CEP68_HUMAN - dbPTM
CEP68_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CEP68_HUMAN
UniProt AC Q76N32
Protein Name Centrosomal protein of 68 kDa
Gene Name CEP68
Organism Homo sapiens (Human).
Sequence Length 757
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Localizes to thin fibers protruding away from the proximal ends of the two centrioles. Dissociates from interphase centrosomes at the onset of mitosis.
Protein Description Involved in maintenance of centrosome cohesion, probably as part of a linker structure which prevents centrosome splitting. [PubMed: 18042621 Required for localization of CDK5RAP2 to the centrosome during interphase]
Protein Sequence MALGEEKAEAEASEDTKAQSYGRGSCRERELDIPGPMSGEQPPRLEAEGGLISPVWGAEGIPAPTCWIGTDPGGPSRAHQPQASDANREPVAERSEPALSGLPPATMGSGDLLLSGESQVEKTKLSSSEEFPQTLSLPRTTTICSGHDADTEDDPSLADLPQALDLSQQPHSSGLSCLSQWKSVLSPGSAAQPSSCSISASSTGSSLQGHQERAEPRGGSLAKVSSSLEPVVPQEPSSVVGLGPRPQWSPQPVFSGGDASGLGRRRLSFQAEYWACVLPDSLPPSPDRHSPLWNPNKEYEDLLDYTYPLRPGPQLPKHLDSRVPADPVLQDSGVDLDSFSVSPASTLKSPTNVSPNCPPAEATALPFSGPREPSLKQWPSRVPQKQGGMGLASWSQLASTPRAPGSRDARWERREPALRGAKDRLTIGKHLDMGSPQLRTRDRGWPSPRPEREKRTSQSARRPTCTESRWKSEEEVESDDEYLALPARLTQVSSLVSYLGSISTLVTLPTGDIKGQSPLEVSDSDGPASFPSSSSQSQLPPGAALQGSGDPEGQNPCFLRSFVRAHDSAGEGSLGSSQALGVSSGLLKTRPSLPARLDRWPFSDPDVEGQLPRKGGEQGKESLVQCVKTFCCQLEELICWLYNVADVTDHGTAARSNLTSLKSSLQLYRQFKKDIDEHQSLTESVLQKGEILLQCLLENTPVLEDVLGRIAKQSGELESHADRLYDSILASLDMLAGCTLIPDKKPMAAMEHPCEGV
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
25PhosphorylationAQSYGRGSCRERELD
HHHCCCCCCCCEECC		14.5122210691
53PhosphorylationEAEGGLISPVWGAEG
EECCCEECCCCCCCC		20.6027251275
76PhosphorylationGTDPGGPSRAHQPQA
ECCCCCCCCCCCCCC		45.43-
84PhosphorylationRAHQPQASDANREPV
CCCCCCCCCCCCCCC		31.82-
106PhosphorylationLSGLPPATMGSGDLL
HCCCCCCCCCCCCEE		28.04-
123PhosphorylationGESQVEKTKLSSSEE
CCCHHHEECCCCCCC		24.5828857561
126PhosphorylationQVEKTKLSSSEEFPQ
HHHEECCCCCCCCCC		33.1225850435
127PhosphorylationVEKTKLSSSEEFPQT
HHEECCCCCCCCCCH		52.8125850435
128PhosphorylationEKTKLSSSEEFPQTL
HEECCCCCCCCCCHH		37.4625850435
134PhosphorylationSSEEFPQTLSLPRTT
CCCCCCCHHCCCCCE		20.6728348404
136PhosphorylationEEFPQTLSLPRTTTI
CCCCCHHCCCCCEEE		39.4525850435
226PhosphorylationGSLAKVSSSLEPVVP
CCCCHHCCCCCCCCC		41.7626657352
227PhosphorylationSLAKVSSSLEPVVPQ
CCCHHCCCCCCCCCC		29.2826657352
237PhosphorylationPVVPQEPSSVVGLGP
CCCCCCCCCCCCCCC		34.7027251275
238PhosphorylationVVPQEPSSVVGLGPR
CCCCCCCCCCCCCCC		31.3828450419
249PhosphorylationLGPRPQWSPQPVFSG
CCCCCCCCCCCCCCC		14.3828450419
255PhosphorylationWSPQPVFSGGDASGL
CCCCCCCCCCCCCCC		41.9427251275
260PhosphorylationVFSGGDASGLGRRRL
CCCCCCCCCCCCCCC		39.0127251275
268PhosphorylationGLGRRRLSFQAEYWA
CCCCCCCEEEEEEEE		17.3228348404
299PhosphorylationLWNPNKEYEDLLDYT
CCCCCCCHHHHHHCC		19.1627642862
305PhosphorylationEYEDLLDYTYPLRPG
CHHHHHHCCCCCCCC		14.2427642862
317 (in isoform 2)Ubiquitination-66.4521890473
317UbiquitinationRPGPQLPKHLDSRVP
CCCCCCCCCCCCCCC		66.4523000965
317 (in isoform 1)Ubiquitination-66.4521890473
332PhosphorylationADPVLQDSGVDLDSF
CCHHHCCCCCCCCCC		27.9625503564
338PhosphorylationDSGVDLDSFSVSPAS
CCCCCCCCCCCCCCH		27.0727732954
340PhosphorylationGVDLDSFSVSPASTL
CCCCCCCCCCCCHHC		26.1527732954
342PhosphorylationDLDSFSVSPASTLKS
CCCCCCCCCCHHCCC		17.3527732954
345PhosphorylationSFSVSPASTLKSPTN
CCCCCCCHHCCCCCC		37.3427732954
346PhosphorylationFSVSPASTLKSPTNV
CCCCCCHHCCCCCCC		40.0727732954
349PhosphorylationSPASTLKSPTNVSPN
CCCHHCCCCCCCCCC		39.8225159151
351PhosphorylationASTLKSPTNVSPNCP
CHHCCCCCCCCCCCC		56.1725159151
354PhosphorylationLKSPTNVSPNCPPAE
CCCCCCCCCCCCHHH		16.6826074081
363PhosphorylationNCPPAEATALPFSGP
CCCHHHCCCCCCCCC		21.8926074081
368PhosphorylationEATALPFSGPREPSL
HCCCCCCCCCCCCCH		46.0426074081
374PhosphorylationFSGPREPSLKQWPSR
CCCCCCCCHHHCCCC		43.3725159151
376UbiquitinationGPREPSLKQWPSRVP
CCCCCCHHHCCCCCC		55.4429967540
385UbiquitinationWPSRVPQKQGGMGLA
CCCCCCHHHCCCCCC		44.85-
393PhosphorylationQGGMGLASWSQLAST
HCCCCCCCHHHHHCC		32.1022210691
395PhosphorylationGMGLASWSQLASTPR
CCCCCCHHHHHCCCC		16.9022210691
400PhosphorylationSWSQLASTPRAPGSR
CHHHHHCCCCCCCCC		15.9324825855
419MethylationERREPALRGAKDRLT
HHCCHHHCCCHHCCC		45.16-
429AcetylationKDRLTIGKHLDMGSP
HHCCCHHCCCCCCCC		36.8225953088
435PhosphorylationGKHLDMGSPQLRTRD
HCCCCCCCCCCCCCC		11.6625159151
447PhosphorylationTRDRGWPSPRPEREK
CCCCCCCCCCHHHHH		27.3430266825
457PhosphorylationPEREKRTSQSARRPT
HHHHHCCCCCCCCCC		26.60-
464PhosphorylationSQSARRPTCTESRWK
CCCCCCCCCCHHHCC		30.19-
472PhosphorylationCTESRWKSEEEVESD
CCHHHCCCHHHCCCC		43.1930266825
478 (in isoform 2)Phosphorylation-56.3825849741
478PhosphorylationKSEEEVESDDEYLAL
CCHHHCCCCHHHHHH		56.3830266825
482PhosphorylationEVESDDEYLALPARL
HCCCCHHHHHHHHHH		12.3123927012
493PhosphorylationPARLTQVSSLVSYLG
HHHHHHHHHHHHHHH		14.24-
536UbiquitinationSFPSSSSQSQLPPGA
CCCCCCCCCCCCCCC		36.8329967540
568PhosphorylationSFVRAHDSAGEGSLG
HHHHHCCCCCCCCCC		28.4528857561
573PhosphorylationHDSAGEGSLGSSQAL
CCCCCCCCCCHHHHH		25.8428857561
576PhosphorylationAGEGSLGSSQALGVS
CCCCCCCHHHHHCCC		25.2728857561
577PhosphorylationGEGSLGSSQALGVSS
CCCCCCHHHHHCCCC		20.0628857561
583PhosphorylationSSQALGVSSGLLKTR
HHHHHCCCCCCCCCC		19.5223312004
589PhosphorylationVSSGLLKTRPSLPAR
CCCCCCCCCCCCCCC		48.0223532336
592PhosphorylationGLLKTRPSLPARLDR
CCCCCCCCCCCCCCC		43.6328857561
603PhosphorylationRLDRWPFSDPDVEGQ
CCCCCCCCCCCCCCC		44.1227732954
614UbiquitinationVEGQLPRKGGEQGKE
CCCCCCCCCCHHHHH		70.13-
620UbiquitinationRKGGEQGKESLVQCV
CCCCHHHHHHHHHHH		43.7729967540
663PhosphorylationSNLTSLKSSLQLYRQ
HCHHHHHHHHHHHHH		41.3927251275
673UbiquitinationQLYRQFKKDIDEHQS
HHHHHHHHCHHHHHH		62.2929967540
673AcetylationQLYRQFKKDIDEHQS
HHHHHHHHCHHHHHH		62.2920167786
712UbiquitinationDVLGRIAKQSGELES
HHHHHHHHHHCCHHH		42.50-
719PhosphorylationKQSGELESHADRLYD
HHHCCHHHHHHHHHH		36.2822210691
731PhosphorylationLYDSILASLDMLAGC
HHHHHHHHHHHHCCC		22.8122210691
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
332SPhosphorylationKinasePLK1P53350
Uniprot
-KUbiquitinationE3 ubiquitin ligaseFBXW11Q9UKB1
PMID:24658274
-KUbiquitinationE3 ubiquitin ligaseBTRCQ9Y297
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CEP68_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 CEP68_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
USBP1_HUMANUSHBP1physical
25416956
FBW1A_HUMANBTRCphysical
25503564
CK5P2_HUMANCDK5RAP2physical
25503564
PCNT_HUMANPCNTphysical
25503564
VHL_HUMANVHLphysical
28089774
MCM7_HUMANMCM7physical
28578000
VHL_HUMANVHLphysical
28578000
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 CEP68_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-478, AND MASSSPECTROMETRY.

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