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Fibroblast growth factor receptor substrate 2 (FGFR substrate 2) (FGFR-signaling adaptor SNT) (FRS2-alpha) (Suc1-associated neurotrophic factor target 1) (SNT-1)

 FRS2_MOUSE              Reviewed;         508 AA.
Q8C180;
19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
23-MAY-2018, entry version 129.
RecName: Full=Fibroblast growth factor receptor substrate 2;
Short=FGFR substrate 2;
AltName: Full=FGFR-signaling adaptor SNT;
AltName: Full=FRS2-alpha;
AltName: Full=Suc1-associated neurotrophic factor target 1;
Short=SNT-1;
Name=Frs2; Synonyms=Frs2a;
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 [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Skin;
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
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).
[3]
PROTEIN SEQUENCE OF 251-260; 305-320; 344-361 AND 468-480, FUNCTION,
INTERACTION WITH GRB2, IDENTIFICATION IN A COMPLEX WITH GRB2 AND SOS1,
MYRISTOYLATION AT GLY-2, MUTAGENESIS OF GLY-2; TYR-196; TYR-306;
TYR-349 AND TYR-392, PHOSPHORYLATION AT TYR-196; TYR-306; TYR-349 AND
TYR-392, AND TISSUE SPECIFICITY.
PubMed=9182757; DOI=10.1016/S0092-8674(00)80252-4;
Kouhara H., Hadari Y.R., Spivak-Kroizman T., Schilling J.,
Bar-Sagi D., Lax I., Schlessinger J.;
"A lipid-anchored Grb2-binding protein that links FGF-receptor
activation to the Ras/MAPK signaling pathway.";
Cell 89:693-702(1997).
[4]
INTERACTION WITH SUC1 AND GRB2, PHOSPHORYLATION AT TYROSINE RESIDUES,
AND SUBCELLULAR LOCATION.
PubMed=8780727; DOI=10.1006/bbrc.1996.1288;
Ong S.-H., Goh K.C., Lim Y.P., Low B.C., Klint P., Claesson-Welsh L.,
Cao X., Tan Y.H., Guy G.R.;
"Suc1-associated neurotrophic factor target (SNT) protein is a major
FGF-stimulated tyrosine phosphorylated 90-kDa protein which binds to
the SH2 domain of GRB2.";
Biochem. Biophys. Res. Commun. 225:1021-1026(1996).
[5]
INTERACTION WITH PTPN11, FUNCTION, PHOSPHORYLATION AT TYR-196;
TYR-306; TYR-349; TYR-392 AND TYR-436, AND MUTAGENESIS OF TYR-436.
PubMed=9632781; DOI=10.1128/MCB.18.7.3966;
Hadari Y.R., Kouhara H., Lax I., Schlessinger J.;
"Binding of Shp2 tyrosine phosphatase to FRS2 is essential for
fibroblast growth factor-induced PC12 cell differentiation.";
Mol. Cell. Biol. 18:3966-3973(1998).
[6]
PHOSPHORYLATION IN RESPONSE TO FRFR2 AND FGFR3 ACTIVATION.
PubMed=10851026; DOI=10.1083/jcb.149.6.1297;
Mansukhani A., Bellosta P., Sahni M., Basilico C.;
"Signaling by fibroblast growth factors (FGF) and fibroblast growth
factor receptor 2 (FGFR2)-activating mutations blocks mineralization
and induces apoptosis in osteoblasts.";
J. Cell Biol. 149:1297-1308(2000).
[7]
INTERACTION WITH FGFR1 AND NTRK1.
PubMed=10629055; DOI=10.1128/MCB.20.3.979-989.2000;
Ong S.-H., Guy G.R., Hadari Y.R., Laks S., Gotoh N., Schlessinger J.,
Lax I.;
"FRS2 proteins recruit intracellular signaling pathways by binding to
diverse targets on fibroblast growth factor and nerve growth factor
receptors.";
Mol. Cell. Biol. 20:979-989(2000).
[8]
FUNCTION, INTERACTION WITH RET, AND PHOSPHORYLATION AT TYROSINE
RESIDUES.
PubMed=11390647; DOI=10.1128/MCB.21.13.4177-4187.2001;
Melillo R.M., Santoro M., Ong S.-H., Billaud M., Fusco A.,
Hadari Y.R., Schlessinger J., Lax I.;
"Docking protein FRS2 links the protein tyrosine kinase RET and its
oncogenic forms with the mitogen-activated protein kinase signaling
cascade.";
Mol. Cell. Biol. 21:4177-4187(2001).
[9]
IDENTIFICATION IN A COMPLEX WITH NCAM1; CDH2; PLCG1; FRS2; SRC; SHC1;
GAP43 AND CTTN.
PubMed=11433297; DOI=10.1038/35083041;
Cavallaro U., Niedermeyer J., Fuxa M., Christofori G.;
"N-CAM modulates tumour-cell adhesion to matrix by inducing FGF-
receptor signalling.";
Nat. Cell Biol. 3:650-657(2001).
[10]
FUNCTION, INTERACTION WITH GRB2 AND GAB1, AND PHOSPHORYLATION AT
TYR-196; TYR-306; TYR-349; TYR-392; TYR-436 AND TYR-471.
PubMed=11353842; DOI=10.1073/pnas.111114298;
Ong S.H., Hadari Y.R., Gotoh N., Guy G.R., Schlessinger J., Lax I.;
"Stimulation of phosphatidylinositol 3-kinase by fibroblast growth
factor receptors is mediated by coordinated recruitment of multiple
docking proteins.";
Proc. Natl. Acad. Sci. U.S.A. 98:6074-6079(2001).
[11]
FUNCTION IN ACTIVATION OF SIGNALING VIA RAS AND MAP KINASES,
INTERACTION WITH PTPN11, AND PHOSPHORYLATION.
PubMed=12181353; DOI=10.1091/mbc.E02-02-0103;
Cross M.J., Lu L., Magnusson P., Nyqvist D., Holmqvist K., Welsh M.,
Claesson-Welsh L.;
"The Shb adaptor protein binds to tyrosine 766 in the FGFR-1 and
regulates the Ras/MEK/MAPK pathway via FRS2 phosphorylation in
endothelial cells.";
Mol. Biol. Cell 13:2881-2893(2002).
[12]
IDENTIFICATION IN A COMPLEX WITH GRB2 AND CBL, AND UBIQUITINATION.
PubMed=11997436; DOI=10.1073/pnas.052138899;
Wong A., Lamothe B., Lee A., Schlessinger J., Lax I.;
"FRS2 alpha attenuates FGF receptor signaling by Grb2-mediated
recruitment of the ubiquitin ligase Cbl.";
Proc. Natl. Acad. Sci. U.S.A. 99:6684-6689(2002).
[13]
PHOSPHORYLATION BY ULK2.
PubMed=16887332; DOI=10.1016/j.cellsig.2006.06.003;
Avery A.W., Figueroa C., Vojtek A.B.;
"UNC-51-like kinase regulation of fibroblast growth factor receptor
substrate 2/3.";
Cell. Signal. 19:177-184(2007).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[15]
REVIEW ON FUNCTION; SUBUNIT AND PHOSPHORYLATION.
PubMed=18452557; DOI=10.1111/j.1349-7006.2008.00840.x;
Gotoh N.;
"Regulation of growth factor signaling by FRS2 family docking/scaffold
adaptor proteins.";
Cancer Sci. 99:1319-1325(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-349, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Heart, Kidney, Lung, and Spleen;
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).
[19]
REVIEW ON FUNCTION IN FGF SIGNALING.
PubMed=20094046; DOI=10.1038/nrc2780;
Turner N., Grose R.;
"Fibroblast growth factor signalling: from development to cancer.";
Nat. Rev. Cancer 10:116-129(2010).
-!- FUNCTION: Adapter protein that links activated FGR and NGF
receptors to downstream signaling pathways. Plays an important
role in the activation of MAP kinases and in the phosphorylation
of PIK3R1, the regulatory subunit of phosphatidylinositol 3-
kinase, in response to ligand-mediated activation of FGFR1.
Modulates signaling via SHC1 by competing for a common binding
site on NTRK1. {ECO:0000269|PubMed:11353842,
ECO:0000269|PubMed:11390647, ECO:0000269|PubMed:12181353,
ECO:0000269|PubMed:9182757, ECO:0000269|PubMed:9632781}.
-!- SUBUNIT: Part of a complex containing FRS2, GRB2, GAB1, PIK3R1 and
SOS1. Part of a complex containing GRB2 and CBL. Binds ALK, CKS2,
FGFR1, RET, MAPK1/ERK2, MAPK3/ERK1 and SRC. The tyrosine-
phosphorylated protein binds the SH2 domains of GRB2 and PTPN11.
Interacts with NTRK1, NTRK2 and NTRK3 (phosphorylated upon ligand-
binding) (By similarity). Identified in a complex containing
FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN.
{ECO:0000250, ECO:0000269|PubMed:10629055,
ECO:0000269|PubMed:11353842, ECO:0000269|PubMed:11390647,
ECO:0000269|PubMed:11433297, ECO:0000269|PubMed:11997436,
ECO:0000269|PubMed:12181353, ECO:0000269|PubMed:8780727,
ECO:0000269|PubMed:9182757, ECO:0000269|PubMed:9632781}.
-!- INTERACTION:
Q60631:Grb2; NbExp=5; IntAct=EBI-6880000, EBI-1688;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:8780727};
Lipid-anchor {ECO:0000269|PubMed:8780727}.
-!- TISSUE SPECIFICITY: Ubiquitous. Expression is highest in brain,
kidney, lung and testis. {ECO:0000269|PubMed:9182757}.
-!- PTM: Phosphorylated on tyrosine residues upon stimulation by FGF2
or NGFB. Phosphorylated by ULK2 (in vitro). Phosphorylated on
tyrosine residues by activated ALK and FGFR1. Phosphorylated on
tyrosine residues upon activation of FGFR2 and FGFR3.
Phosphorylated on threonine residues by MAP kinases; this inhibits
tyrosine phosphorylation, and thereby down-regulates FRS2-mediated
activation of MAP kinases.
-!- PTM: Ubiquitinated when tyrosine phosphorylated and in a complex
with GRB2. The unphosphorylated form is not subject to
ubiquitination. {ECO:0000269|PubMed:11997436}.
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EMBL; AK028813; BAC26132.1; -; mRNA.
EMBL; BC043109; AAH43109.1; -; mRNA.
EMBL; BC055334; AAH55334.1; -; mRNA.
CCDS; CCDS24190.1; -.
RefSeq; NP_808466.1; NM_177798.3.
UniGene; Mm.135965; -.
ProteinModelPortal; Q8C180; -.
SMR; Q8C180; -.
BioGrid; 236497; 6.
CORUM; Q8C180; -.
IntAct; Q8C180; 2.
MINT; Q8C180; -.
STRING; 10090.ENSMUSP00000020381; -.
iPTMnet; Q8C180; -.
PhosphoSitePlus; Q8C180; -.
SwissPalm; Q8C180; -.
MaxQB; Q8C180; -.
PaxDb; Q8C180; -.
PeptideAtlas; Q8C180; -.
PRIDE; Q8C180; -.
Ensembl; ENSMUST00000020381; ENSMUSP00000020381; ENSMUSG00000020170.
GeneID; 327826; -.
KEGG; mmu:327826; -.
UCSC; uc007hct.1; mouse.
CTD; 10818; -.
MGI; MGI:1100860; Frs2.
eggNOG; KOG4047; Eukaryota.
eggNOG; ENOG410XS2S; LUCA.
GeneTree; ENSGT00510000046707; -.
HOGENOM; HOG000290694; -.
HOVERGEN; HBG062705; -.
InParanoid; Q8C180; -.
KO; K12461; -.
OMA; SAHKVEF; -.
OrthoDB; EOG091G06AV; -.
PhylomeDB; Q8C180; -.
TreeFam; TF324994; -.
Reactome; R-MMU-109704; PI3K Cascade.
Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
Reactome; R-MMU-170968; Frs2-mediated activation.
Reactome; R-MMU-5654689; PI-3K cascade:FGFR1.
Reactome; R-MMU-5654693; FRS-mediated FGFR1 signaling.
Reactome; R-MMU-5654695; PI-3K cascade:FGFR2.
Reactome; R-MMU-5654700; FRS-mediated FGFR2 signaling.
Reactome; R-MMU-5654706; FRS-mediated FGFR3 signaling.
Reactome; R-MMU-5654710; PI-3K cascade:FGFR3.
Reactome; R-MMU-5654712; FRS-mediated FGFR4 signaling.
Reactome; R-MMU-5654720; PI-3K cascade:FGFR4.
Reactome; R-MMU-5654726; Negative regulation of FGFR1 signaling.
Reactome; R-MMU-5654727; Negative regulation of FGFR2 signaling.
Reactome; R-MMU-5654732; Negative regulation of FGFR3 signaling.
Reactome; R-MMU-5654733; Negative regulation of FGFR4 signaling.
Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-MMU-8853659; RET signaling.
Reactome; R-MMU-9028731; Activated NTRK2 signals through FRS2 and FRS3.
PRO; PR:Q8C180; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000020170; -.
CleanEx; MM_FRS2; -.
Genevisible; Q8C180; MM.
GO; GO:0005913; C:cell-cell adherens junction; ISO:MGI.
GO; GO:0005911; C:cell-cell junction; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0005104; F:fibroblast growth factor receptor binding; ISO:MGI.
GO; GO:0005168; F:neurotrophin TRKA receptor binding; ISO:MGI.
GO; GO:0005068; F:transmembrane receptor protein tyrosine kinase adaptor activity; IDA:MGI.
GO; GO:0000187; P:activation of MAPK activity; IMP:MGI.
GO; GO:0008595; P:anterior/posterior axis specification, embryo; IMP:MGI.
GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IMP:MGI.
GO; GO:0030900; P:forebrain development; IMP:MGI.
GO; GO:0001702; P:gastrulation with mouth forming second; IMP:MGI.
GO; GO:0002088; P:lens development in camera-type eye; IMP:MGI.
GO; GO:0070307; P:lens fiber cell development; IMP:MGI.
GO; GO:2000726; P:negative regulation of cardiac muscle cell differentiation; ISO:MGI.
GO; GO:0007405; P:neuroblast proliferation; IMP:MGI.
GO; GO:0046619; P:optic placode formation involved in camera-type eye formation; IMP:MGI.
GO; GO:0001759; P:organ induction; IMP:MGI.
GO; GO:0060527; P:prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis; IMP:MGI.
GO; GO:0042981; P:regulation of apoptotic process; IMP:MGI.
GO; GO:0050678; P:regulation of epithelial cell proliferation; IMP:MGI.
GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IMP:MGI.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IDA:MGI.
GO; GO:0003281; P:ventricular septum development; IMP:MGI.
CDD; cd01202; PTB_FRS2; 1.
InterPro; IPR038742; FRS2_PTB.
InterPro; IPR002404; IRS_PTB.
Pfam; PF02174; IRS; 1.
SMART; SM00310; PTBI; 1.
PROSITE; PS51064; IRS_PTB; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Lipoprotein; Membrane;
Myristate; Phosphoprotein; Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000255}.
CHAIN 2 508 Fibroblast growth factor receptor
substrate 2.
/FTId=PRO_0000087345.
DOMAIN 13 115 IRS-type PTB. {ECO:0000255|PROSITE-
ProRule:PRU00389}.
MOD_RES 177 177 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WU20}.
MOD_RES 196 196 Phosphotyrosine; by FGFR1.
{ECO:0000269|PubMed:11353842,
ECO:0000269|PubMed:9182757,
ECO:0000269|PubMed:9632781}.
MOD_RES 211 211 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 221 221 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WU20}.
MOD_RES 306 306 Phosphotyrosine; by FGFR1.
{ECO:0000269|PubMed:11353842,
ECO:0000269|PubMed:9182757,
ECO:0000269|PubMed:9632781}.
MOD_RES 349 349 Phosphotyrosine; by FGFR1.
{ECO:0000244|PubMed:19131326,
ECO:0000269|PubMed:11353842,
ECO:0000269|PubMed:9182757,
ECO:0000269|PubMed:9632781}.
MOD_RES 365 365 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WU20}.
MOD_RES 392 392 Phosphotyrosine; by FGFR1.
{ECO:0000269|PubMed:11353842,
ECO:0000269|PubMed:9182757,
ECO:0000269|PubMed:9632781}.
MOD_RES 436 436 Phosphotyrosine; by FGFR1.
{ECO:0000269|PubMed:11353842,
ECO:0000269|PubMed:9632781}.
MOD_RES 471 471 Phosphotyrosine; by FGFR1.
{ECO:0000269|PubMed:11353842}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000269|PubMed:9182757}.
MUTAGEN 2 2 G->A: Abolishes myristoylation and
membrane association.
{ECO:0000269|PubMed:9182757}.
MUTAGEN 196 196 Y->F: Abolishes tyrosine phosphorylation
and interactions with GRB2 and PTPN11;
when associated with F-306; F-349; F-392
and F-436. {ECO:0000269|PubMed:9182757}.
MUTAGEN 306 306 Y->F: Abolishes tyrosine phosphorylation
and interactions with GRB2 and PTPN11;
when associated with F-196; F-349; F-392
and F-436. {ECO:0000269|PubMed:9182757}.
MUTAGEN 349 349 Y->F: Abolishes tyrosine phosphorylation
and interactions with GRB2 and PTPN11;
when associated with F-196; F-306; F-392
and F-436. {ECO:0000269|PubMed:9182757}.
MUTAGEN 392 392 Y->F: Abolishes tyrosine phosphorylation
and interactions with GRB2 and PTPN11;
when associated with F-196; F-306; F-349
and F-436. {ECO:0000269|PubMed:9182757}.
MUTAGEN 436 436 Y->F: Abolishes tyrosine phosphorylation
and interactions with GRB2 and PTPN11;
when associated with F-196; F-306; F-349
and F-392. {ECO:0000269|PubMed:9632781}.
SEQUENCE 508 AA; 56794 MW; DFFE8A818BFF8631 CRC64;
MGSCCSCPDK DTVPDNHRNK FKVINVDDDG NELGSGVMEL TDTELILYTR KRDSVKWHYL
CLRRYGYDSN LFSFESGRRC QTGQGIFAFK CARAEELFNM LQEIMQNNSI NVVEEPVVER
SSHQTELEVP RTPRTPTTPG LGAQNLPNGY PRYPSFGDAS SHPSSRHPSV GSARLPSVGE
ESTHPLLVAE EQVHTYVNTT GVQEERKNRA SVHVPPEARV SNAESNTPKE EPSNPEDRDP
QVLLKPEGVR FVLGPTPVQK QLMEKEKLEQ LGKDPVSGSG AGNTEWDTGY DSDERRDVPP
VNKLVYENIN GLSIPSASGV RRGRLTSTST SDTQNINNSA QRRPALLNYE NLPSLPPVWE
ARKLSRDEDD NLGPKTPSLN GYHNNLDPMH NYVNTENVTV PASAHKIDYS KRRDCTPTVF
NFDIRRPSLE HRQLNYIQVD LEGGSDSDNP QTPKTPTTPL PQTPTRRTEL YAVIDIERTA
AMSNLQKALP RDDGTSRKTR HNSTDLPM


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Catalog number Product name Quantity
20-272-191050 FRS2 - Mouse monoclonal [0.T.200] to FRS2; FGFR substrate 2; Suc1-associated neurotrophic factor target 1; SNT-1; FGFR-signaling adaptor SNT Monoclonal 0.05 mg
18-272-195081 FRS2 - Rabbit polyclonal to FRS2; FGFR substrate 2; Suc1-associated neurotrophic factor target 1; SNT-1; FGFR-signaling adaptor SNT Polyclonal 0.1 ml
E02F0125 Rat Fibroblast Growth Factor Receptor SubstRate 2 ELISA , FRS2 96 Tests/kit
201-11-1340 Rat Fibroblast Growth Factor Receptor Substrate 2 (FRS2)ELISA Kit 96T
E02F0125 Rat Fibroblast Growth Factor Receptor SubstRate 2 ELISA , FRS2
E1381725 Fibroblast Growth Factor Receptor Substrate 2 (FRS2) ELISA Kit 1
E92063Ra ELISA Kit for Rat Fibroblast Growth Factor Receptor Substrate 2(FRS2) 96T
UB-E10305 Rat Fibroblast Growth Factor Receptor SubstRate 2(FRS2)ELISA Kit 96T
QY-E10305 Rat Fibroblast Growth Factor Receptor SubstRate 2(FRS2)ELISA Kit 96T
201-11-1340 Rat Fibroblast Growth Factor Receptor SubstRate 2(FRS2)ELISA Kit 96T
FRTS FRS2 Gene fibroblast growth factor receptor substrate 2
E02F0125 Rat Fibroblast Growth Factor Receptor SubstRate 2 Elisa Kit (FRS2) 96 Tests/kit
201-20-2110 FRS2{fibroblast growth factor receptor substrate 2}rabbit.pAb 0.2ml
CSB-EL009004HU Human Fibroblast growth factor receptor substrate 2(FRS2) ELISA kit 96T
E14F0125 Sheep Fibroblast Growth Factor Receptor SubstRate 2 ELISA , FRS2
E09F0125 Monkey Fibroblast Growth Factor Receptor SubstRate 2 ELISA , FRS2 96 Tests/kit
E-EL-MK0841 Monkey FRS2 (Fibroblast Growth Factor Receptor Substrate 2) ELISA Kit 96T
E01F0125 Human Fibroblast Growth Factor Receptor SubstRate 2 ELISA , FRS2 96 Tests/kit
E12F0125 Chicken Fibroblast Growth Factor Receptor SubstRate 2 ELISA , FRS2 96 Tests/kit
E14F0125 Sheep Fibroblast Growth Factor Receptor SubstRate 2 ELISA , FRS2 96 Tests/kit
E06F0125 Goat Fibroblast Growth Factor Receptor SubstRate 2 Elisa Kit (FRS2) 96 Tests/kit
E-EL-P0494 Porcine FRS2 (Fibroblast Growth Factor Receptor Substrate 2) ELISA Kit 96T
E03F0125 Mouse Fibroblast Growth Factor Receptor SubstRate 2 ELISA ,FRS2 96 Tests/kit
E01F0125 Human Fibroblast Growth Factor Receptor SubstRate 2 Elisa Kit (FRS2) 96 Tests/kit
E06F0125 Goat Fibroblast Growth Factor Receptor SubstRate 2 ELISA , FRS2 96 Tests/kit


 

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