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Breast cancer anti-estrogen resistance protein 3 homolog (p130Cas-binding protein AND-34)

 BCAR3_MOUSE             Reviewed;         820 AA.
Q9QZK2; Q3TNC9; Q3UP10;
04-APR-2006, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
22-APR-2020, entry version 135.
RecName: Full=Breast cancer anti-estrogen resistance protein 3 homolog;
AltName: Full=p130Cas-binding protein AND-34;
Name=Bcar3; Synonyms=And34;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY,
PHOSPHORYLATION, INTERACTION WITH BCAR1, AND INDUCTION BY
INTERLEUKIN-1-BETA AND TNF-ALPHA.
STRAIN=C57BL/6J;
PubMed=10438950;
Cai D., Clayton L.K., Smolyar A., Lerner A.;
"AND-34, a novel p130Cas-binding thymic stromal cell protein regulated by
adhesion and inflammatory cytokines.";
J. Immunol. 163:2104-2112(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J; TISSUE=Kidney;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION IN GTPASES ACTIVATION, AND INTERACTION WITH BCAR1; PTK2/FAK1 AND
PTPN1.
PubMed=10896938; DOI=10.1074/jbc.m003074200;
Gotoh T., Cai D., Tian X., Feig L.A., Lerner A.;
"p130Cas regulates the activity of AND-34, a novel Ral, Rap1, and R-Ras
guanine nucleotide exchange factor.";
J. Biol. Chem. 275:30118-30123(2000).
[5]
TISSUE SPECIFICITY, AND INTERACTION WITH NEDD9 AND BCAR1.
PubMed=12517963; DOI=10.4049/jimmunol.170.2.969;
Cai D., Felekkis K.N., Near R.I., O'Neill G.M., van Seventer J.M.,
Golemis E.A., Lerner A.;
"The GDP exchange factor AND-34 is expressed in B cells, associates with
HEF1, and activates Cdc42.";
J. Immunol. 170:969-978(2003).
[6]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=19365570;
Near R.I., Smith R.S., Toselli P.A., Freddo T.F., Bloom A.B.,
Vanden Borre P., Seldin D.C., Lerner A.;
"Loss of AND-34/BCAR3 expression in mice results in rupture of the adult
lens.";
Mol. Vis. 15:685-699(2009).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370 AND SER-466, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, and Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and expression.";
Cell 143:1174-1189(2010).
[8]
FUNCTION, IDENTIFICATION IN A COMPLEX WITH PTPRA; BCAR1 AND SRC,
SUBCELLULAR LOCATION, AND DOMAIN.
PubMed=22801373; DOI=10.1128/mcb.00214-12;
Sun G., Cheng S.Y., Chen M., Lim C.J., Pallen C.J.;
"Protein tyrosine phosphatase alpha phosphotyrosyl-789 binds BCAR3 to
position Cas for activation at integrin-mediated focal adhesions.";
Mol. Cell. Biol. 32:3776-3789(2012).
[9]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=25499443; DOI=10.1186/s13058-014-0476-9;
Guo J., Canaff L., Rajadurai C.V., Fils-Aime N., Tian J., Dai M., Korah J.,
Villatoro M., Park M., Ali S., Lebrun J.J.;
"Breast cancer anti-estrogen resistance 3 inhibits transforming growth
factor beta/Smad signaling and associates with favorable breast cancer
disease outcomes.";
Breast Cancer Res. 16:476-476(2014).
-!- FUNCTION: Acts as an adapter protein downstream of several growth
factor receptors to promote cell proliferation, migration, and
redistribution of actin fibers (PubMed:12517963). Specifically involved
in INS/insulin signaling pathway by mediating MAPK1/ERK2-MAPK3/ERK1
activation and DNA synthesis (By similarity). Promotes insulin-mediated
membrane ruffling (By similarity). In response to vasoconstrictor
peptide EDN1, involved in the activation of RAP1 downstream of PTK2B
via interaction with phosphorylated BCAR1 (PubMed:10896938). Inhibits
cell migration and invasion via regulation of TGFB-mediated matrix
digestion, actin filament rearrangement, and inhibition of invadopodia
activity (PubMed:25499443). May inhibit TGFB-SMAD signaling, via
facilitating BCAR1 and SMAD2 and/or SMAD3 interaction
(PubMed:25499443). Regulates EGF-induced DNA synthesis (By similarity).
Required for the maintenance of ocular lens morphology and structural
integrity, potentially via regulation of focal adhesion complex
signaling (PubMed:19365570). Acts upstream of PTPRA to regulate the
localization of BCAR1 and PTPRA to focal adhesions, via regulation of
SRC-mediated phosphorylation of PTPRA (PubMed:22801373). Positively
regulates integrin-induced tyrosine phosphorylation of BCAR1
(PubMed:22801373). Acts as a guanine nucleotide exchange factor (GEF)
for small GTPases RALA, RAP1A and RRAS (PubMed:10896938). However, in a
contrasting study, lacks GEF activity towards RAP1 (By similarity).
{ECO:0000250|UniProtKB:D3ZAZ5, ECO:0000250|UniProtKB:O75815,
ECO:0000269|PubMed:10896938, ECO:0000269|PubMed:12517963,
ECO:0000269|PubMed:19365570, ECO:0000269|PubMed:22801373,
ECO:0000269|PubMed:25499443}.
-!- SUBUNIT: Part of a complex comprised of PTPRA, BCAR1, BCAR3 (via SH2
domain) and SRC; the formation of the complex is dependent on integrin
mediated-tyrosine phosphorylation of PTPRA (PubMed:22801373). Within
the complex, interacts (via SH2 domain) with PTPRA (when phosphorylated
on 'Tyr-825') (PubMed:22801373). Interacts (via Ras-GEF domain) with
BCAR1 (PubMed:10438950, PubMed:10896938, PubMed:12517963). Interacts
with (via Ras-GEF domain) NEDD9 (PubMed:12517963). Interacts with
PTK2B/FAK1 (PubMed:10896938). Interacts with PTPN1. Interacts (via SH2
domain) with EGFR (when tyrosine-phosphorylated) (By similarity).
{ECO:0000250|UniProtKB:O75815, ECO:0000269|PubMed:10438950,
ECO:0000269|PubMed:10896938, ECO:0000269|PubMed:12517963,
ECO:0000269|PubMed:22801373}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25499443}. Cell
junction, focal adhesion {ECO:0000269|PubMed:22801373}.
Note=Localization to focal adhesions depends on interaction with PTPRA.
{ECO:0000269|PubMed:22801373}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9QZK2-1; Sequence=Displayed;
Name=2;
IsoId=Q9QZK2-2; Sequence=VSP_017815;
-!- TISSUE SPECIFICITY: Abundantly expressed in the lung and brain, with
lower expression in splenic lymphocytes and liver (at protein level)
(PubMed:19365570). Expressed in splenic lymphocytes (at protein level)
(PubMed:19365570). Expressed in the lymph node cortical region,
periphery of the splenic white pulp and in alveolar lung fibroblasts
(PubMed:19365570). Expressed in epithelial cells in the lens equatorial
region and early stage nucleated cortical lens fiber cells
(PubMed:19365570). Expressed in the thymus (PubMed:10438950). Expressed
in B-cells (PubMed:12517963). {ECO:0000269|PubMed:10438950,
ECO:0000269|PubMed:12517963, ECO:0000269|PubMed:19365570}.
-!- INDUCTION: Up-regulated by IL1A and LTA, in thymus cortical reticular
cell lines. {ECO:0000269|PubMed:10438950}.
-!- DOMAIN: The SH2 domain mediates interaction with tyrosine-
phosphorylated proteins (PubMed:10896938, PubMed:22801373). However,
not involved in the binding to phosphorylated BCAR1 (PubMed:10896938).
Required for cell cycle progression in response to INS/insulin (By
similarity). Required for regulation of EGF-induced DNA synthesis (By
similarity). {ECO:0000250|UniProtKB:O75815,
ECO:0000269|PubMed:10896938, ECO:0000269|PubMed:22801373}.
-!- DOMAIN: The Ras-GEF domain appears to adopt a closed conformation
rendering it incapable of carrying out canonical exchange factor
function, this closed conformation is probably required for interaction
with BCAR1. {ECO:0000269|PubMed:10896938}.
-!- PTM: Phosphorylated on tyrosine residues.
{ECO:0000269|PubMed:10438950}.
-!- DISRUPTION PHENOTYPE: Knockout mice are generally normal and viable
(PubMed:19365570). Retinal white circular lesions in anterior chamber
derived from the lens cortex (PubMed:19365570). Retinal lens is
partially opaque and irregular in structure, with rupture leading to
cortical lens fragments floating in the aqueous humor
(PubMed:19365570). Abnormally deep anterior chamber with anterior
synechiae, ectropion uveae, mild to moderate retinal ganglion loss, and
a small pigmented pre-retinal membrane overlying the optic nerve
(PubMed:19365570). Reduced phosphorylation of AKT1 and BCAR1 in lens
epithelial cells (PubMed:19365570). Retinal lens abnormalities develop
progressively postnatally; at postnatal day 3 (P3) there is anterior
lens vacuolization and liquefaction of lens cortical fibers
(PubMed:19365570). At P24 there is evidence of extensive lens cortex
vacuolation and early lens extrusion, progressing to extrusion of lens
cortical material at P33 (PubMed:19365570).
{ECO:0000269|PubMed:19365570}.
-!- CAUTION: The guanine nucleotide exchange factor (GEF) activity is
controversial. One study showed GEF activity towards RALA, RAP1A and
RRAS (PubMed:10896938). However, in another study, a construct
containing only the Ras-GEF domain lacks GEF activity towards RAP1 (By
similarity). {ECO:0000250|UniProtKB:O75815,
ECO:0000269|PubMed:10896938}.
---------------------------------------------------------------------------
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EMBL; AF179566; AAD53182.1; -; mRNA.
EMBL; AK143894; BAE25587.1; -; mRNA.
EMBL; AK165396; BAE38160.1; -; mRNA.
EMBL; BC023930; AAH23930.1; -; mRNA.
CCDS; CCDS17810.1; -. [Q9QZK2-1]
RefSeq; NP_038895.1; NM_013867.2. [Q9QZK2-1]
SMR; Q9QZK2; -.
BioGrid; 205895; 1.
STRING; 10090.ENSMUSP00000029766; -.
iPTMnet; Q9QZK2; -.
PhosphoSitePlus; Q9QZK2; -.
PaxDb; Q9QZK2; -.
PeptideAtlas; Q9QZK2; -.
PRIDE; Q9QZK2; -.
Antibodypedia; 2973; 150 antibodies.
Ensembl; ENSMUST00000029766; ENSMUSP00000029766; ENSMUSG00000028121. [Q9QZK2-1]
GeneID; 29815; -.
KEGG; mmu:29815; -.
UCSC; uc008req.2; mouse. [Q9QZK2-1]
CTD; 8412; -.
MGI; MGI:1352501; Bcar3.
eggNOG; ENOG410IFQG; Eukaryota.
eggNOG; ENOG410XTJR; LUCA.
GeneTree; ENSGT00940000154130; -.
HOGENOM; CLU_015281_0_0_1; -.
InParanoid; Q9QZK2; -.
KO; K23688; -.
OMA; HQSESHL; -.
OrthoDB; 138275at2759; -.
PhylomeDB; Q9QZK2; -.
TreeFam; TF323756; -.
ChiTaRS; Bcar3; mouse.
PRO; PR:Q9QZK2; -.
Proteomes; UP000000589; Chromosome 3.
RNAct; Q9QZK2; protein.
Bgee; ENSMUSG00000028121; Expressed in primary oocyte and 267 other tissues.
ExpressionAtlas; Q9QZK2; baseline and differential.
Genevisible; Q9QZK2; MM.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
GO; GO:0019900; F:kinase binding; ISO:MGI.
GO; GO:0001784; F:phosphotyrosine residue binding; ISS:UniProtKB.
GO; GO:0086100; P:endothelin receptor signaling pathway; ISS:UniProtKB.
GO; GO:0008286; P:insulin receptor signaling pathway; ISS:UniProtKB.
GO; GO:0002089; P:lens morphogenesis in camera-type eye; IMP:MGI.
GO; GO:0045740; P:positive regulation of DNA replication; ISS:UniProtKB.
GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:MGI.
GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
Gene3D; 1.10.840.10; -; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR028849; BCAR3.
InterPro; IPR023578; Ras_GEF_dom_sf.
InterPro; IPR001895; RASGEF_cat_dom.
InterPro; IPR036964; RASGEF_cat_dom_sf.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
PANTHER; PTHR14247:SF10; PTHR14247:SF10; 1.
Pfam; PF00617; RasGEF; 1.
Pfam; PF00017; SH2; 1.
SMART; SM00147; RasGEF; 1.
SMART; SM00252; SH2; 1.
SUPFAM; SSF48366; SSF48366; 1.
SUPFAM; SSF55550; SSF55550; 1.
PROSITE; PS50009; RASGEF_CAT; 1.
PROSITE; PS50001; SH2; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Cell junction; Cytoplasm;
Guanine-nucleotide releasing factor; Methylation; Phosphoprotein;
Reference proteome; SH2 domain.
INIT_MET 1
/note="Removed"
/evidence="ECO:0000250|UniProtKB:O75815"
CHAIN 2..820
/note="Breast cancer anti-estrogen resistance protein 3
homolog"
/id="PRO_0000230286"
DOMAIN 148..247
/note="SH2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
DOMAIN 543..813
/note="Ras-GEF"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
REGION 739..743
/note="Mediates the interaction with BCAR1/p130CAS"
/evidence="ECO:0000250|UniProtKB:O75815"
MOD_RES 2
/note="N-acetylalanine"
/evidence="ECO:0000250|UniProtKB:O75815"
MOD_RES 32
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:O75815"
MOD_RES 72
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:O75815"
MOD_RES 77
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:O75815"
MOD_RES 176
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:O75815"
MOD_RES 284
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:O75815"
MOD_RES 329
/note="N6-methyllysine"
/evidence="ECO:0000250|UniProtKB:O75815"
MOD_RES 353
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:O75815"
MOD_RES 358
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:O75815"
MOD_RES 370
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:21183079"
MOD_RES 437
/note="Omega-N-methylarginine"
/evidence="ECO:0000250|UniProtKB:O75815"
MOD_RES 466
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:21183079"
VAR_SEQ 1..120
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:16141072"
/id="VSP_017815"
CONFLICT 36
/note="E -> G (in Ref. 2; BAE25587)"
/evidence="ECO:0000305"
CONFLICT 525
/note="K -> E (in Ref. 2; BAE25587)"
/evidence="ECO:0000305"
CONFLICT 795
/note="R -> G (in Ref. 2; BAE38160)"
/evidence="ECO:0000305"
SEQUENCE 820 AA; 92263 MW; 69DDACECDE869F01 CRC64;
MAAGKFASLP RNMPVNHQFP LASSMDLLSS KSPLAERRTD AYQDVSIHGT LPRKKKGPPS
IRSCDNAGHS KSPRQSSPLT QDIIQENPLQ DRKGENFIFR DPYLLDPTLE YVKFSKERHI
MDRTPERLKK ELEEELLLSS EDLRSHAWYH GRIPRQVSEN LVQRDGDFLV RDSLSSPGNF
VLTCQWKNLA QHFKINRTVL RLSEAYSRVQ YQFEMESFDS IPGLVRCYVG NRRPISQQSG
AIIFQPINRT VPLWCLEERY GTSPGRGREG SLAEGRPDVV KRLSLTTGSS IQAREHSLPR
GNLLRNKEKS GSQPACLDHV QDRKALTLKA HQSESHLPIG CKLPPQSPSM DTSPCPSSPV
FRTGSEPTLS PALVRRFSSD ARTGEALRGS DSQLCPKPPP KPCKVPFLKT PPSPSPWLTS
EANYCELNPA FAVGCDRGAK LPMQAHDSHE MLLTAKQNGP SGPRNSGINY MILDGDDQAR
HWDPLAVQTD EGQEDKTKFV PPLMETVSSF RPNDFESKLL PPENKPLETA MLKHAKELFT
NHDARVIAQH MLSVDCKVAR ILEVSEDRKR SMGVSSGLEL ITLPHGRQLR LDIIERHNTM
AIGIAVDILG CTGTLENRAG TLNKIIQVAV ELKDAMGDLY AFSAIMKALE MPQITRLEKT
WTALRHHYTQ TAILYEKQLK PFSKILHEGR ESTYVPASNV SVPLLMPLVT LMERQAVTFE
GTDMWENNDE SCEILLNHLA TARFMAEASE SYRMNAERIL ADFQPDEEMT EILRTEFQMR
LLWGSKGAEV NQNERYDKFN QILTALSRKL EPPSGKQAEL


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WP1673: Naphthalene and anthracene degradation
WP2218: sGC
WP1888: Post-translational protein modification
WP1049: G Protein Signaling Pathways
WP1909: Signal regulatory protein (SIRP) family interactions
WP346: Protein Modifications
WP1165: G Protein Signaling Pathways
WP1678: Nucleotide excision repair
WP2272: Pathogenic Escherichia coli infection
WP1613: 1,4-Dichlorobenzene degradation
WP232: G Protein Signaling Pathways
WP1625: Base excision repair
WP1690: Propanoate metabolism
WP73: G Protein Signaling Pathways
WP1694: Pyrimidine metabolism
WP1654: gamma-Hexachlorocyclohexane degradation
WP1984: Integrated Breast Cancer Pathway
WP1661: Glyoxylate and dicarboxylate metabolism
WP813: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways

Related Genes :
[Bcar3 And34] Breast cancer anti-estrogen resistance protein 3 homolog (p130Cas-binding protein AND-34)
[Bcar3] Breast cancer anti-estrogen resistance protein 3 homolog (BCAR3 adapter protein, NSP family member) (Novel SH2-containing protein 2) (SH2 domain-containing protein 3B) (p130Cas-binding protein AND-34)
[MUC1 PUM] Mucin-1 (MUC-1) (Breast carcinoma-associated antigen DF3) (Cancer antigen 15-3) (CA 15-3) (Carcinoma-associated mucin) (Episialin) (H23AG) (Krebs von den Lungen-6) (KL-6) (PEMT) (Peanut-reactive urinary mucin) (PUM) (Polymorphic epithelial mucin) (PEM) (Tumor-associated epithelial membrane antigen) (EMA) (Tumor-associated mucin) (CD antigen CD227) [Cleaved into: Mucin-1 subunit alpha (MUC1-NT) (MUC1-alpha); Mucin-1 subunit beta (MUC1-beta) (MUC1-CT)]
[CDC42] Cell division control protein 42 homolog (EC 3.6.5.2) (G25K GTP-binding protein)
[PRPF31 PRP31] U4/U6 small nuclear ribonucleoprotein Prp31 (Pre-mRNA-processing factor 31) (Serologically defined breast cancer antigen NY-BR-99) (U4/U6 snRNP 61 kDa protein) (Protein 61K) (hPrp31)
[ESR1 ESR NR3A1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
[DPH1 DPH2L DPH2L1 OVCA1] 2-(3-amino-3-carboxypropyl)histidine synthase subunit 1 (EC 2.5.1.108) (Diphthamide biosynthesis protein 1) (Diphtheria toxin resistance protein 1) (Ovarian cancer-associated gene 1 protein) (S-adenosyl-L-methionine:L-histidine 3-amino-3-carboxypropyltransferase 1)
[SRC SRC1] Proto-oncogene tyrosine-protein kinase Src (EC 2.7.10.2) (Proto-oncogene c-Src) (pp60c-src) (p60-Src)
[Ptk2 Fadk Fak Fak1 Kiaa4203] Focal adhesion kinase 1 (FADK 1) (EC 2.7.10.2) (Focal adhesion kinase-related nonkinase) (FRNK) (Protein-tyrosine kinase 2) (p125FAK) (pp125FAK)
[SVEP1 C9orf13 CCP22 SELOB] Sushi, von Willebrand factor type A, EGF and pentraxin domain-containing protein 1 (CCP module-containing protein 22) (Polydom) (Selectin-like osteoblast-derived protein) (SEL-OB) (Serologically defined breast cancer antigen NY-BR-38)
[HSPB1 HSP27 HSP28] Heat shock protein beta-1 (HspB1) (28 kDa heat shock protein) (Estrogen-regulated 24 kDa protein) (Heat shock 27 kDa protein) (HSP 27) (Stress-responsive protein 27) (SRP27)
[PSMD6 KIAA0107 PFAAP4] 26S proteasome non-ATPase regulatory subunit 6 (26S proteasome regulatory subunit RPN7) (26S proteasome regulatory subunit S10) (Breast cancer-associated protein SGA-113M) (Phosphonoformate immuno-associated protein 4) (Proteasome regulatory particle subunit p44S10) (p42A)
[Gper1 Cmkrl2 Gper Gpr30] G-protein coupled estrogen receptor 1 (Chemoattractant receptor-like 2) (G protein-coupled estrogen receptor 1) (G-protein coupled receptor 30) (Membrane estrogen receptor) (mER)
[Casc3 Mln51] Protein CASC3 (Cancer susceptibility candidate gene 3 protein homolog) (Metastatic lymph node gene 51 protein homolog) (MLN 51 homolog) (Protein barentsz) (Btz) (mBtz)
[PTEN MMAC1 TEP1] Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (EC 3.1.3.16) (EC 3.1.3.48) (EC 3.1.3.67) (Mutated in multiple advanced cancers 1) (Phosphatase and tensin homolog)
[TNK2 ACK1] Activated CDC42 kinase 1 (ACK-1) (EC 2.7.10.2) (EC 2.7.11.1) (Tyrosine kinase non-receptor protein 2)
[FN1 FN] Fibronectin (FN) (Cold-insoluble globulin) (CIG) [Cleaved into: Anastellin; Ugl-Y1; Ugl-Y2; Ugl-Y3]
[MLH1 COCA2] DNA mismatch repair protein Mlh1 (MutL protein homolog 1)
[KMT2A ALL1 CXXC7 HRX HTRX MLL MLL1 TRX1] Histone-lysine N-methyltransferase 2A (Lysine N-methyltransferase 2A) (EC 2.1.1.354) (ALL-1) (CXXC-type zinc finger protein 7) (Myeloid/lymphoid or mixed-lineage leukemia) (Myeloid/lymphoid or mixed-lineage leukemia protein 1) (Trithorax-like protein) (Zinc finger protein HRX) [Cleaved into: MLL cleavage product N320 (N-terminal cleavage product of 320 kDa) (p320); MLL cleavage product C180 (C-terminal cleavage product of 180 kDa) (p180)]
[NTG1 OGG2 SCR1 YAL015C FUN33] Endonuclease III homolog 1 (EC 3.2.2.-) (EC 4.2.99.18) (Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase 1) (DNA glycosylase/AP lyase 1) (Endonuclease III-like glycosylase 1) (Redoxyendonuclease 1)
[RAD51 RAD51A RECA] DNA repair protein RAD51 homolog 1 (HsRAD51) (hRAD51) (RAD51 homolog A)
[CHEK2 CDS1 CHK2 RAD53] Serine/threonine-protein kinase Chk2 (EC 2.7.11.1) (CHK2 checkpoint homolog) (Cds1 homolog) (Hucds1) (hCds1) (Checkpoint kinase 2)
[MSH2] DNA mismatch repair protein Msh2 (hMSH2) (MutS protein homolog 2)
[Or22a AN11 DOR22A.1 dor53 Or22A.1 CG12193] Odorant receptor 22a
[SIRT2 SIR2L SIR2L2] NAD-dependent protein deacetylase sirtuin-2 (EC 2.3.1.286) (Regulatory protein SIR2 homolog 2) (SIR2-like protein 2)
[Cdk1 Cdc2 Cdc2a Cdkn1] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[Or22b AN12 DOR22A.2 dor67 Or22A.2 CG4231] Odorant receptor 22b
[CDK1 CDC2 CDC28A CDKN1 P34CDC2] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[SMAD3 MADH3] Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (hMAD-3) (JV15-2) (SMAD family member 3) (SMAD 3) (Smad3) (hSMAD3)
[ABCC6 ARA MRP6] Multidrug resistance-associated protein 6 (ATP-binding cassette sub-family C member 6) (Anthracycline resistance-associated protein) (Multi-specific organic anion transporter E) (MOAT-E)

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