CEP97_HUMAN - dbPTM
CEP97_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CEP97_HUMAN
UniProt AC Q8IW35
Protein Name Centrosomal protein of 97 kDa
Gene Name CEP97
Organism Homo sapiens (Human).
Sequence Length 865
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome .
Protein Description Acts as a key negative regulator of ciliogenesis in collaboration with CCP110 by capping the mother centriole thereby preventing cilia formation. Required for recruitment of CCP110 to the centrosome..
Protein Sequence MAVARVDAALPPGEGSVVNWSGQGLQKLGPNLPCEADIHTLILDKNQIIKLENLEKCKRLIQLSVANNRLVRMMGVAKLTLLRVLNLPHNSIGCVEGLKELVHLEWLNLAGNNLKAMEQINSCTALQHLDLSDNNISQIGDLSKLVSLKTLLLHGNIITSLRMAPAYLPRSLAILSLAENEIRDLNEISFLASLTELEQLSIMNNPCVMATPSIPGFDYRPYIVSWCLNLRVLDGYVISQKESLKAEWLYSQGKGRAYRPGQHIQLVQYLATVCPLTSTLGLQTAEDAKLEKILSKQRFHQRQLMNQSQNEELSPLVPVETRASLIPEHSSPVQDCQISQESEPVIQVNSWVGINSNDDQLFAVKNNFPASVHTTRYSRNDLHLEDIQTDEDKLNCSLLSSESTFMPVASGLSPLSPTVELRLQGINLGLEDDGVADESVKGLESQVLDKEEEQPLWAANENSVQMMRSEINTEVNEKAGLLPCPEPTIISAILKDDNHSLTFFPESTEQKQSDIKKPENTQPENKETISQATSEKLPMILTQRSVALGQDKVALQKLNDAATKLQACWRGFYARNYNPQAKDVRYEIRLRRMQEHIVCLTDEIRRLRKERDEERIKKFVQEEAFRFLWNQVRSLQVWQQTVDQRLSSWHTDVPPISSTLVPSKHPLFTQSQESSCDQNADWFIASDVAPQEKSLPEFPDSGFHSSLTEQVHSLQHSLDFEKSSTEGSESSIMGNSIDTVRYGKESDLGDVSEEHGEWNKESSNNEQDNSLLEQYLTSVQQLEDADERTNFDTETRDSKLHIACFPVQLDTLSDGASVDESHGISPPLQGEISQTQENSKLNAEVQGQQPECDSTFQLLHVGVTV
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
27UbiquitinationWSGQGLQKLGPNLPC
CCCCCHHHHCCCCCC
61.53-
45UbiquitinationIHTLILDKNQIIKLE
EEEEEECHHCEEEEC
47.51-
45 (in isoform 2)Ubiquitination-47.51-
50AcetylationLDKNQIIKLENLEKC
ECHHCEEEECCHHHH
51.9125953088
50UbiquitinationLDKNQIIKLENLEKC
ECHHCEEEECCHHHH
51.91-
64PhosphorylationCKRLIQLSVANNRLV
HHHHHHHHHHCCHHH
11.6524670416
144UbiquitinationSQIGDLSKLVSLKTL
HHHHHHHHHHCHHHH
61.27-
241UbiquitinationDGYVISQKESLKAEW
CCEEEECHHHHCHHH
42.34-
241 (in isoform 2)Ubiquitination-42.34-
245UbiquitinationISQKESLKAEWLYSQ
EECHHHHCHHHHHHC
54.24-
254UbiquitinationEWLYSQGKGRAYRPG
HHHHHCCCCCCCCCC
37.27-
292UbiquitinationAEDAKLEKILSKQRF
HHHHHHHHHHHHHHH
60.42-
308PhosphorylationQRQLMNQSQNEELSP
HHHHHCHHCCCCCCC
29.9325159151
314PhosphorylationQSQNEELSPLVPVET
HHCCCCCCCCCCCHH
21.3325159151
321PhosphorylationSPLVPVETRASLIPE
CCCCCCHHHHHHCCC
31.5920068231
324PhosphorylationVPVETRASLIPEHSS
CCCHHHHHHCCCCCC
24.4426074081
330PhosphorylationASLIPEHSSPVQDCQ
HHHCCCCCCCCCCCC
34.3726074081
331PhosphorylationSLIPEHSSPVQDCQI
HHCCCCCCCCCCCCC
30.8826074081
339PhosphorylationPVQDCQISQESEPVI
CCCCCCCCCCCCCEE
11.3026074081
342PhosphorylationDCQISQESEPVIQVN
CCCCCCCCCCEEEEE
39.2926074081
350PhosphorylationEPVIQVNSWVGINSN
CCEEEEEEEEEECCC
25.0428348404
356PhosphorylationNSWVGINSNDDQLFA
EEEEEECCCCCCEEE
39.4528348404
371PhosphorylationVKNNFPASVHTTRYS
EECCCCCEEEECCCC
18.0525159151
377PhosphorylationASVHTTRYSRNDLHL
CEEEECCCCCCCCCH
15.1928555341
378PhosphorylationSVHTTRYSRNDLHLE
EEEECCCCCCCCCHH
22.7129449344
389PhosphorylationLHLEDIQTDEDKLNC
CCHHHHCCCHHHHCC
41.5127080861
397PhosphorylationDEDKLNCSLLSSEST
CHHHHCCCCCCCCCC
31.1322199227
400PhosphorylationKLNCSLLSSESTFMP
HHCCCCCCCCCCCCC
37.0322199227
401PhosphorylationLNCSLLSSESTFMPV
HCCCCCCCCCCCCCC
35.2222199227
403PhosphorylationCSLLSSESTFMPVAS
CCCCCCCCCCCCCCC
28.9722199227
404PhosphorylationSLLSSESTFMPVASG
CCCCCCCCCCCCCCC
21.6522199227
410PhosphorylationSTFMPVASGLSPLSP
CCCCCCCCCCCCCCC
40.2728450419
413PhosphorylationMPVASGLSPLSPTVE
CCCCCCCCCCCCCEE
27.5923898821
416PhosphorylationASGLSPLSPTVELRL
CCCCCCCCCCEEEEE
23.1625159151
418PhosphorylationGLSPLSPTVELRLQG
CCCCCCCCEEEEECC
24.2028102081
439PhosphorylationDDGVADESVKGLESQ
CCCCCCHHHCCHHHH
29.6730576142
445PhosphorylationESVKGLESQVLDKEE
HHHCCHHHHCCCCCC
30.5421815630
478UbiquitinationINTEVNEKAGLLPCP
HHHHHHHHCCCCCCC
42.42-
488PhosphorylationLLPCPEPTIISAILK
CCCCCCCCEEEEEEC
29.3127251275
491PhosphorylationCPEPTIISAILKDDN
CCCCCEEEEEECCCC
12.8524719451
495UbiquitinationTIISAILKDDNHSLT
CEEEEEECCCCCCCE
57.85-
500PhosphorylationILKDDNHSLTFFPES
EECCCCCCCEECCCC
35.0523401153
502PhosphorylationKDDNHSLTFFPESTE
CCCCCCCEECCCCCC
26.6729255136
507PhosphorylationSLTFFPESTEQKQSD
CCEECCCCCCCCHHH
37.1723403867
511UbiquitinationFPESTEQKQSDIKKP
CCCCCCCCHHHCCCC
45.60-
530PhosphorylationPENKETISQATSEKL
CCCHHHHHHHHHCCC
22.60-
534PhosphorylationETISQATSEKLPMIL
HHHHHHHHCCCCEEH
35.4325627689
542PhosphorylationEKLPMILTQRSVALG
CCCCEEHHHHHHHCC
15.8317525332
545PhosphorylationPMILTQRSVALGQDK
CEEHHHHHHHCCCCH
11.2625159151
552AcetylationSVALGQDKVALQKLN
HHHCCCCHHHHHHHH
22.8623236377
552UbiquitinationSVALGQDKVALQKLN
HHHCCCCHHHHHHHH
22.86-
552 (in isoform 2)Ubiquitination-22.86-
557UbiquitinationQDKVALQKLNDAATK
CCHHHHHHHHHHHHH
50.54-
557 (in isoform 2)Ubiquitination-50.54-
564AcetylationKLNDAATKLQACWRG
HHHHHHHHHHHHHHH
33.6023236377
564UbiquitinationKLNDAATKLQACWRG
HHHHHHHHHHHHHHH
33.60-
564 (in isoform 2)Ubiquitination-33.60-
582UbiquitinationRNYNPQAKDVRYEIR
CCCCCCCCCHHHHHH
52.05-
582 (in isoform 2)Ubiquitination-52.05-
617 (in isoform 2)Ubiquitination-46.51-
618UbiquitinationRDEERIKKFVQEEAF
CCHHHHHHHHHHHHH
48.69-
618 (in isoform 2)Ubiquitination-48.69-
648PhosphorylationTVDQRLSSWHTDVPP
HHHHHHHHHCCCCCC
27.7128555341
651PhosphorylationQRLSSWHTDVPPISS
HHHHHHCCCCCCCCC
32.2228555341
657PhosphorylationHTDVPPISSTLVPSK
CCCCCCCCCCCCCCC
24.0428555341
669PhosphorylationPSKHPLFTQSQESSC
CCCCCCCCCCCCCCC
34.6928857561
671PhosphorylationKHPLFTQSQESSCDQ
CCCCCCCCCCCCCCC
32.6228857561
674PhosphorylationLFTQSQESSCDQNAD
CCCCCCCCCCCCCCC
28.7328857561
675PhosphorylationFTQSQESSCDQNADW
CCCCCCCCCCCCCCE
22.4424719451
694PhosphorylationDVAPQEKSLPEFPDS
CCCCCCCCCCCCCCC
48.69-
708PhosphorylationSGFHSSLTEQVHSLQ
CCCCHHHHHHHHHHH
26.73-
717PhosphorylationQVHSLQHSLDFEKSS
HHHHHHHHCCCCCCC
19.3727251275
723PhosphorylationHSLDFEKSSTEGSES
HHCCCCCCCCCCCCC
34.9825159151
724PhosphorylationSLDFEKSSTEGSESS
HCCCCCCCCCCCCCH
41.3625159151
725PhosphorylationLDFEKSSTEGSESSI
CCCCCCCCCCCCCHH
52.0028985074
728PhosphorylationEKSSTEGSESSIMGN
CCCCCCCCCCHHCCC
28.2426471730
730PhosphorylationSSTEGSESSIMGNSI
CCCCCCCCHHCCCCC
27.1927251275
731PhosphorylationSTEGSESSIMGNSID
CCCCCCCHHCCCCCC
16.7327251275
733SulfoxidationEGSESSIMGNSIDTV
CCCCCHHCCCCCCEE
4.4921406390
736PhosphorylationESSIMGNSIDTVRYG
CCHHCCCCCCEEECC
18.9921815630
739PhosphorylationIMGNSIDTVRYGKES
HCCCCCCEEECCCCC
12.7627251275
742PhosphorylationNSIDTVRYGKESDLG
CCCCEEECCCCCCCC
28.3630576142
744UbiquitinationIDTVRYGKESDLGDV
CCEEECCCCCCCCCC
45.14-
746PhosphorylationTVRYGKESDLGDVSE
EEECCCCCCCCCCCH
41.4430576142
752PhosphorylationESDLGDVSEEHGEWN
CCCCCCCCHHHCCCC
41.8430576142
762PhosphorylationHGEWNKESSNNEQDN
HCCCCCCCCCCHHHH
39.7229116813
763PhosphorylationGEWNKESSNNEQDNS
CCCCCCCCCCHHHHH
44.7821712546
770PhosphorylationSNNEQDNSLLEQYLT
CCCHHHHHHHHHHHH
42.4921712546
775PhosphorylationDNSLLEQYLTSVQQL
HHHHHHHHHHHHHHH
11.5429116813
777PhosphorylationSLLEQYLTSVQQLED
HHHHHHHHHHHHHHC
23.1720873877
778PhosphorylationLLEQYLTSVQQLEDA
HHHHHHHHHHHHHCC
18.4820873877
793PhosphorylationDERTNFDTETRDSKL
CHHCCCCCCCCCCCE
34.8128348404
795PhosphorylationRTNFDTETRDSKLHI
HCCCCCCCCCCCEEE
41.7026074081
798PhosphorylationFDTETRDSKLHIACF
CCCCCCCCCEEEEEE
33.5526074081
799UbiquitinationDTETRDSKLHIACFP
CCCCCCCCEEEEEEE
48.66-
811PhosphorylationCFPVQLDTLSDGASV
EEEEEECCCCCCCCC
36.4328122231
813PhosphorylationPVQLDTLSDGASVDE
EEEECCCCCCCCCCH
35.7728348404
817PhosphorylationDTLSDGASVDESHGI
CCCCCCCCCCHHCCC
35.3128348404
821PhosphorylationDGASVDESHGISPPL
CCCCCCHHCCCCCCC
23.6628348404
825PhosphorylationVDESHGISPPLQGEI
CCHHCCCCCCCCCCC
25.6725159151
833PhosphorylationPPLQGEISQTQENSK
CCCCCCCCCCHHHHH
23.9120873877
835PhosphorylationLQGEISQTQENSKLN
CCCCCCCCHHHHHHC
30.9320873877
839PhosphorylationISQTQENSKLNAEVQ
CCCCHHHHHHCHHHC
37.4526552605

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
-KUbiquitinationE3 ubiquitin ligaseKCTD10Q9H3F6
PMID:30404837

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CEP97_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 CEP97_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CP110_HUMANCCP110physical
17719545
CP110_HUMANCCP110physical
22261722
ARPC2_HUMANARPC2physical
22261722
SNP23_HUMANSNAP23physical
22261722
LYN_HUMANLYNphysical
22261722
ARP3_HUMANACTR3physical
22261722
CAND1_HUMANCAND1physical
22261722
SGT1_HUMANSUGT1physical
22261722
GBB4_HUMANGNB4physical
22261722
NEUL4_HUMANNEURL4physical
22261722
CP110_HUMANCCP110physical
23486064
NEUL4_HUMANNEURL4physical
23486064
ALMS1_HUMANALMS1physical
26638075
CP110_HUMANCCP110physical
26638075
CE104_HUMANCEP104physical
26638075
CLH1_HUMANCLTCphysical
26638075
HAUS8_HUMANHAUS8physical
26638075
MPP9_HUMANMPHOSPH9physical
26638075
NAA15_HUMANNAA15physical
26638075
NEDD1_HUMANNEDD1physical
26638075
RAB2A_HUMANRAB2Aphysical
26638075
RAB35_HUMANRAB35physical
26638075
RAB5B_HUMANRAB5Bphysical
26638075
RAB8A_HUMANRAB8Aphysical
26638075
SMG7_HUMANSMG7physical
26638075
SGT1_HUMANSUGT1physical
26638075
SP16H_HUMANSUPT16Hphysical
26638075
TNIP1_HUMANTNIP1physical
26638075
TNR6B_HUMANTNRC6Bphysical
26638075
ASPP2_HUMANTP53BP2physical
26638075
WDR83_HUMANWDR83physical
26638075
XRN1_HUMANXRN1physical
26638075
YTHD1_HUMANYTHDF1physical
26638075
CENPJ_HUMANCENPJphysical
26638075
ACTBL_HUMANACTBL2physical
27173435
SORL_HUMANSORL1physical
27173435
CP110_HUMANCCP110physical
27173435
CFA91_HUMANMAATS1physical
27173435
IQCB1_HUMANIQCB1physical
27173435
U119A_HUMANUNC119physical
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 CEP97_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 SER-308, 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-763; SER-770; THR-811;SER-813 AND SER-817, 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 THR-542, AND MASSSPECTROMETRY.

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