EHMT1_HUMAN - dbPTM
EHMT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EHMT1_HUMAN
UniProt AC Q9H9B1
Protein Name Histone-lysine N-methyltransferase EHMT1
Gene Name EHMT1
Organism Homo sapiens (Human).
Sequence Length 1298
Subcellular Localization Nucleus. Chromosome. Associates with euchromatic regions.
Protein 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..
Protein Sequence MAAADAEAVPARGEPQQDCCVKTELLGEETPMAADEGSAEKQAGEAHMAADGETNGSCENSDASSHANAAKHTQDSARVNPQDGTNTLTRIAENGVSERDSEAAKQNHVTADDFVQTSVIGSNGYILNKPALQAQPLRTTSTLASSLPGHAAKTLPGGAGKGRTPSAFPQTPAAPPATLGEGSADTEDRKLPAPGADVKVHRARKTMPKSVVGLHAASKDPREVREARDHKEPKEEINKNISDFGRQQLLPPFPSLHQSLPQNQCYMATTKSQTACLPFVLAAAVSRKKKRRMGTYSLVPKKKTKVLKQRTVIEMFKSITHSTVGSKGEKDLGASSLHVNGESLEMDSDEDDSEELEEDDGHGAEQAAAFPTEDSRTSKESMSEADRAQKMDGESEEEQESVDTGEEEEGGDESDLSSESSIKKKFLKRKGKTDSPWIKPARKRRRRSRKKPSGALGSESYKSSAGSAEQTAPGDSTGYMEVSLDSLDLRVKGILSSQAEGLANGPDVLETDGLQEVPLCSCRMETPKSREITTLANNQCMATESVDHELGRCTNSVVKYELMRPSNKAPLLVLCEDHRGRMVKHQCCPGCGYFCTAGNFMECQPESSISHRFHKDCASRVNNASYCPHCGEESSKAKEVTIAKADTTSTVTPVPGQEKGSALEGRADTTTGSAAGPPLSEDDKLQGAASHVPEGFDPTGPAGLGRPTPGLSQGPGKETLESALIALDSEKPKKLRFHPKQLYFSARQGELQKVLLMLVDGIDPNFKMEHQNKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQMDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASLNSQVWSALQMSKALQDSAPDRPSPVERIVSRDIARGYERIPIPCVNAVDSEPCPSNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNCRNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNVSRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHSSAALAQRQASAAQEAQEDGLPDTSSAAAADPL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAAADAEAV
------CCCCCCCCC
23.7425489052
22SumoylationPQQDCCVKTELLGEE
CCCCCEEEEHHCCCC
23.5125114211
38PhosphorylationPMAADEGSAEKQAGE
CCCCCCCHHHHHHCC
31.0725159151
73PhosphorylationHANAAKHTQDSARVN
HHHHHHHCCCCCCCC
33.11-
85PhosphorylationRVNPQDGTNTLTRIA
CCCCCCCCCHHHHHH
33.0624173317
87PhosphorylationNPQDGTNTLTRIAEN
CCCCCCCHHHHHHHC
29.3728555341
110PhosphorylationAAKQNHVTADDFVQT
HHHHCCCCHHHHCCE
19.47-
129AcetylationSNGYILNKPALQAQP
CCCEEECCHHHCCCC
28.3726051181
140PhosphorylationQAQPLRTTSTLASSL
CCCCCCCHHHHHHCC
17.18-
142PhosphorylationQPLRTTSTLASSLPG
CCCCCHHHHHHCCCC
25.0122210691
145PhosphorylationRTTSTLASSLPGHAA
CCHHHHHHCCCCCHH
35.2022210691
146PhosphorylationTTSTLASSLPGHAAK
CHHHHHHCCCCCHHH
32.7322210691
153TrimethylationSLPGHAAKTLPGGAG
CCCCCHHHCCCCCCC
51.91-
153MethylationSLPGHAAKTLPGGAG
CCCCCHHHCCCCCCC
51.9124129315
164PhosphorylationGGAGKGRTPSAFPQT
CCCCCCCCCCCCCCC
30.2025159151
171PhosphorylationTPSAFPQTPAAPPAT
CCCCCCCCCCCCCCC
18.3528555341
178 (in isoform 2)Ubiquitination-40.8621890473
183PhosphorylationPATLGEGSADTEDRK
CCCCCCCCCCCCCCC
20.7628985074
190SumoylationSADTEDRKLPAPGAD
CCCCCCCCCCCCCCC
71.7628112733
199SumoylationPAPGADVKVHRARKT
CCCCCCCEEEECCCC
32.6328112733
208 (in isoform 2)Ubiquitination-30.8821890473
209UbiquitinationRARKTMPKSVVGLHA
ECCCCCCHHHHCHHH
45.0921906983
209 (in isoform 1)Ubiquitination-45.0921906983
219AcetylationVGLHAASKDPREVRE
HCHHHCCCCHHHHHH
68.0123749302
231SumoylationVREARDHKEPKEEIN
HHHHHHCCCCHHHHH
78.8528112733
234SumoylationARDHKEPKEEINKNI
HHHCCCCHHHHHHCC
69.90-
234SumoylationARDHKEPKEEINKNI
HHHCCCCHHHHHHCC
69.9028112733
239UbiquitinationEPKEEINKNISDFGR
CCHHHHHHCCHHHHH
62.4121890473
239UbiquitinationEPKEEINKNISDFGR
CCHHHHHHCCHHHHH
62.4121890473
239 (in isoform 3)Ubiquitination-62.4121890473
272PhosphorylationCYMATTKSQTACLPF
CEECCCCCHHHHHHH
30.5827251275
274PhosphorylationMATTKSQTACLPFVL
ECCCCCHHHHHHHHH
26.8227251275
295PhosphorylationKKKRRMGTYSLVPKK
HHHHCCCCCCCCCCC
10.7028555341
297PhosphorylationKRRMGTYSLVPKKKT
HHCCCCCCCCCCCCC
23.8028555341
301AcetylationGTYSLVPKKKTKVLK
CCCCCCCCCCCHHHH
60.4630588383
302AcetylationTYSLVPKKKTKVLKQ
CCCCCCCCCCHHHHH
60.6530588389
303AcetylationYSLVPKKKTKVLKQR
CCCCCCCCCHHHHHH
60.7630588395
304PhosphorylationSLVPKKKTKVLKQRT
CCCCCCCCHHHHHHH
34.9517081983
305PhosphorylationLVPKKKTKVLKQRTV
CCCCCCCHHHHHHHH
55.2217081983
311PhosphorylationTKVLKQRTVIEMFKS
CHHHHHHHHHHHHHH
24.2828348404
312PhosphorylationKVLKQRTVIEMFKSI
HHHHHHHHHHHHHHH
3.6718669648
317SumoylationRTVIEMFKSITHSTV
HHHHHHHHHHCCCCC
39.3728112733
322PhosphorylationMFKSITHSTVGSKGE
HHHHHCCCCCCCCCC
19.0118669648
327SumoylationTHSTVGSKGEKDLGA
CCCCCCCCCCCCCCC
66.2228112733
327UbiquitinationTHSTVGSKGEKDLGA
CCCCCCCCCCCCCCC
66.22-
335PhosphorylationGEKDLGASSLHVNGE
CCCCCCCCEEEECCC
31.4721406692
336PhosphorylationEKDLGASSLHVNGES
CCCCCCCEEEECCCC
23.2021406692
343PhosphorylationSLHVNGESLEMDSDE
EEEECCCCCCCCCCC
30.9118669648
348PhosphorylationGESLEMDSDEDDSEE
CCCCCCCCCCCCHHH
41.4025137130
353PhosphorylationMDSDEDDSEELEEDD
CCCCCCCHHHHHHCC
45.3425137130
372PhosphorylationEQAAAFPTEDSRTSK
HHHHCCCCCCCCCCH
46.0721406692
375PhosphorylationAAFPTEDSRTSKESM
HCCCCCCCCCCHHHH
31.0921406692
377PhosphorylationFPTEDSRTSKESMSE
CCCCCCCCCHHHHCH
48.37-
378PhosphorylationPTEDSRTSKESMSEA
CCCCCCCCHHHHCHH
33.0628985074
381PhosphorylationDSRTSKESMSEADRA
CCCCCHHHHCHHHHH
31.2028102081
383PhosphorylationRTSKESMSEADRAQK
CCCHHHHCHHHHHHH
38.6223401153
395PhosphorylationAQKMDGESEEEQESV
HHHCCCCCHHHHHCC
56.7025921289
401PhosphorylationESEEEQESVDTGEEE
CCHHHHHCCCCCCCC
25.6125921289
404PhosphorylationEEQESVDTGEEEEGG
HHHHCCCCCCCCCCC
44.3225921289
430UbiquitinationKKKFLKRKGKTDSPW
HHHHHHHCCCCCCCC
64.27-
432SumoylationKFLKRKGKTDSPWIK
HHHHHCCCCCCCCCH
52.79-
432MethylationKFLKRKGKTDSPWIK
HHHHHCCCCCCCCCH
52.79-
432SumoylationKFLKRKGKTDSPWIK
HHHHHCCCCCCCCCH
52.7928112733
433PhosphorylationFLKRKGKTDSPWIKP
HHHHCCCCCCCCCHH
50.8323927012
435PhosphorylationKRKGKTDSPWIKPAR
HHCCCCCCCCCHHHH
27.6323401153
439UbiquitinationKTDSPWIKPARKRRR
CCCCCCCHHHHHHHH
28.85-
448PhosphorylationARKRRRRSRKKPSGA
HHHHHHHHCCCCCCC
46.7920068231
451SumoylationRRRRSRKKPSGALGS
HHHHHCCCCCCCCCC
43.22-
451SumoylationRRRRSRKKPSGALGS
HHHHHCCCCCCCCCC
43.22-
453PhosphorylationRRSRKKPSGALGSES
HHHCCCCCCCCCCCC
45.6528985074
458PhosphorylationKPSGALGSESYKSSA
CCCCCCCCCCCCCCC
24.9922210691
460PhosphorylationSGALGSESYKSSAGS
CCCCCCCCCCCCCCC
39.2920068231
461PhosphorylationGALGSESYKSSAGSA
CCCCCCCCCCCCCCC
15.7322210691
463PhosphorylationLGSESYKSSAGSAEQ
CCCCCCCCCCCCCCC
19.7221406692
464PhosphorylationGSESYKSSAGSAEQT
CCCCCCCCCCCCCCC
32.2821406692
466PhosphorylationESYKSSAGSAEQTAP
CCCCCCCCCCCCCCC
29.3617525332
467PhosphorylationSYKSSAGSAEQTAPG
CCCCCCCCCCCCCCC
28.4821406692
471PhosphorylationSAGSAEQTAPGDSTG
CCCCCCCCCCCCCCC
26.7321406692
476PhosphorylationEQTAPGDSTGYMEVS
CCCCCCCCCCCEEEE
29.6421406692
477PhosphorylationQTAPGDSTGYMEVSL
CCCCCCCCCCEEEEH
36.7521406692
479PhosphorylationAPGDSTGYMEVSLDS
CCCCCCCCEEEEHHH
7.0921406692
483PhosphorylationSTGYMEVSLDSLDLR
CCCCEEEEHHHHHHH
17.1025849741
486PhosphorylationYMEVSLDSLDLRVKG
CEEEEHHHHHHHHHH
29.1321406692
492SumoylationDSLDLRVKGILSSQA
HHHHHHHHHHHHHHH
33.5228112733
496PhosphorylationLRVKGILSSQAEGLA
HHHHHHHHHHHCHHH
20.6226714015
497PhosphorylationRVKGILSSQAEGLAN
HHHHHHHHHHCHHHC
29.9317525332
511PhosphorylationNGPDVLETDGLQEVP
CCCCEECCCCCCCCC
31.0726714015
556PhosphorylationELGRCTNSVVKYELM
HHHHCCCCHHHHEEC
15.3321214269
559SumoylationRCTNSVVKYELMRPS
HCCCCHHHHEECCCC
30.7428112733
560PhosphorylationCTNSVVKYELMRPSN
CCCCHHHHEECCCCC
11.5921214269
568UbiquitinationELMRPSNKAPLLVLC
EECCCCCCCCEEEEE
56.57-
638UbiquitinationGEESSKAKEVTIAKA
CCCCCCCCEEEEEEC
57.35-
644SumoylationAKEVTIAKADTTSTV
CCEEEEEECCCCCCC
42.83-
644SumoylationAKEVTIAKADTTSTV
CCEEEEEECCCCCCC
42.8328112733
644UbiquitinationAKEVTIAKADTTSTV
CCEEEEEECCCCCCC
42.83-
647PhosphorylationVTIAKADTTSTVTPV
EEEEECCCCCCCCCC
27.7525850435
648PhosphorylationTIAKADTTSTVTPVP
EEEECCCCCCCCCCC
23.9725850435
649PhosphorylationIAKADTTSTVTPVPG
EEECCCCCCCCCCCC
23.9925850435
650PhosphorylationAKADTTSTVTPVPGQ
EECCCCCCCCCCCCC
26.7225850435
652PhosphorylationADTTSTVTPVPGQEK
CCCCCCCCCCCCCCC
20.7521815630
659SumoylationTPVPGQEKGSALEGR
CCCCCCCCCCCCCCC
50.7228112733
659UbiquitinationTPVPGQEKGSALEGR
CCCCCCCCCCCCCCC
50.72-
680PhosphorylationSAAGPPLSEDDKLQG
CCCCCCCCCCCCCCC
44.7628985074
684SumoylationPPLSEDDKLQGAASH
CCCCCCCCCCCHHHC
55.8428112733
708PhosphorylationPAGLGRPTPGLSQGP
CCCCCCCCCCCCCCC
28.7325159151
709 (in isoform 2)Ubiquitination-44.4021890473
729PhosphorylationSALIALDSEKPKKLR
HHHHHHCCCCCCCCC
48.6624667141
731SumoylationLIALDSEKPKKLRFH
HHHHCCCCCCCCCCC
67.1228112733
731UbiquitinationLIALDSEKPKKLRFH
HHHHCCCCCCCCCCC
67.12-
740UbiquitinationKKLRFHPKQLYFSAR
CCCCCCHHHHEEECC
44.3521890473
740AcetylationKKLRFHPKQLYFSAR
CCCCCCHHHHEEECC
44.3526051181
740UbiquitinationKKLRFHPKQLYFSAR
CCCCCCHHHHEEECC
44.3521890473
740 (in isoform 3)Ubiquitination-44.3521890473
796 (in isoform 2)Ubiquitination-11.3221890473
823UbiquitinationNNHLEAVKYLIKAGA
HCHHHHHHHHHHCCC
41.19-
827UbiquitinationEAVKYLIKAGALVDP
HHHHHHHHCCCCCCC
37.8721906983
827 (in isoform 1)Ubiquitination-37.8721906983
827 (in isoform 3)Ubiquitination-37.8721890473
852PhosphorylationLAAKKGHYEVVQYLL
HHHHCCHHHHHHHHH
21.0624043423
857PhosphorylationGHYEVVQYLLSNGQM
CHHHHHHHHHHCCCC
9.6724043423
860PhosphorylationEVVQYLLSNGQMDVN
HHHHHHHHCCCCCEE
36.0024043423
875PhosphorylationCQDDGGWTPMIWATE
CCCCCCCCCEEEEEE
13.2724043423
881PhosphorylationWTPMIWATEYKHVDL
CCCEEEEEECCCHHH
25.5024043423
883PhosphorylationPMIWATEYKHVDLVK
CEEEEEECCCHHHHH
11.3124043423
890UbiquitinationYKHVDLVKLLLSKGS
CCCHHHHHHHHHCCC
40.49890473
890 (in isoform 3)Ubiquitination-40.4921890473
895UbiquitinationLVKLLLSKGSDINIR
HHHHHHHCCCCCCCC
63.5021890473
895 (in isoform 3)Ubiquitination-63.5021890473
941PhosphorylationAVNIHGDSPLHIAAR
EEECCCCCHHHHHHC
33.6720873877
952PhosphorylationIAARENRYDCVVLFL
HHHCCCCCCEEEEEE
25.85-
968UbiquitinationRDSDVTLKNKEGETP
CCCCCEECCCCCCCC
57.5221906983
968 (in isoform 1)Ubiquitination-57.5221906983
998PhosphorylationMSKALQDSAPDRPSP
HHHHHHHCCCCCCCH
28.8329255136
1002MethylationLQDSAPDRPSPVERI
HHHCCCCCCCHHHHH
32.32-
1004PhosphorylationDSAPDRPSPVERIVS
HCCCCCCCHHHHHHH
42.3329255136
1018PhosphorylationSRDIARGYERIPIPC
HHHHHCCCCCCCCCC
9.1117081983
1040PhosphorylationPCPSNYKYVSQNCVT
CCCCCCCEECCCCCC
8.5821406692
1042PhosphorylationPSNYKYVSQNCVTSP
CCCCCEECCCCCCCC
16.7621406692
1047PhosphorylationYVSQNCVTSPMNIDR
EECCCCCCCCCCCCC
29.3430108239
1048PhosphorylationVSQNCVTSPMNIDRN
ECCCCCCCCCCCCCC
11.1823401153
1057PhosphorylationMNIDRNITHLQYCVC
CCCCCCCCCCCEEEE
21.7824043423
1061PhosphorylationRNITHLQYCVCIDDC
CCCCCCCEEEEEECC
8.0024043423
1069PhosphorylationCVCIDDCSSSNCMCG
EEEEECCCCCCCCCC
43.7424043423
1070PhosphorylationVCIDDCSSSNCMCGQ
EEEECCCCCCCCCCE
31.7224043423
1071PhosphorylationCIDDCSSSNCMCGQL
EEECCCCCCCCCCEE
20.1124043423
1079PhosphorylationNCMCGQLSMRCWYDK
CCCCCEEEEEEEECC
9.0424043423
1086UbiquitinationSMRCWYDKDGRLLPE
EEEEEECCCCCCCCC
46.52-
1228PhosphorylationFPRIAFFSTRLIEAG
CCHHEEEEHHHHHHH
13.2324114839
1276PhosphorylationALAQRQASAAQEAQE
HHHHHHHHHHHHHHH
18.7927251275

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of EHMT1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EHMT1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of EHMT1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRI15_HUMANTRIM15physical
20211142
CTBP1_HUMANCTBP1physical
16702210
CTBP2_HUMANCTBP2physical
16702210
P53_HUMANTP53physical
20588255
H31_HUMANHIST1H3Aphysical
20118233
P53_HUMANTP53physical
20118233
H31T_HUMANHIST3H3physical
12700765
TF65_HUMANRELAphysical
21131967
DNM3A_HUMANDNMT3Aphysical
22086334
EHMT1_HUMANEHMT1physical
22086334
MPP8_HUMANMPHOSPH8physical
22086334
PRDM6_HUMANPRDM6physical
16537907
DNLI1_HUMANLIG1physical
28803780
DNLI1_MOUSELig1physical
28803780

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
610253Kleefstra syndrome (KLESTS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EHMT1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-497, AND MASSSPECTROMETRY.

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