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P56945

- BCAR1_HUMAN

UniProt

P56945 - BCAR1_HUMAN

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Protein
Breast cancer anti-estrogen resistance protein 1
Gene
BCAR1, CAS, CASS1, CRKAS
Organism
Homo sapiens (Human)
Status
Reviewed - 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. Overexpression confers antiestrogen resistance on breast cancer cells.2 Publications

GO - Molecular functioni

  1. protein binding Source: UniProtKB
  2. protein kinase binding Source: UniProtKB
  3. signal transducer activity Source: ProtInc
Complete GO annotation...

GO - Biological processi

  1. B cell receptor signaling pathway Source: UniProtKB
  2. G-protein coupled receptor signaling pathway Source: UniProtKB
  3. T cell receptor signaling pathway Source: UniProtKB
  4. actin filament organization Source: UniProtKB
  5. antigen receptor-mediated signaling pathway Source: UniProtKB
  6. blood coagulation Source: Reactome
  7. cell adhesion Source: UniProtKB-KW
  8. cell chemotaxis Source: BHF-UCL
  9. cell division Source: UniProtKB
  10. cell migration Source: UniProtKB
  11. cell proliferation Source: ProtInc
  12. cellular response to hepatocyte growth factor stimulus Source: BHF-UCL
  13. epidermal growth factor receptor signaling pathway Source: UniProtKB
  14. hepatocyte growth factor receptor signaling pathway Source: BHF-UCL
  15. insulin receptor signaling pathway Source: UniProtKB
  16. integrin-mediated signaling pathway Source: UniProtKB
  17. neurotrophin TRK receptor signaling pathway Source: UniProtKB
  18. platelet activation Source: Reactome
  19. platelet-derived growth factor receptor signaling pathway Source: UniProtKB
  20. positive regulation of cell migration Source: UniProtKB
  21. positive regulation of endothelial cell migration Source: BHF-UCL
  22. regulation of apoptotic process Source: UniProtKB
  23. regulation of cell growth Source: UniProtKB
  24. vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_15381. p130Cas linkage to MAPK signaling for integrins.
REACT_17025. Downstream signal transduction.
SignaLinkiP56945.

Names & Taxonomyi

Protein namesi
Recommended name:
Breast cancer anti-estrogen resistance protein 1
Alternative name(s):
CRK-associated substrate
Cas scaffolding protein family member 1
p130cas
Gene namesi
Name:BCAR1
Synonyms:CAS, CASS1, CRKAS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:971. BCAR1.

Subcellular locationi

Cell junctionfocal adhesion. Cytoplasm
Note: Unphosphorylated form localizes in the cytoplasm and can move to the membrane upon tyrosine phosphorylation By similarity.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. focal adhesion Source: UniProtKB
  4. lamellipodium Source: Ensembl
  5. nucleolus Source: HPA
  6. plasma membrane Source: HPA
  7. ruffle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25281.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 870870Breast cancer anti-estrogen resistance protein 1
PRO_0000064854Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei128 – 1281Phosphotyrosine; by SRC1 Publication
Modified residuei134 – 1341Phosphoserine2 Publications
Modified residuei139 – 1391Phosphoserine3 Publications
Modified residuei249 – 2491Phosphotyrosine; by ABL1 By similarity
Modified residuei269 – 2691Phosphothreonine1 Publication
Modified residuei292 – 2921Phosphoserine1 Publication
Modified residuei362 – 3621Phosphotyrosine By similarity
Modified residuei372 – 3721Phosphotyrosine By similarity
Modified residuei410 – 4101Phosphotyrosine By similarity
Modified residuei428 – 4281Phosphoserine1 Publication
Modified residuei437 – 4371Phosphoserine1 Publication
Modified residuei639 – 6391Phosphoserine1 Publication

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.4 Publications
Dephosphorylated by PTPN14 at Tyr-128.4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP56945.
PaxDbiP56945.
PRIDEiP56945.

PTM databases

PhosphoSiteiP56945.

Expressioni

Tissue specificityi

Widely expressed with an abundant expression in the testis. Low level of expression seen in the liver, thymus, and peripheral blood leukocytes. The protein has been detected in a B-cell line.

Gene expression databases

ArrayExpressiP56945.
BgeeiP56945.
CleanExiHS_BCAR1.
GenevestigatoriP56945.

Organism-specific databases

HPAiCAB000443.
HPA042282.

Interactioni

Subunit structurei

Forms complexes in vivo with PTK2/FAK1, adapter protein CRKL and LYN kinase. Can heterodimerize with NEDD9. Interacts with BCAR3, the interaction regulates adhesion-dependent serine phosphorylation. Interacts with NPHP1 and SH2D3C. Interacts with activated CSPG4. Interacts with BMX, INPPL1/SHIP2 and PEAK1. Part of a collagen-stimulated complex involved in cell migration made of CDC42, CRK, TNK2 and BCAR1/p130cas. Interacts with TNK2 via SH3 domains. Interacts with PTK2B/PYK2.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CRKP461085EBI-702093,EBI-886
FYNP062413EBI-702093,EBI-515315
INPPL1O153572EBI-702093,EBI-1384248
MMP14P502813EBI-702093,EBI-992788
PTK2Q053972EBI-702093,EBI-702142
PTPN1P180315EBI-702093,EBI-968788
PTPN12Q052094EBI-702093,EBI-2266035
SRCP129313EBI-702093,EBI-621482
SRCIN1Q9C0H93EBI-702093,EBI-1393949
Srcin1Q9QWI63EBI-702093,EBI-775592From a different organism.
TNK2Q079125EBI-702093,EBI-603457
TNSQ042052EBI-702093,EBI-2607590From a different organism.
TNS3Q68CZ28EBI-702093,EBI-1220488

Protein-protein interaction databases

BioGridi114934. 64 interactions.
DIPiDIP-33855N.
IntActiP56945. 32 interactions.
MINTiMINT-1505539.
STRINGi9606.ENSP00000162330.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 128
Beta strandi29 – 346
Helixi37 – 393
Beta strandi43 – 486
Beta strandi51 – 566
Helixi57 – 593
Beta strandi60 – 689
Helixi740 – 77031
Helixi775 – 80127
Helixi806 – 83530
Helixi840 – 87031

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WYXX-ray1.14A/B3-71[»]
3T6GX-ray2.50B/D645-870[»]
ProteinModelPortaliP56945.
SMRiP56945. Positions 3-71, 448-610, 739-870.

Miscellaneous databases

EvolutionaryTraceiP56945.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 6563SH3
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni115 – 416302Substrate for kinases By similarity
Add
BLAST
Regioni746 – 79651Divergent helix-loop-helix motif
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi635 – 6439SH3-binding Reviewed prediction

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi74 – 8714Pro-rich
Add
BLAST
Compositional biasi422 – 614193Ser-rich
Add
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 ABL1 SH2 domains. The HLH motif is absolutely required for the induction of pseudohyphal growth in yeast and mediates heterodimerization with NEDD9 (By similarity).
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/FAK11.

Sequence similaritiesi

Belongs to the CAS family.
Contains 1 SH3 domain.

Keywords - Domaini

SH3 domain, SH3-binding

Phylogenomic databases

eggNOGiNOG82196.
HOGENOMiHOG000261698.
HOVERGENiHBG004354.
KOiK05726.
OMAiFAKAKPF.
OrthoDBiEOG7QRQTD.
PhylomeDBiP56945.
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 (8)i

Sequence statusi: Complete.

This entry describes 8 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P56945-1) [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

MNHLNVLAKA LYDNVAESPD ELSFRKGDIM TVLEQDTQGL DGWWLCSLHG    50
RQGIVPGNRL KILVGMYDKK PAGPGPGPPA TPAQPQPGLH APAPPASQYT 100
PMLPNTYQPQ PDSVYLVPTP SKAQQGLYQV PGPSPQFQSP PAKQTSTFSK 150
QTPHHPFPSP ATDLYQVPPG PGGPAQDIYQ VPPSAGMGHD IYQVPPSMDT 200
RSWEGTKPPA KVVVPTRVGQ GYVYEAAQPE QDEYDIPRHL LAPGPQDIYD 250
VPPVRGLLPS QYGQEVYDTP PMAVKGPNGR DPLLEVYDVP PSVEKGLPPS 300
NHHAVYDVPP SVSKDVPDGP LLREETYDVP PAFAKAKPFD PARTPLVLAA 350
PPPDSPPAED VYDVPPPAPD LYDVPPGLRR PGPGTLYDVP RERVLPPEVA 400
DGGVVDSGVY AVPPPAEREA PAEGKRLSAS STGSTRSSQS ASSLEVAGPG 450
REPLELEVAV EALARLQQGV SATVAHLLDL AGSAGATGSW RSPSEPQEPL 500
VQDLQAAVAA VQSAVHELLE FARSAVGNAA HTSDRALHAK LSRQLQKMED 550
VHQTLVAHGQ ALDAGRGGSG ATLEDLDRLV ACSRAVPEDA KQLASFLHGN 600
ASLLFRRTKA TAPGPEGGGT LHPNPTDKTS SIQSRPLPSP PKFTSQDSPD 650
GQYENSEGGW MEDYDYVHLQ GKEEFEKTQK ELLEKGSITR QGKSQLELQQ 700
LKQFERLEQE VSRPIDHDLA NWTPAQPLAP GRTGGLGPSD RQLLLFYLEQ 750
CEANLTTLTN AVDAFFTAVA TNQPPKIFVA HSKFVILSAH KLVFIGDTLS 800
RQAKAADVRS QVTHYSNLLC DLLRGIVATT KAAALQYPSP SAAQDMVERV 850
KELGHSTQQF RRVLGQLAAA 870
Length:870
Mass (Da):93,372
Last modified:February 9, 2010 - v2
Checksum:iB81EC3430049E795
GO
Isoform 2 (identifier: P56945-2) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:888
Mass (Da):95,469
Checksum:i4CA6EC5C8EFE3DA6
GO
Isoform 3 (identifier: P56945-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     304-304: A → AVSKCQGNARARLRLWGVW

Show »
Length:888
Mass (Da):95,454
Checksum:iFF81642D11EB93AC
GO
Isoform 4 (identifier: P56945-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: MNHL → MQGK
     64-211: Missing.

Note: No experimental confirmation available.

Show »
Length:722
Mass (Da):77,731
Checksum:i2537ED6C3BEBE512
GO
Isoform 5 (identifier: P56945-5) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:868
Mass (Da):93,137
Checksum:iDB6B70B2AB1926CD
GO
Isoform 6 (identifier: P56945-6) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:916
Mass (Da):97,877
Checksum:i3A5FDEB4BA15527B
GO
Isoform 7 (identifier: P56945-7) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:888
Mass (Da):95,216
Checksum:iCD3BA8494536FC76
GO
Isoform 8 (identifier: P56945-8) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:870
Mass (Da):93,291
Checksum:i2262F3718326A675
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti76 – 761P → S.4 Publications
Corresponds to variant rs1035539 [ dbSNP | Ensembl ].
VAR_058970
Natural varianti407 – 4071S → T in a breast cancer sample; somatic mutation. 1 Publication
VAR_035798
Natural varianti491 – 4911R → L.
Corresponds to variant rs16957558 [ dbSNP | Ensembl ].
VAR_057820
Natural varianti558 – 5581H → R.
Corresponds to variant rs16957552 [ dbSNP | Ensembl ].
VAR_057821

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 44MNHL → MLTHRPQEAEQRGRTPGPSF EW in isoform 2.
VSP_043559
Alternative sequencei1 – 44MNHL → MQGK in isoform 4.
VSP_046127
Alternative sequencei1 – 44MNHL → ME in isoform 5.
VSP_046748
Alternative sequencei1 – 44MNHL → MPAKPFLSSVLLSWKVLDFS GPGPQGTGQPCSCGHWAEGQ GGPPEPAGGP in isoform 6.
VSP_046749
Alternative sequencei1 – 44MNHL → MHCPGEAPLAAPRPTPKDPC LR in isoform 7.
VSP_046750
Alternative sequencei1 – 44MNHL → MSVP in isoform 8.
VSP_046751
Alternative sequencei64 – 211148Missing in isoform 4.
VSP_046128Add
BLAST
Alternative sequencei304 – 3041A → AVSKCQGNARARLRLWGVW in isoform 3.
VSP_045355

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti63 – 631L → S in BAB55230. 1 Publication
Sequence conflicti236 – 2361I → T in AAF27527. 1 Publication
Sequence conflicti254 – 2541V → I in BAG54099. 1 Publication
Sequence conflicti349 – 3491A → G in AAF27527. 1 Publication
Sequence conflicti363 – 3631D → Y in AAF27527. 1 Publication
Sequence conflicti385 – 3851T → A in AAS48631. 1 Publication
Sequence conflicti428 – 4281S → P in BAB55230. 1 Publication
Sequence conflicti471 – 4711S → G in BAB55230. 1 Publication
Sequence conflicti600 – 6001N → S in AAS48631. 1 Publication
Sequence conflicti700 – 7001Q → R in BAH13763. 1 Publication
Sequence conflicti714 – 7141P → L in BAG54099. 1 Publication
Sequence conflicti740 – 7401D → G in AAS48631. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ242987 mRNA. Translation: CAB75875.2.
AF218451 mRNA. Translation: AAF27527.1.
AB040024 mRNA. Translation: BAA92711.1.
AY545071 mRNA. Translation: AAS48631.1.
AK027608 mRNA. Translation: BAB55230.1.
AK124815 mRNA. Translation: BAG54099.1.
AK293808 mRNA. Translation: BAG57215.1.
AK294513 mRNA. Translation: BAG57726.1.
AK295809 mRNA. Translation: BAG58627.1.
AK302617 mRNA. Translation: BAH13763.1.
AC009078 Genomic DNA. No translation available.
CCDSiCCDS10915.1. [P56945-1]
CCDS54037.1. [P56945-5]
CCDS54038.1. [P56945-3]
CCDS54039.1. [P56945-4]
CCDS54040.1. [P56945-6]
CCDS54041.1. [P56945-8]
CCDS54042.1. [P56945-2]
CCDS54043.1. [P56945-7]
RefSeqiNP_001164185.1. NM_001170714.1. [P56945-6]
NP_001164186.1. NM_001170715.1. [P56945-7]
NP_001164187.1. NM_001170716.1. [P56945-2]
NP_001164188.1. NM_001170717.1. [P56945-3]
NP_001164189.1. NM_001170718.1. [P56945-8]
NP_001164190.1. NM_001170719.1. [P56945-5]
NP_001164191.1. NM_001170720.1. [P56945-4]
NP_001164192.1. NM_001170721.1.
NP_055382.2. NM_014567.3. [P56945-1]
XP_006721411.1. XM_006721348.1. [P56945-6]
UniGeneiHs.479747.

Genome annotation databases

EnsembliENST00000162330; ENSP00000162330; ENSG00000050820. [P56945-1]
ENST00000393420; ENSP00000377072; ENSG00000050820. [P56945-3]
ENST00000393422; ENSP00000377074; ENSG00000050820. [P56945-7]
ENST00000418647; ENSP00000391669; ENSG00000050820. [P56945-6]
ENST00000420641; ENSP00000392708; ENSG00000050820. [P56945-2]
ENST00000535626; ENSP00000440370; ENSG00000050820. [P56945-4]
ENST00000538440; ENSP00000443841; ENSG00000050820. [P56945-8]
ENST00000542031; ENSP00000440415; ENSG00000050820. [P56945-5]
GeneIDi9564.
KEGGihsa:9564.
UCSCiuc002fdv.3. human. [P56945-1]
uc010vnd.2. human. [P56945-2]

Polymorphism databases

DMDMi288558806.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ242987 mRNA. Translation: CAB75875.2 .
AF218451 mRNA. Translation: AAF27527.1 .
AB040024 mRNA. Translation: BAA92711.1 .
AY545071 mRNA. Translation: AAS48631.1 .
AK027608 mRNA. Translation: BAB55230.1 .
AK124815 mRNA. Translation: BAG54099.1 .
AK293808 mRNA. Translation: BAG57215.1 .
AK294513 mRNA. Translation: BAG57726.1 .
AK295809 mRNA. Translation: BAG58627.1 .
AK302617 mRNA. Translation: BAH13763.1 .
AC009078 Genomic DNA. No translation available.
CCDSi CCDS10915.1. [P56945-1 ]
CCDS54037.1. [P56945-5 ]
CCDS54038.1. [P56945-3 ]
CCDS54039.1. [P56945-4 ]
CCDS54040.1. [P56945-6 ]
CCDS54041.1. [P56945-8 ]
CCDS54042.1. [P56945-2 ]
CCDS54043.1. [P56945-7 ]
RefSeqi NP_001164185.1. NM_001170714.1. [P56945-6 ]
NP_001164186.1. NM_001170715.1. [P56945-7 ]
NP_001164187.1. NM_001170716.1. [P56945-2 ]
NP_001164188.1. NM_001170717.1. [P56945-3 ]
NP_001164189.1. NM_001170718.1. [P56945-8 ]
NP_001164190.1. NM_001170719.1. [P56945-5 ]
NP_001164191.1. NM_001170720.1. [P56945-4 ]
NP_001164192.1. NM_001170721.1.
NP_055382.2. NM_014567.3. [P56945-1 ]
XP_006721411.1. XM_006721348.1. [P56945-6 ]
UniGenei Hs.479747.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1WYX X-ray 1.14 A/B 3-71 [» ]
3T6G X-ray 2.50 B/D 645-870 [» ]
ProteinModelPortali P56945.
SMRi P56945. Positions 3-71, 448-610, 739-870.
ModBasei Search...

Protein-protein interaction databases

BioGridi 114934. 64 interactions.
DIPi DIP-33855N.
IntActi P56945. 32 interactions.
MINTi MINT-1505539.
STRINGi 9606.ENSP00000162330.

PTM databases

PhosphoSitei P56945.

Polymorphism databases

DMDMi 288558806.

Proteomic databases

MaxQBi P56945.
PaxDbi P56945.
PRIDEi P56945.

Protocols and materials databases

DNASUi 9564.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000162330 ; ENSP00000162330 ; ENSG00000050820 . [P56945-1 ]
ENST00000393420 ; ENSP00000377072 ; ENSG00000050820 . [P56945-3 ]
ENST00000393422 ; ENSP00000377074 ; ENSG00000050820 . [P56945-7 ]
ENST00000418647 ; ENSP00000391669 ; ENSG00000050820 . [P56945-6 ]
ENST00000420641 ; ENSP00000392708 ; ENSG00000050820 . [P56945-2 ]
ENST00000535626 ; ENSP00000440370 ; ENSG00000050820 . [P56945-4 ]
ENST00000538440 ; ENSP00000443841 ; ENSG00000050820 . [P56945-8 ]
ENST00000542031 ; ENSP00000440415 ; ENSG00000050820 . [P56945-5 ]
GeneIDi 9564.
KEGGi hsa:9564.
UCSCi uc002fdv.3. human. [P56945-1 ]
uc010vnd.2. human. [P56945-2 ]

Organism-specific databases

CTDi 9564.
GeneCardsi GC16M075262.
H-InvDB HIX0173293.
HGNCi HGNC:971. BCAR1.
HPAi CAB000443.
HPA042282.
MIMi 602941. gene.
neXtProti NX_P56945.
PharmGKBi PA25281.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG82196.
HOGENOMi HOG000261698.
HOVERGENi HBG004354.
KOi K05726.
OMAi FAKAKPF.
OrthoDBi EOG7QRQTD.
PhylomeDBi P56945.
TreeFami TF328782.

Enzyme and pathway databases

Reactomei REACT_15381. p130Cas linkage to MAPK signaling for integrins.
REACT_17025. Downstream signal transduction.
SignaLinki P56945.

Miscellaneous databases

ChiTaRSi BCAR1. human.
EvolutionaryTracei P56945.
GeneWikii BCAR1.
GenomeRNAii 9564.
NextBioi 35471708.
PROi P56945.
SOURCEi Search...

Gene expression databases

ArrayExpressi P56945.
Bgeei P56945.
CleanExi HS_BCAR1.
Genevestigatori P56945.

Family and domain databases

InterProi IPR028848. BCAR1.
IPR021901. CAS_DUF3513.
IPR014928. Serine_rich.
IPR001452. SH3_domain.
IPR013315. Spectrin_alpha_SH3.
[Graphical view ]
PANTHERi PTHR10654:SF5. PTHR10654:SF5. 1 hit.
Pfami PF12026. DUF3513. 1 hit.
PF08824. Serine_rich. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view ]
PRINTSi PR00452. SH3DOMAIN.
PR01887. SPECTRNALPHA.
SMARTi SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
PROSITEi PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "BCAR1, a human homologue of the adapter protein p130Cas, induces anti-estrogen resistance in breast cancer cells."
    Brinkman A., van der Flier S., Kok E.M., Dorssers L.C.J.
    J. Natl. Cancer Inst. 92:112-120(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-76.
    Tissue: Mammary cancer.
  2. "Interaction between human Crk-associated substrate (p130Cas) and nephrocystin."
    Otto E., Birnbaum S., Verbeek M., Hildebrandt F.
    Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-76.
    Tissue: Testis.
  3. "The effects of growth factors on tyrosine phosphorylation of p130Cas in corneal epithelial cell."
    Imoto Y., Ohguro N., Yoshida A., Tsujikawa M., Inoue Y., Tano Y.
    Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-76.
    Tissue: Cornea.
  4. Lin L., Li H., Zhou G., Shen C., Ke R., Zhong G., Yang S.
    Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 4; 5; 6; 7 AND 8), VARIANT SER-76.
    Tissue: Amygdala, Caudate nucleus, Cerebellum, Hippocampus, Teratocarcinoma and Testis.
  6. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Bienvenut W.V., Lempens A., Norman J.C.
    Submitted (OCT-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-9; 380-391 AND 792-801, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Ovarian carcinoma.
  8. "Melanoma chondroitin sulphate proteoglycan regulates cell spreading through Cdc42, Ack-1 and p130cas."
    Eisenmann K.M., McCarthy J.B., Simpson M.A., Keely P.J., Guan J.-L., Tachibana K., Lim L., Manser E., Furcht L.T., Iida J.
    Nat. Cell Biol. 1:507-513(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CSPG4.
  9. "SH2-containing inositol 5'-phosphatase SHIP2 associates with the p130(Cas) adapter protein and regulates cellular adhesion and spreading."
    Prasad N., Topping R.S., Decker S.J.
    Mol. Cell. Biol. 21:1416-1428(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH INPPL1.
  10. "p130Cas Couples the tyrosine kinase Bmx/Etk with regulation of the actin cytoskeleton and cell migration."
    Abassi Y.A., Rehn M., Ekman N., Alitalo K., Vuori K.
    J. Biol. Chem. 278:35636-35643(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH BMX.
  11. "Ack1 mediates Cdc42-dependent cell migration and signaling to p130Cas."
    Modzelewska K., Newman L.P., Desai R., Keely P.J.
    J. Biol. Chem. 281:37527-37535(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL MIGRATION, INTERACTION WITH BCAR1; CDC42 AND CRK.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134; SER-139; THR-269 AND SER-292, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "AND-34/BCAR3 regulates adhesion-dependent p130Cas serine phosphorylation and breast cancer cell growth pattern."
    Makkinje A., Near R.I., Infusini G., Vanden Borre P., Bloom A., Cai D., Costello C.E., Lerner A.
    Cell. Signal. 21:1423-1435(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-139; SER-437 AND SER-639, INTERACTION WITH BCAR3.
  14. "Pyk2 mediates endothelin-1 signaling via p130Cas/BCAR3 cascade and regulates human glomerular mesangial cell adhesion and spreading."
    Rufanova V.A., Alexanian A., Wakatsuki T., Lerner A., Sorokin A.
    J. Cell. Physiol. 219:45-56(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PTK2B/PYK2.
  15. "Ras- and PI3K-dependent breast tumorigenesis in mice and humans requires focal adhesion kinase signaling."
    Pylayeva Y., Gillen K.M., Gerald W., Beggs H.E., Reichardt L.F., Giancotti F.G.
    J. Clin. Invest. 119:252-266(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY SRC UPON ACTIVATION OF PTK2/FAK1.
  16. Cited for: INTERACTION WITH PEAK1.
  17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134 AND SER-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Identification and functional characterization of p130Cas as a substrate of protein tyrosine phosphatase nonreceptor 14."
    Zhang P., Guo A., Possemato A., Wang C., Beard L., Carlin C., Markowitz S.D., Polakiewicz R.D., Wang Z.
    Oncogene 32:2087-2095(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEPHOSPHORYLATION BY PTPN14 AT TYR-128, PHOSPHORYLATION AT TYR-128 BY SRC.
  20. "The 1.1 A resolution crystal structure of the p130cas SH3 domain and ramifications for ligand selectivity."
    Wisniewska M., Bossenmaier B., Georges G., Hesse F., Dangl M., Kunkele K.P., Ioannidis I., Huber R., Engh R.A.
    J. Mol. Biol. 347:1005-1014(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.14 ANGSTROMS) OF 3-71.
  21. "NSP-Cas protein structures reveal a promiscuous interaction module in cell signaling."
    Mace P.D., Wallez Y., Dobaczewska M.K., Lee J.J., Robinson H., Pasquale E.B., Riedl S.J.
    Nat. Struct. Mol. Biol. 18:1381-1387(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 645-870 IN COMPLEX WITH SH2D3C.
  22. Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-407.

Entry informationi

Entry nameiBCAR1_HUMAN
AccessioniPrimary (citable) accession number: P56945
Secondary accession number(s): B3KWD7
, B4DEV4, B4DGB5, B4DIW5, B7Z7X7, E9PCL5, E9PCV2, F5GXA2, F5GXV6, F5H7Z0, F8WA69, Q6QEF7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: February 9, 2010
Last modified: September 3, 2014
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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