O43303 · CP110_HUMAN
- ProteinCentriolar coiled-coil protein of 110 kDa
- GeneCCP110
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1012 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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:17681131, PubMed:17719545, PubMed:23486064, PubMed:30375385, PubMed:35301795).
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 (By similarity).
Required for correct spindle formation and has a role in regulating cytokinesis and genome stability via cooperation with CALM1 and CETN2 (PubMed:16760425).
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 (By similarity).
Required for correct spindle formation and has a role in regulating cytokinesis and genome stability via cooperation with CALM1 and CETN2 (PubMed:16760425).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | centriole | |
Cellular Component | centrosome | |
Cellular Component | cilium | |
Cellular Component | cytosol | |
Cellular Component | protein-containing complex | |
Biological Process | centriole replication | |
Biological Process | centrosome duplication | |
Biological Process | ciliary basal body organization | |
Biological Process | negative regulation of centriole elongation | |
Biological Process | negative regulation of cilium assembly | |
Biological Process | positive regulation of cilium assembly | |
Biological Process | regulation of cytokinesis |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCentriolar coiled-coil protein of 110 kDa
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO43303
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Recruited early and then associates with the growing distal tips. Recruited to the mother centriole by KIF24 (PubMed:21620453).
Removed from centrioles by TTBK2, leading to initiation of ciliogenesis and localizes only to the daughter centriole in ciliated cells. In cytotoxic T lymphocytes remains associated with the mother centriole during docking of the centrosome at the immunological synapse upon target contact (By similarity).
Recruited at the distal end of the mother centriole by MPHOSPH9 (PubMed:30375385).
Removed from centrioles by TTBK2, leading to initiation of ciliogenesis and localizes only to the daughter centriole in ciliated cells. In cytotoxic T lymphocytes remains associated with the mother centriole during docking of the centrosome at the immunological synapse upon target contact (By similarity).
Recruited at the distal end of the mother centriole by MPHOSPH9 (PubMed:30375385).
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_056788 | 69 | in dbSNP:rs16972129 | |||
Sequence: R → S | ||||||
Mutagenesis | 170 | Loss of centrosome clustering and protection from anaphase catastrophe upon CDK2 inhibition in lung cancer cells. | ||||
Sequence: S → A | ||||||
Natural variant | VAR_056789 | 171 | in dbSNP:rs3751821 | |||
Sequence: P → L | ||||||
Mutagenesis | 194 | Loss of centrosome clustering and protection from anaphase catastrophe upon CDK2 inhibition in lung cancer cells. | ||||
Sequence: T → A | ||||||
Natural variant | VAR_019823 | 252 | in dbSNP:rs226891 | |||
Sequence: I → M | ||||||
Natural variant | VAR_056790 | 347 | in dbSNP:rs11645625 | |||
Sequence: F → I | ||||||
Natural variant | VAR_019824 | 375 | in dbSNP:rs7190666 | |||
Sequence: M → I | ||||||
Mutagenesis | 586-588 | Abolishes interaction with CCNF. | ||||
Sequence: RRL → ARA |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 962 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000089460 | 1-1012 | UniProt | Centriolar coiled-coil protein of 110 kDa | |||
Sequence: MEEYEKFCEKSLARIQEASLSTESFLPAQSESISLIRFHGVAILSPLLNIEKRKEMQQEKQKALDVEARKQVNRKKALLTRVQEILDNVQVRKAPNASDFDQWEMETVYSNSEVRNLNVPATFPNSFPSHTEHSTAAKLDKIAGILPLDNEDQCKTDGIDLARDSEGFNSPKQCDSSNISHVENEAFPKTSSATPQETLISDGPFSVNEQQDLPLLAEVIPDPYVMSLQNLMKKSKEYIEREQSRRSLRGSINRIVNESHLDKEHDAVEVADCVKEKGQLTGKHCVSVIPDKPSLNKSNVLLQGASTQASSMSMPVLASFSKVDIPIRTGHPTVLESNSDFKVIPTFVTENNVIKSLTGSYAKLPSPEPSMSPKMHRRRSRTSSACHILINNPINACELSPKGKEQAMDLIIQDTDENTNVPEIMPKLPTDLAGVCSSKVYVGKNTSEVKEDVVLGKSNQVCQSSGNHLENKVTHGLVTVEGQLTSDERGAHIMNSTCAAMPKLHEPYASSQCIASPNFGTVSGLKPASMLEKNCSLQTELNKSYDVKNPSPLLMQNQNTRQQMDTPMVSCGNEQFLDNSFEKVKRRLDLDIDGLQKENCPYVITSGITEQERQHLPEKRYPKGSGFVNKNKMLGTSSKESEELLKSKMLAFEEMRKRLEEQHAQQLSLLIAEQEREQERLQKEIEEQEKMLKEKKAMTAEASELDINNAVELEWRKISDSSLLETMLSQADSLHTSNSNSSGFTNSAMQYSFVSANEAPFYLWGSSTSGLTKLSVTRPFGRAKTRWSQVFSLEIQAKFNKITAVAKGFLTRRLMQTDKLKQLRQTVKDTMEFIRSFQSEAPLKRGIVSAQDASLQERVLAQLRAALYGIHDIFFVMDAAERMSILHHDREVRKEKMLRQMDKMKSPRVALSAATQKSLDRKKYMKAAEMGMPNKKFLVKQNPSETRVLQPNQGQNAPVHRLLSRQGTPKTSVKGVVQNRQKPSQSRVPNRVPVSGVYAGKIQRKRPNVATI | |||||||
Modified residue (large scale data) | 45 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 165 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 170 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 170 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 194 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 337 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 366 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 366 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 370 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 372 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 372 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 400 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 400 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 516 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 551 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 551 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 580 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 854 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 998 | PRIDE | Phosphotyrosine | ||||
Sequence: Y |
Post-translational modification
Phosphorylated by CDKs.
Ubiquitinated by the SCF(CCNF) during G2 phase, leading to its degradation by the proteasome and preventing centrosome reduplication (PubMed:20596027).
Deubiquitinated by USP33 in S and G2/M phase, leading to stabilize CCP110 during the period which centrioles duplicate and elongate (PubMed:23486064).
Ubiquitinated by the EDVP complex, leading to its degradation (PubMed:28242748, PubMed:34259627).
Deubiquitinated by USP33 in S and G2/M phase, leading to stabilize CCP110 during the period which centrioles duplicate and elongate (PubMed:23486064).
Ubiquitinated by the EDVP complex, leading to its degradation (PubMed:28242748, PubMed:34259627).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly expressed in testis. Detected at intermediate levels in spleen, thymus, prostate, small intestine, colon and peripheral blood leukocytes.
Induction
Up-regulated during the transition from G1 to S phase of the cell cycle. The highest levels are observed in S phase, after which the levels decrease markedly.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with CALM1, CETN2, CEP76, CEP104, CEP290 and TALPID3. Interacts with CEP97. Seems to associate with discrete CETN2, CEP97 and CEP290-containing complexes. Interacts with NEURL4 and CCNF; these interactions are not mutually exclusive and both lead to CCP110 ubiquitination and proteasome-dependent degradation. Via its interaction with NEURL4, may indirectly interact with HERC2. Interacts with KIF24, leading to its recruitment to centrioles. Interacts with USP20 and USP33 (PubMed:23486064).
Interacts with MPHOSPH9 (PubMed:30375385).
Interacts (via N-terminal region) with ENKD1 (via central region); ENKD1 competes with CEP97 for binding to CCP110, destabilizing the interaction between CP110 and CEP97 which promotes the removal of CCP110 and CEP97 from the mother centriole and allows the initiation of ciliogenesis (By similarity).
Interacts with MPHOSPH9 (PubMed:30375385).
Interacts (via N-terminal region) with ENKD1 (via central region); ENKD1 competes with CEP97 for binding to CCP110, destabilizing the interaction between CP110 and CEP97 which promotes the removal of CCP110 and CEP97 from the mother centriole and allows the initiation of ciliogenesis (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O43303 | CALM3 P0DP25 | 15 | EBI-1566217, EBI-397435 | |
BINARY | O43303 | CCNF P41002 | 9 | EBI-1566217, EBI-1207574 | |
BINARY | O43303 | CEP290 O15078 | 18 | EBI-1566217, EBI-1811944 | |
BINARY | O43303 | CEP97 Q8IW35 | 30 | EBI-1566217, EBI-1566210 | |
BINARY | O43303 | CETN2 P41208 | 5 | EBI-1566217, EBI-1789926 | |
BINARY | O43303 | KIAA0586 Q9BVV6 | 6 | EBI-1566217, EBI-11286926 | |
BINARY | O43303 | KIF24 Q5T7B8 | 15 | EBI-1566217, EBI-2556811 | |
BINARY | O43303 | NEURL4 Q96JN8 | 9 | EBI-1566217, EBI-1053406 | |
BINARY | O43303 | NUP50 Q9UKX7 | 4 | EBI-1566217, EBI-2371082 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, coiled coil, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-223 | CEP97 binding | ||||
Sequence: MEEYEKFCEKSLARIQEASLSTESFLPAQSESISLIRFHGVAILSPLLNIEKRKEMQQEKQKALDVEARKQVNRKKALLTRVQEILDNVQVRKAPNASDFDQWEMETVYSNSEVRNLNVPATFPNSFPSHTEHSTAAKLDKIAGILPLDNEDQCKTDGIDLARDSEGFNSPKQCDSSNISHVENEAFPKTSSATPQETLISDGPFSVNEQQDLPLLAEVIPDP | ||||||
Coiled coil | 49-90 | |||||
Sequence: NIEKRKEMQQEKQKALDVEARKQVNRKKALLTRVQEILDNVQ | ||||||
Region | 64-82 | Calmodulin-binding | ||||
Sequence: LDVEARKQVNRKKALLTRV | ||||||
Region | 67-82 | Required for interaction with CEP290 | ||||
Sequence: EARKQVNRKKALLTRV | ||||||
Region | 350-565 | Interaction with CEP76 | ||||
Sequence: ENNVIKSLTGSYAKLPSPEPSMSPKMHRRRSRTSSACHILINNPINACELSPKGKEQAMDLIIQDTDENTNVPEIMPKLPTDLAGVCSSKVYVGKNTSEVKEDVVLGKSNQVCQSSGNHLENKVTHGLVTVEGQLTSDERGAHIMNSTCAAMPKLHEPYASSQCIASPNFGTVSGLKPASMLEKNCSLQTELNKSYDVKNPSPLLMQNQNTRQQMD | ||||||
Region | 611-633 | Disordered | ||||
Sequence: QERQHLPEKRYPKGSGFVNKNKM | ||||||
Coiled coil | 640-709 | |||||
Sequence: ESEELLKSKMLAFEEMRKRLEEQHAQQLSLLIAEQEREQERLQKEIEEQEKMLKEKKAMTAEASELDINN | ||||||
Region | 781-821 | Calmodulin-binding | ||||
Sequence: GRAKTRWSQVFSLEIQAKFNKITAVAKGFLTRRLMQTDKLK | ||||||
Region | 909-924 | Calmodulin-binding | ||||
Sequence: VALSAATQKSLDRKKY | ||||||
Compositional bias | 949-991 | Polar residues | ||||
Sequence: LQPNQGQNAPVHRLLSRQGTPKTSVKGVVQNRQKPSQSRVPNR | ||||||
Region | 949-992 | Disordered | ||||
Sequence: LQPNQGQNAPVHRLLSRQGTPKTSVKGVVQNRQKPSQSRVPNRV |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
O43303-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length1,012
- Mass (Da)113,424
- Last updated2007-10-23 v3
- Checksum5459F655CFB9DFD0
O43303-2
- Name2
- Differences from canonical
- 968-1012: TPKTSVKGVVQNRQKPSQSRVPNRVPVSGVYAGKIQRKRPNVATI → SICRKNPKKAAKCCDNLRRQHSLG
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for sequence conflict, compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 628 | in Ref. 5; AAH36654 | ||||
Sequence: V → F | ||||||
Compositional bias | 949-991 | Polar residues | ||||
Sequence: LQPNQGQNAPVHRLLSRQGTPKTSVKGVVQNRQKPSQSRVPNR | ||||||
Alternative sequence | VSP_011897 | 968-1012 | in isoform 2 | |||
Sequence: TPKTSVKGVVQNRQKPSQSRVPNRVPVSGVYAGKIQRKRPNVATI → SICRKNPKKAAKCCDNLRRQHSLG |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB007879 EMBL· GenBank· DDBJ | BAA24849.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
CR749255 EMBL· GenBank· DDBJ | CAH18111.1 EMBL· GenBank· DDBJ | mRNA | ||
AC003108 EMBL· GenBank· DDBJ | AAC05804.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC012621 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC036654 EMBL· GenBank· DDBJ | AAH36654.1 EMBL· GenBank· DDBJ | mRNA |