ZN217_HUMAN - dbPTM
ZN217_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN217_HUMAN
UniProt AC O75362
Protein Name Zinc finger protein 217
Gene Name ZNF217
Organism Homo sapiens (Human).
Sequence Length 1048
Subcellular Localization Nucleus .
Protein Description Binds to the promoters of target genes and functions as repressor. Promotes cell proliferation and antagonizes cell death. Promotes phosphorylation of AKT1 at 'Ser-473'..
Protein Sequence MQSKVTGNMPTQSLLMYMDGPEVIGSSLGSPMEMEDALSMKGTAVVPFRATQEKNVIQIEGYMPLDCMFCSQTFTHSEDLNKHVLMQHRPTLCEPAVLRVEAEYLSPLDKSQVRTEPPKEKNCKENEFSCEVCGQTFRVAFDVEIHMRTHKDSFTYGCNMCGRRFKEPWFLKNHMRTHNGKSGARSKLQQGLESSPATINEVVQVHAAESISSPYKICMVCGFLFPNKESLIEHRKVHTKKTAFGTSSAQTDSPQGGMPSSREDFLQLFNLRPKSHPETGKKPVRCIPQLDPFTTFQAWQLATKGKVAICQEVKESGQEGSTDNDDSSSEKELGETNKGSCAGLSQEKEKCKHSHGEAPSVDADPKLPSSKEKPTHCSECGKAFRTYHQLVLHSRVHKKDRRAGAESPTMSVDGRQPGTCSPDLAAPLDENGAVDRGEGGSEDGSEDGLPEGIHLDKNDDGGKIKHLTSSRECSYCGKFFRSNYYLNIHLRTHTGEKPYKCEFCEYAAAQKTSLRYHLERHHKEKQTDVAAEVKNDGKNQDTEDALLTADSAQTKNLKRFFDGAKDVTGSPPAKQLKEMPSVFQNVLGSAVLSPAHKDTQDFHKNAADDSADKVNKNPTPAYLDLLKKRSAVETQANNLICRTKADVTPPPDGSTTHNLEVSPKEKQTETAADCRYRPSVDCHEKPLNLSVGALHNCPAISLSKSLIPSITCPFCTFKTFYPEVLMMHQRLEHKYNPDVHKNCRNKSLLRSRRTGCPPALLGKDVPPLSSFCKPKPKSAFPAQSKSLPSAKGKQSPPGPGKAPLTSGIDSSTLAPSNLKSHRPQQNVGVQGAATRQQQSEMFPKTSVSPAPDKTKRPETKLKPLPVAPSQPTLGSSNINGSIDYPAKNDSPWAPPGRDYFCNRSASNTAAEFGEPLPKRLKSSVVALDVDQPGANYRRGYDLPKYHMVRGITSLLPQDCVYPSQALPPKPRFLSSSEVDSPNVLTVQKPYGGSGPLYTCVPAGSPASSSTLEGKRPVSYQHLSNSMAQKRNYENFIGNAHYRPNDKKT
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
6Phosphorylation--MQSKVTGNMPTQS
--CCCCCCCCCCCCC
26.9524043423
11PhosphorylationKVTGNMPTQSLLMYM
CCCCCCCCCCEEEEC
21.7424043423
13PhosphorylationTGNMPTQSLLMYMDG
CCCCCCCCEEEECCC
26.4224043423
17PhosphorylationPTQSLLMYMDGPEVI
CCCCEEEECCCCHHC
7.6324043423
26PhosphorylationDGPEVIGSSLGSPME
CCCHHCCCCCCCCCC
15.9724043423
27PhosphorylationGPEVIGSSLGSPMEM
CCHHCCCCCCCCCCH
31.3824043423
30PhosphorylationVIGSSLGSPMEMEDA
HCCCCCCCCCCHHHH
26.7724043423
39PhosphorylationMEMEDALSMKGTAVV
CCHHHHHHCCCEEEE
21.8424043423
51PhosphorylationAVVPFRATQEKNVIQ
EEEEECCCCCCCEEE
32.76-
104PhosphorylationVLRVEAEYLSPLDKS
EHEEEEEECCCCCHH
21.3728796482
106PhosphorylationRVEAEYLSPLDKSQV
EEEEEECCCCCHHHC
23.6325159151
111PhosphorylationYLSPLDKSQVRTEPP
ECCCCCHHHCCCCCC
33.3121712546
115PhosphorylationLDKSQVRTEPPKEKN
CCHHHCCCCCCCCCC
54.7222468782
194PhosphorylationKLQQGLESSPATINE
HHHHHHHCCCCCHHH
46.8225627689
195PhosphorylationLQQGLESSPATINEV
HHHHHHCCCCCHHHH
14.8025627689
242PhosphorylationRKVHTKKTAFGTSSA
HCCCCCCCCCCCCCC
28.86-
246PhosphorylationTKKTAFGTSSAQTDS
CCCCCCCCCCCCCCC
17.0430576142
247PhosphorylationKKTAFGTSSAQTDSP
CCCCCCCCCCCCCCC
24.8523911959
248PhosphorylationKTAFGTSSAQTDSPQ
CCCCCCCCCCCCCCC
25.0023911959
251PhosphorylationFGTSSAQTDSPQGGM
CCCCCCCCCCCCCCC
37.8528985074
253PhosphorylationTSSAQTDSPQGGMPS
CCCCCCCCCCCCCCC
23.6328985074
260PhosphorylationSPQGGMPSSREDFLQ
CCCCCCCCCHHHHHH
32.8928102081
261PhosphorylationPQGGMPSSREDFLQL
CCCCCCCCHHHHHHH
33.5423911959
316PhosphorylationICQEVKESGQEGSTD
EEECHHHHCCCCCCC
39.8123663014
321PhosphorylationKESGQEGSTDNDDSS
HHHCCCCCCCCCCCH
31.6623663014
322PhosphorylationESGQEGSTDNDDSSS
HHCCCCCCCCCCCHH
50.0723663014
327PhosphorylationGSTDNDDSSSEKELG
CCCCCCCCHHHHHHC
38.3325849741
328PhosphorylationSTDNDDSSSEKELGE
CCCCCCCHHHHHHCC
49.8923663014
329PhosphorylationTDNDDSSSEKELGET
CCCCCCHHHHHHCCC
57.5523663014
336PhosphorylationSEKELGETNKGSCAG
HHHHHCCCCCCCCCC
40.1923663014
345PhosphorylationKGSCAGLSQEKEKCK
CCCCCCCHHHHHHHC
35.0625159151
354PhosphorylationEKEKCKHSHGEAPSV
HHHHHCCCCCCCCCC
20.7720068231
360PhosphorylationHSHGEAPSVDADPKL
CCCCCCCCCCCCCCC
39.4120068231
369PhosphorylationDADPKLPSSKEKPTH
CCCCCCCCCCCCCCC
65.5620068231
370PhosphorylationADPKLPSSKEKPTHC
CCCCCCCCCCCCCCH
42.7820068231
407PhosphorylationDRRAGAESPTMSVDG
HHCCCCCCCCCCCCC
25.7419664994
409PhosphorylationRAGAESPTMSVDGRQ
CCCCCCCCCCCCCCC
31.2130266825
411PhosphorylationGAESPTMSVDGRQPG
CCCCCCCCCCCCCCC
21.3823401153
419PhosphorylationVDGRQPGTCSPDLAA
CCCCCCCCCCCCCCC
19.2525850435
421PhosphorylationGRQPGTCSPDLAAPL
CCCCCCCCCCCCCCC
22.6826657352
441PhosphorylationVDRGEGGSEDGSEDG
CCCCCCCCCCCCCCC
43.2929255136
445PhosphorylationEGGSEDGSEDGLPEG
CCCCCCCCCCCCCCC
44.8529255136
492PhosphorylationYLNIHLRTHTGEKPY
EEEEEEEECCCCCCE
30.1028348404
494PhosphorylationNIHLRTHTGEKPYKC
EEEEEECCCCCCEEC
46.5629214152
497UbiquitinationLRTHTGEKPYKCEFC
EEECCCCCCEECCCC
55.80-
527PhosphorylationRHHKEKQTDVAAEVK
HHHHCCCCCHHHHHC
43.43-
568PhosphorylationFDGAKDVTGSPPAKQ
HCCCCCCCCCCCHHH
41.9230266825
570PhosphorylationGAKDVTGSPPAKQLK
CCCCCCCCCCHHHHH
20.5323401153
581PhosphorylationKQLKEMPSVFQNVLG
HHHHHCCHHHHHHHH
33.9620068231
589PhosphorylationVFQNVLGSAVLSPAH
HHHHHHHHHHCCCCC
15.8430266825
593PhosphorylationVLGSAVLSPAHKDTQ
HHHHHHCCCCCCCHH
17.2830266825
619PhosphorylationDKVNKNPTPAYLDLL
HHHCCCCCHHHHHHH
29.9128555341
627UbiquitinationPAYLDLLKKRSAVET
HHHHHHHHHHCCHHH
54.13-
630PhosphorylationLDLLKKRSAVETQAN
HHHHHHHCCHHHHHC
45.6128555341
643PhosphorylationANNLICRTKADVTPP
HCCEEECCCCCCCCC
26.6028450419
648PhosphorylationCRTKADVTPPPDGST
ECCCCCCCCCCCCCC
30.5323401153
654PhosphorylationVTPPPDGSTTHNLEV
CCCCCCCCCCCCEEE
37.2029255136
655PhosphorylationTPPPDGSTTHNLEVS
CCCCCCCCCCCEEEC
37.2929255136
656PhosphorylationPPPDGSTTHNLEVSP
CCCCCCCCCCEEECC
15.5129255136
662PhosphorylationTTHNLEVSPKEKQTE
CCCCEEECCCHHCCC
22.3730266825
676PhosphorylationETAADCRYRPSVDCH
CCHHHCCCCCCCCCC
32.9625311616
679PhosphorylationADCRYRPSVDCHEKP
HHCCCCCCCCCCCCC
22.9125311616
685AcetylationPSVDCHEKPLNLSVG
CCCCCCCCCCCCCCH
31.0126051181
690PhosphorylationHEKPLNLSVGALHNC
CCCCCCCCCHHHHCC
19.8925311616
701PhosphorylationLHNCPAISLSKSLIP
HHCCCCHHCCCCCCC
28.7924719451
705PhosphorylationPAISLSKSLIPSITC
CCHHCCCCCCCCCCC
28.3127251275
741UbiquitinationKYNPDVHKNCRNKSL
HCCCHHHHCCCCHHH
58.55-
747PhosphorylationHKNCRNKSLLRSRRT
HHCCCCHHHHHHHCC
35.8624719451
785AcetylationSAFPAQSKSLPSAKG
CCCCCCCCCCCCCCC
43.8818525467
789PhosphorylationAQSKSLPSAKGKQSP
CCCCCCCCCCCCCCC
48.1624719451
795PhosphorylationPSAKGKQSPPGPGKA
CCCCCCCCCCCCCCC
36.2323401153
805PhosphorylationGPGKAPLTSGIDSST
CCCCCCCCCCCCCCC
24.6930108239
806PhosphorylationPGKAPLTSGIDSSTL
CCCCCCCCCCCCCCC
41.2426074081
810PhosphorylationPLTSGIDSSTLAPSN
CCCCCCCCCCCCCCC
24.2530576142
811PhosphorylationLTSGIDSSTLAPSNL
CCCCCCCCCCCCCCC
24.5626074081
812PhosphorylationTSGIDSSTLAPSNLK
CCCCCCCCCCCCCCC
30.7830576142
816PhosphorylationDSSTLAPSNLKSHRP
CCCCCCCCCCCCCCC
49.5426074081
819UbiquitinationTLAPSNLKSHRPQQN
CCCCCCCCCCCCCCC
48.76-
819SumoylationTLAPSNLKSHRPQQN
CCCCCCCCCCCCCCC
48.7628112733
834PhosphorylationVGVQGAATRQQQSEM
CCCCCCHHHHHHHHH
28.60-
839PhosphorylationAATRQQQSEMFPKTS
CHHHHHHHHHCCCCC
27.0420068231
845PhosphorylationQSEMFPKTSVSPAPD
HHHHCCCCCCCCCCC
34.3023403867
846PhosphorylationSEMFPKTSVSPAPDK
HHHCCCCCCCCCCCC
27.0726657352
848PhosphorylationMFPKTSVSPAPDKTK
HCCCCCCCCCCCCCC
18.3423927012
853AcetylationSVSPAPDKTKRPETK
CCCCCCCCCCCCCCC
55.6930593669
854PhosphorylationVSPAPDKTKRPETKL
CCCCCCCCCCCCCCC
39.4026074081
869PhosphorylationKPLPVAPSQPTLGSS
CCCCCCCCCCCCCCC
38.77-
881PhosphorylationGSSNINGSIDYPAKN
CCCCCCCCCCCCCCC
14.0628555341
890PhosphorylationDYPAKNDSPWAPPGR
CCCCCCCCCCCCCCC
31.5621815630
904PhosphorylationRDYFCNRSASNTAAE
CCCCCCCCCCCHHHH
23.2728450419
906PhosphorylationYFCNRSASNTAAEFG
CCCCCCCCCHHHHHC
35.6428450419
908PhosphorylationCNRSASNTAAEFGEP
CCCCCCCHHHHHCCC
25.4228450419
918UbiquitinationEFGEPLPKRLKSSVV
HHCCCCCHHHHCCEE
77.40-
921UbiquitinationEPLPKRLKSSVVALD
CCCCHHHHCCEEEEE
44.72-
974PhosphorylationPPKPRFLSSSEVDSP
CCCCCCCCCCCCCCC
29.1630576142
975PhosphorylationPKPRFLSSSEVDSPN
CCCCCCCCCCCCCCC
32.4422199227
976PhosphorylationKPRFLSSSEVDSPNV
CCCCCCCCCCCCCCE
37.9625850435
980PhosphorylationLSSSEVDSPNVLTVQ
CCCCCCCCCCEEEEE
24.4522199227
1004PhosphorylationYTCVPAGSPASSSTL
EEEEECCCCCCCCCC
21.2825159151
1007PhosphorylationVPAGSPASSSTLEGK
EECCCCCCCCCCCCC
28.36-
1025PhosphorylationSYQHLSNSMAQKRNY
CHHHHHHHHHHHHCH
16.4828555341

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

Oops, there are no upstream regulatory protein records of ZN217_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN217_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 ZN217_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KDM1A_HUMANKDM1Aphysical
19242095
EHMT2_HUMANEHMT2physical
19242095
CTBP1_HUMANCTBP1physical
19242095
RCOR1_HUMANRCOR1physical
19242095
KDM5B_HUMANKDM5Bphysical
19242095
RCOR1_HUMANRCOR1physical
18625718
KDM1A_HUMANKDM1Aphysical
18625718
HDAC2_HUMANHDAC2physical
18625718
CTBP1_HUMANCTBP1physical
18625718
RCOR1_HUMANRCOR1physical
17967884
KDM1A_HUMANKDM1Aphysical
17967884
HDAC2_HUMANHDAC2physical
17967884
CTBP1_HUMANCTBP1physical
17967884
CTBP2_HUMANCTBP2physical
17967884
H31T_HUMANHIST3H3physical
12700765

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 ZN217_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-407, 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-321; THR-322; SER-327;THR-648 AND SER-662, 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-407; SER-570; SER-795AND SER-848, AND MASS SPECTROMETRY.

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