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Protein

Breast cancer anti-estrogen resistance protein 1

Gene

Bcar1

Organism
Rattus norvegicus (Rat)
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).By similarity

GO - Molecular functioni

  • protein domain specific binding Source: RGD
  • signal transducer activity Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2406. Bcar1.

Subcellular locationi

  • Cell junctionfocal adhesion
  • Cytoplasm

  • Note: Localizes at focal adhesions and stress fibers. Unphosphorylated form localizes in the cytoplasm and can move to the membrane upon tyrosine phosphorylation.

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • plasma membrane Source: RGD
  • ruffle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 968968Breast cancer anti-estrogen resistance protein 1PRO_0000064856Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei226 – 2261Phosphotyrosine; by SRCBy similarity
Modified residuei237 – 2371PhosphoserineBy similarity
Modified residuei332 – 3321PhosphotyrosineBy similarity
Modified residuei347 – 3471Phosphotyrosine; by ABL11 Publication
Modified residuei367 – 3671PhosphothreonineBy similarity
Modified residuei390 – 3901PhosphoserineBy similarity
Modified residuei460 – 4601PhosphotyrosineBy similarity
Modified residuei470 – 4701PhosphotyrosineBy similarity
Modified residuei508 – 5081PhosphotyrosineBy similarity
Modified residuei526 – 5261PhosphoserineBy similarity
Modified residuei535 – 5351PhosphoserineBy similarity
Modified residuei737 – 7371PhosphoserineCombined sources

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.2 Publications
Dephosphorylated by PTPN14 at Tyr-226.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ63767.
PRIDEiQ63767.

PTM databases

iPTMnetiQ63767.
PhosphoSiteiQ63767.

Expressioni

Tissue specificityi

Widely expressed. Higher expression in lung, intestine and testis.

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 BCAR3, the interaction regulates adhesion-dependent serine phosphorylation. Interacts with NPHP1, PTK2B/PYK2 and SH2D3C. 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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
PTPN1P180315EBI-1176801,EBI-968788From a different organism.
SrcP054802EBI-1176801,EBI-298680From a different organism.

GO - Molecular functioni

  • protein domain specific binding Source: RGD

Protein-protein interaction databases

BioGridi247449. 5 interactions.
IntActiQ63767. 7 interactions.
MINTiMINT-93469.
STRINGi10116.ENSRNOP00000039940.

Structurei

Secondary structure

1
968
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi554 – 58128Combined sources
Beta strandi591 – 5944Combined sources
Helixi599 – 62426Combined sources
Helixi634 – 66128Combined sources
Beta strandi664 – 6663Combined sources
Helixi671 – 70232Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X27X-ray2.70I/J/K/L/M/N759-767[»]
1Z23NMR-A546-708[»]
ProteinModelPortaliQ63767.
SMRiQ63767. Positions 99-165, 548-708.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ63767.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini97 – 15963SH3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni213 – 514302Substrate for kinasesAdd
BLAST
Regioni844 – 89451Divergent helix-loop-helix motifAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi733 – 7419SH3-bindingSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi168 – 18114Pro-richAdd
BLAST
Compositional biasi520 – 712193Ser-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).
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

eggNOGiENOG410IEDD. Eukaryota.
ENOG410ZSUM. LUCA.
HOGENOMiHOG000261698.
HOVERGENiHBG004354.
InParanoidiQ63767.
KOiK05726.
PhylomeDBiQ63767.

Family and domain databases

InterProiIPR028848. BCAR1.
IPR021901. CAS_DUF3513.
IPR014928. Serine_rich.
IPR001452. SH3_domain.
IPR013315. Spectrin_alpha_SH3.
[Graphical view]
PANTHERiPTHR10654:SF15. PTHR10654:SF15. 2 hits.
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. AlignAdd to basket

Isoform Long (identifier: Q63767-1) [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
MKYLVSVGAG PARRAGGLED VSWGPRVSRR PQSYRAARHV NESLPRSAFR
60 70 80 90 100
VPAAHGASVT PSAALGSGLP ETQPEAVCRG TEKPRFAEGC KPAASRDKNV
110 120 130 140 150
LAKALYDNVA ESPDELSFRK GDIMTVLERD TQGLDGWWLC SLHGRQGIVP
160 170 180 190 200
GNRLKILVGM YDKKPAAPGP GPPATPPQPQ PSLPQGVHTP VPPASQYSPM
210 220 230 240 250
LPTAYQPQPD NVYLVPTPSK TQQGLYQAPG PNPQFQSPPA KQTSTFSKQT
260 270 280 290 300
PHHSFPSPAT DLYQVPPGPG SPAQDIYQVP PSAGTGHDIY QVPPSLDTRS
310 320 330 340 350
WEGTKPPAKV VVPTRVGQGY VYEASQAEQD EYDTPRHLLA PGSQDIYDVP
360 370 380 390 400
PVRGLLPNQY GQEVYDTPPM AVKGPNGRDP LLDVYDVPPS VEKGLPPSNH
410 420 430 440 450
HSVYDVPPSV SKDVPDGPLL REETYDVPPA FAKPKPFDPT RHPLILAAPP
460 470 480 490 500
PDSPPAEDVY DVPPPAPDLY DVPPGLRRPG PGTLYDVPRE RVLPPEVADG
510 520 530 540 550
SVIDDGVYAV PPPAEREAPT DGKRLSASST GSTRSSQSAS SLEVVVPGRE
560 570 580 590 600
PLELEVAVET LARLQQGVST TVAHLLDLVG SASGPGGWRS TSEPQEPPVQ
610 620 630 640 650
DLKAAVAAVH GAVHELLEFA RSAVSSATHT SDRTLHAKLS RQLQKMEDVY
660 670 680 690 700
QTLVVHGQVL DSGRGGPGFT LDDLDRLVAC SRAVPEDAKQ LASFLHGNAS
710 720 730 740 750
LLFRRTKAPG PGPEGSSSLH LNPTDKASSI QSRPLPSPPK FTSQDSPDGQ
760 770 780 790 800
YENSEGGWME DYDYVHLQGK EEFEKTQKEL LEKGNIVRQG KGQLELQQLK
810 820 830 840 850
QFERLEQEVS RPIDHDLANW TPAQPLVPGR TGGLGPSDRQ LLLFYLEQCE
860 870 880 890 900
ANLTTLTDAV DAFFTAVATN QPPKIFVAHS KFVILSAHKL VFIGDTLSRQ
910 920 930 940 950
AKAADVRSKV THYSNLLCDL LRGIVATTKA AALQYPSPSA AQDMVDRVKE
960
LGHSTQQFRR VLGQLAAA
Length:968
Mass (Da):104,262
Last modified:November 1, 1996 - v1
Checksum:iE861641BFD68D377
GO
Isoform Short (identifier: Q63767-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     5-98: Missing.

Note: No experimental confirmation available.
Show »
Length:874
Mass (Da):94,476
Checksum:iA03B20B8E78548C0
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei5 – 9894Missing in isoform Short. CuratedVSP_004135Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D29766 mRNA. Translation: BAA06169.1.
D29766 mRNA. Translation: BAA06170.1.
PIRiS46992.
RefSeqiNP_037063.1. NM_012931.1. [Q63767-1]
UniGeneiRn.40101.

Genome annotation databases

GeneIDi25414.
KEGGirno:25414.
UCSCiRGD:2406. rat. [Q63767-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D29766 mRNA. Translation: BAA06169.1.
D29766 mRNA. Translation: BAA06170.1.
PIRiS46992.
RefSeqiNP_037063.1. NM_012931.1. [Q63767-1]
UniGeneiRn.40101.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X27X-ray2.70I/J/K/L/M/N759-767[»]
1Z23NMR-A546-708[»]
ProteinModelPortaliQ63767.
SMRiQ63767. Positions 99-165, 548-708.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247449. 5 interactions.
IntActiQ63767. 7 interactions.
MINTiMINT-93469.
STRINGi10116.ENSRNOP00000039940.

PTM databases

iPTMnetiQ63767.
PhosphoSiteiQ63767.

Proteomic databases

PaxDbiQ63767.
PRIDEiQ63767.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25414.
KEGGirno:25414.
UCSCiRGD:2406. rat. [Q63767-1]

Organism-specific databases

CTDi9564.
RGDi2406. Bcar1.

Phylogenomic databases

eggNOGiENOG410IEDD. Eukaryota.
ENOG410ZSUM. LUCA.
HOGENOMiHOG000261698.
HOVERGENiHBG004354.
InParanoidiQ63767.
KOiK05726.
PhylomeDBiQ63767.

Miscellaneous databases

EvolutionaryTraceiQ63767.
PROiQ63767.

Family and domain databases

InterProiIPR028848. BCAR1.
IPR021901. CAS_DUF3513.
IPR014928. Serine_rich.
IPR001452. SH3_domain.
IPR013315. Spectrin_alpha_SH3.
[Graphical view]
PANTHERiPTHR10654:SF15. PTHR10654:SF15. 2 hits.
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...

Entry informationi

Entry nameiBCAR1_RAT
AccessioniPrimary (citable) accession number: Q63767
Secondary accession number(s): Q63766
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.