 GGCVYSKEED 760 GSTCLHHAAK 770 IGNLEMVSLL 780 LSTGQVDVNA 790 QDSGGWTPII 800 WAAEHKHIEV 810 IRMLLTRGAD 820 VTLTDNEENI 830 CLHWASFTGS 840 AAIAEVLLNA 850 RCDLHAVNYH 860 GDTPLHIAAR 870 ESYHDCVLLF 880 LSRGANPELR 890 NKEGDTAWDL 900 TPERSDVWFA 910 LQLNRKLRLG 920 VGNRAIRTEK 930 IICRDVARGY 940 ENVPIPCVNG 950 VDGEPCPEDY 960 KYISENCETS 970 TMNIDRNITH 980 LQHCTCVDDC 990 SSSNCLCGQL 1000 SIRCWYDKDG 1010 RLLQEFNKIE 1020 PPLIFECNQA 1030 CSCWRNCKNR 1040 VVQSGIKVRL 1050 QLYRTAKMGW 1060 GVRALQTIPQ 1070 GTFICEYVGE 1080 LISDAEADVR 1090 EDDSYLFDLD 1100 NKDGEVYCID 1110 ARYYGNISRF 1120 INHLCDPNII 1130 PVRVFMLHQD 1140 LRFPRIAFFS 1150 SRDIRTGEEL 1160 GFDYGDRFWD 1170 IKSKYFTCQC 1180 GSEKCKHSAE 1190 AIALEQSRLA 1200 RLDPHPELLP 1210 ELGSLPPVNT

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000785 chromatin
Cellular Component GO:0016607 nuclear speck
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0070742 C2H2 zinc finger domain binding
Molecular Function GO:0140189 H1-4K26 methyltransferase activity
Molecular Function GO:0046976 histone H3K27 methyltransferase activity
Molecular Function GO:0140759 histone H3K56 methyltransferase activity
Molecular Function GO:0046974 histone H3K9 methyltransferase activity
Molecular Function GO:0140948 histone H3K9 monomethyltransferase activity
Molecular Function GO:0002039 p53 binding
Molecular Function GO:1990841 promoter-specific chromatin binding
Molecular Function GO:0016279 protein-lysine N-methyltransferase activity
Molecular Function GO:0000977 RNA polymerase II transcription regulatory region sequence-specific DNA binding
Molecular Function GO:0001222 transcription corepressor binding
Molecular Function GO:0008270 zinc ion binding
Biological Process GO:0009267 cellular response to starvation
Biological Process GO:0030261 chromosome condensation
Biological Process GO:0006346 DNA methylation-dependent constitutive heterochromatin formation
Biological Process GO:0040029 epigenetic regulation of gene expression
Biological Process GO:0000122 negative regulation of transcription by RNA polymerase II
Biological Process GO:0018027 peptidyl-lysine dimethylation
Biological Process GO:0006275 regulation of DNA replication

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] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[5] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[6] 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.

[7] 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.