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Growth factor receptor-bound protein 2 (Adapter protein GRB2) (SH2/SH3 adapter GRB2)

 GRB2_MOUSE              Reviewed;         217 AA.
Q60631; Q61240;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 191.
RecName: Full=Growth factor receptor-bound protein 2;
AltName: Full=Adapter protein GRB2;
AltName: Full=SH2/SH3 adapter GRB2;
Name=Grb2;
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].
STRAIN=BALB/cJ;
PubMed=7689150; DOI=10.1128/MCB.13.9.5500;
Suen K., Bustelo X.R., Pawson T., Barbacid M.;
"Molecular cloning of the mouse grb2 gene: differential interaction of
the Grb2 adaptor protein with epidermal growth factor and nerve growth
factor receptors.";
Mol. Cell. Biol. 13:5500-5512(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=BALB/cJ;
Tanaka S.;
Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary gland;
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]
PROTEIN SEQUENCE OF 125-136, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Hippocampus;
Lubec G., Klug S.;
Submitted (MAR-2007) to UniProtKB.
[5]
INTERACTION WITH PTK2/FAK1.
PubMed=7997267; DOI=10.1038/372786a0;
Schlaepfer D.D., Hanks S.K., Hunter T., van der Geer P.;
"Integrin-mediated signal transduction linked to Ras pathway by GRB2
binding to focal adhesion kinase.";
Nature 372:786-791(1994).
[6]
INTERACTION WITH PDGFRA AND PTPN11.
PubMed=8943348; DOI=10.1128/MCB.16.12.6926;
Bazenet C.E., Gelderloos J.A., Kazlauskas A.;
"Phosphorylation of tyrosine 720 in the platelet-derived growth factor
alpha receptor is required for binding of Grb2 and SHP-2 but not for
activation of Ras or cell proliferation.";
Mol. Cell. Biol. 16:6926-6936(1996).
[7]
INTERACTION WITH CSF1R, AND PHOSPHORYLATION.
PubMed=9312046; DOI=10.1093/emboj/16.19.5880;
Bourette R.P., Myles G.M., Choi J.L., Rohrschneider L.R.;
"Sequential activation of phoshatidylinositol 3-kinase and
phospholipase C-gamma2 by the M-CSF receptor is necessary for
differentiation signaling.";
EMBO J. 16:5880-5893(1997).
[8]
INTERACTION WITH REPS1.
TISSUE=Muscle;
PubMed=9395447; DOI=10.1074/jbc.272.50.31230;
Yamaguchi A., Urano T., Goi T., Feig L.A.;
"An eps homology (EH) domain protein that binds to the ral-GTPase
target, RalBP1.";
J. Biol. Chem. 272:31230-31234(1997).
[9]
INTERACTION WITH FLT1.
PubMed=9722576; DOI=10.1074/jbc.273.36.23410;
Ito N., Wernstedt C., Engstrom U., Claesson-Welsh L.;
"Identification of vascular endothelial growth factor receptor-1
tyrosine phosphorylation sites and binding of SH2 domain-containing
molecules.";
J. Biol. Chem. 273:23410-23418(1998).
[10]
INTERACTION WITH DAB2.
PubMed=9569023; DOI=10.1038/sj.onc.1201678;
Xu X.X., Yi T., Tang B., Lambeth J.D.;
"Disabled-2 (Dab2) is an SH3 domain-binding partner of Grb2.";
Oncogene 16:1561-1569(1998).
[11]
INTERACTION WITH KIT.
PubMed=10377264; DOI=10.1042/bj3410211;
Thommes K., Lennartsson J., Carlberg M., Ronnstrand L.;
"Identification of Tyr-703 and Tyr-936 as the primary association
sites for Grb2 and Grb7 in the c-Kit/stem cell factor receptor.";
Biochem. J. 341:211-216(1999).
[12]
INTERACTION WITH GAB2.
PubMed=10068651;
Nishida K., Yoshida Y., Itoh M., Fukada T., Ohtani T., Shirogane T.,
Atsumi T., Takahashi-Tezuka M., Ishihara K., Hibi M., Hirano T.;
"Gab-family adapter proteins act downstream of cytokine and growth
factor receptors and T- and B-cell antigen receptors.";
Blood 93:1809-1816(1999).
[13]
INTERACTION WITH TEK/TIE2.
PubMed=10521483; DOI=10.1074/jbc.274.43.30896;
Jones N., Master Z., Jones J., Bouchard D., Gunji Y., Sasaki H.,
Daly R., Alitalo K., Dumont D.J.;
"Identification of Tek/Tie2 binding partners. Binding to a
multifunctional docking site mediates cell survival and migration.";
J. Biol. Chem. 274:30896-30905(1999).
[14]
INTERACTION WITH AJUBA.
PubMed=10330178; DOI=10.1128/MCB.19.6.4379;
Goyal R.K., Lin P., Kanungo J., Payne A.S., Muslin A.J.,
Longmore G.D.;
"Ajuba, a novel LIM protein, interacts with Grb2, augments mitogen-
activated protein kinase activity in fibroblasts, and promotes meiotic
maturation of Xenopus oocytes in a Grb2- and Ras-dependent manner.";
Mol. Cell. Biol. 19:4379-4389(1999).
[15]
INTERACTION WITH SNTA1.
PubMed=11551227; DOI=10.1021/bi010490n;
Oak S.A., Russo K., Petrucci T.C., Jarrett H.W.;
"Mouse alpha1-syntrophin binding to Grb2: further evidence of a role
for syntrophin in cell signaling.";
Biochemistry 40:11270-11278(2001).
[16]
INTERACTION WITH CLNK.
PubMed=11463797; DOI=10.1074/jbc.M106390200;
Goitsuka R., Tatsuno A., Ishiai M., Kurosaki T., Kitamura D.;
"MIST functions through distinct domains in immunoreceptor signaling
in the presence and absence of LAT.";
J. Biol. Chem. 276:36043-36050(2001).
[17]
SUBCELLULAR LOCATION, AND INTERACTION WITH PRNP.
PubMed=11571277; DOI=10.1074/jbc.M103289200;
Spielhaupter C., Schaetzl H.M.;
"PrPC directly interacts with proteins involved in signaling
pathways.";
J. Biol. Chem. 276:44604-44612(2001).
[18]
INTERACTION WITH IRS4.
PubMed=11113178; DOI=10.1128/MCB.21.1.26-38.2001;
Tsuruzoe K., Emkey R., Kriauciunas K.M., Ueki K., Kahn C.R.;
"Insulin receptor substrate 3 (IRS-3) and IRS-4 impair IRS-1- and IRS-
2-mediated signaling.";
Mol. Cell. Biol. 21:26-38(2001).
[19]
INTERACTION WITH TOM1L1.
PubMed=11711534; DOI=10.1074/jbc.M106813200;
Seykora J.T., Mei L., Dotto G.P., Stein P.L.;
"'Srcasm: a novel Src activating and signaling molecule.";
J. Biol. Chem. 277:2812-2822(2002).
[20]
INTERACTION WITH EPHB1 AND SHC1.
PubMed=12925710; DOI=10.1083/jcb.200302073;
Vindis C., Cerretti D.P., Daniel T.O., Huynh-Do U.;
"EphB1 recruits c-Src and p52Shc to activate MAPK/ERK and promote
chemotaxis.";
J. Cell Biol. 162:661-671(2003).
[21]
INTERACTION WITH LIME1.
PubMed=14610044; DOI=10.1084/jem.20030232;
Hur E.M., Son M., Lee O.-H., Choi Y.B., Park C., Lee H., Yun Y.;
"LIME, a novel transmembrane adaptor protein, associates with p56lck
and mediates T cell activation.";
J. Exp. Med. 198:1463-1473(2003).
[22]
INTERACTION WITH LAT2.
PubMed=15477350; DOI=10.1084/jem.20041223;
Zhu M., Liu Y., Koonpaew S., Granillo O., Zhang W.;
"Positive and negative regulation of FcepsilonRI-mediated signaling by
the adaptor protein LAB/NTAL.";
J. Exp. Med. 200:991-1000(2004).
[23]
INTERACTION WITH LAT2.
PubMed=15477348; DOI=10.1084/jem.20041213;
Volna P., Lebduska P., Draberova L., Simova S., Heneberg P.,
Boubelik M., Bugajev V., Malissen B., Wilson B.S., Horejsi V.,
Malissen M., Draber P.;
"Negative regulation of mast cell signaling and function by the
adaptor LAB/NTAL.";
J. Exp. Med. 200:1001-1013(2004).
[24]
INTERACTION WITH LIME1.
PubMed=16249387; DOI=10.1182/blood-2005-05-1859;
Ahn E., Lee H., Yun Y.;
"LIME acts as a transmembrane adapter mediating BCR-dependent B-cell
activation.";
Blood 107:1521-1527(2006).
[25]
INTERACTION WITH KDR.
PubMed=16966330; DOI=10.1074/jbc.M603928200;
Lamalice L., Houle F., Huot J.;
"Phosphorylation of Tyr1214 within VEGFR-2 triggers the recruitment of
Nck and activation of Fyn leading to SAPK2/p38 activation and
endothelial cell migration in response to VEGF.";
J. Biol. Chem. 281:34009-34020(2006).
[26]
INTERACTION WITH HCST.
PubMed=16582911; DOI=10.1038/ni1325;
Upshaw J.L., Arneson L.N., Schoon R.A., Dick C.J., Billadeau D.D.,
Leibson P.J.;
"NKG2D-mediated signaling requires a DAP10-bound Grb2-Vav1
intermediate and phosphatidylinositol-3-kinase in human natural killer
cells.";
Nat. Immunol. 7:524-532(2006).
[27]
INTERACTION WITH THEMIS.
PubMed=19597498; DOI=10.1038/ni.1768;
Lesourne R., Uehara S., Lee J., Song K.-D., Li L., Pinkhasov J.,
Zhang Y., Weng N.-P., Wildt K.F., Wang L., Bosselut R., Love P.E.;
"Themis, a T cell-specific protein important for late thymocyte
development.";
Nat. Immunol. 10:840-847(2009).
[28]
INTERACTION WITH THEMIS.
PubMed=19597497; DOI=10.1038/ni.1769;
Johnson A.L., Aravind L., Shulzhenko N., Morgun A., Choi S.-Y.,
Crockford T.L., Lambe T., Domaschenz H., Kucharska E.M., Zheng L.,
Vinuesa C.G., Lenardo M.J., Goodnow C.C., Cornall R.J., Schwartz R.H.;
"Themis is a member of a new metazoan gene family and is required for
the completion of thymocyte positive selection.";
Nat. Immunol. 10:831-839(2009).
[29]
INTERACTION WITH THEMIS.
PubMed=19805304; DOI=10.1073/pnas.0908593106;
Patrick M.S., Oda H., Hayakawa K., Sato Y., Eshima K., Kirikae T.,
Iemura S., Shirai M., Abe T., Natsume T., Sasazuki T., Suzuki H.;
"Gasp, a Grb2-associating protein, is critical for positive selection
of thymocytes.";
Proc. Natl. Acad. Sci. U.S.A. 106:16345-16350(2009).
[30]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
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).
[31]
INTERACTION WITH PTPRH; PTPRO AND PTPRB.
PubMed=20398064; DOI=10.1111/j.1365-2443.2010.01398.x;
Murata Y., Mori M., Kotani T., Supriatna Y., Okazawa H., Kusakari S.,
Saito Y., Ohnishi H., Matozaki T.;
"Tyrosine phosphorylation of R3 subtype receptor-type protein tyrosine
phosphatases and their complex formations with Grb2 or Fyn.";
Genes Cells 15:513-524(2010).
[32]
INTERACTION WITH THEMIS2.
PubMed=20644716; DOI=10.1371/journal.pone.0011465;
Peirce M.J., Brook M., Morrice N., Snelgrove R., Begum S.,
Lanfrancotti A., Notley C., Hussell T., Cope A.P., Wait R.;
"Themis2/ICB1 is a signaling scaffold that selectively regulates
macrophage Toll-like receptor signaling and cytokine production.";
PLoS ONE 5:E11465-E11465(2010).
[33]
INTERACTION WITH RAB13.
PubMed=21543326; DOI=10.1074/jbc.M111.245209;
Wu C., Agrawal S., Vasanji A., Drazba J., Sarkaria S., Xie J.,
Welch C.M., Liu M., Anand-Apte B., Horowitz A.;
"Rab13-dependent trafficking of RhoA is required for directional
migration and angiogenesis.";
J. Biol. Chem. 286:23511-23520(2011).
[34]
INTERACTION WITH SCIMP.
PubMed=21930792; DOI=10.1128/MCB.05817-11;
Draber P., Vonkova I., Stepanek O., Hrdinka M., Kucova M.,
Skopcova T., Otahal P., Angelisova P., Horejsi V., Yeung M., Weiss A.,
Brdicka T.;
"SCIMP, a transmembrane adapter protein involved in major
histocompatibility complex class II signaling.";
Mol. Cell. Biol. 31:4550-4562(2011).
[35]
INTERACTION WITH LAT; PLCG1 AND THEMIS.
TISSUE=Thymocyte;
PubMed=22561606; DOI=10.1038/ni.2301;
Wang D., Zheng M., Lei L., Ji J., Yao Y., Qiu Y., Ma L., Lou J.,
Ouyang C., Zhang X., He Y., Chi J., Wang L., Kuang Y., Wang J.,
Cao X., Lu L.;
"Tespa1 is involved in late thymocyte development through the
regulation of TCR-mediated signaling.";
Nat. Immunol. 13:560-568(2012).
[36]
STRUCTURE BY NMR OF 1-65.
PubMed=9135122; DOI=10.1006/jmbi.1996.0886;
Wittekind M., Mapelli C., Lee V., Goldfarb V., Friedrichs M.S.,
Meyers C.A., Mueller L.;
"Solution structure of the Grb2 N-terminal SH3 domain complexed with a
ten-residue peptide derived from SOS: direct refinement against NOEs,
J-couplings and 1H and 13C chemical shifts.";
J. Mol. Biol. 267:933-952(1997).
-!- FUNCTION: Adapter protein that provides a critical link between
cell surface growth factor receptors and the Ras signaling
pathway.
-!- FUNCTION: Isoform 2 does not bind to phosphorylated epidermal
growth factor receptor (EGFR) but inhibits EGF-induced.
transactivation of a RAS-responsive element. Isoform 2 acts as a
dominant negative protein over GRB2 and by suppressing
proliferative signals, may trigger active programmed cell death
(By similarity). {ECO:0000250}.
-!- SUBUNIT: Associates (via SH2 domain) with activated EGF and PDGF
receptors (tyrosine phosphorylated) (By similarity). Interacts
with PDGFRA (tyrosine phosphorylated); the interaction may be
indirect (PubMed:8943348). Interacts with IRS4 (when Tyr-
phosphorylated) (PubMed:11113178). Also associates to other
cellular Tyr-phosphorylated proteins such as SIT1, IRS1, SHC and
LNK; probably via the concerted action of both its SH2 and SH3
domains (By similarity). It also seems to interact with RAS in the
signaling pathway leading to DNA synthesis. Interacts with SOS1
(By similarity). Forms a complex with MUC1 and SOS1, through
interaction of the SH3 domains with SOS1 and the SH2 domain with
phosphorylated MUC1 (By similarity). Interacts with phosphorylated
MET (By similarity). Interacts with phosphorylated TOM1L1
(PubMed:11711534). Interacts with the phosphorylated C-terminus of
SH2B2 (By similarity). Interacts with phosphorylated SIT1, LAX1,
LAT, LAT2 and LIME1 upon TCR and/or BCR activation (By similarity)
(PubMed:16249387, PubMed:14610044, PubMed:15477350,
PubMed:15477348, PubMed:22561606). Interacts with NISCH, PTPNS1
and REPS2 (By similarity). Interacts with syntrophin SNTA1
(PubMed:11551227). Interacts (via SH3 domains) with REPS1
(PubMed:9395447). Interacts (via SH3 domains) with PIK3C2B (By
similarity). Interacts with CBL and CBLB (By similarity).
Interacts with AJUBA and CLNK (PubMed:10330178, PubMed:11463797).
Interacts (via SH2 domain) with TEK/TIE2 (tyrosine phosphorylated)
(PubMed:10521483). Interacts with SHB, INPP5D/SHIP1, SKAP1 and
SKAP2 (By similarity). Interacts with PTPN11 (PubMed:8943348).
Interacts with PRNP (PubMed:11571277). Interacts with RALGPS1 (By
similarity). Interacts also with HCST (PubMed:16582911). Interacts
with KDR (PubMed:16966330). Interacts with FLT1 (tyrosine-
phosphorylated) (PubMed:9722576). Interacts with GAPT and PTPRE
(By similarity). Interacts (via SH2 domain) with KIF26A (By
similarity). Interacts (via SH3 2) with GAB2 (PubMed:10068651).
Interacts with ADAM15 (By similarity). Interacts with THEMIS2
(PubMed:20644716). Interacts (via SH2 domain) with AXL
(phosphorylated) (By similarity). Interacts (via SH2 domain) with
KIT (phosphorylated) (PubMed:10377264). Interacts with PTPRJ and
BCR (By similarity). Interacts with PTPN23 (By similarity).
Interacts with FLT4 (tyrosine phosphorylated) (By similarity).
Interacts with EPHB1 and SHC1; activates the MAPK/ERK cascade to
regulate cell migration (PubMed:12925710). Part of a complex
including TNK2, GRB2 and one receptor tyrosine kinase (RTK) such
as AXL and PDGFRL, in which GRB2 promotes RTK recruitment by TNK2
(By similarity). Interacts (via SH2 domain) with CSF1R (tyrosine
phosphorylated) (PubMed:9312046). Interacts with ERBB4 (By
similarity). Interacts with NTRK1 (phosphorylated upon ligand-
binding) (By similarity). Interacts with PTK2/FAK1 (tyrosine
phosphorylated) (PubMed:7997267). Interacts with PTK2B/PYK2
(tyrosine phosphorylated) (By similarity). Interacts with SCIMP
(PubMed:21930792). Interacts (via SH3 domains) with GAREM1 (via
proline-rich domain and tyrosine phosphorylated); the interaction
occurs upon EGF stimulation (By similarity). Interacts with DAB2
(PubMed:9569023). Interacts with TESPA1 (By similarity). Interacts
with THEMIS (PubMed:19597498, PubMed:19597497, PubMed:19805304,
PubMed:22561606). Interacts with PLCG1, LAT and THEMIS upon TCR
activation in thymocytes; the association is weaker in the absence
of TESPA1 (PubMed:22561606). Interacts with CD28 (By similarity).
Interacts with RAB13; may recruit RAB13 to the leading edge of
migrating endothelial cells where it can activate RHOA
(PubMed:21543326). Interacts with ASAP3 (phosphorylated form) (By
similarity). Interacts (via SH2 domain) with PTPRH (phosphorylated
form) (PubMed:20398064). Interacts with PTPRO (phosphorylated
form) (PubMed:20398064). Interacts with PTPRB (phosphorylated
form) (PubMed:20398064). Interacts (via SH3 domain 2) with PRR14
(via proline-rich region) (By similarity).
{ECO:0000250|UniProtKB:P62993, ECO:0000269|PubMed:10068651,
ECO:0000269|PubMed:10330178, ECO:0000269|PubMed:10377264,
ECO:0000269|PubMed:10521483, ECO:0000269|PubMed:11113178,
ECO:0000269|PubMed:11463797, ECO:0000269|PubMed:11551227,
ECO:0000269|PubMed:11571277, ECO:0000269|PubMed:11711534,
ECO:0000269|PubMed:12925710, ECO:0000269|PubMed:14610044,
ECO:0000269|PubMed:15477348, ECO:0000269|PubMed:15477350,
ECO:0000269|PubMed:16249387, ECO:0000269|PubMed:16582911,
ECO:0000269|PubMed:16966330, ECO:0000269|PubMed:19597497,
ECO:0000269|PubMed:19597498, ECO:0000269|PubMed:19805304,
ECO:0000269|PubMed:20398064, ECO:0000269|PubMed:20644716,
ECO:0000269|PubMed:21543326, ECO:0000269|PubMed:21930792,
ECO:0000269|PubMed:22561606, ECO:0000269|PubMed:7997267,
ECO:0000269|PubMed:8943348, ECO:0000269|PubMed:9312046,
ECO:0000269|PubMed:9395447, ECO:0000269|PubMed:9569023,
ECO:0000269|PubMed:9722576}.
-!- INTERACTION:
O54737:Blnk; NbExp=4; IntAct=EBI-1688, EBI-641814;
P35991:Btk; NbExp=4; IntAct=EBI-1688, EBI-625119;
B9EKI5:Cblb; NbExp=3; IntAct=EBI-1688, EBI-682463;
P35329:Cd22; NbExp=4; IntAct=EBI-1688, EBI-300059;
P98078:Dab2; NbExp=4; IntAct=EBI-1688, EBI-1391846;
Q99JZ7:Errfi1; NbExp=3; IntAct=EBI-1688, EBI-643375;
Q8C180:Frs2; NbExp=5; IntAct=EBI-1688, EBI-6880000;
Q9QYY0:Gab1; NbExp=8; IntAct=EBI-1688, EBI-644784;
Q60749:Khdrbs1; NbExp=2; IntAct=EBI-1688, EBI-519077;
Q52KG5:Kif26a; NbExp=2; IntAct=EBI-1688, EBI-2480646;
O54957:Lat; NbExp=5; IntAct=EBI-1688, EBI-6390034;
Q62077:Plcg1; NbExp=2; IntAct=EBI-1688, EBI-300133;
P04925:Prnp; NbExp=7; IntAct=EBI-1688, EBI-768613;
P35235:Ptpn11; NbExp=3; IntAct=EBI-1688, EBI-397236;
P18052:Ptpra; NbExp=4; IntAct=EBI-1688, EBI-6597520;
Q91ZZ2:Rapgef1; NbExp=3; IntAct=EBI-1688, EBI-644719;
P98083:Shc1; NbExp=7; IntAct=EBI-1688, EBI-300201;
Q61234:Snta1; NbExp=3; IntAct=EBI-1688, EBI-295952;
Q62245:Sos1; NbExp=7; IntAct=EBI-1688, EBI-1693;
Q02384:Sos2; NbExp=5; IntAct=EBI-1688, EBI-395573;
Q02858:Tek; NbExp=3; IntAct=EBI-1688, EBI-7099626;
Q8BGW0-1:Themis; NbExp=3; IntAct=EBI-15532571, EBI-15806957;
Q99PM9:Uck2; NbExp=3; IntAct=EBI-1688, EBI-644712;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm
{ECO:0000250}. Endosome {ECO:0000250}. Golgi apparatus
{ECO:0000269|PubMed:11571277}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Comment=Additional isoforms seem to exist.;
Name=1;
IsoId=Q60631-1; Sequence=Displayed;
Name=2; Synonyms=GRB3-3;
IsoId=Q60631-2; Sequence=VSP_001841;
-!- DOMAIN: The SH3 domains mediate interaction with RALGPS1 and SHB.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the GRB2/sem-5/DRK family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Grb2 entry;
URL="https://en.wikipedia.org/wiki/Grb2";
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EMBL; U07617; AAB40022.1; -; mRNA.
EMBL; D85748; BAA12862.1; -; mRNA.
EMBL; BC052377; AAH52377.1; -; mRNA.
EMBL; BC085254; AAH85254.1; -; mRNA.
CCDS; CCDS25645.1; -. [Q60631-1]
PIR; A54688; A54688.
RefSeq; NP_001300865.1; NM_001313936.1. [Q60631-1]
RefSeq; NP_001300866.1; NM_001313937.1. [Q60631-1]
RefSeq; NP_032189.1; NM_008163.4. [Q60631-1]
UniGene; Mm.439649; -.
UniGene; Mm.490413; -.
PDB; 1GBQ; NMR; -; A=1-61.
PDB; 1GBR; NMR; -; A=1-59.
PDB; 2GBQ; NMR; -; A=1-59.
PDB; 3GBQ; NMR; -; A=1-59.
PDB; 4GBQ; NMR; -; A=1-59.
PDBsum; 1GBQ; -.
PDBsum; 1GBR; -.
PDBsum; 2GBQ; -.
PDBsum; 3GBQ; -.
PDBsum; 4GBQ; -.
ProteinModelPortal; Q60631; -.
SMR; Q60631; -.
BioGrid; 200046; 33.
CORUM; Q60631; -.
DIP; DIP-259N; -.
IntAct; Q60631; 73.
MINT; MINT-84889; -.
STRING; 10090.ENSMUSP00000021090; -.
BindingDB; Q60631; -.
ChEMBL; CHEMBL4830; -.
iPTMnet; Q60631; -.
PhosphoSitePlus; Q60631; -.
EPD; Q60631; -.
PaxDb; Q60631; -.
PeptideAtlas; Q60631; -.
PRIDE; Q60631; -.
Ensembl; ENSMUST00000021090; ENSMUSP00000021090; ENSMUSG00000059923. [Q60631-1]
Ensembl; ENSMUST00000106497; ENSMUSP00000102106; ENSMUSG00000059923. [Q60631-1]
Ensembl; ENSMUST00000106499; ENSMUSP00000102108; ENSMUSG00000059923. [Q60631-2]
GeneID; 14784; -.
KEGG; mmu:14784; -.
UCSC; uc007mii.1; mouse. [Q60631-2]
UCSC; uc007mij.1; mouse. [Q60631-1]
CTD; 2885; -.
MGI; MGI:95805; Grb2.
eggNOG; KOG3601; Eukaryota.
eggNOG; ENOG410XR1G; LUCA.
GeneTree; ENSGT00820000126999; -.
HOGENOM; HOG000251625; -.
HOVERGEN; HBG005404; -.
InParanoid; Q60631; -.
KO; K04364; -.
OMA; HWWHGEI; -.
OrthoDB; EOG091G0HWS; -.
PhylomeDB; Q60631; -.
TreeFam; TF354288; -.
Reactome; R-MMU-109704; PI3K Cascade.
Reactome; R-MMU-112412; SOS-mediated signalling.
Reactome; R-MMU-114604; GPVI-mediated activation cascade.
Reactome; R-MMU-1250347; SHC1 events in ERBB4 signaling.
Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
Reactome; R-MMU-1295596; Spry regulation of FGF signaling.
Reactome; R-MMU-1433557; Signaling by SCF-KIT.
Reactome; R-MMU-1433559; Regulation of KIT signaling.
Reactome; R-MMU-167044; Signalling to RAS.
Reactome; R-MMU-179812; GRB2 events in EGFR signaling.
Reactome; R-MMU-180292; GAB1 signalosome.
Reactome; R-MMU-180336; SHC1 events in EGFR signaling.
Reactome; R-MMU-182971; EGFR downregulation.
Reactome; R-MMU-186763; Downstream signal transduction.
Reactome; R-MMU-1963640; GRB2 events in ERBB2 signaling.
Reactome; R-MMU-1963642; PI3K events in ERBB2 signaling.
Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-MMU-210993; Tie2 Signaling.
Reactome; R-MMU-2179392; EGFR Transactivation by Gastrin.
Reactome; R-MMU-2424491; DAP12 signaling.
Reactome; R-MMU-2428933; SHC-related events triggered by IGF1R.
Reactome; R-MMU-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
Reactome; R-MMU-2871796; FCERI mediated MAPK activation.
Reactome; R-MMU-2871809; FCERI mediated Ca+2 mobilization.
Reactome; R-MMU-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
Reactome; R-MMU-375165; NCAM signaling for neurite out-growth.
Reactome; R-MMU-388841; Costimulation by the CD28 family.
Reactome; R-MMU-389359; CD28 dependent Vav1 pathway.
Reactome; R-MMU-391160; Signal regulatory protein family interactions.
Reactome; R-MMU-392451; G beta:gamma signalling through PI3Kgamma.
Reactome; R-MMU-512988; Interleukin-3, 5 and GM-CSF signaling.
Reactome; R-MMU-5654688; SHC-mediated cascade:FGFR1.
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-5654699; SHC-mediated cascade:FGFR2.
Reactome; R-MMU-5654700; FRS-mediated FGFR2 signaling.
Reactome; R-MMU-5654704; SHC-mediated cascade:FGFR3.
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-5654719; SHC-mediated cascade:FGFR4.
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-5663213; RHO GTPases Activate WASPs and WAVEs.
Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
Reactome; R-MMU-6807004; Negative regulation of MET activity.
Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-MMU-74749; Signal attenuation.
Reactome; R-MMU-74751; Insulin receptor signalling cascade.
Reactome; R-MMU-8851805; MET activates RAS signaling.
Reactome; R-MMU-8851907; MET activates PI3K/AKT signaling.
Reactome; R-MMU-8853659; RET signaling.
Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
Reactome; R-MMU-8865999; MET activates PTPN11.
Reactome; R-MMU-8875555; MET activates RAP1 and RAC1.
Reactome; R-MMU-8875656; MET receptor recycling.
Reactome; R-MMU-912526; Interleukin receptor SHC signaling.
Reactome; R-MMU-912631; Regulation of signaling by CBL.
Reactome; R-MMU-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
ChiTaRS; Grb2; mouse.
EvolutionaryTrace; Q60631; -.
PRO; PR:Q60631; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000059923; -.
CleanEx; MM_GRB2; -.
ExpressionAtlas; Q60631; baseline and differential.
Genevisible; Q60631; MM.
GO; GO:0005911; C:cell-cell junction; IDA:MGI.
GO; GO:0008180; C:COP9 signalosome; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005768; C:endosome; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0070436; C:Grb2-EGFR complex; ISO:MGI.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0005730; C:nucleolus; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0012506; C:vesicle membrane; IDA:MGI.
GO; GO:0046875; F:ephrin receptor binding; IPI:UniProtKB.
GO; GO:0005154; F:epidermal growth factor receptor binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0043560; F:insulin receptor substrate binding; ISO:MGI.
GO; GO:0005168; F:neurotrophin TRKA receptor binding; ISO:MGI.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
GO; GO:0001784; F:phosphotyrosine residue binding; ISO:MGI.
GO; GO:0019904; F:protein domain specific binding; IPI:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; ISO:MGI.
GO; GO:0017124; F:SH3 domain binding; ISS:UniProtKB.
GO; GO:0005070; F:SH3/SH2 adaptor activity; IDA:MGI.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0048646; P:anatomical structure formation involved in morphogenesis; IMP:MGI.
GO; GO:0060670; P:branching involved in labyrinthine layer morphogenesis; IMP:MGI.
GO; GO:0030154; P:cell differentiation; IMP:MGI.
GO; GO:0016477; P:cell migration; IBA:GO_Central.
GO; GO:0071479; P:cellular response to ionizing radiation; ISO:MGI.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0008286; P:insulin receptor signaling pathway; ISO:MGI.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0030838; P:positive regulation of actin filament polymerization; IGI:MGI.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISO:MGI.
GO; GO:0051291; P:protein heterooligomerization; IEA:Ensembl.
GO; GO:0007265; P:Ras protein signal transduction; TAS:MGI.
GO; GO:0031623; P:receptor internalization; ISO:MGI.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0043408; P:regulation of MAPK cascade; IGI:MGI.
GO; GO:0042770; P:signal transduction in response to DNA damage; ISO:MGI.
CDD; cd11949; SH3_GRB2_C; 1.
CDD; cd11946; SH3_GRB2_N; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR030219; Grb2.
InterPro; IPR035643; GRB2_C_SH3.
InterPro; IPR035641; GRB2_N_SH3.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR036028; SH3-like_dom.
InterPro; IPR001452; SH3_domain.
PANTHER; PTHR24418:SF290; PTHR24418:SF290; 1.
Pfam; PF00017; SH2; 1.
Pfam; PF00018; SH3_1; 2.
PRINTS; PR00401; SH2DOMAIN.
PRINTS; PR00452; SH3DOMAIN.
SMART; SM00252; SH2; 1.
SMART; SM00326; SH3; 2.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF55550; SSF55550; 2.
PROSITE; PS50001; SH2; 1.
PROSITE; PS50002; SH3; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Direct protein sequencing; Endosome; Golgi apparatus;
Nucleus; Phosphoprotein; Reference proteome; Repeat; SH2 domain;
SH3 domain.
CHAIN 1 217 Growth factor receptor-bound protein 2.
/FTId=PRO_0000088199.
DOMAIN 1 58 SH3 1. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 60 152 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 156 215 SH3 2. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P62993}.
MOD_RES 6 6 N6-acetyllysine.
{ECO:0000250|UniProtKB:P62993}.
MOD_RES 50 50 N6-acetyllysine.
{ECO:0000250|UniProtKB:P62993}.
MOD_RES 109 109 N6-acetyllysine.
{ECO:0000250|UniProtKB:P62993}.
MOD_RES 211 211 Phosphothreonine.
{ECO:0000250|UniProtKB:P62993}.
VAR_SEQ 60 100 Missing (in isoform 2).
{ECO:0000303|Ref.2}.
/FTId=VSP_001841.
STRAND 2 7 {ECO:0000244|PDB:1GBQ}.
STRAND 13 16 {ECO:0000244|PDB:2GBQ}.
STRAND 24 26 {ECO:0000244|PDB:1GBQ}.
STRAND 34 41 {ECO:0000244|PDB:1GBQ}.
STRAND 44 49 {ECO:0000244|PDB:1GBQ}.
HELIX 50 52 {ECO:0000244|PDB:1GBQ}.
STRAND 53 56 {ECO:0000244|PDB:1GBQ}.
SEQUENCE 217 AA; 25238 MW; 97F4A4FE4B248DDF CRC64;
MEAIAKYDFK ATADDELSFK RGDILKVLNE ECDQNWYKAE LNGKDGFIPK NYIEMKPHPW
FFGKIPRAKA EEMLSKQRHD GAFLIRESES APGDFSLSVK FGNDVQHFKV LRDGAGKYFL
WVVKFNSLNE LVDYHRSTSV SRNQQIFLRD IEQMPQQPTY VQALFDFDPQ EDGELGFRRG
DFIHVMDNSD PNWWKGACHG QTGMFPRNYV TPVNRNV


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