WIZ_HUMAN - dbPTM
WIZ_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID WIZ_HUMAN
UniProt AC O95785
Protein Name Protein Wiz
Gene Name WIZ
Organism Homo sapiens (Human).
Sequence Length 1651
Subcellular Localization Nucleus.
Protein Description May link EHMT1 and EHMT2 histone methyltransferases to the CTBP corepressor machinery. May be involved in EHMT1-EHMT2 heterodimer formation and stabilization (By similarity)..
Protein Sequence MEGSLAGSLAAPDRPQGPERLPGPAPRENIEGGAEAAEGEGGIFRSTRYLPVTKEGPRDILDGRGGISGTPDGRGPWEHPLVQEAGEGILSERRFEDSVIVRTMKPHAELEGSRRFLHHRGEPRLLEKHAQGRPRFDWLQDEDEQGSPQDAGLHLDLPAQPPPLAPFRRVFVPVEDTPKTLDMAVVGGREDLEDLEGLAQPSEWGLPTSASEVATQTWTVNSEASVERLQPLLPPIRTGPYLCELLEEVAEGVASPDEDEDEEPAVFPCIECSIYFKQKEHLLEHMSQHRRAPGQEPPADLAPLACGECGWAFADPTALEQHRQLHQASREKIIEEIQKLKQVPGDEGREARLQCPKCVFGTNSSRAYVQHAKLHMREPPGQTTKEPFGGSSGAGSPSPEASALLYQPYGAAVGLSACVFCGFPAPSESLLREHVRLVHAHPHWEEDGEAYEEDPASQPGTSQDAHACFPDTAVDYFGKAEPSLAPMWRENPAGYDPSLAFGPGCQQLSIRDFPLSKPLLHGTGQRPLGRLAFPSTLASTPYSLQLGRNKSTVHPQGLGERRRPWSEEEEEEEEEEDVVLTSEMDFSPENGVFSPLATPSLIPQAALELKQAFREALQAVEATQGQQQQLRGMVPIVLVAKLGPQVMAAARVPPRLQPEELGLAGAHPLDFLLLDAPLGGPLGLDTLLDGDPAMALKHEERKCPYCPDRFHNGIGLANHVRGHLNRVGVSYNVRHFISAEEVKAIERRFSFQKKKKKVANFDPGTFSLMRCDFCGAGFDTRAGLSSHARAHLRDFGITNWELTVSPINILQELLATSAAEQPPSPLGREPGGPPGSFLTSRRPRLPLTVPFPPTWAEDPGPAYGDAQSLTTCEVCGACFETRKGLSSHARSHLRQLGVAESESSGAPIDLLYELVKQKGLPDAHLGLPPGLAKKSSSLKEVVAGAPRPGLLSLAKPLDAPAVNKAIKSPPGFSAKGLGHPPSSPLLKKTPLALAGSPTPKNPEDKSPQLSLSPRPASPKAQWPQSEDEGPLNLTSGPEPARDIRCEFCGEFFENRKGLSSHARSHLRQMGVTEWYVNGSPIDTLREILKRRTQSRPGGPPNPPGPSPKALAKMMGGAGPGSSLEARSPSDLHISPLAKKLPPPPGSPLGHSPTASPPPTARKMFPGLAAPSLPKKLKPEQIRVEIKREMLPGALHGELHPSEGPWGAPREDMTPLNLSSRAEPVRDIRCEFCGEFFENRKGLSSHARSHLRQMGVTEWSVNGSPIDTLREILKKKSKPCLIKKEPPAGDLAPALAEDGPPTVAPGPVQSPLPLSPLAGRPGKPGAGPAQVPRELSLTPITGAKPSATGYLGSVAAKRPLQEDRLLPAEVKAKTYIQTELPFKAKTLHEKTSHSSTEACCELCGLYFENRKALASHARAHLRQFGVTEWCVNGSPIETLSEWIKHRPQKVGAYRSYIQGGRPFTKKFRSAGHGRDSDKRPSLGLAPGGLAVVGRSAGGEPGPEAGRAADGGERPLAASPPGTVKAEEHQRQNINKFERRQARPPDASAARGGEDTNDLQQKLEEVRQPPPRVRPVPSLVPRPPQTSLVKFVGNIYTLKCRFCEVEFQGPLSIQEEWVRHLQRHILEMNFSKADPPPEESQAPQAQTAAAEAP
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
5 (in isoform 3)Phosphorylation-10.3325627689
7 (in isoform 3)Phosphorylation-28.6120068231
8 (in isoform 4)Phosphorylation-14.8221815630
10 (in isoform 4)Phosphorylation-20.7420068231
27MethylationRLPGPAPRENIEGGA
CCCCCCCHHHCCCCC		52.26-
27 (in isoform 3)Phosphorylation-52.2625627689
28 (in isoform 3)Phosphorylation-62.5925627689
30 (in isoform 4)Phosphorylation-4.4525627689
31 (in isoform 4)Phosphorylation-64.2625627689
135PhosphorylationKHAQGRPRFDWLQDE
HHCCCCCCCCCCCCC		40.57-
148MethylationDEDEQGSPQDAGLHL
CCCCCCCCCCCCCCC		42.78-
206 (in isoform 3)Phosphorylation-4.3625159151
215 (in isoform 2)Phosphorylation-31.5424719451
215PhosphorylationTSASEVATQTWTVNS
CCHHHHHCEEEECCC		31.54-
215 (in isoform 3)Phosphorylation-31.5425159151
218 (in isoform 3)Phosphorylation-6.6325159151
222PhosphorylationTQTWTVNSEASVERL
CEEEECCCHHHHHHH		30.1520068231
222 (in isoform 2)Phosphorylation-30.1524719451
249 (in isoform 2)Phosphorylation-4.2524719451
249PhosphorylationLCELLEEVAEGVASP
HHHHHHHHHHCCCCC		4.25-
251MethylationELLEEVAEGVASPDE
HHHHHHHHCCCCCCC		60.42-
251SumoylationELLEEVAEGVASPDE
HHHHHHHHCCCCCCC		60.42-
253 (in isoform 3)Phosphorylation-3.4325159151
255MethylationEVAEGVASPDEDEDE
HHHHCCCCCCCCCCC		30.40-
255SumoylationEVAEGVASPDEDEDE
HHHHCCCCCCCCCCC		30.40-
260 (in isoform 3)Phosphorylation-66.3326055452
264 (in isoform 2)Phosphorylation-31.51-
264PhosphorylationDEDEDEEPAVFPCIE
CCCCCCCCCCHHEEE		31.51-
265 (in isoform 2)Phosphorylation-20.89-
265PhosphorylationEDEDEEPAVFPCIEC
CCCCCCCCCHHEEEE		20.89-
270 (in isoform 2)Phosphorylation-6.4424719451
270PhosphorylationEPAVFPCIECSIYFK
CCCCHHEEEEEEEEC		6.44-
272 (in isoform 2)Phosphorylation-1.20-
272PhosphorylationAVFPCIECSIYFKQK
CCHHEEEEEEEECCH		1.20-
277 (in isoform 2)Phosphorylation-43.4124719451
277PhosphorylationIECSIYFKQKEHLLE
EEEEEEECCHHHHHH		43.41-
281UbiquitinationIYFKQKEHLLEHMSQ
EEECCHHHHHHHHHH		42.63-
282MethylationYFKQKEHLLEHMSQH
EECCHHHHHHHHHHH		6.69-
289 (in isoform 2)Phosphorylation-17.5624719451
289PhosphorylationLLEHMSQHRRAPGQE
HHHHHHHHCCCCCCC		17.56-
294 (in isoform 2)Phosphorylation-43.4224719451
294PhosphorylationSQHRRAPGQEPPADL
HHHCCCCCCCCCCHH		43.42-
296 (in isoform 2)Phosphorylation-60.2024719451
296PhosphorylationHRRAPGQEPPADLAP
HCCCCCCCCCCHHHC		60.20-
298 (in isoform 2)Phosphorylation-37.34-
298PhosphorylationRAPGQEPPADLAPLA
CCCCCCCCCHHHCHH		37.34-
302 (in isoform 2)Phosphorylation-9.52-
302PhosphorylationQEPPADLAPLACGEC
CCCCCHHHCHHCCCC		9.52-
305MethylationPADLAPLACGECGWA
CCHHHCHHCCCCCCC		9.75-
319 (in isoform 3)Phosphorylation-7.7725159151
320SumoylationFADPTALEQHRQLHQ
CCCHHHHHHHHHHHH		41.71-
361PhosphorylationQCPKCVFGTNSSRAY
CCCCEEECCCCCHHH		12.00-
406 (in isoform 2)Phosphorylation-14.3224719451
406PhosphorylationPEASALLYQPYGAAV
HHHHHHHCCCCCHHH		14.32-
425SumoylationCVFCGFPAPSESLLR
HHHCCCCCCCHHHHH		20.28-
426MethylationVFCGFPAPSESLLRE
HHCCCCCCCHHHHHH		38.58-
452 (in isoform 2)Phosphorylation-64.0727251275
452PhosphorylationEEDGEAYEEDPASQP
HHCCCCCCCCCCCCC		64.07-
457PhosphorylationAYEEDPASQPGTSQD
CCCCCCCCCCCCCCC		42.1518691976
457 (in isoform 2)Phosphorylation-42.1527251275
465MethylationQPGTSQDAHACFPDT
CCCCCCCHHHCCCCH		5.64-
476MethylationFPDTAVDYFGKAEPS
CCCHHHHHCCCCCCC		13.97-
478 (in isoform 2)Phosphorylation-23.2627251275
478PhosphorylationDTAVDYFGKAEPSLA
CHHHHHCCCCCCCCC		23.26-
480 (in isoform 2)Phosphorylation-34.0224719451
480PhosphorylationAVDYFGKAEPSLAPM
HHHHCCCCCCCCCCH		34.02-
483PhosphorylationYFGKAEPSLAPMWRE
HCCCCCCCCCCHHCC		28.77-
490PhosphorylationSLAPMWRENPAGYDP
CCCCHHCCCCCCCCH		52.64-
492PhosphorylationAPMWRENPAGYDPSL
CCHHCCCCCCCCHHH		23.47-
495 (in isoform 2)Phosphorylation-27.13-
495PhosphorylationWRENPAGYDPSLAFG
HCCCCCCCCHHHCCC		27.13-
499MethylationPAGYDPSLAFGPGCQ
CCCCCHHHCCCCCCC		5.80-
499SumoylationPAGYDPSLAFGPGCQ
CCCCCHHHCCCCCCC		5.80-
499UbiquitinationPAGYDPSLAFGPGCQ
CCCCCHHHCCCCCCC		5.80-
506MethylationLAFGPGCQQLSIRDF
HCCCCCCCCCEECCC		53.84-
513SumoylationQQLSIRDFPLSKPLL
CCCEECCCCCCCCCC		4.75-
515SumoylationLSIRDFPLSKPLLHG
CEECCCCCCCCCCCC		11.82-
516PhosphorylationSIRDFPLSKPLLHGT
EECCCCCCCCCCCCC		32.2524719451
525MethylationPLLHGTGQRPLGRLA
CCCCCCCCCCCCCCC		43.59-
525SumoylationPLLHGTGQRPLGRLA
CCCCCCCCCCCCCCC		43.59-
525UbiquitinationPLLHGTGQRPLGRLA
CCCCCCCCCCCCCCC		43.59-
527MethylationLHGTGQRPLGRLAFP
CCCCCCCCCCCCCCC		31.14-
536PhosphorylationGRLAFPSTLASTPYS
CCCCCCCCCCCCCCE		26.95-
576 (in isoform 2)Phosphorylation-60.43-
603MethylationLATPSLIPQAALELK
CCCCCHHHHHHHHHH		24.05-
607MethylationSLIPQAALELKQAFR
CHHHHHHHHHHHHHH		9.93-
623 (in isoform 2)Phosphorylation-21.5224719451
623PhosphorylationALQAVEATQGQQQQL
HHHHHHHHHHHHHHH		21.52-
636MethylationQLRGMVPIVLVAKLG
HHCCCCEEEEEEECC		2.26-
660 (in isoform 2)Phosphorylation-55.6224719451
660PhosphorylationPPRLQPEELGLAGAH
CCCCCHHHHCCCCCC		55.62-
664PhosphorylationQPEELGLAGAHPLDF
CHHHHCCCCCCCCCE		16.01-
666SumoylationEELGLAGAHPLDFLL
HHHCCCCCCCCCEEE		8.77-
677SumoylationDFLLLDAPLGGPLGL
CEEEECCCCCCCCCH		31.07-
677UbiquitinationDFLLLDAPLGGPLGL
CEEEECCCCCCCCCH		31.07-
692MethylationDTLLDGDPAMALKHE
HHHCCCCHHHHCCCC		29.48-
703SumoylationLKHEERKCPYCPDRF
CCCCCCCCCCCCCHH		3.48-
703UbiquitinationLKHEERKCPYCPDRF
CCCCCCCCCCCCCHH		3.48-
740UbiquitinationVRHFISAEEVKAIER
HHCCCCHHHHHHHHH		57.44-
740 (in isoform 2)Ubiquitination-57.4421890473
740UbiquitinationVRHFISAEEVKAIER
HHCCCCHHHHHHHHH		57.4421890473
773 (in isoform 2)Ubiquitination-4.79-
781UbiquitinationCGAGFDTRAGLSSHA
CCCCCCCCCCCCHHH		28.6221890473
785PhosphorylationFDTRAGLSSHARAHL
CCCCCCCCHHHHHHH		21.1129396449
786PhosphorylationDTRAGLSSHARAHLR
CCCCCCCHHHHHHHH		26.6329396449
824PhosphorylationSAAEQPPSPLGREPG
CCCCCCCCCCCCCCC		39.1724275569
883SumoylationGACFETRKGLSSHAR
CHHHHHCCCCHHHHH		72.1728112733
886PhosphorylationFETRKGLSSHARSHL
HHHCCCCHHHHHHHH		28.8429396449
887PhosphorylationETRKGLSSHARSHLR
HHCCCCHHHHHHHHH		26.6329396449
891PhosphorylationGLSSHARSHLRQLGV
CCHHHHHHHHHHHCC		27.88-
911UbiquitinationSGAPIDLLYELVKQK
CCCCHHHHHHHHHHC		2.50-
933AcetylationGLPPGLAKKSSSLKE
CCCCCHHHCCCCHHH		59.2225953088
935PhosphorylationPPGLAKKSSSLKEVV
CCCHHHCCCCHHHHH		25.1826074081
936PhosphorylationPGLAKKSSSLKEVVA
CCHHHCCCCHHHHHC		48.8726074081
937PhosphorylationGLAKKSSSLKEVVAG
CHHHCCCCHHHHHCC		51.0226074081
939SumoylationAKKSSSLKEVVAGAP
HHCCCCHHHHHCCCC		50.8728112733
944UbiquitinationSLKEVVAGAPRPGLL
CHHHHHCCCCCCCHH		25.22-
955AcetylationPGLLSLAKPLDAPAV
CCHHHHCCCCCCHHH		51.9425953088
955SumoylationPGLLSLAKPLDAPAV
CCHHHHCCCCCCHHH		51.9428112733
967MethylationPAVNKAIKSPPGFSA
HHHHHHCCCCCCCCC		62.8723583077
967"N6,N6-dimethyllysine"PAVNKAIKSPPGFSA
HHHHHHCCCCCCCCC		62.87-
967AcetylationPAVNKAIKSPPGFSA
HHHHHHCCCCCCCCC		62.8725953088
967SumoylationPAVNKAIKSPPGFSA
HHHHHHCCCCCCCCC		62.8728112733
968PhosphorylationAVNKAIKSPPGFSAK
HHHHHCCCCCCCCCC		30.1625159151
973PhosphorylationIKSPPGFSAKGLGHP
CCCCCCCCCCCCCCC		34.6824732914
975MethylationSPPGFSAKGLGHPPS
CCCCCCCCCCCCCCC		54.17-
982PhosphorylationKGLGHPPSSPLLKKT
CCCCCCCCCCHHHCC		49.3823401153
983PhosphorylationGLGHPPSSPLLKKTP
CCCCCCCCCHHHCCC		25.9129255136
988SumoylationPSSPLLKKTPLALAG
CCCCHHHCCCCHHCC		56.17-
988SumoylationPSSPLLKKTPLALAG
CCCCHHHCCCCHHCC		56.1728112733
989PhosphorylationSSPLLKKTPLALAGS
CCCHHHCCCCHHCCC		23.1930266825
996PhosphorylationTPLALAGSPTPKNPE
CCCHHCCCCCCCCCC		21.7229255136
998PhosphorylationLALAGSPTPKNPEDK
CHHCCCCCCCCCCCC		48.9029255136
1000SumoylationLAGSPTPKNPEDKSP
HCCCCCCCCCCCCCC		83.8328112733
1005SumoylationTPKNPEDKSPQLSLS
CCCCCCCCCCCCCCC		63.4728112733
1006PhosphorylationPKNPEDKSPQLSLSP
CCCCCCCCCCCCCCC		30.1529255136
1010PhosphorylationEDKSPQLSLSPRPAS
CCCCCCCCCCCCCCC		22.8922167270
1012PhosphorylationKSPQLSLSPRPASPK
CCCCCCCCCCCCCCC		18.5822167270
1017PhosphorylationSLSPRPASPKAQWPQ
CCCCCCCCCCCCCCC		29.6222167270
1025PhosphorylationPKAQWPQSEDEGPLN
CCCCCCCCCCCCCCC		42.8330576142
1034PhosphorylationDEGPLNLTSGPEPAR
CCCCCCCCCCCCCCC		30.4826714015
1035PhosphorylationEGPLNLTSGPEPARD
CCCCCCCCCCCCCCC		56.3626714015
1056SumoylationGEFFENRKGLSSHAR
HHHHHCCCCCCHHHH		75.6428112733
1059PhosphorylationFENRKGLSSHARSHL
HHCCCCCCHHHHHHH		28.8429396449
1060PhosphorylationENRKGLSSHARSHLR
HCCCCCCHHHHHHHH		26.6329396449
1064PhosphorylationGLSSHARSHLRQMGV
CCCHHHHHHHHHCCC		27.88-
1072PhosphorylationHLRQMGVTEWYVNGS
HHHHCCCCEEEECCC		18.3124719451
1075PhosphorylationQMGVTEWYVNGSPID
HCCCCEEEECCCHHH		4.2727174698
1079PhosphorylationTEWYVNGSPIDTLRE
CEEEECCCHHHHHHH		17.3024732914
1083PhosphorylationVNGSPIDTLREILKR
ECCCHHHHHHHHHHH		28.5627174698
1092PhosphorylationREILKRRTQSRPGGP
HHHHHHHHCCCCCCC		34.6228555341
1094PhosphorylationILKRRTQSRPGGPPN
HHHHHHCCCCCCCCC		39.5726074081
1106PhosphorylationPPNPPGPSPKALAKM
CCCCCCCCHHHHHHH		44.9730266825
1108MethylationNPPGPSPKALAKMMG
CCCCCCHHHHHHHHC		61.44110924177
1108SumoylationNPPGPSPKALAKMMG
CCCCCCHHHHHHHHC		61.44-
1108SumoylationNPPGPSPKALAKMMG
CCCCCCHHHHHHHHC		61.4428112733
1112MethylationPSPKALAKMMGGAGP
CCHHHHHHHHCCCCC		30.2123644510
1112SumoylationPSPKALAKMMGGAGP
CCHHHHHHHHCCCCC		30.21-
1112SumoylationPSPKALAKMMGGAGP
CCHHHHHHHHCCCCC		30.2128112733
1121PhosphorylationMGGAGPGSSLEARSP
HCCCCCCCCCCCCCC		34.5821712546
1122PhosphorylationGGAGPGSSLEARSPS
CCCCCCCCCCCCCCC		35.8225159151
1127PhosphorylationGSSLEARSPSDLHIS
CCCCCCCCCCCCCCC		35.4823927012
1129PhosphorylationSLEARSPSDLHISPL
CCCCCCCCCCCCCHH		54.7923401153
1134PhosphorylationSPSDLHISPLAKKLP
CCCCCCCCHHHHCCC		11.7822167270
1138AcetylationLHISPLAKKLPPPPG
CCCCHHHHCCCCCCC		63.6325953088
1138SumoylationLHISPLAKKLPPPPG
CCCCHHHHCCCCCCC		63.6328112733
1139MethylationHISPLAKKLPPPPGS
CCCHHHHCCCCCCCC		61.7081424251
1139SumoylationHISPLAKKLPPPPGS
CCCHHHHCCCCCCCC		61.7028112733
1146PhosphorylationKLPPPPGSPLGHSPT
CCCCCCCCCCCCCCC		23.7929255136
1151PhosphorylationPGSPLGHSPTASPPP
CCCCCCCCCCCCCCC		23.3423927012
1153PhosphorylationSPLGHSPTASPPPTA
CCCCCCCCCCCCCCH		42.6625159151
1155PhosphorylationLGHSPTASPPPTARK
CCCCCCCCCCCCHHH		40.1825159151
1159PhosphorylationPTASPPPTARKMFPG
CCCCCCCCHHHHCCC		44.8823927012
1162"N6,N6,N6-trimethyllysine"SPPPTARKMFPGLAA
CCCCCHHHHCCCCCC		42.29-
1162MethylationSPPPTARKMFPGLAA
CCCCCHHHHCCCCCC		42.2918438403
1171PhosphorylationFPGLAAPSLPKKLKP
CCCCCCCCCCCCCCH		53.2122210691
1177AcetylationPSLPKKLKPEQIRVE
CCCCCCCCHHHHHHH		56.2218586567
1177SumoylationPSLPKKLKPEQIRVE
CCCCCCCCHHHHHHH		56.22-
1177SumoylationPSLPKKLKPEQIRVE
CCCCCCCCHHHHHHH		56.2228112733
1213PhosphorylationGAPREDMTPLNLSSR
CCCCCCCCCCCCCCC		36.6321815630
1218PhosphorylationDMTPLNLSSRAEPVR
CCCCCCCCCCCCCCC		19.3921815630
1219PhosphorylationMTPLNLSSRAEPVRD
CCCCCCCCCCCCCCC		38.3829978859
1240SumoylationGEFFENRKGLSSHAR
HHHHHCCCCCCHHHH		75.6428112733
1243PhosphorylationFENRKGLSSHARSHL
HHCCCCCCHHHHHHH		28.8422210691
1244PhosphorylationENRKGLSSHARSHLR
HCCCCCCHHHHHHHH		26.6329396449
1248PhosphorylationGLSSHARSHLRQMGV
CCCHHHHHHHHHCCC		27.88-
1256PhosphorylationHLRQMGVTEWSVNGS
HHHHCCCCCCEECCC		26.4724719451
1259PhosphorylationQMGVTEWSVNGSPID
HCCCCCCEECCCHHH		10.2422115753
1263PhosphorylationTEWSVNGSPIDTLRE
CCCEECCCHHHHHHH		17.3025159151
1267PhosphorylationVNGSPIDTLREILKK
ECCCHHHHHHHHHHH		28.5622199227
1282SumoylationKSKPCLIKKEPPAGD
CCCCCEECCCCCCCC		37.83-
1282SumoylationKSKPCLIKKEPPAGD
CCCCCEECCCCCCCC		37.8325772364
1301PhosphorylationLAEDGPPTVAPGPVQ
HHCCCCCCCCCCCCC		32.2229255136
1309PhosphorylationVAPGPVQSPLPLSPL
CCCCCCCCCCCCCCC		28.7429255136
1314PhosphorylationVQSPLPLSPLAGRPG
CCCCCCCCCCCCCCC		18.8729255136
1322MethylationPLAGRPGKPGAGPAQ
CCCCCCCCCCCCCCC		42.85116251991
1335PhosphorylationAQVPRELSLTPITGA
CCCCCEECCCCCCCC		25.9925159151
1337PhosphorylationVPRELSLTPITGAKP
CCCEECCCCCCCCCC		14.8529255136
1340PhosphorylationELSLTPITGAKPSAT
EECCCCCCCCCCCCC		32.0824732914
1343AcetylationLTPITGAKPSATGYL
CCCCCCCCCCCCCCC		40.6326051181
1343SumoylationLTPITGAKPSATGYL
CCCCCCCCCCCCCCC		40.6328112733
1345PhosphorylationPITGAKPSATGYLGS
CCCCCCCCCCCCCCC		37.4420068231
1347PhosphorylationTGAKPSATGYLGSVA
CCCCCCCCCCCCCCC		30.6020068231
1349PhosphorylationAKPSATGYLGSVAAK
CCCCCCCCCCCCCCC		11.9720068231
1352PhosphorylationSATGYLGSVAAKRPL
CCCCCCCCCCCCCCC		13.1420068231
1356MethylationYLGSVAAKRPLQEDR
CCCCCCCCCCCCCCC		44.8212654425
1356AcetylationYLGSVAAKRPLQEDR
CCCCCCCCCCCCCCC		44.8225953088
1356SumoylationYLGSVAAKRPLQEDR
CCCCCCCCCCCCCCC		44.82-
1356SumoylationYLGSVAAKRPLQEDR
CCCCCCCCCCCCCCC		44.8228112733
1363MethylationKRPLQEDRLLPAEVK
CCCCCCCCCCCHHHH		37.05115920069
1370SumoylationRLLPAEVKAKTYIQT
CCCCHHHHHHEEEEE		35.35-
1370SumoylationRLLPAEVKAKTYIQT
CCCCHHHHHHEEEEE		35.3528112733
1372SumoylationLPAEVKAKTYIQTEL
CCHHHHHHEEEEEEC		35.82-
1372SumoylationLPAEVKAKTYIQTEL
CCHHHHHHEEEEEEC		35.8228112733
1373PhosphorylationPAEVKAKTYIQTELP
CHHHHHHEEEEEECC		30.6228796482
1374PhosphorylationAEVKAKTYIQTELPF
HHHHHHEEEEEECCC		7.1328796482
1382MethylationIQTELPFKAKTLHEK
EEEECCCCCEECCHH		47.218275591
1382SumoylationIQTELPFKAKTLHEK
EEEECCCCCEECCHH		47.21-
1382SumoylationIQTELPFKAKTLHEK
EEEECCCCCEECCHH		47.2128112733
1384MethylationTELPFKAKTLHEKTS
EECCCCCEECCHHCC		52.818275601
1391PhosphorylationKTLHEKTSHSSTEAC
EECCHHCCCCHHHHH		32.2328555341
1393PhosphorylationLHEKTSHSSTEACCE
CCHHCCCCHHHHHHH		38.4321712546
1395PhosphorylationEKTSHSSTEACCELC
HHCCCCHHHHHHHHH		30.5328555341
1426PhosphorylationHLRQFGVTEWCVNGS
HHHHHCCCCHHCCCC		24.9320068231
1433PhosphorylationTEWCVNGSPIETLSE
CCHHCCCCCCHHHHH		19.9420068231
1437PhosphorylationVNGSPIETLSEWIKH
CCCCCCHHHHHHHHC		35.9820068231
1439PhosphorylationGSPIETLSEWIKHRP
CCCCHHHHHHHHCCC		38.0020068231
1448SumoylationWIKHRPQKVGAYRSY
HHHCCCCCCCHHHHH		45.3728112733
1460MethylationRSYIQGGRPFTKKFR
HHHHCCCCCCCHHHH		29.9581453791
1464MethylationQGGRPFTKKFRSAGH
CCCCCCCHHHHHCCC		50.74115978507
1464SumoylationQGGRPFTKKFRSAGH
CCCCCCCHHHHHCCC		50.7428112733
1468PhosphorylationPFTKKFRSAGHGRDS
CCCHHHHHCCCCCCC		41.5624144214
1475PhosphorylationSAGHGRDSDKRPSLG
HCCCCCCCCCCCCCC		43.6123401153
1477AcetylationGHGRDSDKRPSLGLA
CCCCCCCCCCCCCCC		70.8825953088
1477SumoylationGHGRDSDKRPSLGLA
CCCCCCCCCCCCCCC		70.8828112733
1480PhosphorylationRDSDKRPSLGLAPGG
CCCCCCCCCCCCCCC		38.8223401153
1493MethylationGGLAVVGRSAGGEPG
CCEEEECCCCCCCCC		16.24115920073
1494PhosphorylationGLAVVGRSAGGEPGP
CEEEECCCCCCCCCC		25.9021815630
1517PhosphorylationGERPLAASPPGTVKA
CCCCCCCCCCCCCCH		26.4830266825
1521PhosphorylationLAASPPGTVKAEEHQ
CCCCCCCCCCHHHHH		25.3021712546
1523SumoylationASPPGTVKAEEHQRQ
CCCCCCCCHHHHHHH		50.33-
1523SumoylationASPPGTVKAEEHQRQ
CCCCCCCCHHHHHHH		50.3325114211
1534SumoylationHQRQNINKFERRQAR
HHHHHHHHHHHHHCC		44.82-
1534SumoylationHQRQNINKFERRQAR
HHHHHHHHHHHHHCC		44.8228112733
1549MethylationPPDASAARGGEDTND
CCCHHHHCCCCCHHH		54.06115920077
1554PhosphorylationAARGGEDTNDLQQKL
HHCCCCCHHHHHHHH		26.7421955146
1560SumoylationDTNDLQQKLEEVRQP
CHHHHHHHHHHHHCC		44.92-
1560SumoylationDTNDLQQKLEEVRQP
CHHHHHHHHHHHHCC		44.9228112733
1594PhosphorylationVKFVGNIYTLKCRFC
EEECCCEEEEEEEEE		15.26-
1597UbiquitinationVGNIYTLKCRFCEVE
CCCEEEEEEEEEEEE		18.6321890473
1597 (in isoform 1)Ubiquitination-18.6321890473
1629PhosphorylationHILEMNFSKADPPPE
HHHHCCCCCCCCCCH		23.1724719451
1630UbiquitinationILEMNFSKADPPPEE
HHHCCCCCCCCCCHH		53.31-
1630SumoylationILEMNFSKADPPPEE
HHHCCCCCCCCCCHH		53.3128112733
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
1129SPhosphorylationKinaseCHEK1O14757
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of WIZ_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 WIZ_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EHMT2_HUMANEHMT2physical
16702210
CTBP1_HUMANCTBP1physical
16702210
CTBP2_HUMANCTBP2physical
16702210
ZC3H4_HUMANZC3H4physical
22939629
SUV91_HUMANSUV39H1physical
23455924
SUV92_HUMANSUV39H2physical
23455924
EHMT1_HUMANEHMT1physical
26344197
CDYL_HUMANCDYLphysical
26496610
EHMT2_HUMANEHMT2physical
26496610
PRP31_HUMANPRPF31physical
26496610
UACA_HUMANUACAphysical
26496610
MIER1_HUMANMIER1physical
26496610
RPA49_HUMANPOLR1Ephysical
26496610
MEP50_HUMANWDR77physical
26496610
EHMT1_HUMANEHMT1physical
26496610
ZN644_HUMANZNF644physical
26496610
UBP45_HUMANUSP45physical
26496610
CDYL2_HUMANCDYL2physical
26496610
BAP18_HUMANC17orf49physical
26496610
MIER3_HUMANMIER3physical
26496610
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of WIZ_HUMAN

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Related Literatures of Post-Translational Modification
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-1162, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-996; SER-1006; SER-1012AND SER-1017, AND MASS 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-996; SER-1012 ANDSER-1017, AND MASS SPECTROMETRY.
"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-1006; SER-1012;SER-1017; SER-1127; SER-1134; SER-1146; SER-1151 AND SER-1155, ANDMASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-996; SER-1127; SER-1134AND SER-1517, AND MASS SPECTROMETRY.
"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-1012 AND SER-1017, ANDMASS SPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1127, 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-1012 AND SER-1017, ANDMASS SPECTROMETRY.

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