Q61140 · BCAR1_MOUSE
- ProteinBreast cancer anti-estrogen resistance protein 1
- GeneBcar1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids874 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Docking protein which plays a central coordinating role for tyrosine kinase-based signaling related to cell adhesion (By similarity).
Implicated in induction of cell migration and cell branching (PubMed:25499443).
Involved in the BCAR3-mediated inhibition of TGFB signaling (PubMed:25499443).
Implicated in induction of cell migration and cell branching (PubMed:25499443).
Involved in the BCAR3-mediated inhibition of TGFB signaling (PubMed:25499443).
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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Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBreast cancer anti-estrogen resistance protein 1
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ61140
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
PTM/Processing
Features
Showing features for modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000064855 | 1-874 | Breast cancer anti-estrogen resistance protein 1 | |||
Sequence: MTVPNVLAKALYDNVAESPDELSFRKGDIMTVLERDTQGLDGWWLCSLHGRQGIVPGNRLKILVGMYDKKPVGPGPGPPATPPQPQPSLPQGVHAPVPPASQYSPMLPTAYQPQSDNVYLVPTPSKTQQGLYQAPGPNPQFQSPPAKQTSTFSKQTPHHSFPSPATDLYQVPPGPGSPAQDIYQVPPSAGIGHDIYQVPPSLDTRGWEGTKPPAKVVVPTRVGQGYVYEAAQTEQDEYDTPRHLLAPGPQDIYDVPPVRGLLPNQYGQEVYDTPPMAVKGPNGRDPLLDVYDVPPSVEKGLLSSSHHSVYDVPPSVSKDVPDGPLLREETYDVPPAFAKPKPFDPTRHPLILAAPPPDSPAAEDVYDVPPPAPDLYDVPPGLRRPGPGTLYDVPRERVLPPEVADGSVVDDGVYAVPPPAEREAPTDGKRLSASSTGSTRSSQSASSLEVVVPGREPLELEVAVESLARLQQGVSTTVAHLLDLVGSASGPGGWRGTSEPQEPPAQDLKAAVAAVHGAVHELLEFARGAVSNATHTSDRTLHAKLSRQLQKMEDVYQTLVVHGQVLDSGRGSPGFTPEDLDRLVACSRAVPEDAKQLASFLHGNASLLFRRTKAPGPGPEGSSSLHPNPTDKASSIQSRPLPSPPKFTSQDSPDGQYENSEGGWMEDYDYVHLQGKEEFEKTQKELLERGNIMRQGKGQLELQQLKQFERLEQEVSRPIDHDLANWTPAQPLVPGRTGGLGPSDRQLLLFYLEQCEANLTTLTDAVDAFFTAVATNQPPKIFVAHSKFVILSAHKLVFIGDTLSRQAKAADVRSQVTHYSNLLCDLLRGIVATTKAAALQYPSPSAAQDMVDRVKELGHSTQQFRRVLGQLAAA | ||||||
Modified residue | 132 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 143 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 238 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 253 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 273 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 296 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 366 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 376 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 414 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 432 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 441 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 643 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
PTK2/FAK1 activation mediates phosphorylation at the YDYVHL motif; phosphorylation is most likely catalyzed by SRC family members. SRC-family kinases are recruited to the phosphorylated sites and can phosphorylate other tyrosine residues. Tyrosine phosphorylation is triggered by integrin mediated adhesion of cells to the extracellular matrix (By similarity).
Dephosphorylated by PTPN14 at Tyr-132.
Phosphorylated by SRC kinase in a EDN1- and PTK2B-mediated manner; phosphorylation strengthens its interaction with BCAR3 as part of the PTK2B/BCAR1/BCAR3/RAP1 signaling pathway.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Forms complexes in vivo with PTK2/FAK1, adapter protein CRKL and LYN kinase. Can heterodimerize with NEDD9. Component of a complex comprised of SH2D3C, BCAR1/CAS, and CRK (By similarity).
Within the complex, interacts with SH2D3C (via C-terminus), and CRK (By similarity).
Part of a complex comprised of PTPRA, BCAR1, BCAR3 (via SH2 domain) and SRC; the formation of the complex is dependent on intergrin mediated-tyrosine phosphorylation of PTPRA (PubMed:22801373).
Interacts with BCAR3 (via Ras-GEF domain); the interaction regulates adhesion-dependent serine phosphorylation (PubMed:10896938, PubMed:22801373).
Interacts with SMAD2 and SMAD3 (PubMed:25499443).
Interacts with NPHP1 (PubMed:10739664).
Interacts with PTK2B/PYK2 (By similarity).
Interacts (via C-terminus) with SH2D3C/CHAT isoform 2 (via C-terminus) (PubMed:10692442, PubMed:12486027, PubMed:17174122).
Interacts with activated CSPG4. Interacts with BMX, INPPL1/SHIP2 and PEAK1 (By similarity).
Part of a collagen stimulated complex involved in cell migration composed of CDC42, CRK, TNK2 and BCAR1/p130cas (By similarity).
Interacts with TNK2 via SH3 domains. Interacts (when tyrosine-phosphorylated) with tensin TNS1; the interaction is increased by phosphorylation of TNS1 (By similarity).
Within the complex, interacts with SH2D3C (via C-terminus), and CRK (By similarity).
Part of a complex comprised of PTPRA, BCAR1, BCAR3 (via SH2 domain) and SRC; the formation of the complex is dependent on intergrin mediated-tyrosine phosphorylation of PTPRA (PubMed:22801373).
Interacts with BCAR3 (via Ras-GEF domain); the interaction regulates adhesion-dependent serine phosphorylation (PubMed:10896938, PubMed:22801373).
Interacts with SMAD2 and SMAD3 (PubMed:25499443).
Interacts with NPHP1 (PubMed:10739664).
Interacts with PTK2B/PYK2 (By similarity).
Interacts (via C-terminus) with SH2D3C/CHAT isoform 2 (via C-terminus) (PubMed:10692442, PubMed:12486027, PubMed:17174122).
Interacts with activated CSPG4. Interacts with BMX, INPPL1/SHIP2 and PEAK1 (By similarity).
Part of a collagen stimulated complex involved in cell migration composed of CDC42, CRK, TNK2 and BCAR1/p130cas (By similarity).
Interacts with TNK2 via SH3 domains. Interacts (when tyrosine-phosphorylated) with tensin TNS1; the interaction is increased by phosphorylation of TNS1 (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q61140 | Nphp1 Q9QY53 | 2 | EBI-77088, EBI-77230 | |
BINARY | Q61140 | Ptk2 P34152 | 3 | EBI-77088, EBI-77070 | |
XENO | Q61140 | PTPN1 P18031 | 5 | EBI-77088, EBI-968788 | |
BINARY | Q61140 | Srcin1 Q9QWI6 | 2 | EBI-77088, EBI-775592 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 3-65 | SH3 | ||||
Sequence: VPNVLAKALYDNVAESPDELSFRKGDIMTVLERDTQGLDGWWLCSLHGRQGIVPGNRLKILVG | ||||||
Region | 71-177 | Disordered | ||||
Sequence: PVGPGPGPPATPPQPQPSLPQGVHAPVPPASQYSPMLPTAYQPQSDNVYLVPTPSKTQQGLYQAPGPNPQFQSPPAKQTSTFSKQTPHHSFPSPATDLYQVPPGPGS | ||||||
Compositional bias | 72-94 | Pro residues | ||||
Sequence: VGPGPGPPATPPQPQPSLPQGVH | ||||||
Compositional bias | 105-163 | Polar residues | ||||
Sequence: PMLPTAYQPQSDNVYLVPTPSKTQQGLYQAPGPNPQFQSPPAKQTSTFSKQTPHHSFPS | ||||||
Region | 119-420 | Substrate for kinases | ||||
Sequence: YLVPTPSKTQQGLYQAPGPNPQFQSPPAKQTSTFSKQTPHHSFPSPATDLYQVPPGPGSPAQDIYQVPPSAGIGHDIYQVPPSLDTRGWEGTKPPAKVVVPTRVGQGYVYEAAQTEQDEYDTPRHLLAPGPQDIYDVPPVRGLLPNQYGQEVYDTPPMAVKGPNGRDPLLDVYDVPPSVEKGLLSSSHHSVYDVPPSVSKDVPDGPLLREETYDVPPAFAKPKPFDPTRHPLILAAPPPDSPAAEDVYDVPPPAPDLYDVPPGLRRPGPGTLYDVPRERVLPPEVADGSVVDDGVYAVPPPA | ||||||
Region | 374-394 | Disordered | ||||
Sequence: DLYDVPPGLRRPGPGTLYDVP | ||||||
Region | 409-450 | Disordered | ||||
Sequence: VDDGVYAVPPPAEREAPTDGKRLSASSTGSTRSSQSASSLEV | ||||||
Compositional bias | 429-449 | Polar residues | ||||
Sequence: KRLSASSTGSTRSSQSASSLE | ||||||
Region | 610-662 | Disordered | ||||
Sequence: RRTKAPGPGPEGSSSLHPNPTDKASSIQSRPLPSPPKFTSQDSPDGQYENSEG | ||||||
Compositional bias | 623-657 | Polar residues | ||||
Sequence: SSLHPNPTDKASSIQSRPLPSPPKFTSQDSPDGQY | ||||||
Motif | 639-647 | SH3-binding | ||||
Sequence: RPLPSPPKF | ||||||
Region | 750-800 | Divergent helix-loop-helix motif | ||||
Sequence: FYLEQCEANLTTLTDAVDAFFTAVATNQPPKIFVAHSKFVILSAHKLVFIG |
Domain
Contains a central domain (substrate domain) containing multiple potential SH2-binding sites and a C-terminal domain containing a divergent helix-loop-helix (HLH) motif. The SH2-binding sites putatively bind CRK, NCK and ABL SH2 domains. The HLH motif is absolutely required for the induction of pseudohyphal growth in yeast and mediates heterodimerization with NEDD9.
A serine-rich region promotes activation of the serum response element (SRE).
The SH3 domain is necessary for the localization of the protein to focal adhesions and interacts with one proline-rich region of PTK2/FAK1.
Sequence similarities
Belongs to the CAS family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q61140-1
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.
- NameCas-B
- Length874
- Mass (Da)94,285
- Last updated2011-07-27 v2
- Checksum81E56BC7AD87B095
Q61140-2
- NameCas-A
- Differences from canonical
- 1-4: MTVP → MKYL
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_004134 | 1-4 | in isoform Cas-A | |||
Sequence: MTVP → MKYL | ||||||
Sequence conflict | 72 | in Ref. 1; AAA93381/AAA93248 | ||||
Sequence: V → A | ||||||
Compositional bias | 72-94 | Pro residues | ||||
Sequence: VGPGPGPPATPPQPQPSLPQGVH | ||||||
Compositional bias | 105-163 | Polar residues | ||||
Sequence: PMLPTAYQPQSDNVYLVPTPSKTQQGLYQAPGPNPQFQSPPAKQTSTFSKQTPHHSFPS | ||||||
Compositional bias | 429-449 | Polar residues | ||||
Sequence: KRLSASSTGSTRSSQSASSLE | ||||||
Compositional bias | 623-657 | Polar residues | ||||
Sequence: SSLHPNPTDKASSIQSRPLPSPPKFTSQDSPDGQY |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U48853 EMBL· GenBank· DDBJ | AAA93381.1 EMBL· GenBank· DDBJ | mRNA | ||
U28151 EMBL· GenBank· DDBJ | AAA93248.1 EMBL· GenBank· DDBJ | mRNA | ||
AK145863 EMBL· GenBank· DDBJ | BAE26705.1 EMBL· GenBank· DDBJ | mRNA | ||
BC057578 EMBL· GenBank· DDBJ | AAH57578.1 EMBL· GenBank· DDBJ | mRNA |