Q9P287 · BCCIP_HUMAN
- ProteinBRCA2 and CDKN1A-interacting protein
- GeneBCCIP
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids314 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
During interphase, required for microtubule organizing and anchoring activities. During mitosis, required for the organization and stabilization of the spindle pole (PubMed:28394342).
Isoform 2/alpha is particularly important for the regulation of microtubule anchoring, microtubule stability, spindle architecture and spindle orientation, compared to isoform 1/beta (PubMed:28394342).
May promote cell cycle arrest by enhancing the inhibition of CDK2 activity by CDKN1A. May be required for repair of DNA damage by homologous recombination in conjunction with BRCA2. May not be involved in non-homologous end joining (NHEJ)
Isoform 2/alpha is particularly important for the regulation of microtubule anchoring, microtubule stability, spindle architecture and spindle orientation, compared to isoform 1/beta (PubMed:28394342).
May promote cell cycle arrest by enhancing the inhibition of CDK2 activity by CDKN1A. May be required for repair of DNA damage by homologous recombination in conjunction with BRCA2. May not be involved in non-homologous end joining (NHEJ)
Miscellaneous
HT1080 cells that constitutively express low levels of BCCIP display increased levels of spontaneous single-stranded DNA and double-strand breaks.
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 | cytosol | |
Cellular Component | mitotic spindle pole | |
Cellular Component | nuclear cyclin-dependent protein kinase holoenzyme complex | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | kinase regulator activity | |
Molecular Function | RNA binding | |
Molecular Function | tubulin binding | |
Biological Process | DNA repair | |
Biological Process | establishment of mitotic spindle orientation | |
Biological Process | microtubule anchoring | |
Biological Process | microtubule cytoskeleton organization | |
Biological Process | mitotic spindle assembly | |
Biological Process | mitotic spindle organization | |
Biological Process | neuroendocrine cell differentiation | |
Biological Process | regulation of cyclin-dependent protein serine/threonine kinase activity |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBRCA2 and CDKN1A-interacting protein
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9P287
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Isoform 1
Isoform 2
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_046642 | 254 | in dbSNP:rs17153610 | |||
Sequence: E → Q |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 380 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, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000249687 | 1-314 | UniProt | BRCA2 and CDKN1A-interacting protein | |||
Sequence: MASRSKRRAVESGVPQPPDPPVQRDEEEEKEVENEDEDDDDSDKEKDEEDEVIDEEVNIEFEAYSLSDNDYDGIKKLLQQLFLKAPVNTAELTDLLIQQNHIGSVIKQTDVSEDSNDDMDEDEVFGFISLLNLTERKGTQCVEQIQELVLRFCEKNCEKSMVEQLDKFLNDTTKPVGLLLSERFINVPPQIALPMYQQLQKELAGAHRTNKPCGKCYFYLLISKTFVEAGKNNSKKKPSNKKKAALMFANAEEEFFYEKAILKFNYSVQEESDTCLGGKWSFDDVPMTPLRTVMLIPGDKMNEIMDKLKEYLSV | |||||||
Modified residue | 42 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 42 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 112 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 112 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 115 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 234 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 281 | UniProt | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed at high levels in testis and skeletal muscle and at lower levels in brain, heart, kidney, liver, lung, ovary, pancreas, placenta, and spleen.
Developmental stage
Isoform 1 is expressed throughout the cell cycle. Isoform 2 is expressed following mitosis and peaks in the G1/S phase of the cell cycle.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with BRCA2, CDKN1A and MTDH/LYRIC (PubMed:10878006, PubMed:11313963, PubMed:14726710, PubMed:15713648, PubMed:18440304).
Isoform 2/alpha, but not isoform 1/beta, interacts with DCTN1/p150-glued and ACTR1A/ARP1 (PubMed:28394342).
Both isoform 1 and isoform 2 interact with alpha-, beta- and gamma-tubulins (PubMed:28394342).
Interacts with TENT5C; the interaction has no effect on TENT5C poly(A) polymerase function (PubMed:28931820).
Isoform 2/alpha, but not isoform 1/beta, interacts with DCTN1/p150-glued and ACTR1A/ARP1 (PubMed:28394342).
Both isoform 1 and isoform 2 interact with alpha-, beta- and gamma-tubulins (PubMed:28394342).
Interacts with TENT5C; the interaction has no effect on TENT5C poly(A) polymerase function (PubMed:28931820).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9P287 | CENPJ Q9HC77 | 3 | EBI-711154, EBI-946194 | |
BINARY | Q9P287 | FCF1 Q9Y324 | 3 | EBI-711154, EBI-5455734 | |
BINARY | Q9P287 | MRPS9 P82933 | 3 | EBI-711154, EBI-721385 | |
BINARY | Q9P287 | PDGFB P01127 | 3 | EBI-711154, EBI-1554925 | |
BINARY | Q9P287 | RALY Q53GL6 | 3 | EBI-711154, EBI-9512693 | |
BINARY | Q9P287 | RPL23 P62829 | 8 | EBI-711154, EBI-353303 | |
BINARY | Q9P287 | RPL38 P63173 | 3 | EBI-711154, EBI-359141 | |
BINARY | Q9P287 | ZNF138 P52744 | 3 | EBI-711154, EBI-10746567 | |
BINARY | Q9P287 | ZNF19 P17023 | 3 | EBI-711154, EBI-12884200 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-56 | Disordered | ||||
Sequence: MASRSKRRAVESGVPQPPDPPVQRDEEEEKEVENEDEDDDDSDKEKDEEDEVIDEE | ||||||
Compositional bias | 28-56 | Acidic residues | ||||
Sequence: EEKEVENEDEDDDDSDKEKDEEDEVIDEE | ||||||
Region | 59-167 | Interaction with BRCA2 | ||||
Sequence: IEFEAYSLSDNDYDGIKKLLQQLFLKAPVNTAELTDLLIQQNHIGSVIKQTDVSEDSNDDMDEDEVFGFISLLNLTERKGTQCVEQIQELVLRFCEKNCEKSMVEQLDK | ||||||
Region | 161-259 | Interaction with CDKN1A | ||||
Sequence: MVEQLDKFLNDTTKPVGLLLSERFINVPPQIALPMYQQLQKELAGAHRTNKPCGKCYFYLLISKTFVEAGKNNSKKKPSNKKKAALMFANAEEEFFYEK |
Sequence similarities
Belongs to the BCP1 family.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
Q9P287-1
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
- SynonymsBeta
- Length314
- Mass (Da)35,979
- Last updated2000-10-01 v1
- Checksum203CA32F7BE0A806
Q9P287-2
- Name2
- SynonymsAlpha
- Differences from canonical
- 259-314: KAILKFNYSVQEESDTCLGGKWSFDDVPMTPLRTVMLIPGDKMNEIMDKLKEYLSV → EQGKPEVLGGPDTRRGLEPVPIQHNGGSRGQVTALVSLKAGLIQSRSTLSDFQGTFMTVGIALS
Q9P287-3
- Name3
- Differences from canonical
- 285-314: VPMTPLRTVMLIPGDKMNEIMDKLKEYLSV → WSVPPVLE
Q9P287-4
- Name4
- Differences from canonical
- 259-314: KAILKFNYSVQEESDTCLGGKWSFDDVPMTPLRTVMLIPGDKMNEIMDKLKEYLSV → EQGKPEVLGGPDTRRGLEPVPIQHNGWSVPPVLE
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 28-56 | Acidic residues | ||||
Sequence: EEKEVENEDEDDDDSDKEKDEEDEVIDEE | ||||||
Sequence conflict | 75 | in Ref. 3; BAG51557 | ||||
Sequence: K → R | ||||||
Sequence conflict | 230 | in Ref. 6; AAH09771 | ||||
Sequence: G → E | ||||||
Alternative sequence | VSP_020540 | 259-314 | in isoform 2 | |||
Sequence: KAILKFNYSVQEESDTCLGGKWSFDDVPMTPLRTVMLIPGDKMNEIMDKLKEYLSV → EQGKPEVLGGPDTRRGLEPVPIQHNGGSRGQVTALVSLKAGLIQSRSTLSDFQGTFMTVGIALS | ||||||
Alternative sequence | VSP_042023 | 259-314 | in isoform 4 | |||
Sequence: KAILKFNYSVQEESDTCLGGKWSFDDVPMTPLRTVMLIPGDKMNEIMDKLKEYLSV → EQGKPEVLGGPDTRRGLEPVPIQHNGWSVPPVLE | ||||||
Alternative sequence | VSP_020541 | 285-314 | in isoform 3 | |||
Sequence: VPMTPLRTVMLIPGDKMNEIMDKLKEYLSV → WSVPPVLE |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB040450 EMBL· GenBank· DDBJ | BAA92927.1 EMBL· GenBank· DDBJ | mRNA | ||
AB040451 EMBL· GenBank· DDBJ | BAA92928.1 EMBL· GenBank· DDBJ | mRNA | ||
AY064247 EMBL· GenBank· DDBJ | AAL55436.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY064247 EMBL· GenBank· DDBJ | AAL55438.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY064248 EMBL· GenBank· DDBJ | AAL55439.1 EMBL· GenBank· DDBJ | mRNA | ||
AY064249 EMBL· GenBank· DDBJ | AAL55440.1 EMBL· GenBank· DDBJ | mRNA | ||
AK055691 EMBL· GenBank· DDBJ | BAG51557.1 EMBL· GenBank· DDBJ | mRNA | ||
AL834458 EMBL· GenBank· DDBJ | CAD39118.1 EMBL· GenBank· DDBJ | mRNA | ||
AL360176 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC009771 EMBL· GenBank· DDBJ | AAH09771.1 EMBL· GenBank· DDBJ | mRNA |