ZN638_HUMAN - dbPTM
ZN638_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN638_HUMAN
UniProt AC Q14966
Protein Name Zinc finger protein 638
Gene Name ZNF638
Organism Homo sapiens (Human).
Sequence Length 1978
Subcellular Localization Nucleus speckle .
Protein Description Early regulator of adipogenesis that works as a transcription cofactor of CEBPs, controlling the expression of PPARG and probably of other proadipogenic genes, such as SREBF1 (By similarity). Binds to cytidine clusters in double-stranded DNA. [PubMed: 8647861 May also regulate alternative splicing of target genes during adipogenesis (By similarity]
Protein Sequence MSRPRFNPRGDFPLQRPRAPNPSGMRPPGPFMRPGSMGLPRFYPAGRARGIPHRFAGHESYQNMGPQRMNVQVTQHRTDPRLTKEKLDFHEAQQKKGKPHGSRWDDEPHISASVAVKQSSVTQVTEQSPKVQSRYTKESASSILASFGLSNEDLEELSRYPDEQLTPENMPLILRDIRMRKMGRRLPNLPSQSRNKETLGSEAVSSNVIDYGHASKYGYTEDPLEVRIYDPEIPTDEVENEFQSQQNISASVPNPNVICNSMFPVEDVFRQMDFPGESSNNRSFFSVESGTKMSGLHISGGQSVLEPIKSVNQSINQTVSQTMSQSLIPPSMNQQPFSSELISSVSQQERIPHEPVINSSNVHVGSRGSKKNYQSQADIPIRSPFGIVKASWLPKFSHADAQKMKRLPTPSMMNDYYAASPRIFPHLCSLCNVECSHLKDWIQHQNTSTHIESCRQLRQQYPDWNPEILPSRRNEGNRKENETPRRRSHSPSPRRSRRSSSSHRFRRSRSPMHYMYRPRSRSPRICHRFISRYRSRSRSRSPYRIRNPFRGSPKCFRSVSPERMSRRSVRSSDRKKALEDVVQRSGHGTEFNKQKHLEAADKGHSPAQKPKTSSGTKPSVKPTSATKSDSNLGGHSIRCKSKNLEDDTLSECKQVSDKAVSLQRKLRKEQSLHYGSVLLITELPEDGCTEEDVRKLFQPFGKVNDVLIVPYRKEAYLEMEFKEAITAIMKYIETTPLTIKGKSVKICVPGKKKAQNKEVKKKTLESKKVSASTLKRDADASKAVEIVTSTSAAKTGQAKASVAKVNKSTGKSASSVKSVVTVAVKGNKASIKTAKSGGKKSLEAKKTGNVKNKDSNKPVTIPENSEIKTSIEVKATENCAKEAISDAALEATENEPLNKETEEMCVMLVSNLPNKGYSVEEVYDLAKPFGGLKDILILSSHKKAYIEINRKAAESMVKFYTCFPVLMDGNQLSISMAPENMNIKDEEAIFITLVKENDPEANIDTIYDRFVHLDNLPEDGLQCVLCVGLQFGKVDHHVFISNRNKAILQLDSPESAQSMYSFLKQNPQNIGDHMLTCSLSPKIDLPEVQIEHDPELEKESPGLKNSPIDESEVQTATDSPSVKPNELEEESTPSIQTETLVQQEEPCEEEAEKATCDSDFAVETLELETQGEEVKEEIPLVASASVSIEQFTENAEECALNQQMFNSDLEKKGAEIINPKTALLPSDSVFAEERNLKGILEESPSEAEDFISGITQTMVEAVAEVEKNETVSEILPSTCIVTLVPGIPTGDEKTVDKKNISEKKGNMDEKEEKEFNTKETRMDLQIGTEKAEKNEGRMDAEKVEKMAAMKEKPAENTLFKAYPNKGVGQANKPDETSKTSILAVSDVSSSKPSIKAVIVSSPKAKATVSKTENQKSFPKSVPRDQINAEKKLSAKEFGLLKPTSARSGLAESSSKFKPTQSSLTRGGSGRISALQGKLSKLDYRDITKQSQETEARPSIMKRDDSNNKTLAEQNTKNPKSTTGRSSKSKEEPLFPFNLDEFVTVDEVIEEVNPSQAKQNPLKGKRKETLKNVPFSELNLKKKKGKTSTPRGVEGELSFVTLDEIGEEEDAAAHLAQALVTVDEVIDEEELNMEEMVKNSNSLFTLDELIDQDDCISHSEPKDVTVLSVAEEQDLLKQERLVTVDEIGEVEELPLNESADITFATLNTKGNEGDTVRDSIGFISSQVPEDPSTLVTVDEIQDDSSDLHLVTLDEVTEEDEDSLADFNNLKEELNFVTVDEVGEEEDGDNDLKVELAQSKNDHPTDKKGNRKKRAVDTKKTKLESLSQVGPVNENVMEEDLKTMIERHLTAKTPTKRVRIGKTLPSEKAVVTEPAKGEEAFQMSEVDEESGLKDSEPERKRKKTEDSSSGKSVASDVPEELDFLVPKAGFFCPICSLFYSGEKAMTNHCKSTRHKQNTEKFMAKQRKEKEQNEAEERSSR
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
33DimethylationRPPGPFMRPGSMGLP
CCCCCCCCCCCCCCC
32.57-
33MethylationRPPGPFMRPGSMGLP
CCCCCCCCCCCCCCC
32.5754561969
36PhosphorylationGPFMRPGSMGLPRFY
CCCCCCCCCCCCCCC
16.6224719451
41DimethylationPGSMGLPRFYPAGRA
CCCCCCCCCCCCCCC
49.09-
41MethylationPGSMGLPRFYPAGRA
CCCCCCCCCCCCCCC
49.0954561985
47Asymmetric dimethylargininePRFYPAGRARGIPHR
CCCCCCCCCCCCCCC
24.18-
47MethylationPRFYPAGRARGIPHR
CCCCCCCCCCCCCCC
24.1824129315
49Asymmetric dimethylarginineFYPAGRARGIPHRFA
CCCCCCCCCCCCCCC
42.06-
49MethylationFYPAGRARGIPHRFA
CCCCCCCCCCCCCCC
42.0624129315
54Asymmetric dimethylarginineRARGIPHRFAGHESY
CCCCCCCCCCCCHHH
20.11-
54MethylationRARGIPHRFAGHESY
CCCCCCCCCCCCHHH
20.1124129315
61PhosphorylationRFAGHESYQNMGPQR
CCCCCHHHHCCCCCC
10.8317360941
68DimethylationYQNMGPQRMNVQVTQ
HHCCCCCCCCEEEEE
23.06-
68MethylationYQNMGPQRMNVQVTQ
HHCCCCCCCCEEEEE
23.0630763587
86UbiquitinationDPRLTKEKLDFHEAQ
CCCCCHHHCCHHHHH
55.71-
96UbiquitinationFHEAQQKKGKPHGSR
HHHHHHHCCCCCCCC
68.76-
119PhosphorylationASVAVKQSSVTQVTE
CEEEEECCCCEEECC
22.5123403867
120PhosphorylationSVAVKQSSVTQVTEQ
EEEEECCCCEEECCC
27.0424732914
122PhosphorylationAVKQSSVTQVTEQSP
EEECCCCEEECCCCC
21.1928348404
125PhosphorylationQSSVTQVTEQSPKVQ
CCCCEEECCCCCCHH
20.6325159151
128PhosphorylationVTQVTEQSPKVQSRY
CEEECCCCCCHHCCC
22.0619664994
130UbiquitinationQVTEQSPKVQSRYTK
EECCCCCCHHCCCCH
59.14-
133PhosphorylationEQSPKVQSRYTKESA
CCCCCHHCCCCHHHH
30.1824732914
191PhosphorylationRRLPNLPSQSRNKET
HCCCCCCCCCCCCHH
43.9123186163
193PhosphorylationLPNLPSQSRNKETLG
CCCCCCCCCCCHHHC
42.0023186163
196AcetylationLPSQSRNKETLGSEA
CCCCCCCCHHHCCHH
51.4726051181
196UbiquitinationLPSQSRNKETLGSEA
CCCCCCCCHHHCCHH
51.47-
216UbiquitinationIDYGHASKYGYTEDP
CCCCCHHHCCCCCCC
43.40-
219PhosphorylationGHASKYGYTEDPLEV
CCHHHCCCCCCCCEE
12.1327642862
279PhosphorylationMDFPGESSNNRSFFS
CCCCCCCCCCCCEEE
33.5529214152
283PhosphorylationGESSNNRSFFSVESG
CCCCCCCCEEEECCC
32.5425159151
286PhosphorylationSNNRSFFSVESGTKM
CCCCCEEEECCCCCC
23.9823312004
289PhosphorylationRSFFSVESGTKMSGL
CCEEEECCCCCCEEE
50.0023917254
291PhosphorylationFFSVESGTKMSGLHI
EEEECCCCCCEEEEE
32.6225627689
292SumoylationFSVESGTKMSGLHIS
EEECCCCCCEEEEEC
34.3028112733
294PhosphorylationVESGTKMSGLHISGG
ECCCCCCEEEEECCC
39.5023312004
299PhosphorylationKMSGLHISGGQSVLE
CCEEEEECCCCCCHH
26.5625159151
303PhosphorylationLHISGGQSVLEPIKS
EEECCCCCCHHHHHH
31.7628450419
359PhosphorylationPHEPVINSSNVHVGS
CCCCCCCCCCCEECC
16.5021406692
360PhosphorylationHEPVINSSNVHVGSR
CCCCCCCCCCEECCC
38.0820068231
366PhosphorylationSSNVHVGSRGSKKNY
CCCCEECCCCCCCCC
32.1720068231
367MethylationSNVHVGSRGSKKNYQ
CCCEECCCCCCCCCC
47.69115920557
369PhosphorylationVHVGSRGSKKNYQSQ
CEECCCCCCCCCCCC
39.0725159151
371UbiquitinationVGSRGSKKNYQSQAD
ECCCCCCCCCCCCCC
63.69-
373PhosphorylationSRGSKKNYQSQADIP
CCCCCCCCCCCCCCC
20.5824732914
375PhosphorylationGSKKNYQSQADIPIR
CCCCCCCCCCCCCCC
19.5823898821
382MethylationSQADIPIRSPFGIVK
CCCCCCCCCCCCEEE
32.68115920561
383PhosphorylationQADIPIRSPFGIVKA
CCCCCCCCCCCEEEH
25.8725159151
409PhosphorylationQKMKRLPTPSMMNDY
HHHHCCCCHHHHCCH
32.3721712546
411PhosphorylationMKRLPTPSMMNDYYA
HHCCCCHHHHCCHHH
32.8923312004
416PhosphorylationTPSMMNDYYAASPRI
CHHHHCCHHHCCCCH
7.0426462736
417PhosphorylationPSMMNDYYAASPRIF
HHHHCCHHHCCCCHH
9.8828450419
420PhosphorylationMNDYYAASPRIFPHL
HCCHHHCCCCHHHHH
13.4125159151
488PhosphorylationNETPRRRSHSPSPRR
CCCCCCCCCCCCCCC
26.8927362937
490PhosphorylationTPRRRSHSPSPRRSR
CCCCCCCCCCCCCCC
28.4620363803
492PhosphorylationRRRSHSPSPRRSRRS
CCCCCCCCCCCCCCC
33.7727362937
496PhosphorylationHSPSPRRSRRSSSSH
CCCCCCCCCCCCCCC
33.0717081983
499PhosphorylationSPRRSRRSSSSHRFR
CCCCCCCCCCCCCHH
33.2023663014
500PhosphorylationPRRSRRSSSSHRFRR
CCCCCCCCCCCCHHH
33.7723663014
501PhosphorylationRRSRRSSSSHRFRRS
CCCCCCCCCCCHHHC
31.2623663014
502PhosphorylationRSRRSSSSHRFRRSR
CCCCCCCCCCHHHCC
22.1923663014
508PhosphorylationSSHRFRRSRSPMHYM
CCCCHHHCCCCCCHH
32.6223401153
510PhosphorylationHRFRRSRSPMHYMYR
CCHHHCCCCCCHHCC
28.0223401153
514PhosphorylationRSRSPMHYMYRPRSR
HCCCCCCHHCCCCCC
6.9230631047
516PhosphorylationRSPMHYMYRPRSRSP
CCCCCHHCCCCCCCH
15.4223403867
520PhosphorylationHYMYRPRSRSPRICH
CHHCCCCCCCHHHHH
39.5320068231
522PhosphorylationMYRPRSRSPRICHRF
HCCCCCCCHHHHHHH
21.5620068231
527 (in isoform 5)Ubiquitination-25.8921906983
537PhosphorylationISRYRSRSRSRSPYR
HHHHHHCCCCCCCCC
35.5424144214
539PhosphorylationRYRSRSRSRSPYRIR
HHHHCCCCCCCCCCC
38.0520068231
541PhosphorylationRSRSRSRSPYRIRNP
HHCCCCCCCCCCCCC
27.7720068231
543PhosphorylationRSRSRSPYRIRNPFR
CCCCCCCCCCCCCCC
21.6624719451
552PhosphorylationIRNPFRGSPKCFRSV
CCCCCCCCCCCCCCC
19.5522167270
557MethylationRGSPKCFRSVSPERM
CCCCCCCCCCCHHHH
45.69115386535
558PhosphorylationGSPKCFRSVSPERMS
CCCCCCCCCCHHHHH
13.4923401153
560PhosphorylationPKCFRSVSPERMSRR
CCCCCCCCHHHHHHH
23.4523401153
565PhosphorylationSVSPERMSRRSVRSS
CCCHHHHHHHCCCHH
30.6623090842
568PhosphorylationPERMSRRSVRSSDRK
HHHHHHHCCCHHHHH
22.29-
571PhosphorylationMSRRSVRSSDRKKAL
HHHHCCCHHHHHHHH
34.1428102081
572PhosphorylationSRRSVRSSDRKKALE
HHHCCCHHHHHHHHH
30.7628102081
576UbiquitinationVRSSDRKKALEDVVQ
CCHHHHHHHHHHHHH
60.13-
585PhosphorylationLEDVVQRSGHGTEFN
HHHHHHHCCCCHHHC
20.3225159151
589PhosphorylationVQRSGHGTEFNKQKH
HHHCCCCHHHCHHHH
31.5620068231
593UbiquitinationGHGTEFNKQKHLEAA
CCCHHHCHHHHHHHH
67.07-
602AcetylationKHLEAADKGHSPAQK
HHHHHHHCCCCCCCC
54.5225953088
602UbiquitinationKHLEAADKGHSPAQK
HHHHHHHCCCCCCCC
54.52-
605PhosphorylationEAADKGHSPAQKPKT
HHHHCCCCCCCCCCC
30.5123927012
612PhosphorylationSPAQKPKTSSGTKPS
CCCCCCCCCCCCCCC
36.3329496963
613PhosphorylationPAQKPKTSSGTKPSV
CCCCCCCCCCCCCCC
32.6622199227
614PhosphorylationAQKPKTSSGTKPSVK
CCCCCCCCCCCCCCC
56.5725159151
616PhosphorylationKPKTSSGTKPSVKPT
CCCCCCCCCCCCCCC
41.5522199227
619PhosphorylationTSSGTKPSVKPTSAT
CCCCCCCCCCCCCCC
44.3127174698
623PhosphorylationTKPSVKPTSATKSDS
CCCCCCCCCCCCCCC
25.8522199227
624PhosphorylationKPSVKPTSATKSDSN
CCCCCCCCCCCCCCC
42.3325159151
626PhosphorylationSVKPTSATKSDSNLG
CCCCCCCCCCCCCCC
30.7425159151
628PhosphorylationKPTSATKSDSNLGGH
CCCCCCCCCCCCCCC
41.7525159151
630PhosphorylationTSATKSDSNLGGHSI
CCCCCCCCCCCCCCE
40.8325159151
636PhosphorylationDSNLGGHSIRCKSKN
CCCCCCCCEEEECCC
18.2723401153
641PhosphorylationGHSIRCKSKNLEDDT
CCCEEEECCCCCCCC
30.3323401153
642AcetylationHSIRCKSKNLEDDTL
CCEEEECCCCCCCCH
51.5526051181
648PhosphorylationSKNLEDDTLSECKQV
CCCCCCCCHHHHHHH
44.5026552605
650PhosphorylationNLEDDTLSECKQVSD
CCCCCCHHHHHHHHH
42.9423401153
653UbiquitinationDDTLSECKQVSDKAV
CCCHHHHHHHHHHHH
50.08-
656PhosphorylationLSECKQVSDKAVSLQ
HHHHHHHHHHHHHHH
30.7929116813
658AcetylationECKQVSDKAVSLQRK
HHHHHHHHHHHHHHH
43.0925953088
658UbiquitinationECKQVSDKAVSLQRK
HHHHHHHHHHHHHHH
43.09-
661PhosphorylationQVSDKAVSLQRKLRK
HHHHHHHHHHHHHHH
24.5228188228
671PhosphorylationRKLRKEQSLHYGSVL
HHHHHHHCCCCCCEE
20.4328348404
674PhosphorylationRKEQSLHYGSVLLIT
HHHHCCCCCCEEEEE
19.1828348404
676PhosphorylationEQSLHYGSVLLITEL
HHCCCCCCEEEEEEC
11.4828348404
716PhosphorylationVPYRKEAYLEMEFKE
EECCHHHHHHHHHHH
12.32-
731PhosphorylationAITAIMKYIETTPLT
HHHHHHHHHHCCCEE
6.14-
738PhosphorylationYIETTPLTIKGKSVK
HHHCCCEEECCEEEE
23.11-
743PhosphorylationPLTIKGKSVKICVPG
CEEECCEEEEEECCC
36.9925367160
770PhosphorylationTLESKKVSASTLKRD
HHHCCCCCHHHHCCC
25.9423312004
772PhosphorylationESKKVSASTLKRDAD
HCCCCCHHHHCCCCC
27.1123312004
773PhosphorylationSKKVSASTLKRDADA
CCCCCHHHHCCCCCH
35.6923312004
775SumoylationKVSASTLKRDADASK
CCCHHHHCCCCCHHH
48.6028112733
788PhosphorylationSKAVEIVTSTSAAKT
HHCEEEEECCCHHHH
31.7621406692
789PhosphorylationKAVEIVTSTSAAKTG
HCEEEEECCCHHHHC
14.9625159151
790PhosphorylationAVEIVTSTSAAKTGQ
CEEEEECCCHHHHCC
17.0221406692
791PhosphorylationVEIVTSTSAAKTGQA
EEEEECCCHHHHCCC
26.4622199227
795PhosphorylationTSTSAAKTGQAKASV
ECCCHHHHCCCEEEE
29.7822817900
801PhosphorylationKTGQAKASVAKVNKS
HHCCCEEEEEEECCC
23.1522817900
808PhosphorylationSVAKVNKSTGKSASS
EEEEECCCCCCCHHH
36.8722817900
809PhosphorylationVAKVNKSTGKSASSV
EEEECCCCCCCHHHC
50.6822817900
815PhosphorylationSTGKSASSVKSVVTV
CCCCCHHHCEEEEEE
33.0324719451
818PhosphorylationKSASSVKSVVTVAVK
CCHHHCEEEEEEEEE
21.4725954137
821PhosphorylationSSVKSVVTVAVKGNK
HHCEEEEEEEEECCC
10.6924719451
825AcetylationSVVTVAVKGNKASIK
EEEEEEEECCCHHEE
47.2125953088
853AcetylationKTGNVKNKDSNKPVT
HHCCCCCCCCCCCEE
57.747684907
855PhosphorylationGNVKNKDSNKPVTIP
CCCCCCCCCCCEECC
48.6529396449
857AcetylationVKNKDSNKPVTIPEN
CCCCCCCCCEECCCC
44.8326051181
860PhosphorylationKDSNKPVTIPENSEI
CCCCCCEECCCCCCC
39.0629396449
865PhosphorylationPVTIPENSEIKTSIE
CEECCCCCCCCEEEE
38.7520068231
868AcetylationIPENSEIKTSIEVKA
CCCCCCCCEEEEEEE
31.977684917
885PhosphorylationNCAKEAISDAALEAT
HHHHHHHHHHHHHHH
28.3925849741
892PhosphorylationSDAALEATENEPLNK
HHHHHHHHCCCCCCC
29.9329255136
927UbiquitinationEEVYDLAKPFGGLKD
HHHHHHHCCCCCHHH
48.45-
9432-HydroxyisobutyrylationLILSSHKKAYIEINR
EEEECCCCEEEHHCH
40.78-
943UbiquitinationLILSSHKKAYIEINR
EEEECCCCEEEHHCH
40.78-
945PhosphorylationLSSHKKAYIEINRKA
EECCCCEEEHHCHHH
14.1528102081
951AcetylationAYIEINRKAAESMVK
EEEHHCHHHHHHHHH
47.677976059
951UbiquitinationAYIEINRKAAESMVK
EEEHHCHHHHHHHHH
47.67-
1052PhosphorylationKAILQLDSPESAQSM
EEEEECCCHHHHHHH
38.8824719451
1055PhosphorylationLQLDSPESAQSMYSF
EECCCHHHHHHHHHH
34.6828348404
1060PhosphorylationPESAQSMYSFLKQNP
HHHHHHHHHHHHHCC
11.08-
1061PhosphorylationESAQSMYSFLKQNPQ
HHHHHHHHHHHHCCC
18.5624719451
1076PhosphorylationNIGDHMLTCSLSPKI
CCCCCEEEEECCCCC
7.7720873877
1078PhosphorylationGDHMLTCSLSPKIDL
CCCEEEEECCCCCCC
27.0124719451
1080PhosphorylationHMLTCSLSPKIDLPE
CEEEEECCCCCCCCC
14.0924719451
1098AcetylationEHDPELEKESPGLKN
CCCHHHHHCCCCCCC
75.9126051181
1098UbiquitinationEHDPELEKESPGLKN
CCCHHHHHCCCCCCC
75.91-
1100PhosphorylationDPELEKESPGLKNSP
CHHHHHCCCCCCCCC
35.0229255136
1106PhosphorylationESPGLKNSPIDESEV
CCCCCCCCCCCHHHC
22.9625159151
1115PhosphorylationIDESEVQTATDSPSV
CCHHHCCCCCCCCCC
36.3830576142
1117PhosphorylationESEVQTATDSPSVKP
HHHCCCCCCCCCCCC
40.1630576142
1119PhosphorylationEVQTATDSPSVKPNE
HCCCCCCCCCCCCCC
18.0825849741
1121PhosphorylationQTATDSPSVKPNELE
CCCCCCCCCCCCCCC
46.8830576142
1131PhosphorylationPNELEEESTPSIQTE
CCCCCCCCCCCHHHH
49.2330576142
1132PhosphorylationNELEEESTPSIQTET
CCCCCCCCCCHHHHH
25.0830576142
1134PhosphorylationLEEESTPSIQTETLV
CCCCCCCCHHHHHHC
27.6728348404
1137PhosphorylationESTPSIQTETLVQQE
CCCCCHHHHHHCCCC
29.3028348404
1139PhosphorylationTPSIQTETLVQQEEP
CCCHHHHHHCCCCCC
35.3028348404
1155PhosphorylationEEEAEKATCDSDFAV
HHHHHHCCCCCCCHH
28.1025159151
1158PhosphorylationAEKATCDSDFAVETL
HHHCCCCCCCHHEEE
36.4525159151
1226PhosphorylationPKTALLPSDSVFAEE
CCCCCCCCCHHHCHH
42.3528348404
1228PhosphorylationTALLPSDSVFAEERN
CCCCCCCHHHCHHHC
24.3828348404
1243PhosphorylationLKGILEESPSEAEDF
CCHHHHCCHHHHHHH
25.0920068231
1245PhosphorylationGILEESPSEAEDFIS
HHHHCCHHHHHHHHH
59.7325849741
1252PhosphorylationSEAEDFISGITQTMV
HHHHHHHHHHHHHHH
24.9228464451
1255PhosphorylationEDFISGITQTMVEAV
HHHHHHHHHHHHHHH
22.8520068231
1257PhosphorylationFISGITQTMVEAVAE
HHHHHHHHHHHHHHH
17.9730301811
1328PhosphorylationRMDLQIGTEKAEKNE
HHHHHHCHHHHHHCC
35.6220860994
1330AcetylationDLQIGTEKAEKNEGR
HHHHCHHHHHHCCCC
62.7820167786
1352AcetylationKMAAMKEKPAENTLF
HHHHHCCCCCCCCCC
43.9725953088
1372AcetylationKGVGQANKPDETSKT
CCCCCCCCCCCCCCC
57.7826051181
1376PhosphorylationQANKPDETSKTSILA
CCCCCCCCCCCEEEE
42.79-
1377PhosphorylationANKPDETSKTSILAV
CCCCCCCCCCEEEEE
31.71-
1379PhosphorylationKPDETSKTSILAVSD
CCCCCCCCEEEEEEC
22.2928450419
1380PhosphorylationPDETSKTSILAVSDV
CCCCCCCEEEEEECC
21.2428450419
1385PhosphorylationKTSILAVSDVSSSKP
CCEEEEEECCCCCCC
27.0428450419
1388PhosphorylationILAVSDVSSSKPSIK
EEEEECCCCCCCCEE
33.6128450419
1389PhosphorylationLAVSDVSSSKPSIKA
EEEECCCCCCCCEEE
42.0828450419
1390PhosphorylationAVSDVSSSKPSIKAV
EEECCCCCCCCEEEE
40.8728450419
1391AcetylationVSDVSSSKPSIKAVI
EECCCCCCCCEEEEE
44.7426822725
1391UbiquitinationVSDVSSSKPSIKAVI
EECCCCCCCCEEEEE
44.74-
1393PhosphorylationDVSSSKPSIKAVIVS
CCCCCCCCEEEEEEC
40.2220068231
1400PhosphorylationSIKAVIVSSPKAKAT
CEEEEEECCCCCCCE
29.7829255136
1401PhosphorylationIKAVIVSSPKAKATV
EEEEEECCCCCCCEE
21.3729255136
1407PhosphorylationSSPKAKATVSKTENQ
CCCCCCCEECCCCCC
25.3023186163
1409PhosphorylationPKAKATVSKTENQKS
CCCCCEECCCCCCCC
29.5223917254
1430AcetylationRDQINAEKKLSAKEF
HHHCCHHHHCCHHHH
57.5125953088
1430UbiquitinationRDQINAEKKLSAKEF
HHHCCHHHHCCHHHH
57.512190698
1430 (in isoform 1)Ubiquitination-57.5121906983
1430 (in isoform 3)Ubiquitination-57.5121906983
1433PhosphorylationINAEKKLSAKEFGLL
CCHHHHCCHHHHCCC
46.2923898821
1441AcetylationAKEFGLLKPTSARSG
HHHHCCCCCCCCCCC
51.8223954790
1443O-linked_GlycosylationEFGLLKPTSARSGLA
HHCCCCCCCCCCCCC
33.17OGP
1443PhosphorylationEFGLLKPTSARSGLA
HHCCCCCCCCCCCCC
33.1728555341
1444PhosphorylationFGLLKPTSARSGLAE
HCCCCCCCCCCCCCC
30.1628555341
1455AcetylationGLAESSSKFKPTQSS
CCCCCCCCCCCCCCC
60.3925953088
1459PhosphorylationSSSKFKPTQSSLTRG
CCCCCCCCCCCCCCC
41.4926074081
1461PhosphorylationSKFKPTQSSLTRGGS
CCCCCCCCCCCCCCC
29.7820860994
1462PhosphorylationKFKPTQSSLTRGGSG
CCCCCCCCCCCCCCH
24.7626074081
1464PhosphorylationKPTQSSLTRGGSGRI
CCCCCCCCCCCCHHH
29.2623401153
1465MethylationPTQSSLTRGGSGRIS
CCCCCCCCCCCHHHH
53.4180701595
1468PhosphorylationSSLTRGGSGRISALQ
CCCCCCCCHHHHHHH
27.9426074081
1472PhosphorylationRGGSGRISALQGKLS
CCCCHHHHHHHHHHH
22.9026074081
1477AcetylationRISALQGKLSKLDYR
HHHHHHHHHHCCCHH
36.3025953088
1477UbiquitinationRISALQGKLSKLDYR
HHHHHHHHHHCCCHH
36.30-
1479PhosphorylationSALQGKLSKLDYRDI
HHHHHHHHCCCHHHH
34.3622817900
1480AcetylationALQGKLSKLDYRDIT
HHHHHHHCCCHHHHH
56.6725953088
1480UbiquitinationALQGKLSKLDYRDIT
HHHHHHHCCCHHHHH
56.67-
1487PhosphorylationKLDYRDITKQSQETE
CCCHHHHHHHCCCCC
27.5923312004
1490PhosphorylationYRDITKQSQETEARP
HHHHHHHCCCCCCCC
31.3829214152
1493PhosphorylationITKQSQETEARPSIM
HHHHCCCCCCCCCCC
27.5823312004
1498PhosphorylationQETEARPSIMKRDDS
CCCCCCCCCCCCCCC
29.7523312004
1575PhosphorylationTLKNVPFSELNLKKK
HHHCCCHHHHCCCCC
34.7927251275
15802-HydroxyisobutyrylationPFSELNLKKKKGKTS
CHHHHCCCCCCCCCC
62.57-
1639PhosphorylationMEEMVKNSNSLFTLD
HHHHHHHCCCCCCHH
23.2923663014
1641PhosphorylationEMVKNSNSLFTLDEL
HHHHHCCCCCCHHHH
25.3623663014
1656PhosphorylationIDQDDCISHSEPKDV
CCCCCCCCCCCCCCC
27.5623663014
1658PhosphorylationQDDCISHSEPKDVTV
CCCCCCCCCCCCCEE
49.1323663014
1664PhosphorylationHSEPKDVTVLSVAEE
CCCCCCCEEEEHHHH
26.3430266825
1667PhosphorylationPKDVTVLSVAEEQDL
CCCCEEEEHHHHHHH
18.2319664994
1676SumoylationAEEQDLLKQERLVTV
HHHHHHHHHCCCEEE
58.3628112733
1676UbiquitinationAEEQDLLKQERLVTV
HHHHHHHHHCCCEEE
58.36-
1697PhosphorylationEELPLNESADITFAT
EECCCCCCCCEEEEE
30.1229496963
1701PhosphorylationLNESADITFATLNTK
CCCCCCEEEEEECCC
14.0428122231
1704PhosphorylationSADITFATLNTKGNE
CCCEEEEEECCCCCC
19.1528122231
1707PhosphorylationITFATLNTKGNEGDT
EEEEEECCCCCCCCC
43.3628122231
1744PhosphorylationDEIQDDSSDLHLVTL
EECCCCCCCEEEEEH
51.7022468782
1761PhosphorylationVTEEDEDSLADFNNL
CCCCCCCCHHHHHCH
24.3322468782
1797PhosphorylationLKVELAQSKNDHPTD
HHHEHHHHCCCCCCC
28.0225599653
1803PhosphorylationQSKNDHPTDKKGNRK
HHCCCCCCCCCCCCC
57.9625599653
1819PhosphorylationRAVDTKKTKLESLSQ
CCCCCCCHHHHHHHH
42.2828348404
1820SumoylationAVDTKKTKLESLSQV
CCCCCCHHHHHHHHC
60.1728112733
1823PhosphorylationTKKTKLESLSQVGPV
CCCHHHHHHHHCCCC
43.7028348404
1825PhosphorylationKTKLESLSQVGPVNE
CHHHHHHHHCCCCCC
31.9017525332
1848PhosphorylationTMIERHLTAKTPTKR
HHHHHHHCCCCCCCC
21.7123403867
1851PhosphorylationERHLTAKTPTKRVRI
HHHHCCCCCCCCEEC
33.4523927012
1853PhosphorylationHLTAKTPTKRVRIGK
HHCCCCCCCCEECCC
36.3928152594
1860AcetylationTKRVRIGKTLPSEKA
CCCEECCCCCCCCCE
44.5125953088
1866AcetylationGKTLPSEKAVVTEPA
CCCCCCCCEEECCCC
51.3123236377
1870PhosphorylationPSEKAVVTEPAKGEE
CCCCEEECCCCCCCC
29.6530108239
1874AcetylationAVVTEPAKGEEAFQM
EEECCCCCCCCCCCC
77.0426051181
1882PhosphorylationGEEAFQMSEVDEESG
CCCCCCCCCCCHHCC
24.5630266825
1888PhosphorylationMSEVDEESGLKDSEP
CCCCCHHCCCCCCCH
47.5923403867
1891AcetylationVDEESGLKDSEPERK
CCHHCCCCCCCHHHH
63.8319818679
1893PhosphorylationEESGLKDSEPERKRK
HHCCCCCCCHHHHHC
54.1630108239
1910PhosphorylationEDSSSGKSVASDVPE
CCCCCCCCHHCCCCH
26.8328450419
1913PhosphorylationSSGKSVASDVPEELD
CCCCCHHCCCCHHHC
36.6628450419
1938PhosphorylationPICSLFYSGEKAMTN
CHHHHHHCCHHHHCC
32.8921712546
1958AcetylationRHKQNTEKFMAKQRK
HHHHHHHHHHHHHHH
38.1025953088
1976PhosphorylationQNEAEERSSR-----
HHHHHHHHCC-----
100.0028102081
1977PhosphorylationNEAEERSSR------
HHHHHHHCC------
100.0030576142

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
375SPhosphorylationKinaseCHEK1O14757
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN638_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 ZN638_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KR412_HUMANKRTAP4-12physical
16189514
FBLN4_HUMANEFEMP2physical
16189514
HOOK2_HUMANHOOK2physical
16189514
FHL2_HUMANFHL2physical
11813260
SF3A3_HUMANSF3A3physical
26344197
KCTD3_HUMANKCTD3physical
27173435
KI13B_HUMANKIF13Bphysical
27173435
ZBT21_HUMANZBTB21physical
27173435
GGYF1_HUMANGIGYF1physical
27173435
LRFN1_HUMANLRFN1physical
27173435
SRGP2_HUMANSRGAP2physical
27173435
SI1L1_HUMANSIPA1L1physical
27173435
LIMA1_HUMANLIMA1physical
27173435
MAGI1_HUMANMAGI1physical
27173435
TESK2_HUMANTESK2physical
27173435
DCLK1_HUMANDCLK1physical
27173435
SRS12_HUMANSRSF12physical
27173435
SYDE1_HUMANSYDE1physical
27173435
AGAP1_HUMANAGAP1physical
27173435
CDK16_HUMANCDK16physical
27173435
MAST3_HUMANMAST3physical
27173435
F110B_HUMANFAM110Bphysical
27173435
UBP21_HUMANUSP21physical
27173435
AN34A_HUMANANKRD34Aphysical
27173435
FA53C_HUMANFAM53Cphysical
27173435
F110A_HUMANFAM110Aphysical
27173435
HDAC4_HUMANHDAC4physical
27173435
CING_HUMANCGNphysical
27173435
TBC25_HUMANTBC1D25physical
27173435
NF1_HUMANNF1physical
27173435
NADK_HUMANNADKphysical
27173435
CBY1_HUMANCBY1physical
27173435
TIAM1_HUMANTIAM1physical
27173435
M3K21_HUMANKIAA1804physical
27173435
NGAP_HUMANRASAL2physical
27173435
MELK_HUMANMELKphysical
27173435
PKHA7_HUMANPLEKHA7physical
27173435
KIF1C_HUMANKIF1Cphysical
27173435
LPIN3_HUMANLPIN3physical
27173435
DEP1B_HUMANDEPDC1Bphysical
27173435
GGYF2_HUMANGIGYF2physical
27173435
NAV1_HUMANNAV1physical
27173435
AFAD_HUMANMLLT4physical
27173435
STA13_HUMANSTARD13physical
27173435
SH3B4_HUMANSH3BP4physical
27173435
PKHA5_HUMANPLEKHA5physical
27173435
RPTOR_HUMANRPTORphysical
27173435
HDAC7_HUMANHDAC7physical
27173435
LARP1_HUMANLARP1physical
27173435
RAB3I_HUMANRAB3IPphysical
27173435
INP5E_HUMANINPP5Ephysical
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 ZN638_HUMAN

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Related Literatures of Post-Translational Modification
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-128; SER-1100 ANDSER-1401, AND MASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-795; SER-801; SER-808AND THR-809, 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-128; SER-558 ANDSER-560, 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-128; SER-383; SER-420;SER-552; SER-558; SER-560; SER-1100; SER-1401 AND SER-1882, AND MASSSPECTROMETRY.
"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-128, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-125; SER-128 ANDSER-770, AND MASS SPECTROMETRY.
"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-1825, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383, AND MASSSPECTROMETRY.
"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-128; SER-605 ANDSER-1100, AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128, 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-508; SER-510; SER-520;SER-522; SER-552; SER-558; SER-560 AND SER-605, 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-128, AND MASSSPECTROMETRY.

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