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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

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 kinase binding Source: UniProtKB
  2. signal transducer activity Source: ProtInc

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. blood coagulation Source: Reactome
  5. cell adhesion Source: UniProtKB-KW
  6. cell chemotaxis Source: BHF-UCL
  7. cell division Source: UniProtKB
  8. cell migration Source: UniProtKB
  9. cell proliferation Source: ProtInc
  10. cellular response to hepatocyte growth factor stimulus Source: BHF-UCL
  11. epidermal growth factor receptor signaling pathway Source: UniProtKB
  12. G-protein coupled receptor signaling pathway Source: UniProtKB
  13. hepatocyte growth factor receptor signaling pathway Source: BHF-UCL
  14. insulin receptor signaling pathway Source: UniProtKB
  15. integrin-mediated signaling pathway Source: UniProtKB
  16. neurotrophin TRK receptor signaling pathway Source: UniProtKB
  17. platelet activation Source: Reactome
  18. platelet-derived growth factor receptor signaling pathway Source: UniProtKB
  19. positive regulation of cell migration Source: UniProtKB
  20. positive regulation of endothelial cell migration Source: BHF-UCL
  21. regulation of apoptotic process Source: UniProtKB
  22. regulation of cell growth Source: UniProtKB
  23. T cell receptor signaling pathway 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.
REACT_228166. VEGFA-VEGFR2 Pathway.
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 1 Publication. Cytoplasm 1 Publication
Note: Unphosphorylated form localizes in the cytoplasm and can move to the membrane upon tyrosine phosphorylation.By similarity

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 1PRO_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 ABL1By similarity
Modified residuei269 – 2691Phosphothreonine1 Publication
Modified residuei292 – 2921Phosphoserine1 Publication
Modified residuei362 – 3621PhosphotyrosineBy similarity
Modified residuei372 – 3721PhosphotyrosineBy similarity
Modified residuei410 – 4101PhosphotyrosineBy 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.7 Publications
Dephosphorylated by PTPN14 at Tyr-128.

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

BgeeiP56945.
CleanExiHS_BCAR1.
ExpressionAtlasiP56945. baseline and differential.
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/PYK2.8 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

1
870
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 128Combined sources
Beta strandi29 – 346Combined sources
Helixi37 – 393Combined sources
Beta strandi43 – 486Combined sources
Beta strandi51 – 566Combined sources
Helixi57 – 593Combined sources
Beta strandi60 – 689Combined sources
Helixi740 – 77031Combined sources
Helixi775 – 80127Combined sources
Helixi806 – 83530Combined sources
Helixi840 – 87031Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP56945.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 6563SH3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni115 – 416302Substrate for kinasesBy similarityAdd
BLAST
Regioni746 – 79651Divergent helix-loop-helix motifAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi635 – 6439SH3-bindingSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi74 – 8714Pro-richAdd
BLAST
Compositional biasi422 – 614193Ser-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 ABL1 SH2 domains. The HLH motif is absolutely required for the induction of pseudohyphal growth in yeast and mediates heterodimerization with NEDD9 (By similarity).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.Curated
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH3 domain, SH3-binding

Phylogenomic databases

eggNOGiNOG82196.
GeneTreeiENSGT00490000043324.
HOGENOMiHOG000261698.
HOVERGENiHBG004354.
InParanoidiP56945.
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

        10         20         30         40         50
MNHLNVLAKA LYDNVAESPD ELSFRKGDIM TVLEQDTQGL DGWWLCSLHG
60 70 80 90 100
RQGIVPGNRL KILVGMYDKK PAGPGPGPPA TPAQPQPGLH APAPPASQYT
110 120 130 140 150
PMLPNTYQPQ PDSVYLVPTP SKAQQGLYQV PGPSPQFQSP PAKQTSTFSK
160 170 180 190 200
QTPHHPFPSP ATDLYQVPPG PGGPAQDIYQ VPPSAGMGHD IYQVPPSMDT
210 220 230 240 250
RSWEGTKPPA KVVVPTRVGQ GYVYEAAQPE QDEYDIPRHL LAPGPQDIYD
260 270 280 290 300
VPPVRGLLPS QYGQEVYDTP PMAVKGPNGR DPLLEVYDVP PSVEKGLPPS
310 320 330 340 350
NHHAVYDVPP SVSKDVPDGP LLREETYDVP PAFAKAKPFD PARTPLVLAA
360 370 380 390 400
PPPDSPPAED VYDVPPPAPD LYDVPPGLRR PGPGTLYDVP RERVLPPEVA
410 420 430 440 450
DGGVVDSGVY AVPPPAEREA PAEGKRLSAS STGSTRSSQS ASSLEVAGPG
460 470 480 490 500
REPLELEVAV EALARLQQGV SATVAHLLDL AGSAGATGSW RSPSEPQEPL
510 520 530 540 550
VQDLQAAVAA VQSAVHELLE FARSAVGNAA HTSDRALHAK LSRQLQKMED
560 570 580 590 600
VHQTLVAHGQ ALDAGRGGSG ATLEDLDRLV ACSRAVPEDA KQLASFLHGN
610 620 630 640 650
ASLLFRRTKA TAPGPEGGGT LHPNPTDKTS SIQSRPLPSP PKFTSQDSPD
660 670 680 690 700
GQYENSEGGW MEDYDYVHLQ GKEEFEKTQK ELLEKGSITR QGKSQLELQQ
710 720 730 740 750
LKQFERLEQE VSRPIDHDLA NWTPAQPLAP GRTGGLGPSD RQLLLFYLEQ
760 770 780 790 800
CEANLTTLTN AVDAFFTAVA TNQPPKIFVA HSKFVILSAH KLVFIGDTLS
810 820 830 840 850
RQAKAADVRS QVTHYSNLLC DLLRGIVATT KAAALQYPSP SAAQDMVERV
860 870
KELGHSTQQF RRVLGQLAAA
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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti63 – 631L → S in BAB55230. (PubMed:14702039)Curated
Sequence conflicti236 – 2361I → T in AAF27527. 1 PublicationCurated
Sequence conflicti254 – 2541V → I in BAG54099. (PubMed:14702039)Curated
Sequence conflicti349 – 3491A → G in AAF27527. 1 PublicationCurated
Sequence conflicti363 – 3631D → Y in AAF27527. 1 PublicationCurated
Sequence conflicti385 – 3851T → A in AAS48631. 1 PublicationCurated
Sequence conflicti428 – 4281S → P in BAB55230. (PubMed:14702039)Curated
Sequence conflicti471 – 4711S → G in BAB55230. (PubMed:14702039)Curated
Sequence conflicti600 – 6001N → S in AAS48631. 1 PublicationCurated
Sequence conflicti700 – 7001Q → R in BAH13763. (PubMed:14702039)Curated
Sequence conflicti714 – 7141P → L in BAG54099. (PubMed:14702039)Curated
Sequence conflicti740 – 7401D → G in AAS48631. 1 PublicationCurated

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. 1 PublicationVSP_043559
Alternative sequencei1 – 44MNHL → MQGK in isoform 4. 1 PublicationVSP_046127
Alternative sequencei1 – 44MNHL → ME in isoform 5. 1 PublicationVSP_046748
Alternative sequencei1 – 44MNHL → MPAKPFLSSVLLSWKVLDFS GPGPQGTGQPCSCGHWAEGQ GGPPEPAGGP in isoform 6. 1 PublicationVSP_046749
Alternative sequencei1 – 44MNHL → MHCPGEAPLAAPRPTPKDPC LR in isoform 7. 1 PublicationVSP_046750
Alternative sequencei1 – 44MNHL → MSVP in isoform 8. 1 PublicationVSP_046751
Alternative sequencei64 – 211148Missing in isoform 4. 1 PublicationVSP_046128Add
BLAST
Alternative sequencei304 – 3041A → AVSKCQGNARARLRLWGVW in isoform 3. 1 PublicationVSP_045355

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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...
MobiDBi 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.
GeneTreei ENSGT00490000043324.
HOGENOMi HOG000261698.
HOVERGENi HBG004354.
InParanoidi P56945.
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.
REACT_228166. VEGFA-VEGFR2 Pathway.
SignaLinki P56945.

Miscellaneous databases

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

Gene expression databases

Bgeei P56945.
CleanExi HS_BCAR1.
ExpressionAtlasi P56945. baseline and differential.
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 AT TYR-128 BY PTPN14, 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: November 26, 2014
This is version 148 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