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Q61140 (BCAR1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Breast cancer anti-estrogen resistance protein 1
Alternative name(s):
CRK-associated substrate
p130cas
Gene names
Name:Bcar1
Synonyms:Cas, Crkas
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length874 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Docking protein which plays a central coordinating role for tyrosine kinase-based signaling related to cell adhesion. Implicated in induction of cell migration By similarity. Has been shown to be essential in cardiovascular development during embryogenesis.

Subunit structure

Forms complexes in vivo with PTK2/FAK1, adapter protein CRKL and LYN kinase. Can heterodimerize with NEDD9. 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 BCAR3, the interaction regulates adhesion-dependent serine phosphorylation. Interacts with NPHP1, PTK2B/PYK2 and SH2D3C. Ref.1 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8

Subcellular location

Cell junctionfocal adhesion By similarity. Cytoplasm By similarity. Note: Unphosphorylated form localizes in the cytoplasm and can move to the membrane upon tyrosine phosphorylation By similarity.

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) By similarity.

The SH3 domain is necessary for the localization of the protein to focal adhesions and interacts with one proline-rich region of PTK2/FAK1.

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 By similarity.

Sequence similarities

Belongs to the CAS family.

Contains 1 SH3 domain.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell junction
Cytoplasm
   Coding sequence diversityAlternative splicing
   DomainSH3 domain
SH3-binding
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

G-protein coupled receptor signaling pathway

Inferred from direct assay PubMed 9083073. Source: UniProtKB

actin filament organization

Inferred from sequence or structural similarity. Source: UniProtKB

antigen receptor-mediated signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

cell chemotaxis

Inferred from electronic annotation. Source: Ensembl

cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to hepatocyte growth factor stimulus

Inferred from electronic annotation. Source: Ensembl

epidermal growth factor receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

hepatocyte growth factor receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

insulin receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

integrin-mediated signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

neurotrophin TRK receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

platelet-derived growth factor receptor signaling pathway

Inferred from direct assay PubMed 9083073. Source: UniProtKB

positive regulation of cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of endothelial cell migration

Inferred from electronic annotation. Source: Ensembl

vascular endothelial growth factor receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

focal adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

lamellipodium

Inferred from direct assay PubMed 15728191. Source: MGI

plasma membrane

Inferred from electronic annotation. Source: Ensembl

ruffle

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionprotein binding

Inferred from physical interaction Ref.1. Source: UniProtKB

signal transducer activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Nphp1Q9QY532EBI-77088,EBI-77230
Ptk2P341523EBI-77088,EBI-77070
PTPN1P180315EBI-77088,EBI-968788From a different organism.
Srcin1Q9QWI62EBI-77088,EBI-775592

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Cas-B (identifier: 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.
Isoform Cas-A (identifier: Q61140-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: MTVP → MKYL

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 874874Breast cancer anti-estrogen resistance protein 1
PRO_0000064855

Regions

Domain6 – 2621SH3
Region119 – 420302Substrate for kinases By similarity
Region750 – 80051Divergent helix-loop-helix motif
Motif639 – 6479SH3-binding Potential
Compositional bias74 – 8714Pro-rich
Compositional bias426 – 618193Ser-rich

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue1321Phosphotyrosine Ref.9
Modified residue1431Phosphoserine By similarity
Modified residue2531Phosphotyrosine; by ABL1 By similarity
Modified residue2731Phosphothreonine By similarity
Modified residue2961Phosphoserine By similarity
Modified residue3661Phosphotyrosine Ref.9
Modified residue3761Phosphotyrosine Ref.9
Modified residue4141Phosphotyrosine Ref.9
Modified residue4321Phosphoserine By similarity
Modified residue4411Phosphoserine By similarity
Modified residue6431Phosphoserine By similarity

Natural variations

Alternative sequence1 – 44MTVP → MKYL in isoform Cas-A.
VSP_004134

Experimental info

Sequence conflict721V → A in AAA93381. Ref.1
Sequence conflict721V → A in AAA93248. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform Cas-B [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 81E56BC7AD87B095

FASTA87494,285
        10         20         30         40         50         60 
MTVPNVLAKA LYDNVAESPD ELSFRKGDIM TVLERDTQGL DGWWLCSLHG RQGIVPGNRL 

        70         80         90        100        110        120 
KILVGMYDKK PVGPGPGPPA TPPQPQPSLP QGVHAPVPPA SQYSPMLPTA YQPQSDNVYL 

       130        140        150        160        170        180 
VPTPSKTQQG LYQAPGPNPQ FQSPPAKQTS TFSKQTPHHS FPSPATDLYQ VPPGPGSPAQ 

       190        200        210        220        230        240 
DIYQVPPSAG IGHDIYQVPP SLDTRGWEGT KPPAKVVVPT RVGQGYVYEA AQTEQDEYDT 

       250        260        270        280        290        300 
PRHLLAPGPQ DIYDVPPVRG LLPNQYGQEV YDTPPMAVKG PNGRDPLLDV YDVPPSVEKG 

       310        320        330        340        350        360 
LLSSSHHSVY DVPPSVSKDV PDGPLLREET YDVPPAFAKP KPFDPTRHPL ILAAPPPDSP 

       370        380        390        400        410        420 
AAEDVYDVPP PAPDLYDVPP GLRRPGPGTL YDVPRERVLP PEVADGSVVD DGVYAVPPPA 

       430        440        450        460        470        480 
EREAPTDGKR LSASSTGSTR SSQSASSLEV VVPGREPLEL EVAVESLARL QQGVSTTVAH 

       490        500        510        520        530        540 
LLDLVGSASG PGGWRGTSEP QEPPAQDLKA AVAAVHGAVH ELLEFARGAV SNATHTSDRT 

       550        560        570        580        590        600 
LHAKLSRQLQ KMEDVYQTLV VHGQVLDSGR GSPGFTPEDL DRLVACSRAV PEDAKQLASF 

       610        620        630        640        650        660 
LHGNASLLFR RTKAPGPGPE GSSSLHPNPT DKASSIQSRP LPSPPKFTSQ DSPDGQYENS 

       670        680        690        700        710        720 
EGGWMEDYDY VHLQGKEEFE KTQKELLERG NIMRQGKGQL ELQQLKQFER LEQEVSRPID 

       730        740        750        760        770        780 
HDLANWTPAQ PLVPGRTGGL GPSDRQLLLF YLEQCEANLT TLTDAVDAFF TAVATNQPPK 

       790        800        810        820        830        840 
IFVAHSKFVI LSAHKLVFIG DTLSRQAKAA DVRSQVTHYS NLLCDLLRGI VATTKAAALQ 

       850        860        870 
YPSPSAAQDM VDRVKELGHS TQQFRRVLGQ LAAA 

« Hide

Isoform Cas-A [UniParc].

Checksum: 25B8F5D1D61CC8B1
Show »

FASTA87494,392

References

« Hide 'large scale' references
[1]"Interaction between focal adhesion kinase and Crk-associated tyrosine kinase substrate p130Cas."
Polte T.R., Hanks S.K.
Proc. Natl. Acad. Sci. U.S.A. 92:10678-10682(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS CAS-A AND CAS-B), INTERACTION WITH PTK2/FAK1.
Tissue: Embryo.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Placenta.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
[4]"AND-34, a novel p130Cas-binding thymic stromal cell protein regulated by adhesion and inflammatory cytokines."
Cai D., Clayton L.K., Smolyar A., Lerner A.
J. Immunol. 163:2104-2112(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BCAR3.
[5]"Crk-associated substrate p130(Cas) interacts with nephrocystin and both proteins localize to cell-cell contacts of polarized epithelial cells."
Donaldson J.C., Dempsey P.J., Reddy S., Bouton A.H., Coffey R.J., Hanks S.K.
Exp. Cell Res. 256:168-178(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NPHP1.
[6]"p130Cas regulates the activity of AND-34, a novel Ral, Rap1, and R-Ras guanine nucleotide exchange factor."
Gotoh T., Cai D., Tian X., Feig L.A., Lerner A.
J. Biol. Chem. 275:30118-30123(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BCAR3.
[7]"Chat, a Cas/HEF1-associated adaptor protein that integrates multiple signaling pathways."
Sakakibara A., Hattori S.
J. Biol. Chem. 275:6404-6410(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SH2D3C.
[8]"A novel hematopoietic adaptor protein, Chat-H, positively regulates T cell receptor-mediated interleukin-2 production by Jurkat cells."
Sakakibara A., Hattori S., Nakamura S., Katagiri T.
J. Biol. Chem. 278:6012-6017(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SH2D3C.
Tissue: Spleen.
[9]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-132; TYR-366; TYR-376 AND TYR-414, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[11]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-253, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U48853 mRNA. Translation: AAA93381.1.
U28151 mRNA. Translation: AAA93248.1.
AK145863 mRNA. Translation: BAE26705.1.
BC057578 mRNA. Translation: AAH57578.1.
CCDSCCDS52675.1. [Q61140-1]
RefSeqNP_001185768.1. NM_001198839.1. [Q61140-2]
NP_034084.2. NM_009954.3. [Q61140-1]
UniGeneMm.3758.

3D structure databases

ProteinModelPortalQ61140.
SMRQ61140. Positions 5-71, 454-614, 743-874.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198886. 6 interactions.
IntActQ61140. 14 interactions.
MINTMINT-100691.

PTM databases

PhosphoSiteQ61140.

Proteomic databases

MaxQBQ61140.
PaxDbQ61140.
PRIDEQ61140.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000166232; ENSMUSP00000129584; ENSMUSG00000031955. [Q61140-1]
GeneID12927.
KEGGmmu:12927.
UCSCuc009nmt.2. mouse. [Q61140-2]
uc009nmu.2. mouse. [Q61140-1]

Organism-specific databases

CTD9564.
MGIMGI:108091. Bcar1.

Phylogenomic databases

eggNOGNOG82196.
GeneTreeENSGT00490000043324.
HOGENOMHOG000261698.
HOVERGENHBG004354.
KOK05726.
OMAFAKAKPF.
OrthoDBEOG7QRQTD.
TreeFamTF328782.

Gene expression databases

BgeeQ61140.
CleanExMM_BCAR1.
GenevestigatorQ61140.

Family and domain databases

InterProIPR028848. BCAR1.
IPR021901. CAS_DUF3513.
IPR014928. Serine_rich.
IPR001452. SH3_domain.
IPR013315. Spectrin_alpha_SH3.
[Graphical view]
PANTHERPTHR10654:SF5. PTHR10654:SF5. 1 hit.
PfamPF12026. DUF3513. 1 hit.
PF08824. Serine_rich. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00452. SH3DOMAIN.
PR01887. SPECTRNALPHA.
SMARTSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio282588.
PROQ61140.
SOURCESearch...

Entry information

Entry nameBCAR1_MOUSE
AccessionPrimary (citable) accession number: Q61140
Secondary accession number(s): Q60869, Q6PFF9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot