ZN281_HUMAN - dbPTM
ZN281_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN281_HUMAN
UniProt AC Q9Y2X9
Protein Name Zinc finger protein 281
Gene Name ZNF281
Organism Homo sapiens (Human).
Sequence Length 895
Subcellular Localization Nucleus .
Protein Description Transcription repressor that plays a role in regulation of embryonic stem cells (ESCs) differentiation. Required for ESCs differentiation and acts by mediating autorepression of NANOG in ESCs: binds to the NANOG promoter and promotes association of NANOG protein to its own promoter and recruits the NuRD complex, which deacetylates histones. Not required for establishement and maintenance of ESCs (By similarity). Represses the transcription of a number of genes including GAST, ODC1 and VIM. Binds to the G-rich box in the enhancer region of these genes..
Protein Sequence MKIGSGFLSGGGGTGSSGGSGSGGGGSGGGGGGGSSGRRAEMEPTFPQGMVMFNHRLPPVTSFTRPAGSAAPPPQCVLSSSTSAAPAAEPPPPPAPDMTFKKEPAASAAAFPSQRTSWGFLQSLVSIKQEKPADPEEQQSHHHHHHHHYGGLFAGAEERSPGLGGGEGGSHGVIQDLSILHQHVQQQPAQHHRDVLLSSSSRTDDHHGTEEPKQDTNVKKAKRPKPESQGIKAKRKPSASSKPSLVGDGEGAILSPSQKPHICDHCSAAFRSSYHLRRHVLIHTGERPFQCSQCSMGFIQKYLLQRHEKIHSREKPFGCDQCSMKFIQKYHMERHKRTHSGEKPYKCDTCQQYFSRTDRLLKHRRTCGEVIVKGATSAEPGSSNHTNMGNLAVLSQGNTSSSRRKTKSKSIAIENKEQKTGKTNESQISNNINMQSYSVEMPTVSSSGGIIGTGIDELQKRVPKLIFKKGSRKNTDKNYLNFVSPLPDIVGQKSLSGKPSGSLGIVSNNSVETIGLLQSTSGKQGQISSNYDDAMQFSKKRRYLPTASSNSAFSINVGHMVSQQSVIQSAGVSVLDNEAPLSLIDSSALNAEIKSCHDKSGIPDEVLQSILDQYSNKSESQKEDPFNIAEPRVDLHTSGEHSELVQEENLSPGTQTPSNDKASMLQEYSKYLQQAFEKSTNASFTLGHGFQFVSLSSPLHNHTLFPEKQIYTTSPLECGFGQSVTSVLPSSLPKPPFGMLFGSQPGLYLSALDATHQQLTPSQELDDLIDSQKNLETSSAFQSSSQKLTSQKEQKNLESSTGFQIPSQELASQIDPQKDIEPRTTYQIENFAQAFGSQFKSGSRVPMTFITNSNGEVDHRVRTSVSDFSGYTNMMSDVSEPCSTRVKTPTSQSYR
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
2Sumoylation------MKIGSGFLS
------CCCCCCCCC
56.63-
2Sumoylation------MKIGSGFLS
------CCCCCCCCC
56.6328112733
5O-linked_Glycosylation---MKIGSGFLSGGG
---CCCCCCCCCCCC
29.8230059200
5Phosphorylation---MKIGSGFLSGGG
---CCCCCCCCCCCC
29.8228674151
9PhosphorylationKIGSGFLSGGGGTGS
CCCCCCCCCCCCCCC
32.8820068231
14PhosphorylationFLSGGGGTGSSGGSG
CCCCCCCCCCCCCCC
36.8520068231
16PhosphorylationSGGGGTGSSGGSGSG
CCCCCCCCCCCCCCC
26.1630576142
16O-linked_GlycosylationSGGGGTGSSGGSGSG
CCCCCCCCCCCCCCC
26.1630059200
17PhosphorylationGGGGTGSSGGSGSGG
CCCCCCCCCCCCCCC
48.8220068231
20O-linked_GlycosylationGTGSSGGSGSGGGGS
CCCCCCCCCCCCCCC
33.0530059200
20PhosphorylationGTGSSGGSGSGGGGS
CCCCCCCCCCCCCCC
33.0530576142
22PhosphorylationGSSGGSGSGGGGSGG
CCCCCCCCCCCCCCC
35.6425954137
27PhosphorylationSGSGGGGSGGGGGGG
CCCCCCCCCCCCCCC
37.2225954137
35PhosphorylationGGGGGGGSSGRRAEM
CCCCCCCCCCCCCCC
32.6627251789
36PhosphorylationGGGGGGSSGRRAEME
CCCCCCCCCCCCCCC
39.3220068231
66UbiquitinationPVTSFTRPAGSAAPP
CCCCCCCCCCCCCCC
37.60-
101SumoylationPAPDMTFKKEPAASA
CCCCCCCCCCCCCCC
47.2428112733
102UbiquitinationAPDMTFKKEPAASAA
CCCCCCCCCCCCCCC
65.81-
107O-linked_GlycosylationFKKEPAASAAAFPSQ
CCCCCCCCCCCCCCC
22.1330059200
116PhosphorylationAAFPSQRTSWGFLQS
CCCCCCHHHHHHHHH
22.6128450419
117PhosphorylationAFPSQRTSWGFLQSL
CCCCCHHHHHHHHHH
27.6529496963
128SumoylationLQSLVSIKQEKPADP
HHHHHHHHCCCCCCH
44.92-
128SumoylationLQSLVSIKQEKPADP
HHHHHHHHCCCCCCH
44.9228112733
160PhosphorylationFAGAEERSPGLGGGE
CCCCCCCCCCCCCCC
26.9729255136
170PhosphorylationLGGGEGGSHGVIQDL
CCCCCCCCCCHHCHH
28.1127251275
177UbiquitinationSHGVIQDLSILHQHV
CCCHHCHHHHHHHHH
1.64-
178PhosphorylationHGVIQDLSILHQHVQ
CCHHCHHHHHHHHHH
31.2427251275
198PhosphorylationHHRDVLLSSSSRTDD
HCCCEECCCCCCCCC
24.8223401153
199PhosphorylationHRDVLLSSSSRTDDH
CCCEECCCCCCCCCC
32.1029255136
200PhosphorylationRDVLLSSSSRTDDHH
CCEECCCCCCCCCCC
22.0629255136
201PhosphorylationDVLLSSSSRTDDHHG
CEECCCCCCCCCCCC
40.9429255136
203PhosphorylationLLSSSSRTDDHHGTE
ECCCCCCCCCCCCCC
47.9620873877
209PhosphorylationRTDDHHGTEEPKQDT
CCCCCCCCCCCCCCC
32.5829978859
213SumoylationHHGTEEPKQDTNVKK
CCCCCCCCCCCCCCC
65.17-
213UbiquitinationHHGTEEPKQDTNVKK
CCCCCCCCCCCCCCC
65.17-
213SumoylationHHGTEEPKQDTNVKK
CCCCCCCCCCCCCCC
65.1728112733
219SumoylationPKQDTNVKKAKRPKP
CCCCCCCCCCCCCCC
49.4328112733
225SumoylationVKKAKRPKPESQGIK
CCCCCCCCCHHHCCC
66.50-
225SumoylationVKKAKRPKPESQGIK
CCCCCCCCCHHHCCC
66.5028112733
225UbiquitinationVKKAKRPKPESQGIK
CCCCCCCCCHHHCCC
66.50-
228PhosphorylationAKRPKPESQGIKAKR
CCCCCCHHHCCCCCC
42.0829083192
232SumoylationKPESQGIKAKRKPSA
CCHHHCCCCCCCCCC
55.47-
232SumoylationKPESQGIKAKRKPSA
CCHHHCCCCCCCCCC
55.4728112733
238PhosphorylationIKAKRKPSASSKPSL
CCCCCCCCCCCCCCC
43.7625627689
242AcetylationRKPSASSKPSLVGDG
CCCCCCCCCCCCCCC
35.8126051181
242SumoylationRKPSASSKPSLVGDG
CCCCCCCCCCCCCCC
35.8128112733
244PhosphorylationPSASSKPSLVGDGEG
CCCCCCCCCCCCCCC
39.1525627689
255PhosphorylationDGEGAILSPSQKPHI
CCCCCCCCCCCCCCC
19.1825159151
257PhosphorylationEGAILSPSQKPHICD
CCCCCCCCCCCCCCC
47.6729052541
259SumoylationAILSPSQKPHICDHC
CCCCCCCCCCCCCCC
42.79-
259SumoylationAILSPSQKPHICDHC
CCCCCCCCCCCCCCC
42.7928112733
279UbiquitinationSSYHLRRHVLIHTGE
HHHHHHCCEEEECCC
16.58-
284PhosphorylationRRHVLIHTGERPFQC
HCCEEEECCCCCCCC
33.4727422710
292PhosphorylationGERPFQCSQCSMGFI
CCCCCCCCCCCHHHH
24.3628348404
293UbiquitinationERPFQCSQCSMGFIQ
CCCCCCCCCCHHHHH
30.82-
301SumoylationCSMGFIQKYLLQRHE
CCHHHHHHHHHHHHH
32.8028112733
307UbiquitinationQKYLLQRHEKIHSRE
HHHHHHHHHHHHCCC
27.95-
310UbiquitinationLLQRHEKIHSREKPF
HHHHHHHHHCCCCCC
3.04-
312PhosphorylationQRHEKIHSREKPFGC
HHHHHHHCCCCCCCC
45.6829214152
315UbiquitinationEKIHSREKPFGCDQC
HHHHCCCCCCCCCHH
44.53-
325SumoylationGCDQCSMKFIQKYHM
CCCHHHHHHHHHHHH
24.03-
325SumoylationGCDQCSMKFIQKYHM
CCCHHHHHHHHHHHH
24.0328112733
325UbiquitinationGCDQCSMKFIQKYHM
CCCHHHHHHHHHHHH
24.03-
329SumoylationCSMKFIQKYHMERHK
HHHHHHHHHHHHHHC
32.10-
329UbiquitinationCSMKFIQKYHMERHK
HHHHHHHHHHHHHHC
32.10-
329SumoylationCSMKFIQKYHMERHK
HHHHHHHHHHHHHHC
32.10-
337UbiquitinationYHMERHKRTHSGEKP
HHHHHHCCCCCCCCC
31.39-
340PhosphorylationERHKRTHSGEKPYKC
HHHCCCCCCCCCCCC
48.2929214152
343UbiquitinationKRTHSGEKPYKCDTC
CCCCCCCCCCCCCHH
58.11-
343AcetylationKRTHSGEKPYKCDTC
CCCCCCCCCCCCCHH
58.1126051181
346SumoylationHSGEKPYKCDTCQQY
CCCCCCCCCCHHHHH
33.87-
346UbiquitinationHSGEKPYKCDTCQQY
CCCCCCCCCCHHHHH
33.87-
346SumoylationHSGEKPYKCDTCQQY
CCCCCCCCCCHHHHH
33.87-
353PhosphorylationKCDTCQQYFSRTDRL
CCCHHHHHHHHHHHH
4.2517360941
357PhosphorylationCQQYFSRTDRLLKHR
HHHHHHHHHHHHHHH
25.0328555341
373SumoylationTCGEVIVKGATSAEP
CCCCEEEECCCCCCC
31.53-
373UbiquitinationTCGEVIVKGATSAEP
CCCCEEEECCCCCCC
31.53-
373SumoylationTCGEVIVKGATSAEP
CCCCEEEECCCCCCC
31.5328112733
373UbiquitinationTCGEVIVKGATSAEP
CCCCEEEECCCCCCC
31.53-
380UbiquitinationKGATSAEPGSSNHTN
ECCCCCCCCCCCCCC
47.91-
382O-linked_GlycosylationATSAEPGSSNHTNMG
CCCCCCCCCCCCCCC
38.3930059200
383UbiquitinationTSAEPGSSNHTNMGN
CCCCCCCCCCCCCCC
38.25-
395PhosphorylationMGNLAVLSQGNTSSS
CCCEEEEECCCCCCC
29.4617525332
399PhosphorylationAVLSQGNTSSSRRKT
EEEECCCCCCCCCCC
36.4925159151
400PhosphorylationVLSQGNTSSSRRKTK
EEECCCCCCCCCCCC
30.2525159151
401PhosphorylationLSQGNTSSSRRKTKS
EECCCCCCCCCCCCC
26.3126074081
402PhosphorylationSQGNTSSSRRKTKSK
ECCCCCCCCCCCCCC
35.5526074081
409SumoylationSRRKTKSKSIAIENK
CCCCCCCCCEEECCC
47.65-
409UbiquitinationSRRKTKSKSIAIENK
CCCCCCCCCEEECCC
47.65-
409SumoylationSRRKTKSKSIAIENK
CCCCCCCCCEEECCC
47.6528112733
410PhosphorylationRRKTKSKSIAIENKE
CCCCCCCCEEECCCC
25.0927251275
416SumoylationKSIAIENKEQKTGKT
CCEEECCCCHHCCCC
49.05-
416UbiquitinationKSIAIENKEQKTGKT
CCEEECCCCHHCCCC
49.05-
416SumoylationKSIAIENKEQKTGKT
CCEEECCCCHHCCCC
49.0528112733
416AcetylationKSIAIENKEQKTGKT
CCEEECCCCHHCCCC
49.0525953088
419UbiquitinationAIENKEQKTGKTNES
EECCCCHHCCCCCHH
61.41-
437UbiquitinationNNINMQSYSVEMPTV
CCCCCCEEEEECCCC
10.39-
438PhosphorylationNINMQSYSVEMPTVS
CCCCCEEEEECCCCC
19.49-
438O-linked_GlycosylationNINMQSYSVEMPTVS
CCCCCEEEEECCCCC
19.49OGP
441UbiquitinationMQSYSVEMPTVSSSG
CCEEEEECCCCCCCC
2.94-
443O-linked_GlycosylationSYSVEMPTVSSSGGI
EEEEECCCCCCCCCC
31.5430059200
445PhosphorylationSVEMPTVSSSGGIIG
EEECCCCCCCCCCCC
22.67-
445O-linked_GlycosylationSVEMPTVSSSGGIIG
EEECCCCCCCCCCCC
22.6730059200
446PhosphorylationVEMPTVSSSGGIIGT
EECCCCCCCCCCCCC
28.76-
447O-linked_GlycosylationEMPTVSSSGGIIGTG
ECCCCCCCCCCCCCC
33.2730059200
453O-linked_GlycosylationSSGGIIGTGIDELQK
CCCCCCCCCHHHHHH
22.1330059200
460SumoylationTGIDELQKRVPKLIF
CCHHHHHHHCCHHHH
68.9028112733
462UbiquitinationIDELQKRVPKLIFKK
HHHHHHHCCHHHHCC
6.72-
464SumoylationELQKRVPKLIFKKGS
HHHHHCCHHHHCCCC
51.89-
464SumoylationELQKRVPKLIFKKGS
HHHHHCCHHHHCCCC
51.89-
477SumoylationGSRKNTDKNYLNFVS
CCCCCCCCCCCCCCC
45.51-
477UbiquitinationGSRKNTDKNYLNFVS
CCCCCCCCCCCCCCC
45.51-
477SumoylationGSRKNTDKNYLNFVS
CCCCCCCCCCCCCCC
45.5128112733
479PhosphorylationRKNTDKNYLNFVSPL
CCCCCCCCCCCCCCC
14.5717360941
484PhosphorylationKNYLNFVSPLPDIVG
CCCCCCCCCCCCCCC
19.3125159151
493SumoylationLPDIVGQKSLSGKPS
CCCCCCCCCCCCCCC
47.6528112733
498SumoylationGQKSLSGKPSGSLGI
CCCCCCCCCCCCEEE
32.41-
498UbiquitinationGQKSLSGKPSGSLGI
CCCCCCCCCCCCEEE
32.41-
498SumoylationGQKSLSGKPSGSLGI
CCCCCCCCCCCCEEE
32.4128112733
498AcetylationGQKSLSGKPSGSLGI
CCCCCCCCCCCCEEE
32.4126051181
503UbiquitinationSGKPSGSLGIVSNNS
CCCCCCCEEEEECCC
6.56-
504UbiquitinationGKPSGSLGIVSNNSV
CCCCCCEEEEECCCE
21.68-
529PhosphorylationGKQGQISSNYDDAMQ
CCCCCCCCCHHHHHH
40.83-
531PhosphorylationQGQISSNYDDAMQFS
CCCCCCCHHHHHHHH
19.69-
538PhosphorylationYDDAMQFSKKRRYLP
HHHHHHHHHHCCCCC
22.0028555341
539SumoylationDDAMQFSKKRRYLPT
HHHHHHHHHCCCCCC
52.14-
539UbiquitinationDDAMQFSKKRRYLPT
HHHHHHHHHCCCCCC
52.1421906983
539SumoylationDDAMQFSKKRRYLPT
HHHHHHHHHCCCCCC
52.1428112733
563UbiquitinationNVGHMVSQQSVIQSA
ECCCCCCHHHHHHHC
28.32-
581UbiquitinationVLDNEAPLSLIDSSA
EECCCCCHHHHCHHH
9.31-
586UbiquitinationAPLSLIDSSALNAEI
CCHHHHCHHHHHHHH
15.54-
595PhosphorylationALNAEIKSCHDKSGI
HHHHHHHHCHHCCCC
23.5021712546
599UbiquitinationEIKSCHDKSGIPDEV
HHHHCHHCCCCCHHH
27.24-
599AcetylationEIKSCHDKSGIPDEV
HHHHCHHCCCCCHHH
27.2426051181
599SumoylationEIKSCHDKSGIPDEV
HHHHCHHCCCCCHHH
27.2428112733
600PhosphorylationIKSCHDKSGIPDEVL
HHHCHHCCCCCHHHH
48.2722199227
615PhosphorylationQSILDQYSNKSESQK
HHHHHHHCCCCHHCC
31.9529507054
617UbiquitinationILDQYSNKSESQKED
HHHHHCCCCHHCCCC
50.05-
617SumoylationILDQYSNKSESQKED
HHHHHCCCCHHCCCC
50.0528112733
618PhosphorylationLDQYSNKSESQKEDP
HHHHCCCCHHCCCCC
46.8930266825
620PhosphorylationQYSNKSESQKEDPFN
HHCCCCHHCCCCCCC
54.3530266825
622SumoylationSNKSESQKEDPFNIA
CCCCHHCCCCCCCCC
73.66-
622UbiquitinationSNKSESQKEDPFNIA
CCCCHHCCCCCCCCC
73.6621906983
622SumoylationSNKSESQKEDPFNIA
CCCCHHCCCCCCCCC
73.6628112733
625UbiquitinationSESQKEDPFNIAEPR
CHHCCCCCCCCCCCC
25.85-
634UbiquitinationNIAEPRVDLHTSGEH
CCCCCCEECCCCCCC
33.73-
637PhosphorylationEPRVDLHTSGEHSEL
CCCEECCCCCCCHHH
45.8023663014
638PhosphorylationPRVDLHTSGEHSELV
CCEECCCCCCCHHHH
31.2825159151
642PhosphorylationLHTSGEHSELVQEEN
CCCCCCCHHHHHHCC
28.4625159151
651PhosphorylationLVQEENLSPGTQTPS
HHHHCCCCCCCCCCC
32.6323401153
654PhosphorylationEENLSPGTQTPSNDK
HCCCCCCCCCCCCHH
32.4323401153
656PhosphorylationNLSPGTQTPSNDKAS
CCCCCCCCCCCHHHH
28.6425159151
658PhosphorylationSPGTQTPSNDKASML
CCCCCCCCCHHHHHH
62.1328102081
661UbiquitinationTQTPSNDKASMLQEY
CCCCCCHHHHHHHHH
46.7621906983
661SumoylationTQTPSNDKASMLQEY
CCCCCCHHHHHHHHH
46.7628112733
670SumoylationSMLQEYSKYLQQAFE
HHHHHHHHHHHHHHH
49.42-
670UbiquitinationSMLQEYSKYLQQAFE
HHHHHHHHHHHHHHH
49.4221906983
670SumoylationSMLQEYSKYLQQAFE
HHHHHHHHHHHHHHH
49.4228112733
679O-linked_GlycosylationLQQAFEKSTNASFTL
HHHHHHHCCCCEEEC
21.5030059200
683PhosphorylationFEKSTNASFTLGHGF
HHHCCCCEEECCCCE
22.3425159151
685O-linked_GlycosylationKSTNASFTLGHGFQF
HCCCCEEECCCCEEE
29.3630059200
694O-linked_GlycosylationGHGFQFVSLSSPLHN
CCCEEEEECCCCCCC
24.6730059200
694PhosphorylationGHGFQFVSLSSPLHN
CCCEEEEECCCCCCC
24.6727174698
696PhosphorylationGFQFVSLSSPLHNHT
CEEEEECCCCCCCCC
23.5425159151
696O-linked_GlycosylationGFQFVSLSSPLHNHT
CEEEEECCCCCCCCC
23.5430059200
697PhosphorylationFQFVSLSSPLHNHTL
EEEEECCCCCCCCCC
36.4525159151
697O-linked_GlycosylationFQFVSLSSPLHNHTL
EEEEECCCCCCCCCC
36.4530059200
703O-linked_GlycosylationSSPLHNHTLFPEKQI
CCCCCCCCCCCCCCE
35.1030059200
713O-linked_GlycosylationPEKQIYTTSPLECGF
CCCCEEECCCCCCCC
16.0430059200
751AcetylationQPGLYLSALDATHQQ
CCCEEHHHHHHHCCC
13.58-
751UbiquitinationQPGLYLSALDATHQQ
CCCEEHHHHHHHCCC
13.58-
759UbiquitinationLDATHQQLTPSQELD
HHHHCCCCCCCHHHH
6.47-
777PhosphorylationDSQKNLETSSAFQSS
HHHHHHHHHHHHHHH
31.0223312004
778PhosphorylationSQKNLETSSAFQSSS
HHHHHHHHHHHHHHH
15.4230266825
778O-linked_GlycosylationSQKNLETSSAFQSSS
HHHHHHHHHHHHHHH
15.4230059200
779PhosphorylationQKNLETSSAFQSSSQ
HHHHHHHHHHHHHHH
40.2930266825
782UbiquitinationLETSSAFQSSSQKLT
HHHHHHHHHHHHHHH
41.96-
783PhosphorylationETSSAFQSSSQKLTS
HHHHHHHHHHHHHHC
26.0430266825
784PhosphorylationTSSAFQSSSQKLTSQ
HHHHHHHHHHHHHCH
26.4630266825
785PhosphorylationSSAFQSSSQKLTSQK
HHHHHHHHHHHHCHH
36.2617525332
787SumoylationAFQSSSQKLTSQKEQ
HHHHHHHHHHCHHHH
56.53-
787UbiquitinationAFQSSSQKLTSQKEQ
HHHHHHHHHHCHHHH
56.5321906983
787SumoylationAFQSSSQKLTSQKEQ
HHHHHHHHHHCHHHH
56.5328112733
787AcetylationAFQSSSQKLTSQKEQ
HHHHHHHHHHCHHHH
56.5323236377
792AcetylationSQKLTSQKEQKNLES
HHHHHCHHHHHCHHH
62.9811922969
792SumoylationSQKLTSQKEQKNLES
HHHHHCHHHHHCHHH
62.9828112733
795SumoylationLTSQKEQKNLESSTG
HHCHHHHHCHHHCCC
65.67-
795UbiquitinationLTSQKEQKNLESSTG
HHCHHHHHCHHHCCC
65.6721906983
795SumoylationLTSQKEQKNLESSTG
HHCHHHHHCHHHCCC
65.6728112733
799PhosphorylationKEQKNLESSTGFQIP
HHHHCHHHCCCCCCC
36.0423663014
800PhosphorylationEQKNLESSTGFQIPS
HHHCHHHCCCCCCCH
24.1523663014
801PhosphorylationQKNLESSTGFQIPSQ
HHCHHHCCCCCCCHH
51.8223663014
804UbiquitinationLESSTGFQIPSQELA
HHHCCCCCCCHHHHH
48.29-
807PhosphorylationSTGFQIPSQELASQI
CCCCCCCHHHHHHCC
37.6117525332
812PhosphorylationIPSQELASQIDPQKD
CCHHHHHHCCCCCCC
40.0529214152
818UbiquitinationASQIDPQKDIEPRTT
HHCCCCCCCCCCCCE
67.09-
818SumoylationASQIDPQKDIEPRTT
HHCCCCCCCCCCCCE
67.0928112733
837PhosphorylationNFAQAFGSQFKSGSR
HHHHHHHHCCCCCCC
26.4521712546
840SumoylationQAFGSQFKSGSRVPM
HHHHHCCCCCCCCCE
46.39-
840UbiquitinationQAFGSQFKSGSRVPM
HHHHHCCCCCCCCCE
46.392190698
840SumoylationQAFGSQFKSGSRVPM
HHHHHCCCCCCCCCE
46.3928112733
841PhosphorylationAFGSQFKSGSRVPMT
HHHHCCCCCCCCCEE
43.2028555341
848PhosphorylationSGSRVPMTFITNSNG
CCCCCCEEEEECCCC
13.0520860994
851PhosphorylationRVPMTFITNSNGEVD
CCCEEEEECCCCCEE
28.5322210691
853O-linked_GlycosylationPMTFITNSNGEVDHR
CEEEEECCCCCEEEE
37.2530059200
853PhosphorylationPMTFITNSNGEVDHR
CEEEEECCCCCEEEE
37.2528555341
863O-linked_GlycosylationEVDHRVRTSVSDFSG
CEEEEEECCHHHHCC
30.5330059200
863PhosphorylationEVDHRVRTSVSDFSG
CEEEEEECCHHHHCC
30.5327251275
864PhosphorylationVDHRVRTSVSDFSGY
EEEEEECCHHHHCCC
14.7327251275
864O-linked_GlycosylationVDHRVRTSVSDFSGY
EEEEEECCHHHHCCC
14.7330059200
866O-linked_GlycosylationHRVRTSVSDFSGYTN
EEEECCHHHHCCCCC
32.4830059200
866PhosphorylationHRVRTSVSDFSGYTN
EEEECCHHHHCCCCC
32.4820860994
872PhosphorylationVSDFSGYTNMMSDVS
HHHHCCCCCCCCCCC
21.84-
876PhosphorylationSGYTNMMSDVSEPCS
CCCCCCCCCCCCCCC
24.8820860994
879PhosphorylationTNMMSDVSEPCSTRV
CCCCCCCCCCCCCCC
40.5930576142
883PhosphorylationSDVSEPCSTRVKTPT
CCCCCCCCCCCCCCC
29.9322210691
884PhosphorylationDVSEPCSTRVKTPTS
CCCCCCCCCCCCCCC
46.3130576142
887UbiquitinationEPCSTRVKTPTSQSY
CCCCCCCCCCCCCCC
45.56-
888PhosphorylationPCSTRVKTPTSQSYR
CCCCCCCCCCCCCCC
29.0125218447
890PhosphorylationSTRVKTPTSQSYR--
CCCCCCCCCCCCC--
44.6323403867
891O-linked_GlycosylationTRVKTPTSQSYR---
CCCCCCCCCCCC---
20.5230059200
891PhosphorylationTRVKTPTSQSYR---
CCCCCCCCCCCC---
20.5223403867
891O-linked_GlycosylationTRVKTPTSQSYR---
CCCCCCCCCCCC---
20.5220068230
893O-linked_GlycosylationVKTPTSQSYR-----
CCCCCCCCCC-----
23.7330059200
893PhosphorylationVKTPTSQSYR-----
CCCCCCCCCC-----
23.7323403867
894PhosphorylationKTPTSQSYR------
CCCCCCCCC------
16.8321406692

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
638SPhosphorylationKinaseGSK3BP49841
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN281_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 ZN281_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NANOG_HUMANNANOGphysical
18757296
PO5F1_HUMANPOU5F1physical
18757296
SOX2_HUMANSOX2physical
18757296
PRCC_HUMANPRCCphysical
26496610
TAP2_HUMANTAP2physical
26496610
KCAB2_HUMANKCNAB2physical
26496610
GOGA5_HUMANGOLGA5physical
26496610
MAGD2_HUMANMAGED2physical
26496610
KI21B_HUMANKIF21Bphysical
26496610
MILK2_HUMANMICALL2physical
26496610
WDCP_HUMANC2orf44physical
26496610
ZN644_HUMANZNF644physical
26496610
GRIN1_HUMANGPRIN1physical
26496610
OSBL5_HUMANOSBPL5physical
26496610
MLKL_HUMANMLKLphysical
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 ZN281_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-255, 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-484, AND MASSSPECTROMETRY.
"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-395; SER-785 ANDSER-807, AND MASS SPECTROMETRY.

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