DNMT1_HUMAN - dbPTM
DNMT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DNMT1_HUMAN
UniProt AC P26358
Protein Name DNA (cytosine-5)-methyltransferase 1
Gene Name DNMT1
Organism Homo sapiens (Human).
Sequence Length 1616
Subcellular Localization Nucleus .
Protein Description Methylates CpG residues. Preferentially methylates hemimethylated DNA. Associates with DNA replication sites in S phase maintaining the methylation pattern in the newly synthesized strand, that is essential for epigenetic inheritance. Associates with chromatin during G2 and M phases to maintain DNA methylation independently of replication. It is responsible for maintaining methylation patterns established in development. DNA methylation is coordinated with methylation of histones. Mediates transcriptional repression by direct binding to HDAC2. In association with DNMT3B and via the recruitment of CTCFL/BORIS, involved in activation of BAG1 gene expression by modulating dimethylation of promoter histone H3 at H3K4 and H3K9. Probably forms a corepressor complex required for activated KRAS-mediated promoter hypermethylation and transcriptional silencing of tumor suppressor genes (TSGs) or other tumor-related genes in colorectal cancer (CRC) cells. [PubMed: 24623306 Also required to maintain a transcriptionally repressive state of genes in undifferentiated embryonic stem cells (ESCs)]
Protein Sequence MPARTAPARVPTLAVPAISLPDDVRRRLKDLERDSLTEKECVKEKLNLLHEFLQTEIKNQLCDLETKLRKEELSEEGYLAKVKSLLNKDLSLENGAHAYNREVNGRLENGNQARSEARRVGMADANSPPKPLSKPRTPRRSKSDGEAKPEPSPSPRITRKSTRQTTITSHFAKGPAKRKPQEESERAKSDESIKEEDKDQDEKRRRVTSRERVARPLPAEEPERAKSGTRTEKEEERDEKEEKRLRSQTKEPTPKQKLKEEPDREARAGVQADEDEDGDEKDEKKHRSQPKDLAAKRRPEEKEPEKVNPQISDEKDEDEKEEKRRKTTPKEPTEKKMARAKTVMNSKTHPPKCIQCGQYLDDPDLKYGQHPPDAVDEPQMLTNEKLSIFDANESGFESYEALPQHKLTCFSVYCKHGHLCPIDTGLIEKNIELFFSGSAKPIYDDDPSLEGGVNGKNLGPINEWWITGFDGGEKALIGFSTSFAEYILMDPSPEYAPIFGLMQEKIYISKIVVEFLQSNSDSTYEDLINKIETTVPPSGLNLNRFTEDSLLRHAQFVVEQVESYDEAGDSDEQPIFLTPCMRDLIKLAGVTLGQRRAQARRQTIRHSTREKDRGPTKATTTKLVYQIFDTFFAEQIEKDDREDKENAFKRRRCGVCEVCQQPECGKCKACKDMVKFGGSGRSKQACQERRCPNMAMKEADDDEEVDDNIPEMPSPKKMHQGKKKKQNKNRISWVGEAVKTDGKKSYYKKVCIDAETLEVGDCVSVIPDDSSKPLYLARVTALWEDSSNGQMFHAHWFCAGTDTVLGATSDPLELFLVDECEDMQLSYIHSKVKVIYKAPSENWAMEGGMDPESLLEGDDGKTYFYQLWYDQDYARFESPPKTQPTEDNKFKFCVSCARLAEMRQKEIPRVLEQLEDLDSRVLYYSATKNGILYRVGDGVYLPPEAFTFNIKLSSPVKRPRKEPVDEDLYPEHYRKYSDYIKGSNLDAPEPYRIGRIKEIFCPKKSNGRPNETDIKIRVNKFYRPENTHKSTPASYHADINLLYWSDEEAVVDFKAVQGRCTVEYGEDLPECVQVYSMGGPNRFYFLEAYNAKSKSFEDPPNHARSPGNKGKGKGKGKGKPKSQACEPSEPEIEIKLPKLRTLDVFSGCGGLSEGFHQAGISDTLWAIEMWDPAAQAFRLNNPGSTVFTEDCNILLKLVMAGETTNSRGQRLPQKGDVEMLCGGPPCQGFSGMNRFNSRTYSKFKNSLVVSFLSYCDYYRPRFFLLENVRNFVSFKRSMVLKLTLRCLVRMGYQCTFGVLQAGQYGVAQTRRRAIILAAAPGEKLPLFPEPLHVFAPRACQLSVVVDDKKFVSNITRLSSGPFRTITVRDTMSDLPEVRNGASALEISYNGEPQSWFQRQLRGAQYQPILRDHICKDMSALVAARMRHIPLAPGSDWRDLPNIEVRLSDGTMARKLRYTHHDRKNGRSSSGALRGVCSCVEAGKACDPAARQFNTLIPWCLPHTGNRHNHWAGLYGRLEWDGFFSTTVTNPEPMGKQGRVLHPEQHRVVSVRECARSQGFPDTYRLFGNILDKHRQVGNAVPPPLAKAIGLEIKLCMLAKARESASAKIKEEEAAKD
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
5Phosphorylation---MPARTAPARVPT
---CCCCCCCCCCCC		38.8125367160
12PhosphorylationTAPARVPTLAVPAIS
CCCCCCCCCCCCCCC		25.2128555341
35PhosphorylationLKDLERDSLTEKECV
HHHHHHCCCCHHHHH		43.3325627689
37PhosphorylationDLERDSLTEKECVKE
HHHHCCCCHHHHHHH		49.3025627689
39AcetylationERDSLTEKECVKEKL
HHCCCCHHHHHHHHH		51.7026051181
43AcetylationLTEKECVKEKLNLLH
CCHHHHHHHHHHHHH		61.8726051181
45AcetylationEKECVKEKLNLLHEF
HHHHHHHHHHHHHHH		36.6425953088
45UbiquitinationEKECVKEKLNLLHEF
HHHHHHHHHHHHHHH		36.64-
49 (in isoform 3)Ubiquitination-3.3721890473
58AcetylationEFLQTEIKNQLCDLE
HHHHHHHHHHHCHHH		32.2026051181
58UbiquitinationEFLQTEIKNQLCDLE
HHHHHHHHHHHCHHH		32.20-
58 (in isoform 2)Ubiquitination-32.20-
67AcetylationQLCDLETKLRKEELS
HHCHHHHHHCHHHHC		36.6025953088
67UbiquitinationQLCDLETKLRKEELS
HHCHHHHHHCHHHHC		36.60-
70"N6,N6-dimethyllysine"DLETKLRKEELSEEG
HHHHHHCHHHHCCCC		67.01-
70AcetylationDLETKLRKEELSEEG
HHHHHHCHHHHCCCC		67.0126051181
70MethylationDLETKLRKEELSEEG
HHHHHHCHHHHCCCC		67.0118438403
70UbiquitinationDLETKLRKEELSEEG
HHHHHHCHHHHCCCC		67.01-
70 (in isoform 2)Ubiquitination-67.01-
74PhosphorylationKLRKEELSEEGYLAK
HHCHHHHCCCCHHHH		36.5620860994
81AcetylationSEEGYLAKVKSLLNK
CCCCHHHHHHHHHCC		47.8325953088
81UbiquitinationSEEGYLAKVKSLLNK
CCCCHHHHHHHHHCC		47.83-
83UbiquitinationEGYLAKVKSLLNKDL
CCHHHHHHHHHCCCC		34.38-
83 (in isoform 2)Ubiquitination-34.38-
84PhosphorylationGYLAKVKSLLNKDLS
CHHHHHHHHHCCCCC		40.8724719451
88UbiquitinationKVKSLLNKDLSLENG
HHHHHHCCCCCCCCC		61.0821890473
88 (in isoform 2)Ubiquitination-61.0821890473
91PhosphorylationSLLNKDLSLENGAHA
HHHCCCCCCCCCCCC		43.7130624053
115PhosphorylationENGNQARSEARRVGM
CCHHHHHHHHHHHCC		38.3326074081
127PhosphorylationVGMADANSPPKPLSK
HCCCCCCCCCCCCCC		44.2829255136
133PhosphorylationNSPPKPLSKPRTPRR
CCCCCCCCCCCCCCC		49.4929255136
134AcetylationSPPKPLSKPRTPRRS
CCCCCCCCCCCCCCC		46.3225953088
134UbiquitinationSPPKPLSKPRTPRRS
CCCCCCCCCCCCCCC		46.3221890473
134 (in isoform 2)Ubiquitination-46.3221890473
137PhosphorylationKPLSKPRTPRRSKSD
CCCCCCCCCCCCCCC		29.6723927012
141PhosphorylationKPRTPRRSKSDGEAK
CCCCCCCCCCCCCCC		37.4823927012
142MethylationPRTPRRSKSDGEAKP
CCCCCCCCCCCCCCC		51.2421151116
143PhosphorylationRTPRRSKSDGEAKPE
CCCCCCCCCCCCCCC		52.6929255136
148SumoylationSKSDGEAKPEPSPSP
CCCCCCCCCCCCCCC		45.68-
148AcetylationSKSDGEAKPEPSPSP
CCCCCCCCCCCCCCC		45.6826051181
148SumoylationSKSDGEAKPEPSPSP
CCCCCCCCCCCCCCC		45.68-
150 (in isoform 1)Ubiquitination-58.6721890473
150 (in isoform 2)Phosphorylation-58.6725159151
152PhosphorylationGEAKPEPSPSPRITR
CCCCCCCCCCCCCCC		36.0329255136
154PhosphorylationAKPEPSPSPRITRKS
CCCCCCCCCCCCCCC		31.0229255136
156 (in isoform 2)Phosphorylation-47.4521815630
158 (in isoform 2)Phosphorylation-33.0721712546
160AcetylationPSPRITRKSTRQTTI
CCCCCCCCCCCCEEC		47.7521947282
161PhosphorylationSPRITRKSTRQTTIT
CCCCCCCCCCCEECH		26.0726074081
161 (in isoform 2)Phosphorylation-26.07-
162PhosphorylationPRITRKSTRQTTITS
CCCCCCCCCCEECHH		29.8126074081
165PhosphorylationTRKSTRQTTITSHFA
CCCCCCCEECHHHHC		19.5126074081
166PhosphorylationRKSTRQTTITSHFAK
CCCCCCEECHHHHCC		17.5828355574
168PhosphorylationSTRQTTITSHFAKGP
CCCCEECHHHHCCCC		17.6626074081
168 (in isoform 2)Phosphorylation-17.6621815630
169PhosphorylationTRQTTITSHFAKGPA
CCCEECHHHHCCCCC		16.8626074081
170 (in isoform 2)Phosphorylation-20.3121815630
173AcetylationTITSHFAKGPAKRKP
ECHHHHCCCCCCCCC		65.5619608861
173UbiquitinationTITSHFAKGPAKRKP
ECHHHHCCCCCCCCC		65.56-
188AcetylationQEESERAKSDESIKE
HHHHHHHCCCHHHHH		65.7421947282
189PhosphorylationEESERAKSDESIKEE
HHHHHHCCCHHHHHH		45.7025159151
192PhosphorylationERAKSDESIKEEDKD
HHHCCCHHHHHHCCC		43.9025849741
194SumoylationAKSDESIKEEDKDQD
HCCCHHHHHHCCCHH		65.41-
194SumoylationAKSDESIKEEDKDQD
HCCCHHHHHHCCCHH		65.41-
196 (in isoform 1)Ubiquitination-66.4221890473
208PhosphorylationDEKRRRVTSRERVAR
HHHHHHCHHHHHCCC		21.9120363803
209PhosphorylationEKRRRVTSRERVARP
HHHHHCHHHHHCCCC		29.3220363803
227PhosphorylationEEPERAKSGTRTEKE
CCHHHHCCCCCCHHH		44.4030624053
229PhosphorylationPERAKSGTRTEKEEE
HHHHCCCCCCHHHHH		41.3228111955
231PhosphorylationRAKSGTRTEKEEERD
HHCCCCCCHHHHHHH		51.7730622161
247PhosphorylationKEEKRLRSQTKEPTP
HHHHHHHHCCCCCCH		46.9526074081
249PhosphorylationEKRLRSQTKEPTPKQ
HHHHHHCCCCCCHHH		38.3226074081
250 (in isoform 3)Ubiquitination-54.8021890473
253PhosphorylationRSQTKEPTPKQKLKE
HHCCCCCCHHHHHCC		44.1826074081
259SumoylationPTPKQKLKEEPDREA
CCHHHHHCCCCCHHH		68.04-
259AcetylationPTPKQKLKEEPDREA
CCHHHHHCCCCCHHH		68.0421947282
259SumoylationPTPKQKLKEEPDREA
CCHHHHHCCCCCHHH		68.0428112733
281AcetylationEDEDGDEKDEKKHRS
CCCCCCHHHHHHHHC		75.7626051181
284AcetylationDGDEKDEKKHRSQPK
CCCHHHHHHHHCCHH		65.1026051181
288PhosphorylationKDEKKHRSQPKDLAA
HHHHHHHCCHHHHHH		51.0224719451
312PhosphorylationEKVNPQISDEKDEDE
CCCCCCCCCCCCHHH		34.1729255136
327PhosphorylationKEEKRRKTTPKEPTE
HHHHHHCCCCCCCCH		46.6626270265
328PhosphorylationEEKRRKTTPKEPTEK
HHHHHCCCCCCCCHH		35.0825159151
333PhosphorylationKTTPKEPTEKKMARA
CCCCCCCCHHHHHHH		62.6223312004
335AcetylationTPKEPTEKKMARAKT
CCCCCCHHHHHHHHH		50.7823749302
336UbiquitinationPKEPTEKKMARAKTV
CCCCCHHHHHHHHHH		31.40-
342PhosphorylationKKMARAKTVMNSKTH
HHHHHHHHHHCCCCC		24.8120068231
346PhosphorylationRAKTVMNSKTHPPKC
HHHHHHCCCCCCCCC		22.3420068231
347AcetylationAKTVMNSKTHPPKCI
HHHHHCCCCCCCCCE		45.9425953088
352AcetylationNSKTHPPKCIQCGQY
CCCCCCCCCEECCCC		48.7126051181
359PhosphorylationKCIQCGQYLDDPDLK
CCEECCCCCCCCCCC		9.4420562096
366AcetylationYLDDPDLKYGQHPPD
CCCCCCCCCCCCCCC		55.5021947282
385UbiquitinationPQMLTNEKLSIFDAN
CCCCCCCCCCCEECC		49.9921906983
387PhosphorylationMLTNEKLSIFDANES
CCCCCCCCCEECCCC		32.0728464451
394PhosphorylationSIFDANESGFESYEA
CCEECCCCCCCCCCC		48.8923401153
398PhosphorylationANESGFESYEALPQH
CCCCCCCCCCCCCCC		26.4730266825
399PhosphorylationNESGFESYEALPQHK
CCCCCCCCCCCCCCC		9.6830266825
401 (in isoform 2)Ubiquitination-19.1321890473
411PhosphorylationQHKLTCFSVYCKHGH
CCCEEEEEEEECCCC		17.8327080861
413PhosphorylationKLTCFSVYCKHGHLC
CEEEEEEEECCCCEE		8.4527080861
415AcetylationTCFSVYCKHGHLCPI
EEEEEEECCCCEECC		34.6326051181
420GlutathionylationYCKHGHLCPIDTGLI
EECCCCEECCCCCCC		2.0022555962
447 (in isoform 1)Ubiquitination-48.0521890473
509PhosphorylationMQEKIYISKIVVEFL
HHCCCHHHHHHHHHH		10.19-
549PhosphorylationLNRFTEDSLLRHAQF
CCCCCHHHHHHHHHH		24.0730108239
586AcetylationPCMRDLIKLAGVTLG
HHHHHHHHHHCCCHH		39.3125953088
586UbiquitinationPCMRDLIKLAGVTLG
HHHHHHHHHHCCCHH		39.3121890473
591PhosphorylationLIKLAGVTLGQRRAQ
HHHHHCCCHHHHHHH		25.0121406692
592 (in isoform 3)Ubiquitination-5.2421890473
602 (in isoform 2)Ubiquitination-35.4121890473
625 (in isoform 3)Ubiquitination-13.3121890473
638UbiquitinationFFAEQIEKDDREDKE
HHHHHHHHCCHHHHH		67.56-
644UbiquitinationEKDDREDKENAFKRR
HHCCHHHHHHHHHHH		48.38-
645 (in isoform 3)Ubiquitination-67.1421890473
648 (in isoform 1)Ubiquitination-10.7621890473
661 (in isoform 3)Ubiquitination-30.5421890473
666UbiquitinationCQQPECGKCKACKDM
CCCCCCCCCCHHHHH		44.19-
668UbiquitinationQPECGKCKACKDMVK
CCCCCCCCHHHHHHH		61.37-
675SumoylationKACKDMVKFGGSGRS
CHHHHHHHCCCCCHH		31.49-
675AcetylationKACKDMVKFGGSGRS
CHHHHHHHCCCCCHH		31.4926051181
675SumoylationKACKDMVKFGGSGRS
CHHHHHHHCCCCCHH		31.49-
675UbiquitinationKACKDMVKFGGSGRS
CHHHHHHHCCCCCHH		31.49-
682 (in isoform 2)Ubiquitination-32.42-
691 (in isoform 2)Ubiquitination-3.41-
714PhosphorylationDNIPEMPSPKKMHQG
CCCCCCCCCCCCCCC		48.3019664994
716UbiquitinationIPEMPSPKKMHQGKK
CCCCCCCCCCCCCCC		68.04-
732PhosphorylationKQNKNRISWVGEAVK
CCCCCCCCCCHHHHC		16.6923401153
739SumoylationSWVGEAVKTDGKKSY
CCCHHHHCCCCCCCE		48.20-
739SumoylationSWVGEAVKTDGKKSY
CCCHHHHCCCCCCCE		48.20-
749AcetylationGKKSYYKKVCIDAET
CCCCEEEEEEEECCE		26.6421947282
755 (in isoform 2)Ubiquitination-50.61-
756 (in isoform 3)Ubiquitination-29.9121890473
771PhosphorylationSVIPDDSSKPLYLAR
EECCCCCCCCEEEEE		45.3324719451
878PhosphorylationQDYARFESPPKTQPT
CCCCCCCCCCCCCCC		43.7325159151
881UbiquitinationARFESPPKTQPTEDN
CCCCCCCCCCCCCCC		64.28-
882PhosphorylationRFESPPKTQPTEDNK
CCCCCCCCCCCCCCC		45.6223312004
885PhosphorylationSPPKTQPTEDNKFKF
CCCCCCCCCCCCHHH		46.2623186163
889UbiquitinationTQPTEDNKFKFCVSC
CCCCCCCCHHHHHHH		63.35-
891AcetylationPTEDNKFKFCVSCAR
CCCCCCHHHHHHHHH		39.1921947282
893S-palmitoylationEDNKFKFCVSCARLA
CCCCHHHHHHHHHHH		1.9629575903
896S-palmitoylationKFKFCVSCARLAEMR
CHHHHHHHHHHHHHH		0.9629575903
897 (in isoform 2)Ubiquitination-11.30-
905 (in isoform 2)Ubiquitination-47.44-
919PhosphorylationEQLEDLDSRVLYYSA
HHHHCCCCCEEEEEE		31.4221712546
928UbiquitinationVLYYSATKNGILYRV
EEEEEECCCCEEEEE		53.5521890473
940PhosphorylationYRVGDGVYLPPEAFT
EEECCEEEECCHHEE		21.0122468782
944 (in isoform 2)Ubiquitination-55.2521890473
947PhosphorylationYLPPEAFTFNIKLSS
EECCHHEEEEEEECC		23.8722468782
953PhosphorylationFTFNIKLSSPVKRPR
EEEEEEECCCCCCCC		27.8230266825
954PhosphorylationTFNIKLSSPVKRPRK
EEEEEECCCCCCCCC		44.1223401153
957SumoylationIKLSSPVKRPRKEPV
EEECCCCCCCCCCCC		61.13-
957AcetylationIKLSSPVKRPRKEPV
EEECCCCCCCCCCCC		61.1321947282
957SumoylationIKLSSPVKRPRKEPV
EEECCCCCCCCCCCC		61.1321947282
957UbiquitinationIKLSSPVKRPRKEPV
EEECCCCCCCCCCCC		61.1321947282
961AcetylationSPVKRPRKEPVDEDL
CCCCCCCCCCCCCCC		69.8821947282
961UbiquitinationSPVKRPRKEPVDEDL
CCCCCCCCCCCCCCC		69.8821947282
969PhosphorylationEPVDEDLYPEHYRKY
CCCCCCCCHHHHHHH		20.9217360941
973PhosphorylationEDLYPEHYRKYSDYI
CCCCHHHHHHHHHHH		13.7226074081
975AcetylationLYPEHYRKYSDYIKG
CCHHHHHHHHHHHCC		41.7721947282
975UbiquitinationLYPEHYRKYSDYIKG
CCHHHHHHHHHHHCC		41.7721947282
977PhosphorylationPEHYRKYSDYIKGSN
HHHHHHHHHHHCCCC		27.2920873877
977 (in isoform 2)Ubiquitination-27.2921890473
981AcetylationRKYSDYIKGSNLDAP
HHHHHHHCCCCCCCC		50.4826051181
981MethylationRKYSDYIKGSNLDAP
HHHHHHHCCCCCCCC		50.48-
981UbiquitinationRKYSDYIKGSNLDAP
HHHHHHHCCCCCCCC		50.4821890473
983PhosphorylationYSDYIKGSNLDAPEP
HHHHHCCCCCCCCCC		29.2621712546
987 (in isoform 3)Ubiquitination-17.3321890473
990 (in isoform 1)Ubiquitination-23.7321890473
991PhosphorylationNLDAPEPYRIGRIKE
CCCCCCCCCCCCEEE		17.1322468782
991 (in isoform 2)Ubiquitination-17.13-
997AcetylationPYRIGRIKEIFCPKK
CCCCCCEEEEECCCC		43.3126051181
997UbiquitinationPYRIGRIKEIFCPKK
CCCCCCEEEEECCCC		43.3121890473
997 (in isoform 2)Ubiquitination-43.3121890473
1013 (in isoform 2)Ubiquitination-33.7221890473
1020AcetylationDIKIRVNKFYRPENT
CEEEEEEEECCCCCC		40.7026051181
1020UbiquitinationDIKIRVNKFYRPENT
CEEEEEEEECCCCCC		40.70-
1022PhosphorylationKIRVNKFYRPENTHK
EEEEEEECCCCCCCC		27.2028152594
1023 (in isoform 1)Ubiquitination-34.8821890473
1027PhosphorylationKFYRPENTHKSTPAS
EECCCCCCCCCCCCC		29.0828152594
1036 (in isoform 2)Ubiquitination-17.90-
1043 (in isoform 1)Ubiquitination-13.1621890473
1054AcetylationEEAVVDFKAVQGRCT
CCEEECEEEECCEEE		43.0921947282
1059 (in isoform 1)Ubiquitination-8.8821890473
1092UbiquitinationFLEAYNAKSKSFEDP
EEEEECCCCCCCCCC		55.5721890473
1094UbiquitinationEAYNAKSKSFEDPPN
EEECCCCCCCCCCCC		59.46-
1095PhosphorylationAYNAKSKSFEDPPNH
EECCCCCCCCCCCCC		40.7423403867
1105PhosphorylationDPPNHARSPGNKGKG
CCCCCCCCCCCCCCC		37.6323401153
1108 (in isoform 2)Ubiquitination-53.9821890473
1110 (in isoform 2)Ubiquitination-48.20-
1111AcetylationRSPGNKGKGKGKGKG
CCCCCCCCCCCCCCC		60.0919608861
1113AcetylationPGNKGKGKGKGKGKP
CCCCCCCCCCCCCCC		62.0219608861
1115AcetylationNKGKGKGKGKGKPKS
CCCCCCCCCCCCCCH		62.0219608861
1117AcetylationGKGKGKGKGKPKSQA
CCCCCCCCCCCCHHC		68.2121947282
1119AcetylationGKGKGKGKPKSQACE
CCCCCCCCCCHHCCC		53.4088299
1121AcetylationGKGKGKPKSQACEPS
CCCCCCCCHHCCCCC		59.7068721
1122PhosphorylationKGKGKPKSQACEPSE
CCCCCCCHHCCCCCC		31.3825159151
1125GlutathionylationGKPKSQACEPSEPEI
CCCCHHCCCCCCCCE		6.4822555962
1128PhosphorylationKSQACEPSEPEIEIK
CHHCCCCCCCCEEEE		43.4128985074
1135SumoylationSEPEIEIKLPKLRTL
CCCCEEEECCCCCEE		46.04-
1135SumoylationSEPEIEIKLPKLRTL
CCCCEEEECCCCCEE		46.04-
1135UbiquitinationSEPEIEIKLPKLRTL
CCCCEEEECCCCCEE		46.04-
1151 (in isoform 2)Ubiquitination-2.27-
1154 (in isoform 1)Ubiquitination-23.2021890473
1196UbiquitinationEDCNILLKLVMAGET
CCHHHHHHHHHCCCC		35.27-
1199 (in isoform 3)Ubiquitination-6.0121890473
1203PhosphorylationKLVMAGETTNSRGQR
HHHHCCCCCCCCCCC		30.2921406692
1204PhosphorylationLVMAGETTNSRGQRL
HHHCCCCCCCCCCCC		27.2221406692
1206PhosphorylationMAGETTNSRGQRLPQ
HCCCCCCCCCCCCCC		35.3821406692
1214UbiquitinationRGQRLPQKGDVEMLC
CCCCCCCCCCCEECC		55.96-
1230 (in isoform 2)Ubiquitination-43.91-
1236 (in isoform 3)Ubiquitination-27.6121890473
1250 (in isoform 3)Ubiquitination-17.0021890473
1254PhosphorylationLVVSFLSYCDYYRPR
HHHHHHHHCCCCCCH		7.47-
1323UbiquitinationLAAAPGEKLPLFPEP
EEECCCCCCCCCCCC		62.4121906983
1339 (in isoform 2)Ubiquitination-4.4021890473
1348AcetylationLSVVVDDKKFVSNIT
EEEEECCHHHHHHHH		43.5826051181
1348UbiquitinationLSVVVDDKKFVSNIT
EEEEECCHHHHHHHH		43.58-
1349AcetylationSVVVDDKKFVSNITR
EEEECCHHHHHHHHH		58.9721947282
1349UbiquitinationSVVVDDKKFVSNITR
EEEECCHHHHHHHHH		58.9721947282
1358PhosphorylationVSNITRLSSGPFRTI
HHHHHHCCCCCCCEE		29.9227251275
1365 (in isoform 2)Ubiquitination-2.67-
1385 (in isoform 1)Ubiquitination-29.6121890473
1401MethylationSWFQRQLRGAQYQPI
CHHHHHHCCCCCHHH		30.02-
1405PhosphorylationRQLRGAQYQPILRDH
HHHCCCCCHHHHHHH		18.74-
1415AcetylationILRDHICKDMSALVA
HHHHHHCCCHHHHHH		56.7321947282
1415UbiquitinationILRDHICKDMSALVA
HHHHHHCCCHHHHHH		56.7321947282
1431 (in isoform 2)Ubiquitination-10.89-
1447PhosphorylationPNIEVRLSDGTMARK
CCCEEECCCCCHHEH		24.3522985185
1473MethylationRSSSGALRGVCSCVE
CCCCHHHHHHHHHHH		34.66-
1483AcetylationCSCVEAGKACDPAAR
HHHHHCHHCCCHHHH		53.5426051181
1483UbiquitinationCSCVEAGKACDPAAR
HHHHHCHHCCCHHHH		53.54-
1499 (in isoform 2)Ubiquitination-3.39-
1524PhosphorylationLEWDGFFSTTVTNPE
EEECCEEEEEECCCC		22.40-
1525PhosphorylationEWDGFFSTTVTNPEP
EECCEEEEEECCCCC		21.82-
1526PhosphorylationWDGFFSTTVTNPEPM
ECCEEEEEECCCCCC		24.92-
1535UbiquitinationTNPEPMGKQGRVLHP
CCCCCCCCCCCCCCH		43.2421906983
1549PhosphorylationPEQHRVVSVRECARS
HHHCCEEEHHHHHHH		16.7624719451
1551 (in isoform 2)Ubiquitination-26.2721890473
1572AcetylationLFGNILDKHRQVGNA
HHHHHHHHCCCCCCC		36.9226051181
1572UbiquitinationLFGNILDKHRQVGNA
HHHHHHHHCCCCCCC		36.9221890473
1586UbiquitinationAVPPPLAKAIGLEIK
CCCHHHHHHHCHHHH		48.502190698
1588 (in isoform 2)Ubiquitination-6.7921890473
1597 (in isoform 1)Ubiquitination-4.2821890473
1599AcetylationIKLCMLAKARESASA
HHHHHHHHHHHHHHH		43.9726051181
1599UbiquitinationIKLCMLAKARESASA
HHHHHHHHHHHHHHH		43.97-
1602 (in isoform 2)Ubiquitination-56.3621890473
1605PhosphorylationAKARESASAKIKEEE
HHHHHHHHHHHHHHH		39.10-
1609SumoylationESASAKIKEEEAAKD
HHHHHHHHHHHHHCC		59.37-
1609AcetylationESASAKIKEEEAAKD
HHHHHHHHHHHHHCC		59.3726051181
1609SumoylationESASAKIKEEEAAKD
HHHHHHHHHHHHHCC		59.3728112733
1634 (in isoform 1)Ubiquitination-21890473
1648 (in isoform 1)Ubiquitination-21890473
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
127SPhosphorylationKinaseCDK4P11802
PSP
143SPhosphorylationKinaseAKT1P31749
Uniprot
154SPhosphorylationKinaseCDK1P06493
PSP
154SPhosphorylationKinaseCDK2P24941
PSP
154SPhosphorylationKinaseCDK5Q00535
PSP
714SPhosphorylationKinaseMTORP42345
PSP
730SPhosphorylationKinaseAMPKA1Q13131
PSP
954SPhosphorylationKinaseCDK4P11802
PSP
-KUbiquitinationE3 ubiquitin ligaseUHRF1Q96T88
PMID:21268065
-KUbiquitinationE3 ubiquitin ligaseFZR1Q9UM11
PMID:15899874
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
142KMethylation

21151116
143SMethylation

18669648
143SPhosphorylation

18669648
154SPhosphorylation

18669648
1349KAcetylation

21947282
1415KAcetylation

21947282
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 DNMT1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DNM3B_HUMANDNMT3Bphysical
12867029
CBX5_HUMANCBX5physical
12867029
SUV91_HUMANSUV39H1physical
12711675
CBX1_HUMANCBX1physical
12711675
HDAC2_HUMANHDAC2physical
10888872
DMAP1_HUMANDMAP1physical
10888872
RB_HUMANRB1physical
10888886
E2F1_HUMANE2F1physical
10888886
HDAC1_HUMANHDAC1physical
10888886
TRI27_HUMANTRIM27physical
16169070
H3_YEASTHHT1physical
18158899
DNM3A_HUMANDNMT3Aphysical
12145218
DNM3B_HUMANDNMT3Bphysical
12145218
PCNA_HUMANPCNAphysical
12354094
UHRF1_HUMANUHRF1physical
17934516
HDAC1_HUMANHDAC1physical
17934516
HDAC1_HUMANHDAC1physical
12473678
CXXC1_HUMANCXXC1physical
18680430
SETD7_HUMANSETD7physical
19282482
UHRF1_HUMANUHRF1physical
19943104
SP1_HUMANSP1physical
17124180
SP3_HUMANSP3physical
17124180
EHMT2_HUMANEHMT2physical
17085482
SUV91_HUMANSUV39H1physical
17085482
EZH2_HUMANEZH2physical
16357870
RB_HUMANRB1physical
11847125
STAT3_HUMANSTAT3physical
15870198
HDAC1_HUMANHDAC1physical
15870198
SMCA5_HUMANSMARCA5physical
15313181
CHK1_HUMANCHEK1physical
17991895
HSP74_HUMANHSPA4physical
21745816
RUXG_HUMANSNRPGphysical
21745816
GRP78_HUMANHSPA5physical
21745816
UBP7_HUMANUSP7physical
21745816
UHRF1_HUMANUHRF1physical
21745816
RAD9A_HUMANRAD9Aphysical
20940144
PCNA_HUMANPCNAphysical
20940144
CHK1_HUMANCHEK1physical
20940144
UBP7_HUMANUSP7physical
21268065
HDAC1_HUMANHDAC1physical
17707923
AKT1_HUMANAKT1physical
21151116
UBP7_HUMANUSP7physical
21045206
UHRF1_HUMANUHRF1physical
21045206
DAXX_HUMANDAXXphysical
14978102
UHRF1_HUMANUHRF1physical
22064703
UHRF2_HUMANUHRF2physical
22064703
SIR1_HUMANSIRT1physical
21947282
DNMT1_HUMANDNMT1physical
19173286
DNM3B_HUMANDNMT3Bgenetic
18095639
UBP7_HUMANUSP7physical
22411829
MTG8_HUMANRUNX1T1physical
15735013
RUNX1_HUMANRUNX1physical
15735013
PCNA_HUMANPCNAphysical
22606318
KDM1A_HUMANKDM1Aphysical
22278882
HDAC1_HUMANHDAC1physical
22274925
NR2C2_HUMANNR2C2physical
21670149
NR2C1_HUMANNR2C1physical
21670149
KDM1A_HUMANKDM1Aphysical
21670149
HDAC1_HUMANHDAC1physical
21670149
HDAC2_HUMANHDAC2physical
21670149
MTA1_HUMANMTA1physical
21670149
MTA2_HUMANMTA2physical
21670149
CHD4_HUMANCHD4physical
21670149
RBBP4_HUMANRBBP4physical
21670149
MBD3_HUMANMBD3physical
21670149
DPOD3_HUMANPOLD3physical
21670149
HDAC3_HUMANHDAC3physical
21670149
UHRF1_HUMANUHRF1physical
17673620
PCNA_HUMANPCNAphysical
20613874
UHRF1_HUMANUHRF1physical
20613874
SIR1_HUMANSIRT1physical
22094255
EZH2_HUMANEZH2physical
22094255
EED_HUMANEEDphysical
22094255
DAXX_HUMANDAXXphysical
23548901
NRIP1_HUMANNRIP1physical
17972916
P53_HUMANTP53physical
23038753
DAXX_HUMANDAXXphysical
23038753
CHD4_HUMANCHD4physical
23708667
EHMT2_HUMANEHMT2physical
23708667
PARP1_HUMANPARP1physical
23708667
MTA2_HUMANMTA2physical
23708667
PCNA_HUMANPCNAphysical
23708667
HDAC1_HUMANHDAC1physical
23708667
HDAC2_HUMANHDAC2physical
23708667
MTA1_HUMANMTA1physical
23708667
MTA1_HUMANMTA1physical
26344197
UHRF1_HUMANUHRF1physical
26065575
H31T_HUMANHIST3H3physical
26065575
H2A2C_HUMANHIST2H2ACphysical
26065575
MKL1_HUMANMKL1physical
25854163
STAT3_HUMANSTAT3physical
25854163
UBP7_HUMANUSP7physical
25960197
UHRF1_HUMANUHRF1physical
27049577
SNAI1_HUMANSNAI1physical
26794444
HDAC1_HUMANHDAC1physical
26794444
UHRF1_HUMANUHRF1physical
27045799
RBBP7_HUMANRBBP7physical
28143904
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614116Neuropathy, hereditary sensory, 1E (HSN1E)
604121Cerebellar ataxia, deafness, and narcolepsy, autosomal dominant (ADCADN)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00928Azacitidine
DB01262Decitabine
DB01099Flucytosine
DB01035Procainamide
Regulatory Network of DNMT1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"SIRT1 deacetylates the DNA methyltransferase 1 (DNMT1) protein andalters its activities.";
Peng L., Yuan Z., Ling H., Fukasawa K., Robertson K., Olashaw N.,Koomen J., Chen J., Lane W.S., Seto E.;
Mol. Cell. Biol. 31:4720-4734(2011).
Cited for: ACETYLATION AT LYS-160; LYS-188; LYS-259; LYS-366; LYS-749; LYS-891;LYS-957; LYS-961; LYS-975; LYS-1054; LYS-1111; LYS-1113; LYS-1115;LYS-1117; LYS-1349 AND LYS-1415, AND DEACETYLATION BY SIRT1.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-173; LYS-1113; LYS-1115 ANDLYS-1117, AND MASS SPECTROMETRY.
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey.";
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
Mol. Cell 23:607-618(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1113; LYS-1115 AND LYS-1117,AND MASS SPECTROMETRY.
Methylation
ReferencePubMed
"Protein lysine methyltransferase G9a acts on non-histone targets.";
Rathert P., Dhayalan A., Murakami M., Zhang X., Tamas R.,Jurkowska R., Komatsu Y., Shinkai Y., Cheng X., Jeltsch A.;
Nat. Chem. Biol. 4:344-346(2008).
Cited for: METHYLATION AT LYS-70, AND MASS SPECTROMETRY.
"A methylation and phosphorylation switch between an adjacent lysineand serine determines human DNMT1 stability.";
Esteve P.O., Chang Y., Samaranayake M., Upadhyay A.K., Horton J.R.,Feehery G.R., Cheng X., Pradhan S.;
Nat. Struct. Mol. Biol. 18:42-48(2011).
Cited for: METHYLATION AT LYS-142, AND PHOSPHORYLATION AT SER-143.
Phosphorylation
ReferencePubMed
"A methylation and phosphorylation switch between an adjacent lysineand serine determines human DNMT1 stability.";
Esteve P.O., Chang Y., Samaranayake M., Upadhyay A.K., Horton J.R.,Feehery G.R., Cheng X., Pradhan S.;
Nat. Struct. Mol. Biol. 18:42-48(2011).
Cited for: METHYLATION AT LYS-142, AND PHOSPHORYLATION AT SER-143.
"Phosphorylation of human DNMT1: implication of cyclin-dependentkinases.";
Lavoie G., St-Pierre Y.;
Biochem. Biophys. Res. Commun. 409:187-192(2011).
Cited for: PHOSPHORYLATION AT SER-154.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127 AND SER-714, ANDMASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-714, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127; THR-137; SER-152;SER-154; SER-394 AND SER-714, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-732, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127; SER-714 ANDSER-1105, AND MASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-714 AND SER-954, ANDMASS SPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-969, AND MASSSPECTROMETRY.

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