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Q61140 - BCAR1_MOUSE

UniProt

Q61140 - BCAR1_MOUSE

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Protein

Breast cancer anti-estrogen resistance protein 1

Gene

Bcar1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity

GO - Molecular functioni

  1. protein kinase binding Source: MGI
  2. signal transducer activity Source: InterPro

GO - Biological processi

  1. actin filament organization Source: UniProtKB
  2. antigen receptor-mediated signaling pathway Source: UniProtKB
  3. B cell receptor signaling pathway Source: UniProtKB
  4. cell adhesion Source: UniProtKB-KW
  5. cell chemotaxis Source: MGI
  6. cell migration Source: UniProtKB
  7. cellular response to hepatocyte growth factor stimulus Source: MGI
  8. epidermal growth factor receptor signaling pathway Source: UniProtKB
  9. G-protein coupled receptor signaling pathway Source: UniProtKB
  10. hepatocyte growth factor receptor signaling pathway Source: MGI
  11. insulin receptor signaling pathway Source: UniProtKB
  12. integrin-mediated signaling pathway Source: UniProtKB
  13. neurotrophin TRK receptor signaling pathway Source: UniProtKB
  14. platelet-derived growth factor receptor signaling pathway Source: UniProtKB
  15. positive regulation of cell migration Source: UniProtKB
  16. positive regulation of endothelial cell migration Source: MGI
  17. vascular endothelial growth factor receptor signaling pathway Source: MGI
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_230639. Downstream signal transduction.
REACT_240371. p130Cas linkage to MAPK signaling for integrins.
REACT_257088. VEGFA-VEGFR2 Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Breast cancer anti-estrogen resistance protein 1
Alternative name(s):
CRK-associated substrate
p130cas
Gene namesi
Name:Bcar1
Synonyms:Cas, Crkas
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:108091. Bcar1.

Subcellular locationi

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

GO - Cellular componenti

  1. actin cytoskeleton Source: MGI
  2. cytoplasm Source: UniProtKB
  3. focal adhesion Source: UniProtKB
  4. lamellipodium Source: MGI
  5. nucleolus Source: MGI
  6. plasma membrane Source: MGI
  7. ruffle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 874874Breast cancer anti-estrogen resistance protein 1PRO_0000064855Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei132 – 1321Phosphotyrosine1 Publication
Modified residuei143 – 1431PhosphoserineBy similarity
Modified residuei253 – 2531Phosphotyrosine; by ABL1By similarity
Modified residuei273 – 2731PhosphothreonineBy similarity
Modified residuei296 – 2961PhosphoserineBy similarity
Modified residuei366 – 3661Phosphotyrosine1 Publication
Modified residuei376 – 3761Phosphotyrosine1 Publication
Modified residuei414 – 4141Phosphotyrosine1 Publication
Modified residuei432 – 4321PhosphoserineBy similarity
Modified residuei441 – 4411PhosphoserineBy similarity
Modified residuei643 – 6431PhosphoserineBy similarity

Post-translational modificationi

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).By similarity
Dephosphorylated by PTPN14 at Tyr-132.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ61140.
PaxDbiQ61140.
PRIDEiQ61140.

PTM databases

PhosphoSiteiQ61140.

Expressioni

Gene expression databases

BgeeiQ61140.
CleanExiMM_BCAR1.
GenevestigatoriQ61140.

Interactioni

Subunit structurei

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.By similarity6 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi198886. 6 interactions.
IntActiQ61140. 14 interactions.
MINTiMINT-100691.

Structurei

3D structure databases

ProteinModelPortaliQ61140.
SMRiQ61140. Positions 5-71, 454-614, 743-874.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 2621SH3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni119 – 420302Substrate for kinasesBy similarityAdd
BLAST
Regioni750 – 80051Divergent helix-loop-helix motifAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi639 – 6479SH3-bindingSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi74 – 8714Pro-richAdd
BLAST
Compositional biasi426 – 618193Ser-richAdd
BLAST

Domaini

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.

Sequence similaritiesi

Belongs to the CAS family.Curated
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH3 domain, SH3-binding

Phylogenomic databases

eggNOGiNOG82196.
GeneTreeiENSGT00490000043324.
HOGENOMiHOG000261698.
HOVERGENiHBG004354.
InParanoidiQ61140.
KOiK05726.
OMAiAKAKPFD.
OrthoDBiEOG7QRQTD.
TreeFamiTF328782.

Family and domain databases

InterProiIPR028848. BCAR1.
IPR021901. CAS_DUF3513.
IPR014928. Serine_rich.
IPR001452. SH3_domain.
IPR013315. Spectrin_alpha_SH3.
[Graphical view]
PANTHERiPTHR10654:SF5. PTHR10654:SF5. 1 hit.
PfamiPF12026. DUF3513. 1 hit.
PF08824. Serine_rich. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
PR01887. SPECTRNALPHA.
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS50002. SH3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform Cas-B (identifier: Q61140-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MTVPNVLAKA LYDNVAESPD ELSFRKGDIM TVLERDTQGL DGWWLCSLHG 
        60         70         80         90        100
RQGIVPGNRL KILVGMYDKK PVGPGPGPPA TPPQPQPSLP QGVHAPVPPA 
       110        120        130        140        150
SQYSPMLPTA YQPQSDNVYL VPTPSKTQQG LYQAPGPNPQ FQSPPAKQTS 
       160        170        180        190        200
TFSKQTPHHS FPSPATDLYQ VPPGPGSPAQ DIYQVPPSAG IGHDIYQVPP 
       210        220        230        240        250
SLDTRGWEGT KPPAKVVVPT RVGQGYVYEA AQTEQDEYDT PRHLLAPGPQ 
       260        270        280        290        300
DIYDVPPVRG LLPNQYGQEV YDTPPMAVKG PNGRDPLLDV YDVPPSVEKG 
       310        320        330        340        350
LLSSSHHSVY DVPPSVSKDV PDGPLLREET YDVPPAFAKP KPFDPTRHPL 
       360        370        380        390        400
ILAAPPPDSP AAEDVYDVPP PAPDLYDVPP GLRRPGPGTL YDVPRERVLP 
       410        420        430        440        450
PEVADGSVVD DGVYAVPPPA EREAPTDGKR LSASSTGSTR SSQSASSLEV 
       460        470        480        490        500
VVPGREPLEL EVAVESLARL QQGVSTTVAH LLDLVGSASG PGGWRGTSEP 
       510        520        530        540        550
QEPPAQDLKA AVAAVHGAVH ELLEFARGAV SNATHTSDRT LHAKLSRQLQ 
       560        570        580        590        600
KMEDVYQTLV VHGQVLDSGR GSPGFTPEDL DRLVACSRAV PEDAKQLASF 
       610        620        630        640        650
LHGNASLLFR RTKAPGPGPE GSSSLHPNPT DKASSIQSRP LPSPPKFTSQ 
       660        670        680        690        700
DSPDGQYENS EGGWMEDYDY VHLQGKEEFE KTQKELLERG NIMRQGKGQL 
       710        720        730        740        750
ELQQLKQFER LEQEVSRPID HDLANWTPAQ PLVPGRTGGL GPSDRQLLLF 
       760        770        780        790        800
YLEQCEANLT TLTDAVDAFF TAVATNQPPK IFVAHSKFVI LSAHKLVFIG 
       810        820        830        840        850
DTLSRQAKAA DVRSQVTHYS NLLCDLLRGI VATTKAAALQ YPSPSAAQDM 
       860        870 
VDRVKELGHS TQQFRRVLGQ LAAA
Length:874
Mass (Da):94,285
Last modified:July 27, 2011 - v2
Checksum:i81E56BC7AD87B095
GO
Isoform Cas-A (identifier: Q61140-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:874
Mass (Da):94,392
Checksum:i25B8F5D1D61CC8B1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti72 – 721V → A in AAA93381. (PubMed:7479864)Curated
Sequence conflicti72 – 721V → A in AAA93248. (PubMed:7479864)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 44MTVP → MKYL in isoform Cas-A. 1 PublicationVSP_004134

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U48853 mRNA. Translation: AAA93381.1.
U28151 mRNA. Translation: AAA93248.1.
AK145863 mRNA. Translation: BAE26705.1.
BC057578 mRNA. Translation: AAH57578.1.
CCDSiCCDS52675.1. [Q61140-1]
RefSeqiNP_001185768.1. NM_001198839.1. [Q61140-2]
NP_034084.2. NM_009954.3. [Q61140-1]
UniGeneiMm.3758.

Genome annotation databases

EnsembliENSMUST00000166232; ENSMUSP00000129584; ENSMUSG00000031955. [Q61140-1]
GeneIDi12927.
KEGGimmu:12927.
UCSCiuc009nmt.2. mouse. [Q61140-2]
uc009nmu.2. mouse. [Q61140-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U48853 mRNA. Translation: AAA93381.1.
U28151 mRNA. Translation: AAA93248.1.
AK145863 mRNA. Translation: BAE26705.1.
BC057578 mRNA. Translation: AAH57578.1.
CCDSiCCDS52675.1. [Q61140-1]
RefSeqiNP_001185768.1. NM_001198839.1. [Q61140-2]
NP_034084.2. NM_009954.3. [Q61140-1]
UniGeneiMm.3758.

3D structure databases

ProteinModelPortaliQ61140.
SMRiQ61140. Positions 5-71, 454-614, 743-874.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198886. 6 interactions.
IntActiQ61140. 14 interactions.
MINTiMINT-100691.

PTM databases

PhosphoSiteiQ61140.

Proteomic databases

MaxQBiQ61140.
PaxDbiQ61140.
PRIDEiQ61140.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000166232; ENSMUSP00000129584; ENSMUSG00000031955. [Q61140-1]
GeneIDi12927.
KEGGimmu:12927.
UCSCiuc009nmt.2. mouse. [Q61140-2]
uc009nmu.2. mouse. [Q61140-1]

Organism-specific databases

CTDi9564.
MGIiMGI:108091. Bcar1.

Phylogenomic databases

eggNOGiNOG82196.
GeneTreeiENSGT00490000043324.
HOGENOMiHOG000261698.
HOVERGENiHBG004354.
InParanoidiQ61140.
KOiK05726.
OMAiAKAKPFD.
OrthoDBiEOG7QRQTD.
TreeFamiTF328782.

Enzyme and pathway databases

ReactomeiREACT_230639. Downstream signal transduction.
REACT_240371. p130Cas linkage to MAPK signaling for integrins.
REACT_257088. VEGFA-VEGFR2 Pathway.

Miscellaneous databases

NextBioi282588.
PROiQ61140.
SOURCEiSearch...

Gene expression databases

BgeeiQ61140.
CleanExiMM_BCAR1.
GenevestigatoriQ61140.

Family and domain databases

InterProiIPR028848. BCAR1.
IPR021901. CAS_DUF3513.
IPR014928. Serine_rich.
IPR001452. SH3_domain.
IPR013315. Spectrin_alpha_SH3.
[Graphical view]
PANTHERiPTHR10654:SF5. PTHR10654:SF5. 1 hit.
PfamiPF12026. DUF3513. 1 hit.
PF08824. Serine_rich. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
PR01887. SPECTRNALPHA.
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiBCAR1_MOUSE
AccessioniPrimary (citable) accession number: Q61140
Secondary accession number(s): Q60869, Q6PFF9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 27, 2011
Last modified: February 4, 2015
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.