CEP78_HUMAN - dbPTM
CEP78_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CEP78_HUMAN
UniProt AC Q5JTW2
Protein Name Centrosomal protein of 78 kDa
Gene Name CEP78
Organism Homo sapiens (Human).
Sequence Length 689
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole . Cytoplasm, cytoskeleton, cilium basal body . Mainly localizes at the centriolar wall, but also found
Protein Description May be required for efficient PLK4 centrosomal localization and PLK4-induced overduplication of centrioles. [PubMed: 27246242 May play a role in cilium biogenesis]
Protein Sequence MIDSVKLRRDSAADFFSHYEYLCALQNSVPLPAVRACLREGVLDFNADRLRGVDWAPLLSTLKINKDLPLVSIKSFFQPWLGDTGSDMNKFCRSRVPAIRYKDVTFQLCKALKGCLSISSVLKNLELNGLILRERDLTILAKGLNKSASLVHLSLANCPIGDGGLEIICQGIKSSITLKTVNFTGCNLTWQGADHMAKILKYQTMRRHEETWAESLRYRRPDLDCMAGLRRITLNCNTLIGDLGACAFADSLSEDLWLRALDLQQCGLTNEGAKALLEALETNTTLVVLDIRKNPLIDHSMMKAVIKKVLQNGRSAKSEYQWITSPSVKEPSKTAKQKRRTIILGSGHKGKATIRIGLATKKPVSSGRKHSLGKEYYAPAPLPPGVSGFLPWRTAERAKRHRGFPLIKTRDICNQLQQPGFPVTVTVESPSSSEVEEVDDSSESVHEVPEKTSIEQEALQEKLEECLKQLKEERVIRLKVDKRVSELEHENAQLRNINFSLSEALHAQSLTNMILDDEGVLGSIENSFQKFHAFLDLLKDAGLGQLATMAGIDQSDFQLLGHPQMTSTVSNPPKEEKKALEDEKPEPKQNALGQMQNIQFQKITGDARIPLPLDSFPVPVSTPEGLGTSSNNLGVPATEQRQESFEGFIARMCSPSPDATSGTGSQRKEEELSRNSRSSSEKKTKTESH
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
6Ubiquitination--MIDSVKLRRDSAA
--CCCCCCCCCCCHH		39.98-
60PhosphorylationVDWAPLLSTLKINKD
CCCHHHHHHCCCCCC		39.1020860994
61PhosphorylationDWAPLLSTLKINKDL
CCHHHHHHCCCCCCC		31.8520860994
63UbiquitinationAPLLSTLKINKDLPL
HHHHHHCCCCCCCCE		44.30-
66UbiquitinationLSTLKINKDLPLVSI
HHHCCCCCCCCEEEH		65.20-
84PhosphorylationFQPWLGDTGSDMNKF
CCHHHCCCCCHHHHH		36.4728348404
86PhosphorylationPWLGDTGSDMNKFCR
HHHCCCCCHHHHHHH		35.4628348404
90UbiquitinationDTGSDMNKFCRSRVP
CCCCHHHHHHHCCCC		38.92-
102UbiquitinationRVPAIRYKDVTFQLC
CCCCCCHHHHHHHHH		35.55-
138PhosphorylationILRERDLTILAKGLN
EEEHHHHHHHHHCCC		20.45-
147PhosphorylationLAKGLNKSASLVHLS
HHHCCCCCCCHHEEE		23.24-
149PhosphorylationKGLNKSASLVHLSLA
HCCCCCCCHHEEECC		37.71-
174PhosphorylationIICQGIKSSITLKTV
EEECCCCCEEEEEEE		25.67-
175PhosphorylationICQGIKSSITLKTVN
EECCCCCEEEEEEEC		18.00-
198UbiquitinationQGADHMAKILKYQTM
CCHHHHHHHHHHHHH		40.78-
201UbiquitinationDHMAKILKYQTMRRH
HHHHHHHHHHHHHHC		38.49-
211PhosphorylationTMRRHEETWAESLRY
HHHHCHHHHHHHHHH		27.3020873877
215PhosphorylationHEETWAESLRYRRPD
CHHHHHHHHHHCCCC		15.4820873877
300PhosphorylationKNPLIDHSMMKAVIK
CCCCCCHHHHHHHHH		19.4729978859
303UbiquitinationLIDHSMMKAVIKKVL
CCCHHHHHHHHHHHH		30.75-
317 (in isoform 2)Ubiquitination-45.1021890473
317 (in isoform 1)Ubiquitination-45.1021890473
317UbiquitinationLQNGRSAKSEYQWIT
HHHCCCCCCCCEECC		45.1021890473
317 (in isoform 3)Ubiquitination-45.1021890473
318PhosphorylationQNGRSAKSEYQWITS
HHCCCCCCCCEECCC		41.0529396449
320PhosphorylationGRSAKSEYQWITSPS
CCCCCCCCEECCCCC		19.0828796482
324PhosphorylationKSEYQWITSPSVKEP
CCCCEECCCCCCCCC		31.4623663014
325PhosphorylationSEYQWITSPSVKEPS
CCCEECCCCCCCCCC		13.1725159151
327PhosphorylationYQWITSPSVKEPSKT
CEECCCCCCCCCCCC		45.6628176443
329UbiquitinationWITSPSVKEPSKTAK
ECCCCCCCCCCCCCC		69.14-
329 (in isoform 1)Ubiquitination-69.1421890473
329 (in isoform 3)Ubiquitination-69.1421890473
329 (in isoform 2)Ubiquitination-69.1421890473
332PhosphorylationSPSVKEPSKTAKQKR
CCCCCCCCCCCCCCC		43.6728450419
334PhosphorylationSVKEPSKTAKQKRRT
CCCCCCCCCCCCCCE		43.3423312004
336UbiquitinationKEPSKTAKQKRRTII
CCCCCCCCCCCCEEE		62.68-
341PhosphorylationTAKQKRRTIILGSGH
CCCCCCCEEEECCCC		19.1924173317
346PhosphorylationRRTIILGSGHKGKAT
CCEEEECCCCCCCEE		33.99-
349UbiquitinationIILGSGHKGKATIRI
EEECCCCCCCEEEEE		66.68-
351UbiquitinationLGSGHKGKATIRIGL
ECCCCCCCEEEEEEE		47.35-
361UbiquitinationIRIGLATKKPVSSGR
EEEEEECCCCCCCCC		49.85-
361AcetylationIRIGLATKKPVSSGR
EEEEEECCCCCCCCC		49.8525953088
361 (in isoform 2)Phosphorylation-49.85-
361 (in isoform 5)Phosphorylation-49.85-
371PhosphorylationVSSGRKHSLGKEYYA
CCCCCCCCCCCEEEE		41.6824719451
372PhosphorylationSSGRKHSLGKEYYAP
CCCCCCCCCCEEEEC		13.05-
374 (in isoform 1)Ubiquitination-48.0821890473
374 (in isoform 3)Ubiquitination-48.0821890473
374UbiquitinationGRKHSLGKEYYAPAP
CCCCCCCCEEEECCC		48.082189047
375UbiquitinationRKHSLGKEYYAPAPL
CCCCCCCEEEECCCC		41.81-
375 (in isoform 2)Ubiquitination-41.8121890473
376PhosphorylationKHSLGKEYYAPAPLP
CCCCCCEEEECCCCC		14.38-
377PhosphorylationHSLGKEYYAPAPLPP
CCCCCEEEECCCCCC		13.75-
408UbiquitinationHRGFPLIKTRDICNQ
HCCCCCEEHHHHHHH		45.23-
409UbiquitinationRGFPLIKTRDICNQL
CCCCCEEHHHHHHHC		26.95-
424PhosphorylationQQPGFPVTVTVESPS
CCCCCCEEEEEECCC		15.6523898821
431PhosphorylationTVTVESPSSSEVEEV
EEEEECCCCCCCEEC		56.6323898821
432PhosphorylationVTVESPSSSEVEEVD
EEEECCCCCCCEECC		33.6222468782
453PhosphorylationHEVPEKTSIEQEALQ
CCCCCCCCHHHHHHH		34.8825627689
463UbiquitinationQEALQEKLEECLKQL
HHHHHHHHHHHHHHH		7.06-
469UbiquitinationKLEECLKQLKEERVI
HHHHHHHHHHHHHHH		44.83-
485PhosphorylationLKVDKRVSELEHENA
HCCCHHHHHHHHHCH		40.2628450419
486PhosphorylationKVDKRVSELEHENAQ
CCCHHHHHHHHHCHH		56.15-
579UbiquitinationPPKEEKKALEDEKPE
CCHHHHHHHCCCCCC		27.53-
579 (in isoform 2)Ubiquitination-27.53-
585 (in isoform 2)Ubiquitination-62.16-
585UbiquitinationKALEDEKPEPKQNAL
HHHCCCCCCHHCCHH		62.16-
602UbiquitinationMQNIQFQKITGDARI
HHCEEEEECCCCCCC		43.45-
615O-linked_GlycosylationRIPLPLDSFPVPVST
CCCCCCCCCCCCCCC		38.8530620550
619 (in isoform 2)Ubiquitination-17.99-
621PhosphorylationDSFPVPVSTPEGLGT
CCCCCCCCCCCCCCC		31.9828348404
622O-linked_GlycosylationSFPVPVSTPEGLGTS
CCCCCCCCCCCCCCC		26.1230620550
622PhosphorylationSFPVPVSTPEGLGTS
CCCCCCCCCCCCCCC		26.1224173317
628PhosphorylationSTPEGLGTSSNNLGV
CCCCCCCCCCCCCCC		33.7428348404
629PhosphorylationTPEGLGTSSNNLGVP
CCCCCCCCCCCCCCC		29.3028348404
630O-linked_GlycosylationPEGLGTSSNNLGVPA
CCCCCCCCCCCCCCC		29.5830620550
630PhosphorylationPEGLGTSSNNLGVPA
CCCCCCCCCCCCCCC		29.5828348404
644PhosphorylationATEQRQESFEGFIAR
CHHHHHHHHHHHHHH		21.9125850435
652SulfoxidationFEGFIARMCSPSPDA
HHHHHHHHCCCCCCC		1.6421406390
654PhosphorylationGFIARMCSPSPDATS
HHHHHHCCCCCCCCC		21.0429255136
656PhosphorylationIARMCSPSPDATSGT
HHHHCCCCCCCCCCC		21.0829255136
660PhosphorylationCSPSPDATSGTGSQR
CCCCCCCCCCCCHHH		34.7629255136
661PhosphorylationSPSPDATSGTGSQRK
CCCCCCCCCCCHHHH		35.7629255136
663PhosphorylationSPDATSGTGSQRKEE
CCCCCCCCCHHHHHH		33.1729255136
665PhosphorylationDATSGTGSQRKEEEL
CCCCCCCHHHHHHHH		27.0129255136
671PhosphorylationGSQRKEEELSRNSRS
CHHHHHHHHHHCCCC		53.81-
673PhosphorylationQRKEEELSRNSRSSS
HHHHHHHHHCCCCCC		32.47-
682UbiquitinationNSRSSSEKKTKTESH
CCCCCCCCCCCCCCC		68.63-
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 CEP78_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CEP78_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 CEP78_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CEP76_HUMANCEP76physical
28242748
CP110_HUMANCCP110physical
28242748
DCAF1_HUMANVPRBPphysical
28242748
DDB1_HUMANDDB1physical
28242748
UBR5_HUMANUBR5physical
28242748
DYRK2_HUMANDYRK2physical
28242748
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 CEP78_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-325, AND MASSSPECTROMETRY.

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