SETB1_HUMAN - dbPTM
SETB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SETB1_HUMAN
UniProt AC Q15047
Protein Name Histone-lysine N-methyltransferase SETDB1
Gene Name SETDB1
Organism Homo sapiens (Human).
Sequence Length 1291
Subcellular Localization Nucleus. Chromosome. Associated with non-pericentromeric regions of chromatin. Excluded from nucleoli and islands of condensed chromatin.
Protein Description Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. H3 'Lys-9' trimethylation is coordinated with DNA methylation. Probably forms a complex with MBD1 and ATF7IP that represses transcription and couples DNA methylation and histone 'Lys-9' trimethylation. Its activity is dependent on MBD1 and is heritably maintained through DNA replication by being recruited by CAF-1. SETDB1 is targeted to histone H3 by TRIM28/TIF1B, a factor recruited by KRAB zinc-finger proteins. 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 MSSLPGCIGLDAATATVESEEIAELQQAVVEELGISMEELRHFIDEELEKMDCVQQRKKQLAELETWVIQKESEVAHVDQLFDDASRAVTNCESLVKDFYSKLGLQYRDSSSEDESSRPTEIIEIPDEDDDVLSIDSGDAGSRTPKDQKLREAMAALRKSAQDVQKFMDAVNKKSSSQDLHKGTLSQMSGELSKDGDLIVSMRILGKKRTKTWHKGTLIAIQTVGPGKKYKVKFDNKGKSLLSGNHIAYDYHPPADKLYVGSRVVAKYKDGNQVWLYAGIVAETPNVKNKLRFLIFFDDGYASYVTQSELYPICRPLKKTWEDIEDISCRDFIEEYVTAYPNRPMVLLKSGQLIKTEWEGTWWKSRVEEVDGSLVRILFLDDKRCEWIYRGSTRLEPMFSMKTSSASALEKKQGQLRTRPNMGAVRSKGPVVQYTQDLTGTGTQFKPVEPPQPTAPPAPPFPPAPPLSPQAGDSDLESQLAQSRKQVAKKSTSFRPGSVGSGHSSPTSPALSENVSGGKPGINQTYRSPLGSTASAPAPSALPAPPAPPVFHGMLERAPAEPSYRAPMEKLFYLPHVCSYTCLSRVRPMRNEQYRGKNPLLVPLLYDFRRMTARRRVNRKMGFHVIYKTPCGLCLRTMQEIERYLFETGCDFLFLEMFCLDPYVLVDRKFQPYKPFYYILDITYGKEDVPLSCVNEIDTTPPPQVAYSKERIPGKGVFINTGPEFLVGCDCKDGCRDKSKCACHQLTIQATACTPGGQINPNSGYQYKRLEECLPTGVYECNKRCKCDPNMCTNRLVQHGLQVRLQLFKTQNKGWGIRCLDDIAKGSFVCIYAGKILTDDFADKEGLEMGDEYFANLDHIESVENFKEGYESDAPCSSDSSGVDLKDQEDGNSGTEDPEESNDDSSDDNFCKDEDFSTSSVWRSYATRRQTRGQKENGLSETTSKDSHPPDLGPPHIPVPPSIPVGGCNPPSSEETPKNKVASWLSCNSVSEGGFADSDSHSSFKTNEGGEGRAGGSRMEAEKASTSGLGIKDEGDIKQAKKEDTDDRNKMSVVTESSRNYGYNPSPVKPEGLRRPPSKTSMHQSRRLMASAQSNPDDVLTLSSSTESEGESGTSRKPTAGQTSATAVDSDDIQTISSGSEGDDFEDKKNMTGPMKRQVAVKSTRGFALKSTHGIAIKSTNMASVDKGESAPVRKNTRQFYDGEESCYIIDAKLEGNLGRYLNHSCSPNLFVQNVFVDTHDLRFPWVAFFASKRIRAGTELTWDYNYEVGSVEGKELLCCCGAIECRGRLL
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
58UbiquitinationMDCVQQRKKQLAELE
CHHHHHHHHHHHHHH
40.3022817900
59UbiquitinationDCVQQRKKQLAELET
HHHHHHHHHHHHHHH
53.3722817900
59 (in isoform 1)Ubiquitination-53.3721890473
59 (in isoform 2)Ubiquitination-53.3721890473
59 (in isoform 3)Ubiquitination-53.3721890473
94PhosphorylationRAVTNCESLVKDFYS
HHHHCHHHHHHHHHH
40.4325159151
97UbiquitinationTNCESLVKDFYSKLG
HCHHHHHHHHHHHHC
47.6229967540
102UbiquitinationLVKDFYSKLGLQYRD
HHHHHHHHHCCCCCC
34.8829967540
107PhosphorylationYSKLGLQYRDSSSED
HHHHCCCCCCCCCCC
22.7921406692
110PhosphorylationLGLQYRDSSSEDESS
HCCCCCCCCCCCCCC
27.1121406692
111PhosphorylationGLQYRDSSSEDESSR
CCCCCCCCCCCCCCC
41.8721406692
112PhosphorylationLQYRDSSSEDESSRP
CCCCCCCCCCCCCCC
53.6821406692
116PhosphorylationDSSSEDESSRPTEII
CCCCCCCCCCCCEEE
43.9225137130
117PhosphorylationSSSEDESSRPTEIIE
CCCCCCCCCCCEEEE
39.9925137130
120PhosphorylationEDESSRPTEIIEIPD
CCCCCCCCEEEECCC
38.4125137130
134PhosphorylationDEDDDVLSIDSGDAG
CCCCCCEECCCCCCC
24.9725137130
137PhosphorylationDDVLSIDSGDAGSRT
CCCEECCCCCCCCCC
36.5825137130
142PhosphorylationIDSGDAGSRTPKDQK
CCCCCCCCCCHHHHH
34.4021406692
144PhosphorylationSGDAGSRTPKDQKLR
CCCCCCCCHHHHHHH
36.0721406692
166UbiquitinationKSAQDVQKFMDAVNK
HHHHHHHHHHHHHHH
42.3729967540
173AcetylationKFMDAVNKKSSSQDL
HHHHHHHHHCCCCHH
47.657711297
173UbiquitinationKFMDAVNKKSSSQDL
HHHHHHHHHCCCCHH
47.65-
174UbiquitinationFMDAVNKKSSSQDLH
HHHHHHHHCCCCHHH
50.8229967540
175PhosphorylationMDAVNKKSSSQDLHK
HHHHHHHCCCCHHHH
36.5122817900
177PhosphorylationAVNKKSSSQDLHKGT
HHHHHCCCCHHHHCC
34.5029214152
182SumoylationSSSQDLHKGTLSQMS
CCCCHHHHCCHHHHH
61.9728112733
182UbiquitinationSSSQDLHKGTLSQMS
CCCCHHHHCCHHHHH
61.9722817900
189PhosphorylationKGTLSQMSGELSKDG
HCCHHHHHCCCCCCC
22.8328555341
207UbiquitinationVSMRILGKKRTKTWH
EEEEECCCCCCCCCC
35.3232015554
230PhosphorylationTVGPGKKYKVKFDNK
EECCCCEEEEEECCC
25.2122817900
257UbiquitinationDYHPPADKLYVGSRV
CCCCCHHHEEEECEE
43.7729967540
259PhosphorylationHPPADKLYVGSRVVA
CCCHHHEEEECEEEE
14.4320068231
288UbiquitinationVAETPNVKNKLRFLI
EEECCCCCCCEEEEE
55.8130230243
319UbiquitinationPICRPLKKTWEDIED
HHHHCCCCCHHCHHH
67.5629967540
338PhosphorylationDFIEEYVTAYPNRPM
HHHHHHHHHCCCCCE
21.41-
349UbiquitinationNRPMVLLKSGQLIKT
CCCEEEEECCCEEEE
48.6721963094
350PhosphorylationRPMVLLKSGQLIKTE
CCEEEEECCCEEEEE
31.57-
355SumoylationLKSGQLIKTEWEGTW
EECCCEEEEEEECCC
49.32-
355SumoylationLKSGQLIKTEWEGTW
EECCCEEEEEEECCC
49.32-
355UbiquitinationLKSGQLIKTEWEGTW
EECCCEEEEEEECCC
49.3221963094
364UbiquitinationEWEGTWWKSRVEEVD
EEECCCHHHHEEEEC
21.68-
383UbiquitinationRILFLDDKRCEWIYR
EEEEECCCCCEEEEC
59.62-
400PhosphorylationTRLEPMFSMKTSSAS
CCCEECCCCCCCCCH
17.0824719451
407PhosphorylationSMKTSSASALEKKQG
CCCCCCCHHHHHHCC
35.0221964256
411UbiquitinationSSASALEKKQGQLRT
CCCHHHHHHCCCCCC
51.7729967540
427PhosphorylationPNMGAVRSKGPVVQY
CCCCCCCCCCCEEEE
35.0523663014
434PhosphorylationSKGPVVQYTQDLTGT
CCCCEEEEEECCCCC
8.5123663014
435PhosphorylationKGPVVQYTQDLTGTG
CCCEEEEEECCCCCC
9.8723663014
439PhosphorylationVQYTQDLTGTGTQFK
EEEEECCCCCCCCCC
40.7723663014
441PhosphorylationYTQDLTGTGTQFKPV
EEECCCCCCCCCCCC
31.6423663014
443PhosphorylationQDLTGTGTQFKPVEP
ECCCCCCCCCCCCCC
30.5823663014
468PhosphorylationFPPAPPLSPQAGDSD
CCCCCCCCCCCCCCH
22.2726074081
474PhosphorylationLSPQAGDSDLESQLA
CCCCCCCCHHHHHHH
43.0822817900
490TrimethylationSRKQVAKKSTSFRPG
HHHHHHHHCCCCCCC
49.59-
490MethylationSRKQVAKKSTSFRPG
HHHHHHHHCCCCCCC
49.5923644510
491PhosphorylationRKQVAKKSTSFRPGS
HHHHHHHCCCCCCCC
28.6922496350
492PhosphorylationKQVAKKSTSFRPGSV
HHHHHHCCCCCCCCC
40.5423312004
493PhosphorylationQVAKKSTSFRPGSVG
HHHHHCCCCCCCCCC
26.7523312004
495MethylationAKKSTSFRPGSVGSG
HHHCCCCCCCCCCCC
34.14115916537
498PhosphorylationSTSFRPGSVGSGHSS
CCCCCCCCCCCCCCC
26.4527732954
501PhosphorylationFRPGSVGSGHSSPTS
CCCCCCCCCCCCCCC
31.0427732954
504PhosphorylationGSVGSGHSSPTSPAL
CCCCCCCCCCCCHHH
41.3522496350
505PhosphorylationSVGSGHSSPTSPALS
CCCCCCCCCCCHHHC
26.9027732954
507PhosphorylationGSGHSSPTSPALSEN
CCCCCCCCCHHHCCC
49.6527732954
508PhosphorylationSGHSSPTSPALSENV
CCCCCCCCHHHCCCC
16.1527732954
512PhosphorylationSPTSPALSENVSGGK
CCCCHHHCCCCCCCC
29.2727732954
516PhosphorylationPALSENVSGGKPGIN
HHHCCCCCCCCCCCC
54.1027732954
525PhosphorylationGKPGINQTYRSPLGS
CCCCCCCCCCCCCCC
19.2025627689
528PhosphorylationGINQTYRSPLGSTAS
CCCCCCCCCCCCCCC
17.6729255136
532PhosphorylationTYRSPLGSTASAPAP
CCCCCCCCCCCCCCC
28.6029255136
533PhosphorylationYRSPLGSTASAPAPS
CCCCCCCCCCCCCCC
23.8829255136
535PhosphorylationSPLGSTASAPAPSAL
CCCCCCCCCCCCCCC
34.5729255136
540PhosphorylationTASAPAPSALPAPPA
CCCCCCCCCCCCCCC
44.5427080861
570UbiquitinationSYRAPMEKLFYLPHV
CCCCCHHHHHCCHHH
37.33-
579PhosphorylationFYLPHVCSYTCLSRV
HCCHHHHHHHHHHCC
23.5324719451
597UbiquitinationRNEQYRGKNPLLVPL
CCHHHCCCCCCHHHH
46.5221963094
597 (in isoform 1)Ubiquitination-46.5221890473
597 (in isoform 3)Ubiquitination-46.5221890473
598UbiquitinationNEQYRGKNPLLVPLL
CHHHCCCCCCHHHHH
34.9621890473
620AcetylationARRRVNRKMGFHVIY
HHHHHHHHCCEEEEE
37.8726051181
627PhosphorylationKMGFHVIYKTPCGLC
HCCEEEEEECCCCHH
14.02-
628AcetylationMGFHVIYKTPCGLCL
CCEEEEEECCCCHHH
34.5626051181
673PhosphorylationVDRKFQPYKPFYYIL
ECCCCCCCCCEEEEE
22.10-
677PhosphorylationFQPYKPFYYILDITY
CCCCCCEEEEEECCC
9.72-
678PhosphorylationQPYKPFYYILDITYG
CCCCCEEEEEECCCC
8.72-
699PhosphorylationSCVNEIDTTPPPQVA
HHEEECCCCCCCCEE
47.0325627689
700PhosphorylationCVNEIDTTPPPQVAY
HEEECCCCCCCCEEC
30.0125627689
715NeddylationSKERIPGKGVFINTG
CCCCCCCCCEEEECC
46.6932015554
715UbiquitinationSKERIPGKGVFINTG
CCCCCCCCCEEEECC
46.6932015554
716NeddylationKERIPGKGVFINTGP
CCCCCCCCEEEECCC
26.0332015554
716UbiquitinationKERIPGKGVFINTGP
CCCCCCCCEEEECCC
26.0332015554
732UbiquitinationFLVGCDCKDGCRDKS
CEECCCCCCCCCCCC
43.8532015554
733UbiquitinationLVGCDCKDGCRDKSK
EECCCCCCCCCCCCC
68.6932015554
779PhosphorylationECLPTGVYECNKRCK
HHCCCCHHHCCCCCC
18.9925159151
786AcetylationYECNKRCKCDPNMCT
HHCCCCCCCCCCCHH
45.7819824909
786UbiquitinationYECNKRCKCDPNMCT
HHCCCCCCCCCCCHH
45.78-
809AcetylationQVRLQLFKTQNKGWG
HHHHHHEECCCCCCC
58.7724471143
809UbiquitinationQVRLQLFKTQNKGWG
HHHHHHEECCCCCCC
58.77-
813UbiquitinationQLFKTQNKGWGIRCL
HHEECCCCCCCEEEH
46.3429967540
838PhosphorylationIYAGKILTDDFADKE
EECCCEECCCCCCHH
36.6816097034
862PhosphorylationANLDHIESVENFKEG
HCCHHHHHHHHHHCC
33.8422817900
867SumoylationIESVENFKEGYESDA
HHHHHHHHCCCCCCC
62.91-
867UbiquitinationIESVENFKEGYESDA
HHHHHHHHCCCCCCC
62.91-
872PhosphorylationNFKEGYESDAPCSSD
HHHCCCCCCCCCCCC
30.5025159151
877PhosphorylationYESDAPCSSDSSGVD
CCCCCCCCCCCCCCC
35.8025627689
878PhosphorylationESDAPCSSDSSGVDL
CCCCCCCCCCCCCCC
48.5025627689
880PhosphorylationDAPCSSDSSGVDLKD
CCCCCCCCCCCCCCC
30.8225627689
905PhosphorylationPEESNDDSSDDNFCK
CCCCCCCCCCCCCCC
38.2322817900
906PhosphorylationEESNDDSSDDNFCKD
CCCCCCCCCCCCCCC
56.8522817900
917PhosphorylationFCKDEDFSTSSVWRS
CCCCCCCCHHHHHHH
39.4425159151
918PhosphorylationCKDEDFSTSSVWRSY
CCCCCCCHHHHHHHH
25.6425159151
919PhosphorylationKDEDFSTSSVWRSYA
CCCCCCHHHHHHHHH
22.9927732954
920PhosphorylationDEDFSTSSVWRSYAT
CCCCCHHHHHHHHHH
26.2825159151
972PhosphorylationVGGCNPPSSEETPKN
CCCCCCCCCCCCCCC
52.1925627689
973PhosphorylationGGCNPPSSEETPKNK
CCCCCCCCCCCCCCC
45.2725627689
976PhosphorylationNPPSSEETPKNKVAS
CCCCCCCCCCCCCCH
35.2025159151
983PhosphorylationTPKNKVASWLSCNSV
CCCCCCCHHHCCCCC
31.3823312004
986PhosphorylationNKVASWLSCNSVSEG
CCCCHHHCCCCCCCC
12.6623312004
991PhosphorylationWLSCNSVSEGGFADS
HHCCCCCCCCCCCCC
30.2830576142
998PhosphorylationSEGGFADSDSHSSFK
CCCCCCCCCCCCCCC
37.2724247654
1000PhosphorylationGGFADSDSHSSFKTN
CCCCCCCCCCCCCCC
29.2630576142
1002PhosphorylationFADSDSHSSFKTNEG
CCCCCCCCCCCCCCC
41.2323312004
1003PhosphorylationADSDSHSSFKTNEGG
CCCCCCCCCCCCCCC
25.9130576142
1004PhosphorylationDSDSHSSFKTNEGGE
CCCCCCCCCCCCCCC
14.6933259812
1006PhosphorylationDSHSSFKTNEGGEGR
CCCCCCCCCCCCCCC
36.1723312004
1017PhosphorylationGEGRAGGSRMEAEKA
CCCCCCCCHHHHHHH
27.7722985185
1025PhosphorylationRMEAEKASTSGLGIK
HHHHHHHHCCCCCCC
33.8920873877
1026PhosphorylationMEAEKASTSGLGIKD
HHHHHHHCCCCCCCC
31.5120873877
1027PhosphorylationEAEKASTSGLGIKDE
HHHHHHCCCCCCCCC
29.5320873877
1032SumoylationSTSGLGIKDEGDIKQ
HCCCCCCCCCCCHHH
48.18-
1032AcetylationSTSGLGIKDEGDIKQ
HCCCCCCCCCCCHHH
48.1826051181
1032SumoylationSTSGLGIKDEGDIKQ
HCCCCCCCCCCCHHH
48.1828112733
1038SumoylationIKDEGDIKQAKKEDT
CCCCCCHHHHHHHCC
49.2828112733
1042UbiquitinationGDIKQAKKEDTDDRN
CCHHHHHHHCCCCCC
64.93-
1045PhosphorylationKQAKKEDTDDRNKMS
HHHHHHCCCCCCCCE
40.67-
1050UbiquitinationEDTDDRNKMSVVTES
HCCCCCCCCEEEECC
33.18-
1055PhosphorylationRNKMSVVTESSRNYG
CCCCEEEECCCCCCC
28.1720068231
1057PhosphorylationKMSVVTESSRNYGYN
CCEEEECCCCCCCCC
25.8220068231
1058PhosphorylationMSVVTESSRNYGYNP
CEEEECCCCCCCCCC
20.5028555341
1061PhosphorylationVTESSRNYGYNPSPV
EECCCCCCCCCCCCC
21.6323927012
1063PhosphorylationESSRNYGYNPSPVKP
CCCCCCCCCCCCCCC
17.3422167270
1066PhosphorylationRNYGYNPSPVKPEGL
CCCCCCCCCCCCCCC
38.3922167270
1066 (in isoform 3)Phosphorylation-38.39-
1067PhosphorylationNYGYNPSPVKPEGLR
CCCCCCCCCCCCCCC
39.1332645325
1069SumoylationGYNPSPVKPEGLRRP
CCCCCCCCCCCCCCC
40.51-
1069AcetylationGYNPSPVKPEGLRRP
CCCCCCCCCCCCCCC
40.5126051181
1069SumoylationGYNPSPVKPEGLRRP
CCCCCCCCCCCCCCC
40.5128112733
1078PhosphorylationEGLRRPPSKTSMHQS
CCCCCCCCCCCHHHH
51.7724719451
1080PhosphorylationLRRPPSKTSMHQSRR
CCCCCCCCCHHHHHH
35.3020860994
1081PhosphorylationRRPPSKTSMHQSRRL
CCCCCCCCHHHHHHH
20.2920860994
1085PhosphorylationSKTSMHQSRRLMASA
CCCCHHHHHHHHHHH
12.5120860994
1101PhosphorylationSNPDDVLTLSSSTES
CCCCCEEEEECCCCC
25.1722817900
1103PhosphorylationPDDVLTLSSSTESEG
CCCEEEEECCCCCCC
19.6022817900
1104PhosphorylationDDVLTLSSSTESEGE
CCEEEEECCCCCCCC
44.3822817900
1106PhosphorylationVLTLSSSTESEGESG
EEEEECCCCCCCCCC
45.5422817900
1108PhosphorylationTLSSSTESEGESGTS
EEECCCCCCCCCCCC
51.4922817900
1112PhosphorylationSTESEGESGTSRKPT
CCCCCCCCCCCCCCC
59.2222210691
1119PhosphorylationSGTSRKPTAGQTSAT
CCCCCCCCCCCCCCE
46.5925072903
1123PhosphorylationRKPTAGQTSATAVDS
CCCCCCCCCCEEECH
21.2921406692
1124PhosphorylationKPTAGQTSATAVDSD
CCCCCCCCCEEECHH
18.7421406692
1126PhosphorylationTAGQTSATAVDSDDI
CCCCCCCEEECHHHC
27.2921406692
1130PhosphorylationTSATAVDSDDIQTIS
CCCEEECHHHCCEEC
30.5020363803
1135PhosphorylationVDSDDIQTISSGSEG
ECHHHCCEECCCCCC
24.1425072903
1137PhosphorylationSDDIQTISSGSEGDD
HHHCCEECCCCCCCC
31.8425072903
1138PhosphorylationDDIQTISSGSEGDDF
HHCCEECCCCCCCCC
42.3525072903
1140PhosphorylationIQTISSGSEGDDFED
CCEECCCCCCCCCCC
40.1125072903
1149SumoylationGDDFEDKKNMTGPMK
CCCCCCCCCCCCCCH
65.36-
1149SumoylationGDDFEDKKNMTGPMK
CCCCCCCCCCCCCCH
65.3628112733
1152PhosphorylationFEDKKNMTGPMKRQV
CCCCCCCCCCCHHEE
47.7520860994
1162MethylationMKRQVAVKSTRGFAL
CHHEEEEEECCCEEE
36.0583136539
1163PhosphorylationKRQVAVKSTRGFALK
HHEEEEEECCCEEEE
19.41-
1170"N6,N6,N6-trimethyllysine"STRGFALKSTHGIAI
ECCCEEEEECCEEEE
50.29-
1170MethylationSTRGFALKSTHGIAI
ECCCEEEEECCEEEE
50.2924129315
1178"N6,N6,N6-trimethyllysine"STHGIAIKSTNMASV
ECCEEEEEECCCCCC
42.05-
1178MethylationSTHGIAIKSTNMASV
ECCEEEEEECCCCCC
42.0524129315
1178UbiquitinationSTHGIAIKSTNMASV
ECCEEEEEECCCCCC
42.0529967540
1179PhosphorylationTHGIAIKSTNMASVD
CCEEEEEECCCCCCC
20.9223312004
1180PhosphorylationHGIAIKSTNMASVDK
CEEEEEECCCCCCCC
24.8222817900
1180 (in isoform 3)Phosphorylation-24.82-
1184PhosphorylationIKSTNMASVDKGESA
EEECCCCCCCCCCCC
21.7823312004
1187UbiquitinationTNMASVDKGESAPVR
CCCCCCCCCCCCCCC
63.5229967540
1190PhosphorylationASVDKGESAPVRKNT
CCCCCCCCCCCCCCC
46.6820068231
1190 (in isoform 3)Phosphorylation-46.68-
1197PhosphorylationSAPVRKNTRQFYDGE
CCCCCCCCCCEECCC
28.9620068231
1197 (in isoform 3)Phosphorylation-28.96-
1271PhosphorylationDYNYEVGSVEGKELL
ECCCCCCCCCCCEEE
23.3627251275

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
976TPhosphorylationKinaseNLKQ9UBE8
Uniprot
1066SPhosphorylationKinaseCDK2P24941
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SETB1_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 SETB1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SUZ12_HUMANSUZ12physical
14536086
TIF1B_HUMANTRIM28physical
11959841
PO5F1_HUMANPOU5F1physical
19884257
DNM3A_HUMANDNMT3Aphysical
16682412
DNM3B_HUMANDNMT3Bphysical
16682412
ESCO2_HUMANESCO2physical
18501190
H31_HUMANHIST1H3Aphysical
11252719
MBD1_HUMANMBD1physical
15327775
CAF1A_HUMANCHAF1Aphysical
15327775
H31_HUMANHIST1H3Aphysical
21243721
ESCO1_HUMANESCO1physical
20331966
ZN274_HUMANZNF274physical
21170338
PSME1_HUMANPSME1physical
21900206
MZT2B_HUMANMZT2Bphysical
21900206
LC7L2_HUMANLUC7L2physical
21900206
JARD2_HUMANJARID2physical
22110129
PML_HUMANPMLphysical
21921037
TCRG1_HUMANTCERG1physical
15383276
LRIF1_HUMANLRIF1physical
15383276
AT2A1_HUMANATP2A1physical
26186194
TTC1_HUMANTTC1physical
26186194
EXOC4_HUMANEXOC4physical
26186194
MCAF1_HUMANATF7IPphysical
26186194
HECD1_HUMANHECTD1physical
26186194
MCUB_HUMANCCDC109Bphysical
26186194
FAF2_HUMANFAF2physical
26186194
CC85C_HUMANCCDC85Cphysical
26186194
EXOC5_HUMANEXOC5physical
26186194
FBX30_HUMANFBXO30physical
26186194
ACOT9_HUMANACOT9physical
26186194
MCAF1_HUMANATF7IPphysical
28514442
MCUB_HUMANCCDC109Bphysical
28514442
FAF2_HUMANFAF2physical
28514442
AT2A1_HUMANATP2A1physical
28514442
EXOC4_HUMANEXOC4physical
28514442
EXOC5_HUMANEXOC5physical
28514442
TTC1_HUMANTTC1physical
28514442
CC85C_HUMANCCDC85Cphysical
28514442
FBX30_HUMANFBXO30physical
28514442
ACOT9_HUMANACOT9physical
28514442
SUCA_HUMANSUCLG1physical
27173435

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 SETB1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-1066, AND MASSSPECTROMETRY.
"Quantitative analysis of global ubiquitination in HeLa cells by massspectrometry.";
Meierhofer D., Wang X., Huang L., Kaiser P.;
J. Proteome Res. 7:4566-4576(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, UBIQUITINATION[LARGE SCALE ANALYSIS] AT LYS-182, 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-1066, 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-1179; THR-1180 ANDSER-1190, AND MASS SPECTROMETRY.
"Global phosphoproteome analysis on human HepG2 hepatocytes usingreversed-phase diagonal LC.";
Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K.,Demol H., Martens L., Goethals M., Vandekerckhove J.;
Proteomics 5:3589-3599(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-838, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"Quantitative analysis of global ubiquitination in HeLa cells by massspectrometry.";
Meierhofer D., Wang X., Huang L., Kaiser P.;
J. Proteome Res. 7:4566-4576(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, UBIQUITINATION[LARGE SCALE ANALYSIS] AT LYS-182, AND MASS SPECTROMETRY.

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