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Protein

Breast cancer anti-estrogen resistance protein 3

Gene

Bcar3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May act as an adapter protein and couple activated growth factor receptors to signaling molecules that regulate src kinase activity and promote cell migration.2 Publications

GO - Molecular functioni

GO - Biological processi

  • lens morphogenesis in camera-type eye Source: MGI
  • positive regulation of peptidyl-serine phosphorylation Source: MGI
  • small GTPase mediated signal transduction Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Names & Taxonomyi

Protein namesi
Recommended name:
Breast cancer anti-estrogen resistance protein 3
Alternative name(s):
p130Cas-binding protein AND-34
Gene namesi
Name:Bcar3
Synonyms:And34
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1352501. Bcar3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 820819Breast cancer anti-estrogen resistance protein 3PRO_0000230286Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei32 – 321PhosphoserineBy similarity
Modified residuei77 – 771PhosphoserineBy similarity
Modified residuei176 – 1761PhosphoserineBy similarity
Modified residuei284 – 2841PhosphoserineBy similarity
Modified residuei353 – 3531PhosphoserineBy similarity
Modified residuei358 – 3581PhosphoserineBy similarity
Modified residuei370 – 3701PhosphoserineCombined sources
Modified residuei466 – 4661PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated on tyrosine.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9QZK2.
PaxDbiQ9QZK2.
PRIDEiQ9QZK2.

PTM databases

iPTMnetiQ9QZK2.
PhosphoSiteiQ9QZK2.

Expressioni

Tissue specificityi

Expressed in B-cells.2 Publications

Inductioni

Up-regulated by IL1A and LTA, in thymus cortical reticular cell lines.1 Publication

Gene expression databases

BgeeiQ9QZK2.
CleanExiMM_BCAR3.
ExpressionAtlasiQ9QZK2. baseline and differential.
GenevisibleiQ9QZK2. MM.

Interactioni

Subunit structurei

Interacts with BCAR1, NEDD9, PTK2/FAK1 and PTPN1.3 Publications

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000029766.

Structurei

3D structure databases

ProteinModelPortaliQ9QZK2.
SMRiQ9QZK2. Positions 110-276, 506-813.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini148 – 247100SH2PROSITE-ProRule annotationAdd
BLAST
Domaini543 – 813271Ras-GEFPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 Ras-GEF domain.PROSITE-ProRule annotation
Contains 1 SH2 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH2 domain

Phylogenomic databases

eggNOGiENOG410IFQG. Eukaryota.
ENOG410XTJR. LUCA.
GeneTreeiENSGT00390000008976.
HOGENOMiHOG000231595.
HOVERGENiHBG053174.
InParanoidiQ9QZK2.
OMAiLPYGHQL.
OrthoDBiEOG77126R.
PhylomeDBiQ9QZK2.
TreeFamiTF323756.

Family and domain databases

Gene3Di1.10.840.10. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR028849. BCAR3.
IPR023578. Ras_GEF_dom.
IPR001895. RASGEF_cat_dom.
IPR000980. SH2.
[Graphical view]
PANTHERiPTHR14247:SF10. PTHR14247:SF10. 1 hit.
PfamiPF00617. RasGEF. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
SMARTiSM00147. RasGEF. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
SUPFAMiSSF48366. SSF48366. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEiPS50009. RASGEF_CAT. 1 hit.
PS50001. SH2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9QZK2-1) [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
MAAGKFASLP RNMPVNHQFP LASSMDLLSS KSPLAERRTD AYQDVSIHGT
60 70 80 90 100
LPRKKKGPPS IRSCDNAGHS KSPRQSSPLT QDIIQENPLQ DRKGENFIFR
110 120 130 140 150
DPYLLDPTLE YVKFSKERHI MDRTPERLKK ELEEELLLSS EDLRSHAWYH
160 170 180 190 200
GRIPRQVSEN LVQRDGDFLV RDSLSSPGNF VLTCQWKNLA QHFKINRTVL
210 220 230 240 250
RLSEAYSRVQ YQFEMESFDS IPGLVRCYVG NRRPISQQSG AIIFQPINRT
260 270 280 290 300
VPLWCLEERY GTSPGRGREG SLAEGRPDVV KRLSLTTGSS IQAREHSLPR
310 320 330 340 350
GNLLRNKEKS GSQPACLDHV QDRKALTLKA HQSESHLPIG CKLPPQSPSM
360 370 380 390 400
DTSPCPSSPV FRTGSEPTLS PALVRRFSSD ARTGEALRGS DSQLCPKPPP
410 420 430 440 450
KPCKVPFLKT PPSPSPWLTS EANYCELNPA FAVGCDRGAK LPMQAHDSHE
460 470 480 490 500
MLLTAKQNGP SGPRNSGINY MILDGDDQAR HWDPLAVQTD EGQEDKTKFV
510 520 530 540 550
PPLMETVSSF RPNDFESKLL PPENKPLETA MLKHAKELFT NHDARVIAQH
560 570 580 590 600
MLSVDCKVAR ILEVSEDRKR SMGVSSGLEL ITLPHGRQLR LDIIERHNTM
610 620 630 640 650
AIGIAVDILG CTGTLENRAG TLNKIIQVAV ELKDAMGDLY AFSAIMKALE
660 670 680 690 700
MPQITRLEKT WTALRHHYTQ TAILYEKQLK PFSKILHEGR ESTYVPASNV
710 720 730 740 750
SVPLLMPLVT LMERQAVTFE GTDMWENNDE SCEILLNHLA TARFMAEASE
760 770 780 790 800
SYRMNAERIL ADFQPDEEMT EILRTEFQMR LLWGSKGAEV NQNERYDKFN
810 820
QILTALSRKL EPPSGKQAEL
Length:820
Mass (Da):92,263
Last modified:May 1, 2000 - v1
Checksum:i69DDACECDE869F01
GO
Isoform 2 (identifier: Q9QZK2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-120: Missing.

Note: No experimental confirmation available.
Show »
Length:700
Mass (Da):78,735
Checksum:i569413486AA3F464
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti36 – 361E → G in BAE25587 (PubMed:16141072).Curated
Sequence conflicti525 – 5251K → E in BAE25587 (PubMed:16141072).Curated
Sequence conflicti795 – 7951R → G in BAE38160 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 120120Missing in isoform 2. 1 PublicationVSP_017815Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF179566 mRNA. Translation: AAD53182.1.
AK143894 mRNA. Translation: BAE25587.1.
AK165396 mRNA. Translation: BAE38160.1.
BC023930 mRNA. Translation: AAH23930.1.
CCDSiCCDS17810.1. [Q9QZK2-1]
RefSeqiNP_038895.1. NM_013867.2. [Q9QZK2-1]
UniGeneiMm.45815.

Genome annotation databases

EnsembliENSMUST00000029766; ENSMUSP00000029766; ENSMUSG00000028121. [Q9QZK2-1]
GeneIDi29815.
KEGGimmu:29815.
UCSCiuc008req.2. mouse. [Q9QZK2-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF179566 mRNA. Translation: AAD53182.1.
AK143894 mRNA. Translation: BAE25587.1.
AK165396 mRNA. Translation: BAE38160.1.
BC023930 mRNA. Translation: AAH23930.1.
CCDSiCCDS17810.1. [Q9QZK2-1]
RefSeqiNP_038895.1. NM_013867.2. [Q9QZK2-1]
UniGeneiMm.45815.

3D structure databases

ProteinModelPortaliQ9QZK2.
SMRiQ9QZK2. Positions 110-276, 506-813.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000029766.

PTM databases

iPTMnetiQ9QZK2.
PhosphoSiteiQ9QZK2.

Proteomic databases

MaxQBiQ9QZK2.
PaxDbiQ9QZK2.
PRIDEiQ9QZK2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029766; ENSMUSP00000029766; ENSMUSG00000028121. [Q9QZK2-1]
GeneIDi29815.
KEGGimmu:29815.
UCSCiuc008req.2. mouse. [Q9QZK2-1]

Organism-specific databases

CTDi8412.
MGIiMGI:1352501. Bcar3.

Phylogenomic databases

eggNOGiENOG410IFQG. Eukaryota.
ENOG410XTJR. LUCA.
GeneTreeiENSGT00390000008976.
HOGENOMiHOG000231595.
HOVERGENiHBG053174.
InParanoidiQ9QZK2.
OMAiLPYGHQL.
OrthoDBiEOG77126R.
PhylomeDBiQ9QZK2.
TreeFamiTF323756.

Miscellaneous databases

ChiTaRSiBcar3. mouse.
NextBioi306974.
PROiQ9QZK2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QZK2.
CleanExiMM_BCAR3.
ExpressionAtlasiQ9QZK2. baseline and differential.
GenevisibleiQ9QZK2. MM.

Family and domain databases

Gene3Di1.10.840.10. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR028849. BCAR3.
IPR023578. Ras_GEF_dom.
IPR001895. RASGEF_cat_dom.
IPR000980. SH2.
[Graphical view]
PANTHERiPTHR14247:SF10. PTHR14247:SF10. 1 hit.
PfamiPF00617. RasGEF. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
SMARTiSM00147. RasGEF. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
SUPFAMiSSF48366. SSF48366. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEiPS50009. RASGEF_CAT. 1 hit.
PS50001. SH2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "AND-34, a novel p130Cas-binding thymic stromal cell protein regulated by adhesion and inflammatory cytokines."
    Cai D., Clayton L.K., Smolyar A., Lerner A.
    J. Immunol. 163:2104-2112(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, PHOSPHORYLATION, INTERACTION WITH BCAR1, INDUCTION BY INTERLEUKIN-1-BETA AND TNF-ALPHA.
    Strain: C57BL/6J.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Kidney.
  3. "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).
    Strain: FVB/N.
    Tissue: Mammary tumor.
  4. "p130Cas regulates the activity of AND-34, a novel Ral, Rap1, and R-Ras guanine nucleotide exchange factor."
    Gotoh T., Cai D., Tian X., Feig L.A., Lerner A.
    J. Biol. Chem. 275:30118-30123(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN GTPASES ACTIVATION, INTERACTION WITH BCAR1; PTK2/FAK1 AND PTPN1.
  5. "The GDP exchange factor AND-34 is expressed in B cells, associates with HEF1, and activates Cdc42."
    Cai D., Felekkis K.N., Near R.I., O'Neill G.M., van Seventer J.M., Golemis E.A., Lerner A.
    J. Immunol. 170:969-978(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INTERACTION WITH NEDD9, FUNCTION.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370 AND SER-466, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney and Lung.

Entry informationi

Entry nameiBCAR3_MOUSE
AccessioniPrimary (citable) accession number: Q9QZK2
Secondary accession number(s): Q3TNC9, Q3UP10
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: May 1, 2000
Last modified: March 16, 2016
This is version 108 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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.