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Breast cancer anti-estrogen resistance protein 3 (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.
20-JUN-2018, entry version 122.
RecName: Full=Breast cancer anti-estrogen resistance protein 3;
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, INTERACTION WITH NEDD9, AND FUNCTION.
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]
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).
-!- FUNCTION: May act as an adapter protein and couple activated
growth factor receptors to signaling molecules that regulate src
kinase activity and promote cell migration.
{ECO:0000269|PubMed:10896938, ECO:0000269|PubMed:12517963}.
-!- SUBUNIT: Interacts with BCAR1, NEDD9, PTK2/FAK1 and PTPN1.
{ECO:0000269|PubMed:10438950, ECO:0000269|PubMed:10896938,
ECO:0000269|PubMed:12517963}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9QZK2-1; Sequence=Displayed;
Name=2;
IsoId=Q9QZK2-2; Sequence=VSP_017815;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in B-cells.
{ECO:0000269|PubMed:10438950, ECO:0000269|PubMed:12517963}.
-!- INDUCTION: Up-regulated by IL1A and LTA, in thymus cortical
reticular cell lines. {ECO:0000269|PubMed:10438950}.
-!- PTM: Phosphorylated on tyrosine. {ECO:0000269|PubMed:10438950}.
-----------------------------------------------------------------------
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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]
UniGene; Mm.398478; -.
UniGene; Mm.45815; -.
ProteinModelPortal; Q9QZK2; -.
SMR; Q9QZK2; -.
BioGrid; 205895; 1.
STRING; 10090.ENSMUSP00000029766; -.
iPTMnet; Q9QZK2; -.
PhosphoSitePlus; Q9QZK2; -.
PaxDb; Q9QZK2; -.
PeptideAtlas; Q9QZK2; -.
PRIDE; Q9QZK2; -.
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; ENSGT00390000008976; -.
HOGENOM; HOG000231595; -.
HOVERGEN; HBG053174; -.
InParanoid; Q9QZK2; -.
OMA; NYCELNP; -.
OrthoDB; EOG091G01KG; -.
PhylomeDB; Q9QZK2; -.
TreeFam; TF323756; -.
ChiTaRS; Bcar3; mouse.
PRO; PR:Q9QZK2; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000028121; -.
CleanEx; MM_BCAR3; -.
ExpressionAtlas; Q9QZK2; baseline and differential.
Genevisible; Q9QZK2; MM.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
GO; GO:0005070; F:SH3/SH2 adaptor activity; IBA:GO_Central.
GO; GO:0002089; P:lens morphogenesis in camera-type eye; IMP:MGI.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:MGI.
GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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; Complete proteome;
Guanine-nucleotide releasing factor; Methylation; Phosphoprotein;
Reference proteome; SH2 domain.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:O75815}.
CHAIN 2 820 Breast cancer anti-estrogen resistance
protein 3.
/FTId=PRO_0000230286.
DOMAIN 148 247 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 543 813 Ras-GEF. {ECO:0000255|PROSITE-
ProRule:PRU00168}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:O75815}.
MOD_RES 32 32 Phosphoserine.
{ECO:0000250|UniProtKB:O75815}.
MOD_RES 72 72 Phosphoserine.
{ECO:0000250|UniProtKB:O75815}.
MOD_RES 77 77 Phosphoserine.
{ECO:0000250|UniProtKB:O75815}.
MOD_RES 176 176 Phosphoserine.
{ECO:0000250|UniProtKB:O75815}.
MOD_RES 284 284 Phosphoserine.
{ECO:0000250|UniProtKB:O75815}.
MOD_RES 329 329 N6-methyllysine.
{ECO:0000250|UniProtKB:O75815}.
MOD_RES 353 353 Phosphoserine.
{ECO:0000250|UniProtKB:O75815}.
MOD_RES 358 358 Phosphoserine.
{ECO:0000250|UniProtKB:O75815}.
MOD_RES 370 370 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 437 437 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:O75815}.
MOD_RES 466 466 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
VAR_SEQ 1 120 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_017815.
CONFLICT 36 36 E -> G (in Ref. 2; BAE25587).
{ECO:0000305}.
CONFLICT 525 525 K -> E (in Ref. 2; BAE25587).
{ECO:0000305}.
CONFLICT 795 795 R -> G (in Ref. 2; BAE38160).
{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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