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O75815 (BCAR3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Breast cancer anti-estrogen resistance protein 3
Alternative name(s):
Novel SH2-containing protein 2
SH2 domain-containing protein 3B
Gene names
Name:BCAR3
Synonyms:NSP2, SH2D3B
ORF Names:UNQ271/PRO308
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length825 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May act as an adapter protein and couple activated growth factor receptors to a signaling pathway that regulates the proliferation in breast cancer cells. When overexpressed, it confers anti-estrogen resistance in breast cancer cell lines. May also be regulated by cellular adhesion to extracellular matrix proteins. Ref.1

Subunit structure

Interacts with BCAR1, NEDD9, PTK2/FAK1 and PTPN1 By similarity.

Tissue specificity

Ubiquitously expressed. Found in several cancer cell lines, but not in nonmalignant breast tissue. Ref.1 Ref.2

Sequence similarities

Contains 1 Ras-GEF domain.

Contains 1 SH2 domain.

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75815-1)

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.
Isoform 2 (identifier: O75815-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-324: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: O75815-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-91: Missing.
     92-117: ESPWQDRHGETFTFRDPHLLDPTVEY → MPKECSAFHALSAALCCFYHRKSFIG
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.12
Chain2 – 825824Breast cancer anti-estrogen resistance protein 3
PRO_0000230284

Regions

Domain154 – 253100SH2
Domain548 – 818271Ras-GEF
Compositional bias479 – 4824Poly-Asp

Amino acid modifications

Modified residue21N-acetylalanine Ref.12
Modified residue321Phosphoserine Ref.9
Modified residue831Phosphoserine Ref.9
Modified residue1821Phosphoserine Ref.8
Modified residue2901Phosphoserine Ref.9
Modified residue3581Phosphoserine Ref.9
Modified residue3631Phosphoserine Ref.9
Modified residue3751Phosphoserine Ref.8 Ref.9

Natural variations

Alternative sequence1 – 324324Missing in isoform 2.
VSP_017814
Alternative sequence1 – 9191Missing in isoform 3.
VSP_046716
Alternative sequence92 – 11726ESPWQ…PTVEY → MPKECSAFHALSAALCCFYH RKSFIG in isoform 3.
VSP_046717
Natural variant4641E → G.
Corresponds to variant rs12062278 [ dbSNP | Ensembl ].
VAR_050689
Natural variant5931Q → H.
Corresponds to variant rs17110107 [ dbSNP | Ensembl ].
VAR_050690

Experimental info

Sequence conflict5191E → G in AL833121. Ref.4
Sequence conflict5431L → P in AL833121. Ref.4

Secondary structure

.............................................. 825
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: C55D61BB4AC7D0F2

FASTA82592,566
        10         20         30         40         50         60 
MAAGKFASLP RNMPVNHQFP LASSMDLLSS RSPLAEHRPD AYQDVSIHGT LPRKKKGPPP 

        70         80         90        100        110        120 
IRSCDDFSHM GTLPHSKSPR QNSPVTQDGI QESPWQDRHG ETFTFRDPHL LDPTVEYVKF 

       130        140        150        160        170        180 
SKERHIMDRT PEKLKKELEE ELLLSSEDLR SHAWYHGRIP RQVSENLVQR DGDFLVRDSL 

       190        200        210        220        230        240 
SSPGNFVLTC QWKNLAQHFK INRTVLRLSE AYSRVQYQFE MESFDSIPGL VRCYVGNRRP 

       250        260        270        280        290        300 
ISQQSGAIIF QPINRTVPLR CLEEHYGTSP GQAREGSLTK GRPDVAKRLS LTMGGVQARE 

       310        320        330        340        350        360 
QNLPRGNLLR NKEKSGSQPA CLDHMQDRRA LSLKAHQSES YLPIGCKLPP QSSGVDTSPC 

       370        380        390        400        410        420 
PNSPVFRTGS EPALSPAVVR RVSSDARAGE ALRGSDSQLC PKPPPKPCKV PFLKVPSSPS 

       430        440        450        460        470        480 
AWLNSEANYC ELNPAFATGC GRGAKLPSCA QGSHTELLTA KQNEAPGPRN SGVNYLILDD 

       490        500        510        520        530        540 
DDRERPWEPA AAQMEKGQWD KGEFVTPLLE TVSSFRPNEF ESKFLPPENK PLETAMLKRA 

       550        560        570        580        590        600 
KELFTNNDPK VIAQHVLSMD CRVARILGVS EEMRRNMGVS SGLELITLPH GHQLRLDIIE 

       610        620        630        640        650        660 
RHNTMAIGIA VDILGCTGTL EDRAATLSKI IQVAVELKDS MGDLYSFSAL MKALEMPQIT 

       670        680        690        700        710        720 
RLEKTWTALR HQYTQTAILY EKQLKPFSKL LHEGRESTCV PPNNVSVPLL MPLVTLMERQ 

       730        740        750        760        770        780 
AVTFEGTDMW EKNDQSCEIM LNHLATARFM AEAADSYRMN AERILAGFQP DEEMNEICKT 

       790        800        810        820 
EFQMRLLWGS KGAQVNQTER YEKFNQILTA LSRKLEPPPV KQAEL 

« Hide

Isoform 2 [UniParc].

Checksum: 50F3B53FB4BAF59E
Show »

FASTA50155,745
Isoform 3 [UniParc].

Checksum: F48AF61CA484420A
Show »

FASTA73482,357

References

« Hide 'large scale' references
[1]"Identification of BCAR3 by a random search for genes involved in antiestrogen resistance of human breast cancer cells."
van Agthoven T., van Agthoven T.L.A., Dekker A., van der Spek P.J., Vreede L., Dorssers L.C.J.
EMBO J. 17:2799-2808(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION.
Tissue: Testis.
[2]"NSP1 defines a novel family of adaptor proteins linking integrin and tyrosine kinase receptors to the c-Jun N-terminal kinase/stress-activated protein kinase signaling pathway."
Lu Y., Brush J., Stewart T.A.
J. Biol. Chem. 274:10047-10052(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Kidney.
[3]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Heart.
[5]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Lung.
[8]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182 AND SER-375, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-83; SER-290; SER-358; SER-363 AND SER-375, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[11]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U92715 mRNA. Translation: AAC39777.1.
AF124250 mRNA. Translation: AAD28245.1.
AY358996 mRNA. Translation: AAQ89355.1.
AL833121 mRNA. No translation available.
AL049796 Genomic DNA. No translation available.
AL109613, AL359820 Genomic DNA. Translation: CAI18950.1.
AL359820, AL109613 Genomic DNA. Translation: CAH73975.1.
AL512488 Genomic DNA. No translation available.
CH471097 Genomic DNA. Translation: EAW73065.1.
CH471097 Genomic DNA. Translation: EAW73066.1.
CH471097 Genomic DNA. Translation: EAW73068.1.
BC039895 mRNA. Translation: AAH39895.1.
CCDSCCDS58010.1. [O75815-3]
CCDS745.1. [O75815-1]
RefSeqNP_001248337.1. NM_001261408.1. [O75815-1]
NP_001248338.1. NM_001261409.1. [O75815-1]
NP_001248339.1. NM_001261410.1. [O75815-3]
NP_003558.1. NM_003567.3. [O75815-1]
UniGeneHs.36958.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3T6AX-ray2.40A/B/C/D502-825[»]
ProteinModelPortalO75815.
SMRO75815. Positions 78-318, 511-818.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114000. 11 interactions.
DIPDIP-33857N.
IntActO75815. 8 interactions.
STRING9606.ENSP00000260502.

PTM databases

PhosphoSiteO75815.

Proteomic databases

MaxQBO75815.
PaxDbO75815.
PRIDEO75815.

Protocols and materials databases

DNASU8412.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000260502; ENSP00000260502; ENSG00000137936. [O75815-1]
ENST00000370243; ENSP00000359263; ENSG00000137936. [O75815-1]
ENST00000370244; ENSP00000359264; ENSG00000137936. [O75815-1]
ENST00000370247; ENSP00000359267; ENSG00000137936. [O75815-3]
ENST00000539242; ENSP00000441343; ENSG00000137936. [O75815-2]
GeneID8412.
KEGGhsa:8412.
UCSCuc001dpx.5. human. [O75815-1]
uc009wdm.1. human. [O75815-2]

Organism-specific databases

CTD8412.
GeneCardsGC01M094027.
HGNCHGNC:973. BCAR3.
HPAHPA014858.
MIM604704. gene.
neXtProtNX_O75815.
PharmGKBPA25283.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG149796.
HOGENOMHOG000231595.
HOVERGENHBG053174.
InParanoidO75815.
OMALPYGHQL.
OrthoDBEOG77126R.
PhylomeDBO75815.
TreeFamTF323756.

Enzyme and pathway databases

SignaLinkO75815.

Gene expression databases

ArrayExpressO75815.
BgeeO75815.
CleanExHS_BCAR3.
GenevestigatorO75815.

Family and domain databases

Gene3D1.10.840.10. 1 hit.
3.30.505.10. 1 hit.
InterProIPR028849. BCAR3.
IPR023578. Ras_GEF_dom.
IPR001895. RasGRF_CDC25.
IPR000980. SH2.
[Graphical view]
PANTHERPTHR14247:SF10. PTHR14247:SF10. 1 hit.
PfamPF00617. RasGEF. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
SMARTSM00147. RasGEF. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
SUPFAMSSF48366. SSF48366. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEPS50009. RASGEF_CAT. 1 hit.
PS50001. SH2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSBCAR3. human.
GeneWikiBCAR3.
GenomeRNAi8412.
NextBio31494.
PROO75815.
SOURCESearch...

Entry information

Entry nameBCAR3_HUMAN
AccessionPrimary (citable) accession number: O75815
Secondary accession number(s): D3DT43 expand/collapse secondary AC list , Q5TEW3, Q6UW40, Q9BR50
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: November 1, 1998
Last modified: July 9, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM