CP110_MOUSE - dbPTM
CP110_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CP110_MOUSE
UniProt AC Q7TSH4
Protein Name Centriolar coiled-coil protein of 110 kDa
Gene Name Ccp110
Organism Mus musculus (Mouse).
Sequence Length 1004
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, cilium basal body . Recruited early and then associates with the growing dis
Protein Description Necessary for centrosome duplication at different stages of procentriole formation. Acts as a key negative regulator of ciliogenesis in collaboration with CEP97 by capping the mother centriole thereby preventing cilia formation. [PubMed: 23141541 Also involved in promoting ciliogenesis. May play a role in the assembly of the mother centriole subdistal appendages (SDA) thereby effecting the fusion of recycling endosomes to basal bodies during cilia formation]
Protein Sequence MEEYEEFCEKALGRAQEASLSTGSFLPAQAESVSLIRFHGVAVLSPLLTIEKRKKIQEEKQKALDVQSRKQANRKKALLTRVQEILENVQVRKAPNASDFDQWATETIYSNPEVTDLNVPVRVPNSLPSPTEHCTSVKLEKITGLLPVNNEDQQTPKRVGLPGDSEVSGSLRQCESPESRQAEDGAALRLSSASPQETIISDVLGKEEQDPSCLAEVTPDPYIMSLQNLMKRSKEYVERELSSRSLRNSLKRSVNETHSDRENDAAKASDCVKEKAPPMPIGRHCGSAIPDKPSLNKSNVLLQGASQASSMGTAGLASFSKIDLPAGAAPPAAPDAGSDFTVIPTFVTENKVKSLKGPYAKLPSPEPSMSPTMHRRHSRSASACQILINNPVNACELSPKGKEEAVDRTAPAAAETTNESETVPKSPTDLTGVCSSNVSATKITSESTREMVVGKPSQRQQALGAHLGNNVTVERSAMEGPFIADDRGAQKVDGTCMAVPKLHELQPSSQCVSSQTLEDVCELKSASLLAKNSCNLQMELNKSYDVKHPSPLLTQTQTSRQQMDTPPVFRGNEQFVDNSFEKVKRRLDLDVDSLQKENCPYIITAGVAEQERDRLLERRYPKGFVHINKNKMLETSPKEGQELLKSKMLAFEEMRKRLEEQHAQQLSLLIAEQEREQEQLQKEIEEQEKMLKEKAVTTDVSDLNSALEWRQRTDSALLETMLSQVDSLQTSNNSGFITSALQYSFGSAGEAPFYLWGSLTSGVTRVSGTRPCGRAQAKWSQVFNPEIHAKFNKITAVAKGFLTRKLMQTDKLKQLRQTVKDTMEFIRSFQSEAPLKRGVVSAQDASLQERVLAQLRAALYGIHDIFFVMDAAERMSILHHDREARKEKLLRQMDKMKSPRVALSVATQKSLDRKKFMKVAEMGMPNKKFLLKQNPSETRVLQPNQGQNAPVHRLLSRQGTPKTSVKGVVQNRQKPSQSRVPNRAPVSGAYAGKTQRKRPNVATI
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
49PhosphorylationAVLSPLLTIEKRKKI
EEEHHHHHHHHHHHH
34.47-
126PhosphorylationVPVRVPNSLPSPTEH
CCEECCCCCCCCCCC
35.2728066266
129PhosphorylationRVPNSLPSPTEHCTS
ECCCCCCCCCCCCCC
50.1528066266
131PhosphorylationPNSLPSPTEHCTSVK
CCCCCCCCCCCCCCE
42.5728066266
135PhosphorylationPSPTEHCTSVKLEKI
CCCCCCCCCCEEEEE
38.1628066266
136PhosphorylationSPTEHCTSVKLEKIT
CCCCCCCCCEEEEEC
23.7328066266
155PhosphorylationVNNEDQQTPKRVGLP
CCCCCCCCCCCCCCC
25.7428066266
170PhosphorylationGDSEVSGSLRQCESP
CCCCCCCCCEECCCC
16.93-
176PhosphorylationGSLRQCESPESRQAE
CCCEECCCCCHHHCC
41.4129514104
191PhosphorylationDGAALRLSSASPQET
CCCCHHCCCCCCCCC
19.8821743459
192PhosphorylationGAALRLSSASPQETI
CCCHHCCCCCCCCCH
37.0427180971
194PhosphorylationALRLSSASPQETIIS
CHHCCCCCCCCCHHH
29.1222817900
198PhosphorylationSSASPQETIISDVLG
CCCCCCCCHHHHHCC
20.5429472430
201PhosphorylationSPQETIISDVLGKEE
CCCCCHHHHHCCCCC
20.1629472430
242PhosphorylationEYVERELSSRSLRNS
HHHHHHHHHHHHHHH
20.9622802335
249PhosphorylationSSRSLRNSLKRSVNE
HHHHHHHHHHHHHHH
28.9125338131
364PhosphorylationGPYAKLPSPEPSMSP
CCCCCCCCCCCCCCC
52.9422817900
368PhosphorylationKLPSPEPSMSPTMHR
CCCCCCCCCCCCCCH
30.1722817900
370PhosphorylationPSPEPSMSPTMHRRH
CCCCCCCCCCCCHHH
22.8926745281
372PhosphorylationPEPSMSPTMHRRHSR
CCCCCCCCCCHHHCC
20.5026745281
380PhosphorylationMHRRHSRSASACQIL
CCHHHCCCCCHHHHH
29.5925619855
382PhosphorylationRRHSRSASACQILIN
HHHCCCCCHHHHHHC
30.7225619855
398PhosphorylationPVNACELSPKGKEEA
CCCCCCCCCCCCHHH
11.4121082442
409PhosphorylationKEEAVDRTAPAAAET
CHHHCCCCCCCHHHC
32.3125619855
416PhosphorylationTAPAAAETTNESETV
CCCCHHHCCCCCCCC
30.1425619855
417PhosphorylationAPAAAETTNESETVP
CCCHHHCCCCCCCCC
28.6125619855
420PhosphorylationAAETTNESETVPKSP
HHHCCCCCCCCCCCC
40.4125619855
422PhosphorylationETTNESETVPKSPTD
HCCCCCCCCCCCCCC
51.9225619855
426PhosphorylationESETVPKSPTDLTGV
CCCCCCCCCCCCCCC
27.2825619855
428PhosphorylationETVPKSPTDLTGVCS
CCCCCCCCCCCCCCC
51.2125619855
431PhosphorylationPKSPTDLTGVCSSNV
CCCCCCCCCCCCCCC
30.3125619855
435PhosphorylationTDLTGVCSSNVSATK
CCCCCCCCCCCCCCE
23.6525619855
436PhosphorylationDLTGVCSSNVSATKI
CCCCCCCCCCCCCEE
35.8025619855
439PhosphorylationGVCSSNVSATKITSE
CCCCCCCCCCEECCC
34.1825619855
441PhosphorylationCSSNVSATKITSEST
CCCCCCCCEECCCHH
18.5725619855
550PhosphorylationSYDVKHPSPLLTQTQ
CCCCCCCCCCCCCCC
28.09-
579PhosphorylationNEQFVDNSFEKVKRR
CHHHCCCCHHHHHHH
30.2528066266
620PhosphorylationDRLLERRYPKGFVHI
HHHHHHHCCCCEEEE
18.6022817900
907PhosphorylationRVALSVATQKSLDRK
HHHHHHHCCCCCCHH
34.08-
914AcetylationTQKSLDRKKFMKVAE
CCCCCCHHHHHHHHH
50.457613267
915AcetylationQKSLDRKKFMKVAEM
CCCCCHHHHHHHHHC
52.147613277
1003PhosphorylationRKRPNVATI------
CCCCCCCCC------
23.96-

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 CP110_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CP110_MOUSE !!

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 CP110_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KI67_HUMANMKI67physical
26496610
PCM1_HUMANPCM1physical
26496610
OFD1_HUMANOFD1physical
26496610
MOONR_HUMANKIAA0753physical
26496610
CP131_HUMANCEP131physical
26496610
CEP72_HUMANCEP72physical
26496610
CEP97_HUMANCEP97physical
26496610

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CP110_MOUSE

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Related Literatures of Post-Translational Modification

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