ZC11A_HUMAN - dbPTM
ZC11A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZC11A_HUMAN
UniProt AC O75152
Protein Name Zinc finger CCCH domain-containing protein 11A
Gene Name ZC3H11A
Organism Homo sapiens (Human).
Sequence Length 810
Subcellular Localization
Protein Description Involved in nuclear mRNA export; probably mediated by assoociation with the TREX complex..
Protein Sequence MPNQGEDCYFFFYSTCTKGDSCPFRHCEAAIGNETVCTLWQEGRCFRQVCRFRHMEIDKKRSEIPCYWENQPTGCQKLNCAFHHNRGRYVDGLFLPPSKTVLPTVPESPEEEVKASQLSVQQNKLSVQSNPSPQLRSVMKVESSENVPSPTHPPVVINAADDDEDDDDQFSEEGDETKTPTLQPTPEVHNGLRVTSVRKPAVNIKQGECLNFGIKTLEEIKSKKMKEKSKKQGEGSSGVSSLLLHPEPVPGPEKENVRTVVRTVTLSTKQGEEPLVRLSLTERLGKRKFSAGGDSDPPLKRSLAQRLGKKVEAPETNIDKTPKKAQVSKSLKERLGMSADPDNEDATDKVNKVGEIHVKTLEEILLERASQKRGELQTKLKTEGPSKTDDSTSGARSSSTIRIKTFSEVLAEKKHRQQEAERQKSKKDTTCIKLKIDSEIKKTVVLPPIVASRGQSEEPAGKTKSMQEVHIKTLEEIKLEKALRVQQSSESSTSSPSQHEATPGARRLLRITKRTGMKEEKNLQEGNEVDSQSSIRTEAKEASGETTGVDITKIQVKRCETMREKHMQKQQEREKSVLTPLRGDVASCNTQVAEKPVLTAVPGITRHLTKRLPTKSSQKVEVETSGIGDSLLNVKCAAQTLEKRGKAKPKVNVKPSVVKVVSSPKLAPKRKAVEMHAAVIAAVKPLSSSSVLQEPPAKKAAVAVVPLVSEDKSVTVPEAENPRDSLVLPPTQSSSDSSPPEVSGPSSSQMSMKTRRLSSASTGKPPLSVEDDFEKLIWEISGGKLEAEIDLDPGKDEDDLLLELSEMIDS
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
51UbiquitinationRCFRQVCRFRHMEID
HHHHHHHHHHCCCCC
32.5524816145
60SumoylationRHMEIDKKRSEIPCY
HCCCCCCCCCCCCCC
58.36-
60SumoylationRHMEIDKKRSEIPCY
HCCCCCCCCCCCCCC
58.36-
99UbiquitinationGLFLPPSKTVLPTVP
CEEECCCCCCCCCCC
48.7229967540
100PhosphorylationLFLPPSKTVLPTVPE
EEECCCCCCCCCCCC
31.4528464451
104PhosphorylationPSKTVLPTVPESPEE
CCCCCCCCCCCCHHH
44.5223927012
108PhosphorylationVLPTVPESPEEEVKA
CCCCCCCCHHHHHHH
31.3819664994
114SumoylationESPEEEVKASQLSVQ
CCHHHHHHHHHHHHH
45.67-
114SumoylationESPEEEVKASQLSVQ
CCHHHHHHHHHHHHH
45.6728112733
114UbiquitinationESPEEEVKASQLSVQ
CCHHHHHHHHHHHHH
45.6729967540
116PhosphorylationPEEEVKASQLSVQQN
HHHHHHHHHHHHHHH
26.4117525332
119PhosphorylationEVKASQLSVQQNKLS
HHHHHHHHHHHHCCC
15.3924732914
124SumoylationQLSVQQNKLSVQSNP
HHHHHHHCCCCCCCC
37.49-
124UbiquitinationQLSVQQNKLSVQSNP
HHHHHHHCCCCCCCC
37.4922817900
124SumoylationQLSVQQNKLSVQSNP
HHHHHHHCCCCCCCC
37.4928112733
124AcetylationQLSVQQNKLSVQSNP
HHHHHHHCCCCCCCC
37.4925953088
126PhosphorylationSVQQNKLSVQSNPSP
HHHHHCCCCCCCCCH
21.5119691289
129PhosphorylationQNKLSVQSNPSPQLR
HHCCCCCCCCCHHHH
48.8622167270
132PhosphorylationLSVQSNPSPQLRSVM
CCCCCCCCHHHHHEE
29.5429255136
137PhosphorylationNPSPQLRSVMKVESS
CCCHHHHHEEEEECC
34.8526074081
140SumoylationPQLRSVMKVESSENV
HHHHHEEEEECCCCC
40.4728112733
143PhosphorylationRSVMKVESSENVPSP
HHEEEEECCCCCCCC
46.0323927012
144PhosphorylationSVMKVESSENVPSPT
HEEEEECCCCCCCCC
21.4925850435
149PhosphorylationESSENVPSPTHPPVV
ECCCCCCCCCCCCEE
37.8423927012
151PhosphorylationSENVPSPTHPPVVIN
CCCCCCCCCCCEEEE
51.8823927012
171PhosphorylationEDDDDQFSEEGDETK
CCCCCCCCCCCCCCC
29.1623927012
177PhosphorylationFSEEGDETKTPTLQP
CCCCCCCCCCCCCCC
44.9830278072
179PhosphorylationEEGDETKTPTLQPTP
CCCCCCCCCCCCCCC
29.0028464451
181PhosphorylationGDETKTPTLQPTPEV
CCCCCCCCCCCCCCC
43.1730266825
185PhosphorylationKTPTLQPTPEVHNGL
CCCCCCCCCCCCCCE
21.0830266825
185UbiquitinationKTPTLQPTPEVHNGL
CCCCCCCCCCCCCCE
21.0824816145
195PhosphorylationVHNGLRVTSVRKPAV
CCCCEEEEEECCCCC
18.3123186163
196PhosphorylationHNGLRVTSVRKPAVN
CCCEEEEEECCCCCC
19.6425159151
199UbiquitinationLRVTSVRKPAVNIKQ
EEEEEECCCCCCCCC
34.8629967540
215UbiquitinationECLNFGIKTLEEIKS
CHHHHCCHHHHHHHH
47.6529967540
215AcetylationECLNFGIKTLEEIKS
CHHHHCCHHHHHHHH
47.6526051181
221SumoylationIKTLEEIKSKKMKEK
CHHHHHHHHHHHHHH
60.55-
221SumoylationIKTLEEIKSKKMKEK
CHHHHHHHHHHHHHH
60.55-
221UbiquitinationIKTLEEIKSKKMKEK
CHHHHHHHHHHHHHH
60.5529967540
229PhosphorylationSKKMKEKSKKQGEGS
HHHHHHHHHHCCCCC
46.29-
231UbiquitinationKMKEKSKKQGEGSSG
HHHHHHHHCCCCCCC
71.3029967540
237PhosphorylationKKQGEGSSGVSSLLL
HHCCCCCCCCHHHHC
54.8128555341
241PhosphorylationEGSSGVSSLLLHPEP
CCCCCCHHHHCCCCC
22.1928555341
254UbiquitinationEPVPGPEKENVRTVV
CCCCCCCCCCCEEEE
58.69-
263PhosphorylationNVRTVVRTVTLSTKQ
CCEEEEEEEEECCCC
13.2623312004
265PhosphorylationRTVVRTVTLSTKQGE
EEEEEEEEECCCCCC
17.8729514088
267PhosphorylationVVRTVTLSTKQGEEP
EEEEEEECCCCCCCC
24.9629514088
268PhosphorylationVRTVTLSTKQGEEPL
EEEEEECCCCCCCCE
30.4229514088
269SumoylationRTVTLSTKQGEEPLV
EEEEECCCCCCCCEE
53.59-
269SumoylationRTVTLSTKQGEEPLV
EEEEECCCCCCCCEE
53.59-
269UbiquitinationRTVTLSTKQGEEPLV
EEEEECCCCCCCCEE
53.5933845483
269AcetylationRTVTLSTKQGEEPLV
EEEEECCCCCCCCEE
53.5925953088
279PhosphorylationEEPLVRLSLTERLGK
CCCEEEEEHHHHHCC
23.7625159151
281PhosphorylationPLVRLSLTERLGKRK
CEEEEEHHHHHCCCC
18.7127251275
286AcetylationSLTERLGKRKFSAGG
EHHHHHCCCCCCCCC
57.9420167786
288MethylationTERLGKRKFSAGGDS
HHHHCCCCCCCCCCC
47.35115978381
290PhosphorylationRLGKRKFSAGGDSDP
HHCCCCCCCCCCCCH
29.1029255136
295PhosphorylationKFSAGGDSDPPLKRS
CCCCCCCCCHHHHHH
56.1223927012
300MethylationGDSDPPLKRSLAQRL
CCCCHHHHHHHHHHH
45.79115978389
300UbiquitinationGDSDPPLKRSLAQRL
CCCCHHHHHHHHHHH
45.7933845483
3002-HydroxyisobutyrylationGDSDPPLKRSLAQRL
CCCCHHHHHHHHHHH
45.79-
300AcetylationGDSDPPLKRSLAQRL
CCCCHHHHHHHHHHH
45.7925953088
310SumoylationLAQRLGKKVEAPETN
HHHHHCCCCCCCCCC
43.43-
310SumoylationLAQRLGKKVEAPETN
HHHHHCCCCCCCCCC
43.43-
310UbiquitinationLAQRLGKKVEAPETN
HHHHHCCCCCCCCCC
43.4329967540
310AcetylationLAQRLGKKVEAPETN
HHHHHCCCCCCCCCC
43.4326051181
316PhosphorylationKKVEAPETNIDKTPK
CCCCCCCCCCCCCCC
36.0930266825
320AcetylationAPETNIDKTPKKAQV
CCCCCCCCCCCHHHH
64.0325953088
321PhosphorylationPETNIDKTPKKAQVS
CCCCCCCCCCHHHHC
36.2729255136
328PhosphorylationTPKKAQVSKSLKERL
CCCHHHHCHHHHHHH
12.40-
329UbiquitinationPKKAQVSKSLKERLG
CCHHHHCHHHHHHHC
62.0329967540
329AcetylationPKKAQVSKSLKERLG
CCHHHHCHHHHHHHC
62.0325953088
332UbiquitinationAQVSKSLKERLGMSA
HHHCHHHHHHHCCCC
48.1329967540
337SulfoxidationSLKERLGMSADPDNE
HHHHHHCCCCCCCCC
3.3621406390
338PhosphorylationLKERLGMSADPDNED
HHHHHCCCCCCCCCC
27.9330108239
349UbiquitinationDNEDATDKVNKVGEI
CCCCCCHHHHCCCEE
43.2729967540
349AcetylationDNEDATDKVNKVGEI
CCCCCCHHHHCCCEE
43.2725953088
352UbiquitinationDATDKVNKVGEIHVK
CCCHHHHCCCEEEHH
55.3829967540
359UbiquitinationKVGEIHVKTLEEILL
CCCEEEHHCHHHHHH
32.9829967540
370PhosphorylationEILLERASQKRGELQ
HHHHHHHHHHHCCHH
42.3228112733
378PhosphorylationQKRGELQTKLKTEGP
HHHCCHHHHHCCCCC
51.47-
379UbiquitinationKRGELQTKLKTEGPS
HHCCHHHHHCCCCCC
34.7229967540
381SumoylationGELQTKLKTEGPSKT
CCHHHHHCCCCCCCC
46.19-
381SumoylationGELQTKLKTEGPSKT
CCHHHHHCCCCCCCC
46.19-
381UbiquitinationGELQTKLKTEGPSKT
CCHHHHHCCCCCCCC
46.19-
387UbiquitinationLKTEGPSKTDDSTSG
HCCCCCCCCCCCCCC
60.1424816145
391PhosphorylationGPSKTDDSTSGARSS
CCCCCCCCCCCCCCC
27.5521712546
398PhosphorylationSTSGARSSSTIRIKT
CCCCCCCCCEEEEEE
26.4121712546
399PhosphorylationTSGARSSSTIRIKTF
CCCCCCCCEEEEEEH
29.1521712546
400PhosphorylationSGARSSSTIRIKTFS
CCCCCCCEEEEEEHH
19.07-
404SumoylationSSSTIRIKTFSEVLA
CCCEEEEEEHHHHHH
33.40-
404SumoylationSSSTIRIKTFSEVLA
CCCEEEEEEHHHHHH
33.40-
404UbiquitinationSSSTIRIKTFSEVLA
CCCEEEEEEHHHHHH
33.4032142685
407PhosphorylationTIRIKTFSEVLAEKK
EEEEEEHHHHHHHHH
31.8421815630
413AcetylationFSEVLAEKKHRQQEA
HHHHHHHHHHHHHHH
48.5523236377
413UbiquitinationFSEVLAEKKHRQQEA
HHHHHHHHHHHHHHH
48.5529967540
414UbiquitinationSEVLAEKKHRQQEAE
HHHHHHHHHHHHHHH
35.21-
425PhosphorylationQEAERQKSKKDTTCI
HHHHHHHCCCCCEEE
36.2830387612
429PhosphorylationRQKSKKDTTCIKLKI
HHHCCCCCEEEEEEE
32.2329083192
430PhosphorylationQKSKKDTTCIKLKID
HHCCCCCEEEEEEEC
23.5129083192
433AcetylationKKDTTCIKLKIDSEI
CCCCEEEEEEECCCC
45.9625953088
435UbiquitinationDTTCIKLKIDSEIKK
CCEEEEEEECCCCCE
39.1929967540
442UbiquitinationKIDSEIKKTVVLPPI
EECCCCCEEEECCCE
52.81-
443PhosphorylationIDSEIKKTVVLPPIV
ECCCCCEEEECCCEE
15.7328555341
452PhosphorylationVLPPIVASRGQSEEP
ECCCEECCCCCCCCC
26.5025159151
456PhosphorylationIVASRGQSEEPAGKT
EECCCCCCCCCCCCC
46.9128985074
462UbiquitinationQSEEPAGKTKSMQEV
CCCCCCCCCCCCEEE
55.6929967540
462AcetylationQSEEPAGKTKSMQEV
CCCCCCCCCCCCEEE
55.6925953088
464UbiquitinationEEPAGKTKSMQEVHI
CCCCCCCCCCEEEEE
47.6329967540
465PhosphorylationEPAGKTKSMQEVHIK
CCCCCCCCCEEEEEE
30.8125159151
478SumoylationIKTLEEIKLEKALRV
EEEHHHHHHHHHHHH
54.60-
478SumoylationIKTLEEIKLEKALRV
EEEHHHHHHHHHHHH
54.6028112733
478UbiquitinationIKTLEEIKLEKALRV
EEEHHHHHHHHHHHH
54.6029967540
478AcetylationIKTLEEIKLEKALRV
EEEHHHHHHHHHHHH
54.6026051181
481UbiquitinationLEEIKLEKALRVQQS
HHHHHHHHHHHHHCC
64.26-
488PhosphorylationKALRVQQSSESSTSS
HHHHHHCCCCCCCCC
20.9827461979
489PhosphorylationALRVQQSSESSTSSP
HHHHHCCCCCCCCCC
36.8427461979
491PhosphorylationRVQQSSESSTSSPSQ
HHHCCCCCCCCCCCH
40.6421955146
492PhosphorylationVQQSSESSTSSPSQH
HHCCCCCCCCCCCHH
28.4021955146
493PhosphorylationQQSSESSTSSPSQHE
HCCCCCCCCCCCHHC
42.3721955146
494PhosphorylationQSSESSTSSPSQHEA
CCCCCCCCCCCHHCC
42.0523401153
495PhosphorylationSSESSTSSPSQHEAT
CCCCCCCCCCHHCCC
28.7625159151
497PhosphorylationESSTSSPSQHEATPG
CCCCCCCCHHCCCHH
46.2321955146
502PhosphorylationSPSQHEATPGARRLL
CCCHHCCCHHHHHHH
21.1925159151
512PhosphorylationARRLLRITKRTGMKE
HHHHHHHHHHHCCCC
14.1920068231
515PhosphorylationLLRITKRTGMKEEKN
HHHHHHHHCCCCCCC
43.0920068231
518AcetylationITKRTGMKEEKNLQE
HHHHHCCCCCCCCCC
65.1626051181
521UbiquitinationRTGMKEEKNLQEGNE
HHCCCCCCCCCCCCC
65.1424816145
531PhosphorylationQEGNEVDSQSSIRTE
CCCCCCCCHHHHHHH
36.8221815630
533PhosphorylationGNEVDSQSSIRTEAK
CCCCCCHHHHHHHHH
31.5227732954
534PhosphorylationNEVDSQSSIRTEAKE
CCCCCHHHHHHHHHH
14.4127732954
540UbiquitinationSSIRTEAKEASGETT
HHHHHHHHHHCCCCC
47.80-
543PhosphorylationRTEAKEASGETTGVD
HHHHHHHCCCCCCCC
37.9522210691
546PhosphorylationAKEASGETTGVDITK
HHHHCCCCCCCCCEE
32.1630576142
547PhosphorylationKEASGETTGVDITKI
HHHCCCCCCCCCEEE
30.7922210691
552PhosphorylationETTGVDITKIQVKRC
CCCCCCCEEEEEEEH
20.0322210691
553UbiquitinationTTGVDITKIQVKRCE
CCCCCCEEEEEEEHH
31.3229967540
553AcetylationTTGVDITKIQVKRCE
CCCCCCEEEEEEEHH
31.3226051181
561PhosphorylationIQVKRCETMREKHMQ
EEEEEHHHHHHHHHH
25.75-
575UbiquitinationQKQQEREKSVLTPLR
HHHHHHHHHCCHHCC
52.6829967540
575AcetylationQKQQEREKSVLTPLR
HHHHHHHHHCCHHCC
52.6825953088
576PhosphorylationKQQEREKSVLTPLRG
HHHHHHHHCCHHCCC
20.0130576142
579PhosphorylationEREKSVLTPLRGDVA
HHHHHCCHHCCCCHH
20.3725159151
587PhosphorylationPLRGDVASCNTQVAE
HCCCCHHHCCCHHCC
14.0326074081
590PhosphorylationGDVASCNTQVAEKPV
CCHHHCCCHHCCCCH
28.8430576142
595AcetylationCNTQVAEKPVLTAVP
CCCHHCCCCHHHCCC
30.5923954790
595UbiquitinationCNTQVAEKPVLTAVP
CCCHHCCCCHHHCCC
30.5929967540
599PhosphorylationVAEKPVLTAVPGITR
HCCCCHHHCCCCHHH
26.3322199227
605PhosphorylationLTAVPGITRHLTKRL
HHCCCCHHHHHHHCC
20.2522199227
609PhosphorylationPGITRHLTKRLPTKS
CCHHHHHHHCCCCCC
14.16-
615UbiquitinationLTKRLPTKSSQKVEV
HHHCCCCCCCCCEEE
46.2829967540
616PhosphorylationTKRLPTKSSQKVEVE
HHCCCCCCCCCEEEE
40.2421130716
619SumoylationLPTKSSQKVEVETSG
CCCCCCCCEEEEECC
42.16-
619SumoylationLPTKSSQKVEVETSG
CCCCCCCCEEEEECC
42.1628112733
619UbiquitinationLPTKSSQKVEVETSG
CCCCCCCCEEEEECC
42.1629967540
619AcetylationLPTKSSQKVEVETSG
CCCCCCCCEEEEECC
42.1625953088
624PhosphorylationSQKVEVETSGIGDSL
CCCEEEEECCCCHHH
37.1127251275
625PhosphorylationQKVEVETSGIGDSLL
CCEEEEECCCCHHHH
18.2025159151
630PhosphorylationETSGIGDSLLNVKCA
EECCCCHHHHHHHHH
29.5527251275
635UbiquitinationGDSLLNVKCAAQTLE
CHHHHHHHHHHHHHH
19.6532015554
643AcetylationCAAQTLEKRGKAKPK
HHHHHHHHCCCCCCC
70.3525953088
654UbiquitinationAKPKVNVKPSVVKVV
CCCCCCCCCCEEEEE
26.7729967540
654AcetylationAKPKVNVKPSVVKVV
CCCCCCCCCCEEEEE
26.7725953088
656PhosphorylationPKVNVKPSVVKVVSS
CCCCCCCCEEEEECC
33.5528555341
659UbiquitinationNVKPSVVKVVSSPKL
CCCCCEEEEECCCCC
34.4629967540
659AcetylationNVKPSVVKVVSSPKL
CCCCCEEEEECCCCC
34.4625953088
662PhosphorylationPSVVKVVSSPKLAPK
CCEEEEECCCCCCCC
43.8624732914
663PhosphorylationSVVKVVSSPKLAPKR
CEEEEECCCCCCCCC
17.9124732914
665AcetylationVKVVSSPKLAPKRKA
EEEECCCCCCCCCHH
60.2623749302
665UbiquitinationVKVVSSPKLAPKRKA
EEEECCCCCCCCCHH
60.2629967540
684AcetylationAAVIAAVKPLSSSSV
HHHHHHHCCCCCCHH
35.2023749302
687PhosphorylationIAAVKPLSSSSVLQE
HHHHCCCCCCHHHCC
36.3825159151
688PhosphorylationAAVKPLSSSSVLQEP
HHHCCCCCCHHHCCC
34.0225159151
689PhosphorylationAVKPLSSSSVLQEPP
HHCCCCCCHHHCCCC
22.53-
690PhosphorylationVKPLSSSSVLQEPPA
HCCCCCCHHHCCCCC
28.88-
698AcetylationVLQEPPAKKAAVAVV
HHCCCCCCCCEEEEE
49.0326051181
699UbiquitinationLQEPPAKKAAVAVVP
HCCCCCCCCEEEEEE
43.6229967540
709PhosphorylationVAVVPLVSEDKSVTV
EEEEECCCCCCCCCC
48.0020860994
712UbiquitinationVPLVSEDKSVTVPEA
EECCCCCCCCCCCCC
42.6529967540
713PhosphorylationPLVSEDKSVTVPEAE
ECCCCCCCCCCCCCC
35.0326074081
715PhosphorylationVSEDKSVTVPEAENP
CCCCCCCCCCCCCCC
37.1226074081
725PhosphorylationEAENPRDSLVLPPTQ
CCCCCCCCCCCCCCC
22.9620873877
731PhosphorylationDSLVLPPTQSSSDSS
CCCCCCCCCCCCCCC
38.8630278072
733PhosphorylationLVLPPTQSSSDSSPP
CCCCCCCCCCCCCCC
34.0030278072
734PhosphorylationVLPPTQSSSDSSPPE
CCCCCCCCCCCCCCC
28.4830278072
735PhosphorylationLPPTQSSSDSSPPEV
CCCCCCCCCCCCCCC
46.9230278072
737PhosphorylationPTQSSSDSSPPEVSG
CCCCCCCCCCCCCCC
46.8530278072
738PhosphorylationTQSSSDSSPPEVSGP
CCCCCCCCCCCCCCC
49.8430278072
743PhosphorylationDSSPPEVSGPSSSQM
CCCCCCCCCCCHHHH
43.2425262027
746PhosphorylationPPEVSGPSSSQMSMK
CCCCCCCCHHHHCCC
46.2625262027
747PhosphorylationPEVSGPSSSQMSMKT
CCCCCCCHHHHCCCE
27.9420873877
748PhosphorylationEVSGPSSSQMSMKTR
CCCCCCHHHHCCCEE
33.9520873877
751PhosphorylationGPSSSQMSMKTRRLS
CCCHHHHCCCEECCC
14.9720873877
754PhosphorylationSSQMSMKTRRLSSAS
HHHHCCCEECCCCCC
16.6330576142
757PhosphorylationMSMKTRRLSSASTGK
HCCCEECCCCCCCCC
4.2332142685
758PhosphorylationSMKTRRLSSASTGKP
CCCEECCCCCCCCCC
23.2629255136
759PhosphorylationMKTRRLSSASTGKPP
CCEECCCCCCCCCCC
30.7229255136
761PhosphorylationTRRLSSASTGKPPLS
EECCCCCCCCCCCCC
39.3729255136
762PhosphorylationRRLSSASTGKPPLSV
ECCCCCCCCCCCCCC
49.2829255136
764AcetylationLSSASTGKPPLSVED
CCCCCCCCCCCCCHH
43.4823954790
764UbiquitinationLSSASTGKPPLSVED
CCCCCCCCCCCCCHH
43.4819608861
768PhosphorylationSTGKPPLSVEDDFEK
CCCCCCCCCHHHHHH
29.2729255136
781PhosphorylationEKLIWEISGGKLEAE
HHHHHHHHCCEEEEE
29.9421815630

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
321TPhosphorylationKinaseCDK1P06493
PSP
321TPhosphorylationKinaseCDK2P24941
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZC11A_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 ZC11A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZC11A_HUMAN !!

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 ZC11A_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-764, 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-108 AND SER-738, ANDMASS 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-108 AND SER-132, ANDMASS 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-108; SER-132; SER-171;SER-290; THR-321; SER-758; SER-759 AND SER-768, 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-132, 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 SER-132; SER-149 ANDSER-171, 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-108 AND SER-116, ANDMASS 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-758; SER-759; SER-761AND THR-762, AND MASS 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-108; SER-132 ANDSER-495, 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-108 AND SER-132, ANDMASS SPECTROMETRY.
"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-290 AND SER-758, ANDMASS 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-132, AND MASSSPECTROMETRY.

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