Q68D86 · C102B_HUMAN
- ProteinCoiled-coil domain-containing protein 102B
- GeneCCDC102B
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids513 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
During interphase, forms fibers at the proximal ends of centrioles to maintain centrosome cohesion (PubMed:30404835).
During mitosis, dissociates from the centrosome following phosphorylation to allow centrosome separation (PubMed:30404835).
Contributes to CROCC/rootletin filament formation (PubMed:30404835).
During mitosis, dissociates from the centrosome following phosphorylation to allow centrosome separation (PubMed:30404835).
Contributes to CROCC/rootletin filament formation (PubMed:30404835).
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 | cytoplasm | |
Molecular Function | protein serine/threonine kinase binding | |
Biological Process | centriole-centriole cohesion |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCoiled-coil domain-containing protein 102B
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ68D86
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 21 | Substantial decrease in phosphorylation; when associated with A-22, A-34, A-135, A-142, A-194, A-210, A-401, A-404 and A-406. | ||||
Sequence: S → A | ||||||
Mutagenesis | 22 | Substantial decrease in phosphorylation; when associated with A-21, A-34, A-135, A-142, A-194, A-210, A-401, A-404 and A-406. | ||||
Sequence: S → A | ||||||
Mutagenesis | 34 | Substantial decrease in phosphorylation; when associated with A-21, A-22, A-135, A-142, A-194, A-210, A-401, A-404 and A-406. | ||||
Sequence: S → A | ||||||
Mutagenesis | 135 | Substantial decrease in phosphorylation; when associated with A-21, A-22, A-34, A-142, A-194, A-210, A-401, A-404 and A-406. | ||||
Sequence: S → A | ||||||
Mutagenesis | 142 | Substantial decrease in phosphorylation; when associated with A-21, A-22, A-34, A-135, A-194, A-210, A-401, A-404 and A-406. | ||||
Sequence: S → A | ||||||
Natural variant | VAR_047331 | 153 | in dbSNP:rs572020 | |||
Sequence: K → N | ||||||
Mutagenesis | 194 | Substantial decrease in phosphorylation; when associated with A-21, A-22, A-34, A-135, A-142, A-210, A-401, A-404 and A-406. | ||||
Sequence: S → A | ||||||
Mutagenesis | 210 | Substantial decrease in phosphorylation; when associated with A-21, A-22, A-34, A-135, A-142, A-194, A-401, A-404 and A-406. | ||||
Sequence: S → A | ||||||
Natural variant | VAR_047332 | 298 | in dbSNP:rs2187094 | |||
Sequence: K → R | ||||||
Natural variant | VAR_022893 | 346 | in dbSNP:rs745894 | |||
Sequence: C → F | ||||||
Natural variant | VAR_047333 | 370 | in dbSNP:rs34102373 | |||
Sequence: E → G | ||||||
Mutagenesis | 401 | Substantial decrease in phosphorylation; when associated with A-21, A-22, A-34, A-135, A-142, A-194, A-210, A-404 and A-406. | ||||
Sequence: S → A | ||||||
Mutagenesis | 404 | Substantial decrease in phosphorylation; when associated with A-21, A-22, A-34, A-135, A-142, A-194, A-210, A-401 and A-406. | ||||
Sequence: S → A | ||||||
Mutagenesis | 406 | Substantial decrease in phosphorylation; when associated with A-21, A-22, A-34, A-135, A-142, A-194, A-210, A-401 and A-404. | ||||
Sequence: S → A | ||||||
Natural variant | VAR_047334 | 425 | in dbSNP:rs17080065 | |||
Sequence: N → K | ||||||
Natural variant | VAR_022894 | 429 | in dbSNP:rs9963788 | |||
Sequence: A → P |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 670 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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000079308 | 1-513 | Coiled-coil domain-containing protein 102B | |||
Sequence: MNLDSIHRLIEETQIFQMQQSSIKSRGDMVAPASPPRDTCNTCFPLHGLQSHAAHNFCAHSYNTNKWDICEELRLRELEEVKARAAQMEKTMRWWSDCTANWREKWSKVRAERNSAREEGRQLRIKLEMAMKELSTLKKKQSLPPQKEALEAKVTQDLKLPGFVEESCEHTDQFQLSSQMHESIREYLVKRQFSTKEDTNNKEQGVVIDSLKLSEEMKPNLDGVDLFNNGGSGNGETKTGLRLKAINLPLENEVTEISALQVHLDEFQKILWKEREMRTALEKEIERLESALSLWKWKYEELKESKPKNVKEFDILLGQHNDEMQELSGNIKEESKSQNSKDRVICELRAELERLQAENTSEWDKREILEREKQGLERENRRLKIQVKEMEELLDKKNRLSANSQSPDFKMSQIDLQEKNQELLNLQHAYYKLNRQYQANIAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRKLQRSLDEEKERNENLETELRHLQNW | ||||||
Modified residue | 21 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 22 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 34 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 135 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 142 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 194 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 210 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 401 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 404 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 406 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated directly or indirectly by NEK2 during mitosis which causes dissociation of CCDC102B from the centrosome and allows for centrosome separation.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts (via N-terminus) with centriolar protein CEP250/CNAP1; the interaction results in recruitment of CCDC102B to the proximal ends of centrioles (PubMed:30404835).
Interacts (via N-terminus) with CROCC/rootletin and LRRC45 (PubMed:30404835).
Interacts (via N-terminus) with serine/threonine-protein kinase NEK2; the interaction results in phosphorylation of CCDC102B (PubMed:30404835).
Interacts (via N-terminus) with CROCC/rootletin and LRRC45 (PubMed:30404835).
Interacts (via N-terminus) with serine/threonine-protein kinase NEK2; the interaction results in phosphorylation of CCDC102B (PubMed:30404835).
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-217 | Required for centriolar localization and for interaction with CEP250, CROCC, LRRC45 and NEK2 | ||||
Sequence: MNLDSIHRLIEETQIFQMQQSSIKSRGDMVAPASPPRDTCNTCFPLHGLQSHAAHNFCAHSYNTNKWDICEELRLRELEEVKARAAQMEKTMRWWSDCTANWREKWSKVRAERNSAREEGRQLRIKLEMAMKELSTLKKKQSLPPQKEALEAKVTQDLKLPGFVEESCEHTDQFQLSSQMHESIREYLVKRQFSTKEDTNNKEQGVVIDSLKLSEEM | ||||||
Coiled coil | 72-142 | |||||
Sequence: ELRLRELEEVKARAAQMEKTMRWWSDCTANWREKWSKVRAERNSAREEGRQLRIKLEMAMKELSTLKKKQS | ||||||
Coiled coil | 268-337 | |||||
Sequence: QKILWKEREMRTALEKEIERLESALSLWKWKYEELKESKPKNVKEFDILLGQHNDEMQELSGNIKEESKS | ||||||
Coiled coil | 363-513 | |||||
Sequence: WDKREILEREKQGLERENRRLKIQVKEMEELLDKKNRLSANSQSPDFKMSQIDLQEKNQELLNLQHAYYKLNRQYQANIAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRKLQRSLDEEKERNENLETELRHLQNW | ||||||
Region | 493-513 | Disordered | ||||
Sequence: LDEEKERNENLETELRHLQNW |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q68D86-1
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
- Length513
- Mass (Da)60,448
- Last updated2008-11-25 v4
- Checksum450D36A80D6D88C8
Q68D86-2
- Name2
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 131 | in Ref. 1; CAH18334 | ||||
Sequence: M → T | ||||||
Sequence conflict | 382 | in Ref. 1; CAH18334 | ||||
Sequence: R → G | ||||||
Sequence conflict | 469 | in Ref. 1; CAH18334 | ||||
Sequence: K → R | ||||||
Alternative sequence | VSP_014688 | 479-483 | in isoform 2 | |||
Sequence: LDDSL → VLLYE | ||||||
Alternative sequence | VSP_014689 | 484-513 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CR749520 EMBL· GenBank· DDBJ | CAH18334.2 EMBL· GenBank· DDBJ | mRNA | ||
AL833863 EMBL· GenBank· DDBJ | CAD38721.2 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
AC022035 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC096708 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC011087 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC056269 EMBL· GenBank· DDBJ | AAH56269.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
BC126448 EMBL· GenBank· DDBJ | AAI26449.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC126450 EMBL· GenBank· DDBJ | AAI26451.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK027247 EMBL· GenBank· DDBJ | BAB15706.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |