CP131_MOUSE - dbPTM
CP131_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CP131_MOUSE
UniProt AC Q62036
Protein Name Centrosomal protein of 131 kDa
Gene Name Cep131
Organism Mus musculus (Mouse).
Sequence Length 1060
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite . Cytoplasm, cytoskeleton, cilium basal body . Cytoplasmic vesicle, secretory vesicle, acrosome .
Protein Description Component of centriolar satellites contributing to the building of a complex and dynamic network required to regulate cilia/flagellum formation. In proliferating cells, MIB1-mediated ubiquitination induces its sequestration within centriolar satellites, precluding untimely cilia formation initiation. In contrast, during normal and ultraviolet or heat shock cellular stress-induced ciliogenesis, its non-ubiquitinated form is rapidly displaced from centriolar satellites and recruited to centrosome/basal bodies in a microtubule- and p38 MAPK-dependent manner. Acts also as a negative regulator of BBSome ciliary trafficking (By similarity). Plays a role in sperm flagellar formation; may be involved in the regulation of intraflagellar transport (IFT) and/or intramanchette (IMT) trafficking, which are important for axoneme extension and/or cargo delivery to the nascent sperm tail. [PubMed: 24415959 Required for optimal cell proliferation and cell cycle progression; may play a role in the regulation of genome stability and centriole duplication in non-ciliogenic cells (By similarity Involved in centriole duplication]
Protein Sequence MKGSRTITATPEGSPEAVDLSLIGLPPPMSQRPGSASATRSIFRSMSVATGSEPRKKALEATGPGGPRAINNLRRSNSTTQVNQSWTGSPRPAEPTDFLMLFEGSTSGRRRVASLSKASSEKEATWNVLDEQPRGLALPASAQSPSTLDSALGPRRKECPLAPSFTANNRSNKGAVGNCVTTMVHNHYASSKMVSPPKSSNQTAPSLNNIVKAAAREGGEGSDLGKPRKNLSSASQSARGTTGLLRRREVTEEEAERFIHQVNQAAVTIQRWYRCQVQRRRAGAAALEHLLASKREGQRQRLGGGNLLELHRQEEAARKKAREEKARQARQAAIQVLQQKRAQKASEAEHRRPKDRPETRAPEQPRPMQEPGCVTHPKANNAGASIYPTGPADPCPPASESSPEQWQSPEDKPQDIHSQGEARQDLAVSGSSRGKARARATLDDLLDTLKLLEEEPEPLPHPKAYHKDRYAWTDEEEDANSLTADNLEKFGKLSAAPGPPDDGTLLSEAKLQSIMTFLDEMEKSGQERPAPWRESLVLEAGSGSEGSTSVMRLKLELEEKKQAMALLQRALAQQRDLTVRRVKETEKELTRQLRQQKEQYEATIQRHLSFIDQLIEDKKVLSEKCEAVVAELKHGDQRCRERVAQMQEQHELEIKKLKELMSATEKIRREKWINEKTKKIKEITVRGLEPEIQKLIAKHKQEVRRLRGLHEAELQQREEQAAQRHLRQAEELRQHLDREREVLGQQERERAQQRFEQHLEQEQRALEQQRRRLYNEVAEEKERLGQQAARQRAELEELRQQLEESSAALTRALRAEFERSREEQERRHQMELKALKDQLEAERQAWVASCAKKEEAWLLTRERELKEEIRKGRDQEIELVIHRLEADMTLAKEESERAAESRVKRVRDKYETELSELEQSERKLQERCSELKGRLGEAEGEKERLQSLVRQKEKELEDLRAVNTQMCSERASLAQVVRQEFAEQLAASQEETQRVKVELAELQARQQVELDEVHRRVKTALARKEAAVNSLRKQHEAAVKRADHLEELLEQHKGSSLSSK
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
6Phosphorylation--MKGSRTITATPEG
--CCCCCEEEECCCC
25619855
8PhosphorylationMKGSRTITATPEGSP
CCCCCEEEECCCCCH
25619855
10PhosphorylationGSRTITATPEGSPEA
CCCEEEECCCCCHHH
25619855
14PhosphorylationITATPEGSPEAVDLS
EEECCCCCHHHEEHH
25619855
21PhosphorylationSPEAVDLSLIGLPPP
CHHHEEHHHHCCCCC
25619855
30PhosphorylationIGLPPPMSQRPGSAS
HCCCCCCCCCCCCHH
25619855
35PhosphorylationPMSQRPGSASATRSI
CCCCCCCCHHHHHHH
25619855
37PhosphorylationSQRPGSASATRSIFR
CCCCCCHHHHHHHHH
25619855
39PhosphorylationRPGSASATRSIFRSM
CCCCHHHHHHHHHHH
25619855
45PhosphorylationATRSIFRSMSVATGS
HHHHHHHHHCCCCCC
24759943
47PhosphorylationRSIFRSMSVATGSEP
HHHHHHHCCCCCCCH
25521595
76PhosphorylationAINNLRRSNSTTQVN
HHHHHHHCCCCCCCC
23429704
78PhosphorylationNNLRRSNSTTQVNQS
HHHHHCCCCCCCCCC
23684622
79PhosphorylationNLRRSNSTTQVNQSW
HHHHCCCCCCCCCCC
23429704
80PhosphorylationLRRSNSTTQVNQSWT
HHHCCCCCCCCCCCC
26643407
85PhosphorylationSTTQVNQSWTGSPRP
CCCCCCCCCCCCCCC
23984901
87PhosphorylationTQVNQSWTGSPRPAE
CCCCCCCCCCCCCCC
23984901
89PhosphorylationVNQSWTGSPRPAEPT
CCCCCCCCCCCCCCC
23984901
96PhosphorylationSPRPAEPTDFLMLFE
CCCCCCCCCEEEEEE
26643407
105PhosphorylationFLMLFEGSTSGRRRV
EEEEEECCCCCHHHH
-
114PhosphorylationSGRRRVASLSKASSE
CCHHHHHHHHHCCCC
28066266
116PhosphorylationRRRVASLSKASSEKE
HHHHHHHHHCCCCCC
28066266
119PhosphorylationVASLSKASSEKEATW
HHHHHHCCCCCCCCC
28066266
120PhosphorylationASLSKASSEKEATWN
HHHHHCCCCCCCCCC
28066266
122UbiquitinationLSKASSEKEATWNVL
HHHCCCCCCCCCCCC
-
141PhosphorylationRGLALPASAQSPSTL
CCCCCCCCCCCCHHH
24068923
144PhosphorylationALPASAQSPSTLDSA
CCCCCCCCCHHHHHH
26824392
146PhosphorylationPASAQSPSTLDSALG
CCCCCCCHHHHHHCC
24068923
147PhosphorylationASAQSPSTLDSALGP
CCCCCCHHHHHHCCC
24068923
150PhosphorylationQSPSTLDSALGPRRK
CCCHHHHHHCCCCCC
24068923
164PhosphorylationKECPLAPSFTANNRS
CCCCCCCCCCCCCCC
29514104
188PhosphorylationTTMVHNHYASSKMVS
HHHHHHCCCCCCCCC
25367039
190PhosphorylationMVHNHYASSKMVSPP
HHHHCCCCCCCCCCC
25367039
191PhosphorylationVHNHYASSKMVSPPK
HHHCCCCCCCCCCCC
25367039
195PhosphorylationYASSKMVSPPKSSNQ
CCCCCCCCCCCCCCC
24453211
199PhosphorylationKMVSPPKSSNQTAPS
CCCCCCCCCCCCCCC
25293948
200PhosphorylationMVSPPKSSNQTAPSL
CCCCCCCCCCCCCCH
25293948
203PhosphorylationPPKSSNQTAPSLNNI
CCCCCCCCCCCHHHH
25293948
206PhosphorylationSSNQTAPSLNNIVKA
CCCCCCCCHHHHHHH
27841257
222PhosphorylationAREGGEGSDLGKPRK
HHHCCCCCCCCCCCC
28066266
229UbiquitinationSDLGKPRKNLSSASQ
CCCCCCCCCHHHHHH
-
232PhosphorylationGKPRKNLSSASQSAR
CCCCCCHHHHHHHHH
29514104
235PhosphorylationRKNLSSASQSARGTT
CCCHHHHHHHHHCCC
29514104
251PhosphorylationLLRRREVTEEEAERF
HHHHCCCCHHHHHHH
24719451
294UbiquitinationLEHLLASKREGQRQR
HHHHHHCCCCCCCCC
-
385PhosphorylationKANNAGASIYPTGPA
CCCCCCCCCCCCCCC
25293948
387PhosphorylationNNAGASIYPTGPADP
CCCCCCCCCCCCCCC
25293948
389PhosphorylationAGASIYPTGPADPCP
CCCCCCCCCCCCCCC
25293948
399PhosphorylationADPCPPASESSPEQW
CCCCCCCCCCCHHHH
25293948
401PhosphorylationPCPPASESSPEQWQS
CCCCCCCCCHHHHCC
25293948
402PhosphorylationCPPASESSPEQWQSP
CCCCCCCCHHHHCCC
25293948
408PhosphorylationSSPEQWQSPEDKPQD
CCHHHHCCCCCCCCC
25293948
418PhosphorylationDKPQDIHSQGEARQD
CCCCCCCCCCCHHHH
25293948
431PhosphorylationQDLAVSGSSRGKARA
HHHCCCCCHHHHHHH
22006019
441PhosphorylationGKARARATLDDLLDT
HHHHHHHHHHHHHHH
26643407
448PhosphorylationTLDDLLDTLKLLEEE
HHHHHHHHHHHHHCC
27149854
450UbiquitinationDDLLDTLKLLEEEPE
HHHHHHHHHHHCCCC
-
470PhosphorylationKAYHKDRYAWTDEEE
CCCCCCCCCCCCCHH
25619855
473PhosphorylationHKDRYAWTDEEEDAN
CCCCCCCCCCHHHHH
27087446
481PhosphorylationDEEEDANSLTADNLE
CCHHHHHCCCHHHHH
27087446
483PhosphorylationEEDANSLTADNLEKF
HHHHHCCCHHHHHHH
25619855
492UbiquitinationDNLEKFGKLSAAPGP
HHHHHHCCCCCCCCC
-
494PhosphorylationLEKFGKLSAAPGPPD
HHHHCCCCCCCCCCC
29514104
542PhosphorylationSLVLEAGSGSEGSTS
EEEEECCCCCCCCHH
30635358
544PhosphorylationVLEAGSGSEGSTSVM
EEECCCCCCCCHHHH
30635358
547PhosphorylationAGSGSEGSTSVMRLK
CCCCCCCCHHHHHHE
30635358
548PhosphorylationGSGSEGSTSVMRLKL
CCCCCCCHHHHHHEE
30635358
549PhosphorylationSGSEGSTSVMRLKLE
CCCCCCHHHHHHEEH
30635358
600PhosphorylationLRQQKEQYEATIQRH
HHHHHHHHHHHHHHH
22817900
1033MethylationAAVNSLRKQHEAAVK
HHHHHHHHHHHHHHH
-
1056PhosphorylationLEQHKGSSLSSK---
HHHCCCCCCCCC---
29514104
1058PhosphorylationQHKGSSLSSK-----
HCCCCCCCCC-----
29514104
1059PhosphorylationHKGSSLSSK------
CCCCCCCCC------
29514104

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 CP131_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
47SPhosphorylation

21183079
78SPhosphorylation

-
78SPhosphorylation

-

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 CP131_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CP131_HUMANCEP131physical
20360068
IPO5_HUMANIPO5physical
20360068
MIB1_HUMANMIB1physical
20360068
PCM1_HUMANPCM1physical
20360068
ATP5J_HUMANATP5Jphysical
26496610
BBS4_HUMANBBS4physical
26496610
PCM1_HUMANPCM1physical
26496610
MP2K1_HUMANMAP2K1physical
26496610
OFD1_HUMANOFD1physical
26496610
ARK72_HUMANAKR7A2physical
26496610
DPM1_HUMANDPM1physical
26496610
MOONR_HUMANKIAA0753physical
26496610
CE350_HUMANCEP350physical
26496610
HMGX4_HUMANHMGXB4physical
26496610
PIBF1_HUMANPIBF1physical
26496610
FR1OP_HUMANFGFR1OPphysical
26496610
RFIP2_HUMANRAB11FIP2physical
26496610
TTLL5_HUMANTTLL5physical
26496610
RT27_HUMANMRPS27physical
26496610
WBP2_HUMANWBP2physical
26496610
C2CD3_HUMANC2CD3physical
26496610
RM18_HUMANMRPL18physical
26496610
S18L2_HUMANSS18L2physical
26496610
NIN_HUMANNINphysical
26496610
HEAT3_HUMANHEATR3physical
26496610
CEP72_HUMANCEP72physical
26496610
MIB1_HUMANMIB1physical
26496610
K1328_HUMANKIAA1328physical
26496610
E41L5_HUMANEPB41L5physical
26496610
RBM25_HUMANRBM25physical
26496610
TFB2M_HUMANTFB2Mphysical
26496610
RM11_HUMANMRPL11physical
26496610
CSPP1_HUMANCSPP1physical
26496610
FXRD2_HUMANFOXRED2physical
26496610
YIPF5_HUMANYIPF5physical
26496610
CCD77_HUMANCCDC77physical
26496610
AT2L2_HUMANPHYKPLphysical
26496610
CE295_HUMANCEP295physical
26496610
TBC31_HUMANTBC1D31physical
26496610
ADIP_HUMANSSX2IPphysical
26496610
FOPNL_HUMANFOPNLphysical
26496610
CC138_HUMANCCDC138physical
26496610
WDR90_HUMANWDR90physical
26496610
CCD18_HUMANCCDC18physical
26496610
CCD61_HUMANCCDC61physical
26496610

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CP131_MOUSE

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Related Literatures of Post-Translational Modification

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