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Protein Page:
CP110 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
CP110 Necessary for centrosome duplication at different stages of procentriole formation. Collaborates with CEP97, being involved in the suppression of a cilia assembly program. Required for correct spindle formation and has a role in regulating cytokinesis and genome stability via cooperation with CALM1 and CETN2. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Cell cycle regulation
Cellular Component: centriole; centrosome; protein complex; cytosol
Molecular Function: protein binding
Biological Process: cell projection organization and biogenesis; centriole replication; mitotic cell cycle; G2/M transition of mitotic cell cycle; centrosome duplication; regulation of cytokinesis
Reference #:  O43303 (UniProtKB)
Alt. Names/Synonyms: 9738; CE110; Centrosomal protein of 110 kDa; CEP110; CP110; CP110 protein; DKFZp781G1416; KIAA0419
Gene Symbols: CCP110
Molecular weight: 113,424 Da
Basal Isoelectric point: 8.83  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

CP110

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 N49 AILSPLLNIEKRKEM
0 1 T107-p FDQWEMEtVySNSEV
0 91 Y109-p QWEMEtVySNSEVRN
0 1 S165-p GIDLARDsEGFNsPK
0 3 S170-p RDsEGFNsPKQCDSS
0 1 T194 FPKTSSATPQETLIS
0 1 S244 EYIEREQSRRsLRGs
0 14 S247-p EREQSRRsLRGsINR
0 2 S251-p SRRsLRGsINRIVNE
0 1 S259-p INRIVNEsHLDKEHD
0 8 S366-p GSYAKLPsPEPsMsP
0 4 S370-p KLPsPEPsMsPKMHR
0 7 S372-p PsPEPsMsPKMHRRR
0 1 S380-p PKMHRRRsRtssACH
0 8 T382-p MHRRRsRtssACHIL
0 2 S383-p HRRRsRtssACHILI
0 7 S384-p RRRsRtssACHILIN
0 27 S400-p PINACELsPKGKEQA
0 1 Y441-p GVCSSKVyVGKNTSE
0 3 Y508-p MPKLHEPyASSQCIA
0 1 S516-p ASSQCIAsPNFGTVS
0 3 S551-p SYDVKNPsPLLMQNQ
0 4 Y602-p LQKENCPyVITSGIT
0 1 Y621 QHLPEKRYPKGsGFV
0 1 S625-p EKRYPKGsGFVNkNK
0 1 K630-ub KGsGFVNkNKMLGTS
0 1 K639-ub KMLGTSSkEsEELLK
0 1 S641-p LGTSSkEsEELLKSK
0 14 S788-p GRAKTRWsQVFsLEI
0 1 S792-p TRWsQVFsLEIQAKF
0 1 K821-m2 LMQTDKLkQLRQTVK
0 1 S854-p IVSAQDAsLQERVLA
0 2 T915 RVALSAATQKSLDRK
0 1 K922 TQKSLDRKKYMKAAE
0 1 K923 QKSLDRKKYMKAAEM
0 2 S995-p VPNRVPVsGVyAGKI
0 68 Y998-p RVPVsGVyAGKIQRK
  mouse

 
T49-p AVLSPLLtIEKRKKI
T107 FDQWATETIYSNPEV
Y109 QWATETIYSNPEVTD
S165 RVGLPGDSEVSGSLR
S170 GDSEVSGSLRQCESP
S194-p ALRLSSAsPQETIIS
S242-p EYVERELsSRSLRNS
S245 ERELsSRSLRNSLKR
S249 sSRSLRNSLKRSVNE
T257 LKRSVNETHSDREND
S364-p GPYAKLPsPEPsMsP
S368-p KLPsPEPsMsPTMHR
S370-p PsPEPsMsPTMHRRH
S378 PTMHRRHSRsAsACQ
S380-p MHRRHSRsAsACQIL
A381 HRRHSRsAsACQILI
S382-p RRHSRsAsACQILIN
S398-p PVNACELsPKGKEEA
S439 GVCSSNVSATKITSE
Q506 VPKLHELQPSSQCVS
S514 PSSQCVSSQTLEDVC
S550 SYDVKHPSPLLTQTQ
Y601 LQKENCPYIITAGVA
Y620-p DRLLERRyPKGFVHI
F624 ERRyPKGFVHINKNK
K629 KGFVHINKNKMLETS
K638 KMLETSPKEGQELLK
G640 LETSPKEGQELLKSK
S780 GRAQAKWSQVFNPEI
N784 AKWSQVFNPEIHAKF
K813 LMQTDKLKQLRQTVK
S846 VVSAQDASLQERVLA
T907-p RVALSVAtQKSLDRk
K914-ac tQKSLDRkkFMKVAE
K915-ac QKSLDRkkFMKVAEM
S987 VPNRAPVSGAYAGKT
Y990 RAPVSGAYAGKTQRK
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