Protein detail

BCAR1

Breast cancer anti-estrogen resistance protein 1 (CRK-associated substrate) (Cas scaffolding protein family member 1) (p130cas)

Protein symbol
BCAR1
UniProt ID
EVMP score
0.38
Frequency
1
Transmembrane count
Protein classification
Plasma proteinsPredicted intracellular proteins
EVMP score: annotation confidence score.
Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information
Protein Names
Breast cancer anti-estrogen resistance protein 1 (CRK-associated substrate) (Cas scaffolding protein family member 1) (p130cas)
Protein Class
Plasma proteinsPredicted intracellular proteins
Protein Function
Predicted intracellular proteins
Entrez Gene Symbol
Gene Synonym
CASCASS1CrkasP130Cas
Gene Description
BCAR1 scaffold protein, Cas family member
Chromosome
16
Position
75228181-75268053
Frequency
1
EVMP Score
0.38
Fluorescence & Localization
Tissue Specificadipose tissueCell SpecificMicrogliaSingle-Nuclei Brain Specificcentral nervous system macrophageSecretome LocationSecreted to extracellular matrixSecretome FunctionDevelopmental protein
Function & Pathway
Protein Function
Predicted intracellular proteins
Canonical Pathways
  • M77 Pid wnt signaling pathway
  • M266 Pid ncadherin pathway
  • M5493 Wnt signaling
Mediation Categories
Adhesion and uptake mediationFusion and delivery mediationImmune mediationReceptor-signaling mediation
Relations & Evidence

Enzyme-Mediated Modification

77 records.

Substrate Gene SymbolEnzyme Gene SymbolEnzyme UniProt IDResidue TypeResidue OffsetModificationDatabaseReferences
BCAR1FGFR1P11362Y456phosphorylationMIMPHPRD_MIMPphosphoELM_MIMPPhosphoSite_MIMP
BCAR1FGFR1P11362Y128phosphorylationPhosphoNetworksSIGNORProtMapperKEAphosphoELMLi2012SIGNOR_ProtMapperProtMapper:11019781SIGNOR:11019781phosphoELM:12601080SIGNOR:12601080ProtMapper:12601080KEA:12601080
BCAR1FGFR1P11362Y327phosphorylationPhosphoNetworksSIGNORProtMapperKEAphosphoELMLi2012SIGNOR_ProtMapperProtMapper:12601080SIGNOR:12601080phosphoELM:12601080KEA:12601080
BCAR1FGFR1P11362Y306phosphorylationPhosphoNetworksSIGNORProtMapperKEAphosphoELMLi2012SIGNOR_ProtMapperProtMapper:12601080SIGNOR:12601080phosphoELM:12601080KEA:12601080
BCAR1FGFR1P11362Y249phosphorylationPhosphoNetworksSIGNORProtMapperKEAphosphoELMLi2012SIGNOR_ProtMapperProtMapper:12601080SIGNOR:12601080phosphoELM:12601080KEA:12601080
BCAR1FGFR1P11362Y410phosphorylationPhosphoNetworksSIGNORProtMapperKEAphosphoELMSIGNOR_ProtMapperProtMapper:12601080SIGNOR:12601080phosphoELM:12601080KEA:12601080
BCAR1FGFR1P11362Y165phosphorylationPhosphoNetworks
BCAR1FGFR1P11362Y224phosphorylationPhosphoNetworks
BCAR1FGFR1P11362Y267phosphorylationPhosphoNetworks
BCAR1FGFR1P11362Y287phosphorylationPhosphoNetworks
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Ligand-Receptor Signaling

7 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
intracellularintracellularLOCATENoNoNoNoNo
intracellularintracellularComPPINoNoNoNoNo
intracellularintracellularGO_IntercellNoNoNoNoNo
intracellularintracellularUniProt_locationNoNoNoNoNo
intracellularintracellularOmniPathNoNoNoNoNo
adhesion_cytoskeleton_adaptorintracellular_intercellular_relatedAdhesomeYesNoNoNoNo
intracellular_intercellular_relatedintracellular_intercellular_relatedOmniPathYesNoNoNoNo

Regulatory Interaction Network

13 records.

Source Protein SymbolSource UniProt IDTarget Protein SymbolTarget UniProt IDIs DirectedIs StimulationIs InhibitionDatabaseReferences
FAK1Q05397BCAR1P56945YesYesNoSPIKEHPRD_MIMPSIGNORProtMapperHINTPhosphoSite_KEAphosphoELM_KEADOMINOMPPIHPRDCui2007CA1WangPhosphoSite_ProtMapperphosphoELM_MIMPPhosphoSite_MIMPMIMPPhosphoSite_norefPhosphoPointiPTMnetKEAHPRD_KEASIGNOR_ProtMapperREACH_ProtMapperAdhesomeSPIKE_LCHPRD-phosAdhesome:10753828HINT:11514617HINT:12119061HPRD:12119061MPPI:10545505HINT:8649427ProtMapper:11604500ProtMapper:12119061HPRD:7479864SPIKE_LC:10092764HPRD:9360968HPRD:11514617DOMINO:9285683HINT:9148935SPIKE_LC:9285683SPIKE_LC:9148935KEA:8621540SIGNOR:11604500ProtMapper:9360983SPIKE:9285683Adhesome:7479864Adhesome:9285683Adhesome:8662921KEA:9360968HINT:9360983Adhesome:12135674Adhesome:8810278HPRD-phos:12119061KEA:12119061KEA:12480533ProtMapper:24939893Adhesome:10592173HINT:9285683ProtMapper:9360968Adhesome:11514617ProtMapper:19138410SPIKE:10092764HPRD-phos:9360983KEA:11604500KEA:9360983Adhesome:21855630Adhesome:11119718Adhesome:15673687HPRD:9360983Adhesome:11577104Adhesome:11839772Adhesome:8649427Adhesome:12615911HINT:10545505HPRD-phos:9360968Adhesome:9038154KEA:8670206HINT:21034468HINT:9360968CA1:8662921SPIKE:9148935KEA:12972425Adhesome:18233957HINT:7479864
SRCP12931BCAR1P56945YesYesNoSPIKEHPRD_MIMPSIGNORProtMapperRLIMS-P_ProtMapperHINTPhosphoSite_KEAphosphoELM_KEALi2012Lit-BM-17HPRDCui2007CA1IntActWangNetworKIN_KEAPhosphoSite_ProtMapperBEL-Large-Corpus_ProtMapperphosphoELM_MIMPPhosphoSite_MIMPMIMPPhosphoSite_norefPhosphoPointiPTMnetELMKEABioGRIDHPRD_KEAphosphoELMSIGNOR_ProtMapperREACH_ProtMapperSparser_ProtMapperAdhesomeSPIKE_LCHPRD-phosAdhesome:8070403Adhesome:10542110ELM:10542110ProtMapper:21937722phosphoELM:11604500CA1:8070403ProtMapper:20927395KEA:12972425ELM:9360983ProtMapper:11604500SIGNOR:22710723Lit-BM-17:10085298HINT:10487518Lit-BM-17:15020686ProtMapper:15212693ProtMapper:12972425Adhesome:10487518HINT:9148935KEA:15817476BioGRID:12397603Lit-BM-17:12397603ProtMapper:17016520ProtMapper:21765460SIGNOR:12972425IntAct:17038317ProtMapper:23974298Adhesome:17038317ProtMapper:21301050SIGNOR:11604500ProtMapper:22710723SPIKE:15272013KEA:15316024HINT:10542110ProtMapper:17389395IntAct:10542110BioGRID:17129785KEA:12480533SPIKE_LC:15272013Lit-BM-17:17038317HINT:10739664ProtMapper:21963850ProtMapper:24962474ProtMapper:30422386Lit-BM-17:10487518Adhesome:11514617Lit-BM-17:11514617ProtMapper:19138410ProtMapper:23457577IntAct:21034468KEA:11604500HPRD-phos:19901323Adhesome:10085298HINT:17038317HPRD-phos:12972425Adhesome:12972425HPRD:12972425Adhesome:12615911HINT:12397603HPRD-phos:17389395Lit-BM-17:10739664Lit-BM-17:17129785HINT:17129785ProtMapper:19901323KEA:8670206ProtMapper:25976166HINT:10085298HINT:21034468Lit-BM-17:10542110ProtMapper:20103658KEA:17570479Adhesome:10739664Adhesome:12397603HPRD-phos:17016520ProtMapper:28808245
ABL1P00519BCAR1P56945YesYesNoWangAdhesomeSIGNORPhosphoPointHPRDdbPTMBioGRIDSPIKE_LCSPIKEAdhesome:8810278Adhesome:17129785Adhesome:7780740dbPTM:16212419SPIKE_LC:7780740dbPTM:15951569SPIKE_LC:20841568HPRD:7780740SIGNOR:17615370dbPTM:19534553dbPTM:18083107BioGRID:7780740SPIKE:7780740SPIKE:20841568
FYNP06241BCAR1P56945YesYesYesDOMINOWangAdhesomeNetPathPhosphoPointSIGNORELMHINTHPRDHuRIIntActSPIKE_LCLit-BM-17SPIKEELM:10542110NetPath:9020138Lit-BM-17:17474147Adhesome:17474147IntAct:31413325Lit-BM-17:9360983ELM:9360983SIGNOR:24586768SPIKE:17474147SPIKE_LC:9020138HINT:9188452Adhesome:17129785SPIKE:9020138HINT:9360983HINT:10739664Adhesome:9188452SPIKE_LC:17474147SPIKE:16713569Lit-BM-17:10739664Adhesome:9360983IntAct:9360983HPRD:9188452Lit-BM-17:9188452SPIKE_LC:16713569IntAct:17474147Adhesome:10739664Adhesome:11181827DOMINO:17474147
PTPRFP10586BCAR1P56945YesNoYesHPRDWangSIGNORAdhesomeSIGNOR:10320483Adhesome:10822386HPRD:10320483Adhesome:10320483HPRD:15588985HPRD:10822386
BCAR1P56945SMAD3P84022YesNoYesNetPathSIGNORNetPath:18321991SIGNOR:18321991
FGFR1P11362BCAR1P56945YesYesNoWangPhosphoNetworksphosphoELM_MIMPPhosphoSite_MIMPMIMPHPRD_MIMPiPTMnetPhosphoPointSIGNORProtMapperPhosphoSite_KEAKEAphosphoELM_KEAphosphoELMLi2012SIGNOR_ProtMapperProtMapper:11019781SIGNOR:11019781phosphoELM:12601080SIGNOR:12601080ProtMapper:12601080KEA:12601080
PTN12Q05209BCAR1P56945YesNoYesDOMINOWangAdhesomeSIGNORDEPODHPRDHINTBioGRIDIntActSPIKE_LCBioGRID:12714323SIGNOR:11432829HPRD:12714323DEPOD:9748319DOMINO:9285683SPIKE_LC:9285683HPRD:9285683HINT:9748319HPRD:9920935Adhesome:9285683Adhesome:11432829DEPOD:8887669Adhesome:8887669HINT:9285683IntAct:9285683HINT:8887669DEPOD:9920935DEPOD:9285683HPRD:8887669HPRD:9748319DEPOD:12714323
PTK6Q13882BCAR1P56945YesYesNoSparser_ProtMapperphosphoELM_MIMPPhosphoSite_MIMPMIMPHPRD_MIMPiPTMnetSIGNORProtMapperSIGNOR_ProtMapperREACH_ProtMapperPhosphoSitePhosphoSite_ProtMapperProtMapper:33391524SIGNOR:22084245ProtMapper:25938342PhosphoSite:15870699ProtMapper:22084245
BCAR1P56945PKN3Q6P5Z2YesYesNoSIGNORSIGNOR:30422386
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Protein Complex Composition

9 records.

Component NameComponent Gene SymbolsComponent UniProt IDStoichiometryDatabaseDatabase IDsReferences
FAK\u2013p130Cas\u2013MT1 complexBCAR1MMP14PTK2P50281P56945Q053970:0:0CORUMCORUM:692122291036
HT_SC_Cluster41BCAR1PHB1PHB2P35232P56945Q996231:1:1CompleatCompleat:HC3492
NPHP1-NPHP4-BCAR1 complexBCAR1NPHP1NPHP4O15259O75161P569450:0:0CORUMCORUM:638115661758
ARCN1ARF4ATP9ABCAR1PDE6DRHBDD3SCPEP1SFT2D2SLC66A2TM9SF4UBCZDHHC13O43924O75110O95562P0CG48P18085P48444P56945Q8IUH4Q8N2U9Q92544Q9HB40Q9Y3P41:1:1:1:1:1:1:1:1:1:1:1NetworkBlastCompleatCompleat:HC4577
ARCN1ARF4BCAR1GOLT1BPDE6DRHBDD3SCPEP1SFT2D3SLC66A2TM9SF4UBCZDHHC13O43924P0CG48P18085P48444P56945Q587I9Q8IUH4Q8N2U9Q92544Q9HB40Q9Y3E0Q9Y3P41:1:1:1:1:1:1:1:1:1:1:1NetworkBlastCompleatCompleat:HC3877
ARCN1ARF4BCAR1PDE6DRGP1RHBDD3SCPEP1SFT2D1SLC66A2TM9SF4UBCZDHHC13O43924P0CG48P18085P48444P56945Q8IUH4Q8N2U9Q8WV19Q92544Q92546Q9HB40Q9Y3P41:1:1:1:1:1:1:1:1:1:1:1NetworkBlastCompleatCompleat:HC6145
ARCN1BCAR1GOLT1BPDE6DRHBDD3SCPEP1SFT2D1SLC66A2TM9SF4TRIM23UBCZDHHC12O43924P0CG48P36406P48444P56945Q8N2U9Q8WV19Q92544Q96GR4Q9HB40Q9Y3E0Q9Y3P41:1:1:1:1:1:1:1:1:1:1:1NetworkBlastCompleatCompleat:HC6282
BCAR1P569452PDBPDB:1wyx
BCAR1SH2D3CP56945Q8N5H72:2PDBPDB:3t6g

Isolation & Detection Technology

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationMicrofluidics-Based MethodsMass spectrometry140545963
Sequence, Structure & Domains

Sequences

Length
870
Mass
93,372
Sequence
MNHLNVLAKALYDNVAESPDELSFRKGDIMTVLEQDTQGLDGWWLCSLHGRQGIVPGNRLKILVGMYDKKPAGPGPGPPATPAQPQPGLHAPAPPASQYTPMLPNTYQPQPDSVYLVPTPSKAQQGLYQVPGPSPQFQSPPAKQTSTFSKQTPHHPFPSPATDLYQVPPGPGGPAQDIYQVPPSAGMGHDIYQVPPSMDTRSWEGTKPPAKVVVPTRVGQGYVYEAAQPEQDEYDIPRHLLAPGPQDIYDVPPVRGLLPSQYGQEVYDTPPMAVKGPNGRDPLLEVYDVPPSVEKGLPPSNHHAVYDVPPSVSKDVPDGPLLREETYDVPPAFAKAKPFDPARTPLVLAAPPPDSPPAEDVYDVPPPAPDLYDVPPGLRRPGPGTLYDVPRERVLPPEVADGGVVDSGVYAVPPPAEREAPAEGKRLSASSTGSTRSSQSASSLEVAGPGREPLELEVAVEALARLQQGVSATVAHLLDLAGSAGATGSWRSPSEPQEPLVQDLQAAVAAVQSAVHELLEFARSAVGNAAHTSDRALHAKLSRQLQKMEDVHQTLVAHGQALDAGRGGSGATLEDLDRLVACSRAVPEDAKQLASFLHGNASLLFRRTKATAPGPEGGGTLHPNPTDKTSSIQSRPLPSPPKFTSQDSPDGQYENSEGGWMEDYDYVHLQGKEEFEKTQKELLEKGSITRQGKSQLELQQLKQFERLEQEVSRPIDHDLANWTPAQPLAPGRTGGLGPSDRQLLLFYLEQCEANLTTLTNAVDAFFTAVATNQPPKIFVAHSKFVILSAHKLVFIGDTLSRQAKAADVRSQVTHYSNLLCDLLRGIVATTKAAALQYPSPSAAQDMVERVKELGHSTQQFRRVLGQLAAA
Alternative Products
Event=Alternative splicing; Named isoforms=8; Name=1; IsoId=P56945-1; Sequence=Displayed; Name=2; IsoId=P56945-2; Sequence=VSP_043559; Name=3; IsoId=P56945-3; Sequence=VSP_045355; Name=4; IsoId=P56945-4; Sequence=VSP_046127, VSP_046128; Name=5; IsoId=P56945-5; Sequence=VSP_046748; Name=6; IsoId=P56945-6; Sequence=VSP_046749; Name=7; IsoId=P56945-7; Sequence=VSP_046750; Name=8; IsoId=P56945-8; Sequence=VSP_046751
Alternative Sequence
1..4; MNHL -> MLTHRPQEAEQRGRTPGPSFEW (in isoform 2); 1..4; MNHL -> MQGK (in isoform 4); 1..4; MNHL -> ME (in isoform 5); 1..4; MNHL -> MPAKPFLSSVLLSWKVLDFSGPGPQGTGQPCSCGHWAEGQGGPPEPAGGP (in isoform 6); 1..4; MNHL -> MHCPGEAPLAAPRPTPKDPCLR (in isoform 7); 1..4; MNHL -> MSVP (in isoform 8); 64..211; Missing (in isoform 4); 304; A -> AVSKCQGNARARLRLWGVW (in isoform 3)

3D Structural Models

Helix
37..39; 57..59; 740..770; 775..801; 806..835; 840..870
Beta Strand
5..12; 29..34; 43..48; 51..56; 60..68
3D Structure
NMR spectroscopy (3); X-ray crystallography (2)

Domain & Motif Annotations

Compositional Bias
73..85; Pro residues; 97..111; Polar residues; 135..151; Polar residues; 416..426; Basic and acidic residues; 427..444; Low complexity; 626..655; Polar residues
Motif
635..643; SH3-binding
Domain (CC)
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).; DOMAIN: A serine-rich region promotes activation of the serum response element (SRE).; DOMAIN: The SH3 domain is necessary for the localization of the protein to focal adhesions and interacts with one proline-rich region of PTK2/FAK11.
Domain (FT)
3..65; SH3
Region
70..156; Disordered; 115..416; Substrate for kinases; 411..449; Disordered; 609..658; Disordered; 715..734; Disordered; 746..796; Divergent helix-loop-helix motif
Protein Families
CAS family
Sequence Similarities
Belongs to the CAS family.
Clinical Relevance
Disease Involvement
Diabetes mellitus
Interaction Protein
ENSG00000010810ENSG00000061938ENSG00000095370ENSG00000108953ENSG00000125731ENSG00000126603ENSG00000127947ENSG00000128245ENSG00000136205ENSG00000137936ENSG00000164924ENSG00000166913ENSG00000167193ENSG00000169398ENSG00000170027ENSG00000196396ENSG00000197122ENSG00000241685ENSG00000277363
Interaction Count
19
Interaction Dataset
intact_biogridbiogrid_opencellbiogrid_bioplexbiogrid_opencell_bioplex