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

 GRB2_HUMAN              Reviewed;         217 AA.
P62993; P29354; Q14450; Q63057; Q63059;
31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
31-AUG-2004, sequence version 1.
22-NOV-2017, entry version 176.
RecName: Full=Growth factor receptor-bound protein 2;
AltName: Full=Adapter protein GRB2;
AltName: Full=Protein Ash;
AltName: Full=SH2/SH3 adapter GRB2;
Name=GRB2; Synonyms=ASH;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND MUTAGENESIS OF
PRO-49 AND GLY-203.
TISSUE=Brain;
PubMed=1322798; DOI=10.1016/0092-8674(92)90167-B;
Lowenstein E.J., Daly R.J., Batzer A.G., Li W., Margolis B.,
Lammers R., Ullrich A., Skolnik E.Y., Bar-Sagi D., Schlessinger J.;
"The SH2 and SH3 domain-containing protein GRB2 links receptor
tyrosine kinases to ras signaling.";
Cell 70:431-442(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Fetal lung;
PubMed=1384039; DOI=10.1073/pnas.89.19.9015;
Matuoka K., Yamakawa A., Shibata M., Takenawa T.;
"Cloning of ASH, a ubiquitous protein composed of one Src homology
region (SH) 2 and two SH3 domains, from human and rat cDNA
libraries.";
Proc. Natl. Acad. Sci. U.S.A. 89:9015-9019(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND FUNCTION.
TISSUE=Placenta;
PubMed=8178156; DOI=10.1126/science.8178156;
Fath I., Schweighoffer F., Rey I., Multon M.-C., Boiziau J.,
Duchesne M., Tocque B.;
"Cloning of a Grb2 isoform with apoptotic properties.";
Science 264:971-974(1994).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Epidermis;
PubMed=10051406; DOI=10.1006/geno.1998.5692;
Bochmann H., Gehrisch S., Jaross W.;
"The gene structure of the human growth factor bound protein GRB2.";
Genomics 56:203-207(1999).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lymph;
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).
[9]
PROTEIN SEQUENCE OF 11-20; 27-38; 77-109; 118-136; 143-149 AND
179-195, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[10]
INTERACTION WITH CSF1R.
PubMed=8262059;
van der Geer P., Hunter T.;
"Mutation of Tyr697, a GRB2-binding site, and Tyr721, a PI 3-kinase
binding site, abrogates signal transduction by the murine CSF-1
receptor expressed in Rat-2 fibroblasts.";
EMBO J. 12:5161-5172(1993).
[11]
INTERACTION WITH IRS1.
PubMed=8388384;
Tobe K., Matuoka K., Tamemoto H., Ueki K., Kaburagi Y., Asai S.,
Noguchi T., Matsuda M., Tanaka S., Hattori S., Fukui Y., Akanuma Y.,
Yazaki Y., Takenawa T., Kadowaki T.;
"Insulin stimulates association of insulin receptor substrate-1 with
the protein abundant Src homology/growth factor receptor-bound protein
2.";
J. Biol. Chem. 268:11167-11171(1993).
[12]
INTERACTION WITH IRS1 AND SHC.
PubMed=8491186;
Skolnik E.Y., Lee C.-H., Batzer A.G., Vicentini L.M., Zhou M.,
Daly R.J., Myers M.J. Jr., Backer J.M., Ullrich A., White M.F.,
Schlessinger J.;
"The SH2/SH3 domain-containing protein GRB2 interacts with tyrosine-
phosphorylated IRS1 and Shc: implications for insulin control of ras
signalling.";
EMBO J. 12:1929-1936(1993).
[13]
INTERACTION WITH SOS1, AND MUTAGENESIS OF PRO-49; GLU-89; SER-90 AND
GLY-203.
TISSUE=Brain;
PubMed=8493579; DOI=10.1126/science.8493579;
Chardin P., Camonis J.H., Gale N.W., van Aelst L., Wigler M.H.,
Bar-Sagi D.;
"Human Sos1: a guanine nucleotide exchange factor for Ras that binds
to GRB2.";
Science 260:1338-1343(1993).
[14]
IDENTIFICATION IN A COMPLEX WITH MUC1 AND SOS1, AND INTERACTION WITH
MUC1 AND SOS1.
PubMed=7664271;
Pandey P., Kharbanda S., Kufe D.;
"Association of the DF3/MUC1 breast cancer antigen with Grb2 and the
Sos/Ras exchange protein.";
Cancer Res. 55:4000-4003(1995).
[15]
INTERACTION WITH INPP5D.
PubMed=8723348; DOI=10.1016/S0960-9822(02)00511-0;
Kavanaugh W.M., Pot D.A., Chin S.M., Deuter-Reinhard M.,
Jefferson A.B., Norris F.A., Masiarz F.R., Cousens L.S., Majerus P.W.,
Williams L.T.;
"Multiple forms of an inositol polyphosphate 5-phosphatase form
signaling complexes with Shc and Grb2.";
Curr. Biol. 6:438-445(1996).
[16]
INTERACTION WITH EPHB1.
PubMed=8798570; DOI=10.1074/jbc.271.38.23588;
Stein E., Cerretti D.P., Daniel T.O.;
"Ligand activation of ELK receptor tyrosine kinase promotes its
association with Grb10 and Grb2 in vascular endothelial cells.";
J. Biol. Chem. 271:23588-23593(1996).
[17]
INTERACTION WITH INPP5D.
PubMed=9108392;
Odai H., Sasaki K., Iwamatsu A., Nakamoto T., Ueno H., Yamagata T.,
Mitani K., Yazaki Y., Hirai H.;
"Purification and molecular cloning of SH2- and SH3-containing
inositol polyphosphate-5-phosphatase, which is involved in the
signaling pathway of granulocyte-macrophage colony-stimulating factor,
erythropoietin, and Bcr-Abl.";
Blood 89:2745-2756(1997).
[18]
INTERACTION WITH PTK2/FAK1.
PubMed=9148935; DOI=10.1074/jbc.272.20.13189;
Schlaepfer D.D., Hunter T.;
"Focal adhesion kinase overexpression enhances ras-dependent integrin
signaling to ERK2/mitogen-activated protein kinase through
interactions with and activation of c-Src.";
J. Biol. Chem. 272:13189-13195(1997).
[19]
INTERACTION WITH PTPNS1.
PubMed=9062191; DOI=10.1038/386181a0;
Kharitonenkov A., Chen Z., Sures I., Wang H., Schilling J.,
Ullrich A.;
"A family of proteins that inhibit signalling through tyrosine kinase
receptors.";
Nature 386:181-186(1997).
[20]
INTERACTION WITH AXL.
PubMed=9178760; DOI=10.1038/sj.onc.1201123;
Braunger J., Schleithoff L., Schulz A.S., Kessler H., Lammers R.,
Ullrich A., Bartram C.R., Janssen J.W.;
"Intracellular signaling of the Ufo/Axl receptor tyrosine kinase is
mediated mainly by a multi-substrate docking-site.";
Oncogene 14:2619-2631(1997).
[21]
INTERACTION WITH SH2B2.
PubMed=9233773; DOI=10.1038/sj.onc.1201163;
Yokouchi M., Suzuki R., Masuhara M., Komiya S., Inoue A.,
Yoshimura A.;
"Cloning and characterization of APS, an adaptor molecule containing
PH and SH2 domains that is tyrosine phosphorylated upon B-cell
receptor stimulation.";
Oncogene 15:7-15(1997).
[22]
INTERACTION WITH LAT.
PubMed=9489702; DOI=10.1016/S0092-8674(00)80901-0;
Zhang W., Sloan-Lancaster J., Kitchen J., Trible R.P., Samelson L.E.;
"LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor
to cellular activation.";
Cell 92:83-92(1998).
[23]
INTERACTION WITH REPS2.
PubMed=9422736; DOI=10.1074/jbc.273.2.814;
Ikeda M., Ishida O., Hinoi T., Kishida S., Kikuchi A.;
"Identification and characterization of a novel protein interacting
with Ral-binding protein 1, a putative effector protein of Ral.";
J. Biol. Chem. 273:814-821(1998).
[24]
INTERACTION WITH IRS4.
PubMed=9553137; DOI=10.1074/jbc.273.17.10726;
Fantin V.R., Sparling J.D., Slot J.W., Keller S.R., Lienhard G.E.,
Lavan B.E.;
"Characterization of insulin receptor substrate 4 in human embryonic
kidney 293 cells.";
J. Biol. Chem. 273:10726-10732(1998).
[25]
INTERACTION WITH SHB, AND MUTAGENESIS OF PRO-49 AND PRO-206.
PubMed=9484780; DOI=10.1038/sj.onc.1201607;
Welsh M., Songyang Z., Frantz J.D., Trueb T., Reedquist K.A.,
Karlsson T., Miyazaki M., Cantley L.C., Band H., Shoelson S.E.;
"Stimulation through the T cell receptor leads to interactions between
SHB and several signaling proteins.";
Oncogene 16:891-901(1998).
[26]
INTERACTION WITH EGFR.
PubMed=10026169; DOI=10.1074/jbc.274.9.5542;
Braverman L.E., Quilliam L.A.;
"Identification of Grb4/Nckbeta, a src homology 2 and 3 domain-
containing adapter protein having similar binding and biological
properties to Nck.";
J. Biol. Chem. 274:5542-5549(1999).
[27]
INTERACTION WITH CBLB.
PubMed=10022120; DOI=10.1038/sj.onc.1202411;
Elly C., Witte S., Zhang Z., Rosnet O., Lipkowitz S., Altman A.,
Liu Y.-C.;
"Tyrosine phosphorylation and complex formation of Cbl-b upon T cell
receptor stimulation.";
Oncogene 18:1147-1156(1999).
[28]
INTERACTION WITH CBL AND CBLB.
PubMed=10086340; DOI=10.1038/sj.onc.1202499;
Ettenberg S.A., Keane M.M., Nau M.M., Frankel M., Wang L.-M.,
Pierce J.H., Lipkowitz S.;
"cbl-b inhibits epidermal growth factor receptor signaling.";
Oncogene 18:1855-1866(1999).
[29]
INTERACTION WITH HCV NS5A.
PubMed=10318918; DOI=10.1073/pnas.96.10.5533;
Tan S.-L., Nakao H., He Y., Vijaysri S., Neddermann P., Jacobs B.L.,
Mayer B.J., Katze M.G.;
"NS5A, a nonstructural protein of hepatitis C virus, binds growth
factor receptor-bound protein 2 adaptor protein in a Src homology 3
domain/ligand-dependent manner and perturbs mitogenic signaling.";
Proc. Natl. Acad. Sci. U.S.A. 96:5533-5538(1999).
[30]
INTERACTION WITH RALGPS1.
PubMed=10747847; DOI=10.1074/jbc.C000085200;
Rebhun J.F., Chen H., Quilliam L.A.;
"Identification and characterization of a new family of guanine
nucleotide exchange factors for the ras-related GTPase Ral.";
J. Biol. Chem. 275:13406-13410(2000).
[31]
INTERACTION WITH ERBB4.
PubMed=10867024; DOI=10.1074/jbc.C901015199;
Sweeney C., Lai C., Riese D.J. II, Diamonti A.J., Cantley L.C.,
Carraway K.L. III;
"Ligand discrimination in signaling through an ErbB4 receptor
homodimer.";
J. Biol. Chem. 275:19803-19807(2000).
[32]
INTERACTION WITH SKAP2.
PubMed=10942756; DOI=10.1074/jbc.M001439200;
Asazuma N., Wilde J.I., Berlanga O., Leduc M., Leo A.,
Schweighoffer E., Tybulewicz V., Bon C., Liu S.K., McGlade C.J.,
Schraven B., Watson S.P.;
"Interaction of linker for activation of T cells with multiple adapter
proteins in platelets activated by the glycoprotein VI-selective
ligand, convulxin.";
J. Biol. Chem. 275:33427-33434(2000).
[33]
INTERACTION WITH PTPRE.
PubMed=10980613; DOI=10.1038/sj.onc.1203790;
Gil-Henn H., Volohonsky G., Toledano-Katchalski H., Gandre S.,
Elson A.;
"Generation of novel cytoplasmic forms of protein tyrosine phosphatase
epsilon by proteolytic processing and translational control.";
Oncogene 19:4375-4384(2000).
[34]
INTERACTION WITH SIT1.
PubMed=11433379;
DOI=10.1002/1521-4141(200106)31:6<1825::AID-IMMU1825>3.0.CO;2-V;
Pfrepper K.-I., Marie-Cardine A., Simeoni L., Kuramitsu Y., Leo A.,
Spicka J., Hilgert I., Scherer J., Schraven B.;
"Structural and functional dissection of the cytoplasmic domain of the
transmembrane adaptor protein SIT (SHP2-interacting transmembrane
adaptor protein).";
Eur. J. Immunol. 31:1825-1836(2001).
[35]
INTERACTION WITH HEV ORF3 PROTEIN.
PubMed=11518702; DOI=10.1074/jbc.M101546200;
Korkaya H., Jameel S., Gupta D., Tyagi S., Kumar R., Zafrullah M.,
Mazumdar M., Lal S.K., Xiaofang L., Sehgal D., Das S.R., Sahal D.;
"The ORF3 protein of hepatitis E virus binds to Src homology 3 domains
and activates MAPK.";
J. Biol. Chem. 276:42389-42400(2001).
[36]
IDENTIFICATION IN A COMPLEX WITH PIK3C2B AND EGFR, AND INTERACTION
WITH PIK3C2B.
PubMed=11533253; DOI=10.1128/MCB.21.19.6660-6667.2001;
Wheeler M., Domin J.;
"Recruitment of the class II phosphoinositide 3-kinase C2beta to the
epidermal growth factor receptor: role of Grb2.";
Mol. Cell. Biol. 21:6660-6667(2001).
[37]
INTERACTION WITH NISCH.
PubMed=11912194; DOI=10.1074/jbc.M111838200;
Sano H., Liu S.C.H., Lane W.S., Piletz J.E., Lienhard G.E.;
"Insulin receptor substrate 4 associates with the protein IRAS.";
J. Biol. Chem. 277:19439-19447(2002).
[38]
INTERACTION WITH SKAP1.
PubMed=12171928; DOI=10.1074/jbc.M206023200;
Wu L., Yu Z., Shen S.-H.;
"SKAP55 recruits to lipid rafts and positively mediates the MAPK
pathway upon T cell receptor activation.";
J. Biol. Chem. 277:40420-40427(2002).
[39]
INTERACTION WITH LAX1.
PubMed=12359715; DOI=10.1074/jbc.M208946200;
Zhu M., Janssen E., Leung K., Zhang W.;
"Molecular cloning of a novel gene encoding a membrane-associated
adaptor protein (LAX) in lymphocyte signaling.";
J. Biol. Chem. 277:46151-46158(2002).
[40]
INTERACTION WITH LAT2.
PubMed=12486104; DOI=10.1084/jem.20021405;
Brdicka T., Imrich M., Angelisova P., Brdickova N., Horvath O.,
Spicka J., Hilgert I., Luskova P., Draber P., Novak P., Engels N.,
Wienands J., Simeoni L., Oesterreicher J., Aguado E., Malissen M.,
Schraven B., Horejsi V.;
"Non-T cell activation linker (NTAL): a transmembrane adaptor protein
involved in immunoreceptor signaling.";
J. Exp. Med. 196:1617-1626(2002).
[41]
INTERACTION WITH PTPRJ.
PubMed=12475979; DOI=10.1074/jbc.M210656200;
Palka H.L., Park M., Tonks N.K.;
"Hepatocyte growth factor receptor tyrosine kinase met is a substrate
of the receptor protein-tyrosine phosphatase DEP-1.";
J. Biol. Chem. 278:5728-5735(2003).
[42]
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).
[43]
INTERACTION WITH LAT2.
PubMed=12514734; DOI=10.1038/ni882;
Janssen E., Zhu M., Zhang W., Koonpaew S., Zhang W.;
"LAB: a new membrane-associated adaptor molecule in B cell
activation.";
Nat. Immunol. 4:117-123(2003).
[44]
INTERACTION WITH NTRK1.
PubMed=15488758; DOI=10.1016/j.ccr.2004.09.011;
Tacconelli A., Farina A.R., Cappabianca L., Desantis G., Tessitore A.,
Vetuschi A., Sferra R., Rucci N., Argenti B., Screpanti I., Gulino A.,
Mackay A.R.;
"TrkA alternative splicing: a regulated tumor-promoting switch in
human neuroblastoma.";
Cancer Cell 6:347-360(2004).
[45]
INTERACTION WITH FLT4.
PubMed=15102829; DOI=10.1074/jbc.M314015200;
Wang J.F., Zhang X., Groopman J.E.;
"Activation of vascular endothelial growth factor receptor-3 and its
downstream signaling promote cell survival under oxidative stress.";
J. Biol. Chem. 279:27088-27097(2004).
[46]
REVIEW ON INTERACTION WITH KIT AND ROLE IN KIT SIGNALING.
PubMed=15526160; DOI=10.1007/s00018-004-4189-6;
Ronnstrand L.;
"Signal transduction via the stem cell factor receptor/c-Kit.";
Cell. Mol. Life Sci. 61:2535-2548(2004).
[47]
INTERACTION WITH BCR.
PubMed=15302586; DOI=10.1016/j.yexcr.2004.05.010;
Laurent C.E., Smithgall T.E.;
"The c-Fes tyrosine kinase cooperates with the breakpoint cluster
region protein (Bcr) to induce neurite extension in a Rac- and Cdc42-
dependent manner.";
Exp. Cell Res. 299:188-198(2004).
[48]
REVIEW ON ROLE IN KIT SIGNALING.
PubMed=16129412; DOI=10.1016/j.bbrc.2005.08.055;
Roskoski R. Jr.;
"Signaling by Kit protein-tyrosine kinase--the stem cell factor
receptor.";
Biochem. Biophys. Res. Commun. 337:1-13(2005).
[49]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[50]
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).
[51]
INTERACTION WITH GAPT.
PubMed=18559951; DOI=10.1189/jlb.0208087;
Liu Y., Zhang W.;
"Identification of a new transmembrane adaptor protein that
constitutively binds Grb2 in B cells.";
J. Leukoc. Biol. 84:842-851(2008).
[52]
INTERACTION WITH ADAM15.
PubMed=18296648; DOI=10.1158/1541-7786.MCR-07-2028;
Zhong J.L., Poghosyan Z., Pennington C.J., Scott X., Handsley M.M.,
Warn A., Gavrilovic J., Honert K., Kruger A., Span P.N., Sweep F.C.,
Edwards D.R.;
"Distinct functions of natural ADAM-15 cytoplasmic domain variants in
human mammary carcinoma.";
Mol. Cancer Res. 6:383-394(2008).
[53]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-211, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[54]
INTERACTION WITH EGFR.
PubMed=19836242; DOI=10.1016/j.cub.2009.09.048;
Tarcic G., Boguslavsky S.K., Wakim J., Kiuchi T., Liu A., Reinitz F.,
Nathanson D., Takahashi T., Mischel P.S., Ng T., Yarden Y.;
"An unbiased screen identifies DEP-1 tumor suppressor as a phosphatase
controlling EGFR endocytosis.";
Curr. Biol. 19:1788-1798(2009).
[55]
INTERACTION WITH AXL; LTK; PDGFRL AND TNK2, AND FUNCTION.
PubMed=19815557; DOI=10.1074/jbc.M109.072660;
Pao-Chun L., Chan P.M., Chan W., Manser E.;
"Cytoplasmic ACK1 interaction with multiple receptor tyrosine kinases
is mediated by Grb2: an analysis of ACK1 effects on Axl signaling.";
J. Biol. Chem. 284:34954-34963(2009).
[56]
INTERACTION WITH KIF26A.
PubMed=19914172; DOI=10.1016/j.cell.2009.10.023;
Zhou R., Niwa S., Homma N., Takei Y., Hirokawa N.;
"KIF26A is an unconventional kinesin and regulates GDNF-Ret signaling
in enteric neuronal development.";
Cell 139:802-813(2009).
[57]
INTERACTION WITH GAREM1.
PubMed=19509291; DOI=10.1074/jbc.M109.021139;
Tashiro K., Tsunematsu T., Okubo H., Ohta T., Sano E., Yamauchi E.,
Taniguchi H., Konishi H.;
"GAREM, a novel adaptor protein for growth factor receptor-bound
protein 2, contributes to cellular transformation through the
activation of extracellular signal-regulated kinase signaling.";
J. Biol. Chem. 284:20206-20214(2009).
[58]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[59]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6; LYS-50 AND LYS-109, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[60]
INTERACTION WITH PTK2B/PYK2.
PubMed=20521079; DOI=10.1007/s00018-010-0411-x;
Shen X., Xi G., Radhakrishnan Y., Clemmons D.R.;
"Recruitment of Pyk2 to SHPS-1 signaling complex is required for IGF-
I-dependent mitogenic signaling in vascular smooth muscle cells.";
Cell. Mol. Life Sci. 67:3893-3903(2010).
[61]
INTERACTION WITH PTPN23, AND SUBCELLULAR LOCATION.
PubMed=21179510; DOI=10.1371/journal.pone.0014339;
Tanase C.A.;
"Histidine domain-protein tyrosine phosphatase interacts with Grb2 and
GrpL.";
PLoS ONE 5:E14339-E14339(2010).
[62]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[63]
INTERACTION WITH FCRL6.
PubMed=20933011; DOI=10.1016/j.imlet.2010.09.023;
Kulemzin S.V., Zamoshnikova A.Y., Yurchenko M.Y., Vitak N.Y.,
Najakshin A.M., Fayngerts S.A., Chikaev N.A., Reshetnikova E.S.,
Kashirina N.M., Peclo M.M., Rutkevich P.N., Shevelev A.Y.,
Yanushevskaya E.V., Baranov K.O., Mamonkin M., Vlasik T.N.,
Sidorenko S.P., Taranin A.V., Mechetina L.V.;
"FCRL6 receptor: expression and associated proteins.";
Immunol. Lett. 134:174-182(2011).
[64]
INTERACTION WITH ASAP3.
PubMed=22027826; DOI=10.1074/jbc.M111.278770;
Yu X., Wang F., Liu H., Adams G., Aikhionbare F., Liu D., Cao X.,
Fan L., Hu G., Chen Y., Frost A., Partridge E., Ding X., Yao X.;
"ACAP4 protein cooperates with Grb2 protein to orchestrate epidermal
growth factor-stimulated integrin beta1 recycling in cell migration.";
J. Biol. Chem. 286:43735-43747(2011).
[65]
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).
[66]
INTERACTION WITH TESPA1.
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).
[67]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[68]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[69]
INTERACTION WITH HERPES SIMPLEX VIRUS 1 UL46.
PubMed=23946459; DOI=10.1128/JVI.01702-13;
Strunk U., Saffran H.A., Wu F.W., Smiley J.R.;
"Role of herpes simplex virus VP11/12 tyrosine-based motifs in binding
and activation of the Src family kinase Lck and recruitment of p85,
Grb2, and Shc.";
J. Virol. 87:11276-11286(2013).
[70]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[71]
INTERACTION WITH PRR14.
PubMed=27041574; DOI=10.1038/onc.2016.93;
Yang M., Lewinska M., Fan X., Zhu J., Yuan Z.M.;
"PRR14 is a novel activator of the PI3K pathway promoting lung
carcinogenesis.";
Oncogene 35:5527-5538(2016).
[72]
STRUCTURE BY NMR OF 58-164.
PubMed=8794768; DOI=10.1021/bi952615s;
Thornton K.H., Mueller W.T., McConnell P., Zhu G., Saltiel A.R.,
Thanabal V.;
"Nuclear magnetic resonance solution structure of the growth factor
receptor-bound protein 2 Src homology 2 domain.";
Biochemistry 35:11852-11864(1996).
[73]
STRUCTURE BY NMR OF 52-163.
Senior M.M., Frederick A.F., Black S., Murgolo N.J., Perkins L.M.,
Wilson O., Snow M.E., Wang Y.-S.;
"The three-dimensional solution structure of the Src homology domain-2
of the growth factor receptor-bound protein-2.";
J. Biomol. NMR 11:153-164(1998).
[74]
STRUCTURE BY NMR OF 157-215.
PubMed=7881903; DOI=10.1016/S0969-2126(94)00106-5;
Kohda D., Terasawa H., Ichikawa S., Ogura K., Hatanaka H.,
Mandiyan V., Ullrich A., Schlessinger J., Inagaki F.;
"Solution structure and ligand-binding site of the carboxy-terminal
SH3 domain of GRB2.";
Structure 2:1029-1040(1994).
[75]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).
PubMed=7716522; DOI=10.1126/science.7716522;
Maignan S., Guilloteau J.-P., Fromage N., Arnoux B., Becquart J.,
Ducruix A.;
"Crystal structure of the mammalian Grb2 adaptor.";
Science 268:291-293(1995).
[76]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 56-153.
PubMed=9642078; DOI=10.1006/jmbi.1998.1790;
Rahuel J., Garcia-Echeverria C., Furet P., Strauss A., Caravatti G.,
Fretz H., Schoepfer J., Gay B.;
"Structural basis for the high affinity of amino-aromatic SH2
phosphopeptide ligands.";
J. Mol. Biol. 279:1013-1022(1998).
[77]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 47-163.
PubMed=10090780; DOI=10.1021/jm9811007;
Ettmayer P., France D., Gounarides J., Jarosinski M., Martin M.-S.,
Rondeau J.-M., Sabio M., Topiol S., Weidmann B., Zurini M., Bair K.W.;
"Structural and conformational requirements for high-affinity binding
to the SH2 domain of Grb2(1).";
J. Med. Chem. 42:971-980(1999).
[78]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 57-152.
PubMed=10395476; DOI=10.1021/jm991013u;
Furet P., Garcia-Echeverria C., Gay B., Schoepfer J., Zeller M.,
Rahuel J.;
"Structure-based design, synthesis, and X-ray crystallography of a
high- affinity antagonist of the Grb2-SH2 domain containing an
asparagine mimetic.";
J. Med. Chem. 42:2358-2363(1999).
[79]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 52-160 IN COMPLEX WITH MET.
PubMed=11063574; DOI=10.1021/bi0012336;
Schiering N., Casale E., Caccia P., Giordano P., Battistini C.;
"Dimer formation through domain swapping in the crystal structure of
the Grb2-SH2-Ac-pYVNV complex.";
Biochemistry 39:13376-13382(2000).
[80]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 56-151 IN COMPLEX WITH THE
TYROSINE PHOSPHORYLATED PEPTIDE TYR-VAL-ASN-VAL-GLN-ASN AND IN COMPLEX
WITH A PEPTIDE INHIBITOR.
PubMed=11827484; DOI=10.1006/jmbi.2001.5299;
Nioche P., Liu W.-Q., Broutin I., Charbonnier F., Latreille M.-T.,
Vidal M., Roques B., Garbay C., Ducruix A.;
"Crystal structures of the SH2 domain of Grb2: highlight on the
binding of a new high-affinity inhibitor.";
J. Mol. Biol. 315:1167-1177(2002).
[81]
X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 158-211 IN COMPLEX WITH
GAB2.
PubMed=19523899; DOI=10.1016/j.str.2009.03.017;
Harkiolaki M., Tsirka T., Lewitzky M., Simister P.C., Joshi D.,
Bird L.E., Jones E.Y., O'Reilly N., Feller S.M.;
"Distinct binding modes of two epitopes in Gab2 that interact with the
SH3C domain of Grb2.";
Structure 17:809-822(2009).
[82]
X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 60-152 IN COMPLEX WITH CD28,
AND INTERACTION WITH CD28.
PubMed=24098653; DOI=10.1371/journal.pone.0074482;
Higo K., Ikura T., Oda M., Morii H., Takahashi J., Abe R., Ito N.;
"High resolution crystal structure of the Grb2 SH2 domain with a
phosphopeptide derived from CD28.";
PLoS ONE 8:E74482-E74482(2013).
-!- 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.
-!- SUBUNIT: Associates (via SH2 domain) with activated EGF and PDGF
receptors (tyrosine phosphorylated) (PubMed:10026169,
PubMed:19836242). Interacts with PDGFRA (tyrosine phosphorylated);
the interaction may be indirect (By similarity). Also associates
to other cellular Tyr-phosphorylated proteins such as SIT1, IRS1,
IRS4, SHC and LNK; probably via the concerted action of both its
SH2 and SH3 domains (PubMed:8388384, PubMed:8491186,
PubMed:9553137, PubMed:11433379). It also seems to interact with
RAS in the signaling pathway leading to DNA synthesis. Interacts
with SOS1 (PubMed:8493579, PubMed:7664271). Forms a complex with
MUC1 and SOS1, through interaction of the SH3 domains with SOS1
and the SH2 domain with phosphorylated MUC1 (PubMed:7664271).
Interacts with phosphorylated MET (PubMed:11063574,
PubMed:11827484). Interacts with phosphorylated TOM1L1 (By
similarity). Interacts with the phosphorylated C-terminus of SH2B2
(PubMed:9233773). Interacts with phosphorylated SIT1, LAX1, LAT,
LAT2 and LIME1 upon TCR and/or BCR activation (By similarity)
(PubMed:9489702, PubMed:12359715, PubMed:12486104,
PubMed:12514734). Interacts with NISCH, PTPNS1 and REPS2
(PubMed:9062191, PubMed:9422736, PubMed:11912194). Interacts with
syntrophin SNTA1 (By similarity). Interacts (via SH3 domains) with
REPS1 (By similarity). Interacts (via SH3 domains) with PIK3C2B
(PubMed:11533253). Interacts with CBL and CBLB (PubMed:10022120,
PubMed:10086340). Interacts with AJUBA and CLNK (By similarity).
Interacts (via SH2 domain) with TEK/TIE2 (tyrosine phosphorylated)
(By similarity). Interacts with SHB, INPP5D/SHIP1, SKAP1 and SKAP2
(PubMed:8723348, PubMed:9108392, PubMed:9484780, PubMed:10942756,
PubMed:12171928). Interacts with PTPN11 (By similarity). Interacts
with PRNP (By similarity). Interacts with RALGPS1
(PubMed:10747847). Interacts with HCST (PubMed:16582911).
Interacts with KDR (By similarity). Interacts with FLT1 (tyrosine-
phosphorylated) (By similarity). Interacts with GAPT and PTPRE
(PubMed:10980613, PubMed:18559951). Interacts (via SH2 domain)
with KIF26A (PubMed:19914172). Interacts (via SH3 2) with GAB2
(PubMed:19523899). Interacts with ADAM15 (PubMed:18296648).
Interacts with THEMIS2 (By similarity). Interacts (via SH2 domain)
with AXL (phosphorylated) (PubMed:9178760, PubMed:19815557).
Interacts (via SH2 domain) with KIT (phosphorylated)
(PubMed:15526160, PubMed:16129412). Interacts with PTPRJ and BCR
(PubMed:12475979, PubMed:15302586). Interacts with PTPN23
(PubMed:21179510). Interacts with FLT4 (tyrosine phosphorylated)
(PubMed:15102829). Interacts with EPHB1 and SHC1; activates the
MAPK/ERK cascade to regulate cell migration (PubMed:8798570,
PubMed:12925710). Part of a complex including TNK2, GRB2, LTK and
one receptor tyrosine kinase (RTK) such as AXL and PDGFRL, in
which GRB2 promotes RTK recruitment by TNK2 (PubMed:9178760,
PubMed:19815557). Interacts (via SH2 domain) with CSF1R (tyrosine
phosphorylated) (PubMed:8262059). Interacts with ERBB4
(PubMed:10867024). Interacts with NTRK1 (phosphorylated upon
ligand-binding) (PubMed:15488758). Interacts with PTK2/FAK1
(tyrosine phosphorylated) (PubMed:9148935). Interacts with
PTK2B/PYK2 (tyrosine phosphorylated) (PubMed:20521079). Isoform 1
interacts with SCIMP (PubMed:21930792). Interacts (via SH3
domains) with GAREM1 isoform 1 (via proline-rich domain and
tyrosine phosphorylated); the interaction occurs upon EGF
stimulation (PubMed:19509291). Interacts with DAB2 (By
similarity). Interacts with TESPA1 (PubMed:22561606). Interacts
with PLCG1, LAT and THEMIS upon TCR activation in thymocytes; the
association is weaker in the absence of TESPA1 (By similarity).
Interacts with CD28 (PubMed:24098653). Interacts with RAB13; may
recruit RAB13 to the leading edge of migrating endothelial cells
where it can activate RHOA (By similarity). Interacts with ASAP3
(phosphorylated form) (PubMed:22027826). Interacts (via SH3
domain) with HEV ORF3 protein (PubMed:11518702). Interacts with
HCV NS5A via its SH3 domains (PubMed:10318918). Interacts with
herpes simplex virus 1 UL46 (PubMed:23946459). Interacts (via SH2
domain) with PTPRH (phosphorylated form) (By similarity).
Interacts with PTPRO (phosphorylated form) (By similarity).
Interacts with PTPRB (phosphorylated form) (By similarity).
Interacts (via SH3 domain 2) with PRR14 (via proline-rich region)
(PubMed:27041574). Interacts with FCRL6 (tyrosine phosphorylated
form) (PubMed:20933011). {ECO:0000250|UniProtKB:Q60631,
ECO:0000269|PubMed:10022120, ECO:0000269|PubMed:10026169,
ECO:0000269|PubMed:10086340, ECO:0000269|PubMed:10318918,
ECO:0000269|PubMed:10747847, ECO:0000269|PubMed:10867024,
ECO:0000269|PubMed:10942756, ECO:0000269|PubMed:10980613,
ECO:0000269|PubMed:11063574, ECO:0000269|PubMed:11433379,
ECO:0000269|PubMed:11518702, ECO:0000269|PubMed:11533253,
ECO:0000269|PubMed:11827484, ECO:0000269|PubMed:11912194,
ECO:0000269|PubMed:12171928, ECO:0000269|PubMed:12359715,
ECO:0000269|PubMed:12475979, ECO:0000269|PubMed:12486104,
ECO:0000269|PubMed:12514734, ECO:0000269|PubMed:12925710,
ECO:0000269|PubMed:15102829, ECO:0000269|PubMed:15302586,
ECO:0000269|PubMed:15488758, ECO:0000269|PubMed:16582911,
ECO:0000269|PubMed:18296648, ECO:0000269|PubMed:18559951,
ECO:0000269|PubMed:19509291, ECO:0000269|PubMed:19523899,
ECO:0000269|PubMed:19815557, ECO:0000269|PubMed:19836242,
ECO:0000269|PubMed:19914172, ECO:0000269|PubMed:20521079,
ECO:0000269|PubMed:20933011, ECO:0000269|PubMed:21179510,
ECO:0000269|PubMed:21930792, ECO:0000269|PubMed:22027826,
ECO:0000269|PubMed:22561606, ECO:0000269|PubMed:23946459,
ECO:0000269|PubMed:24098653, ECO:0000269|PubMed:27041574,
ECO:0000269|PubMed:7664271, ECO:0000269|PubMed:8262059,
ECO:0000269|PubMed:8388384, ECO:0000269|PubMed:8491186,
ECO:0000269|PubMed:8493579, ECO:0000269|PubMed:8723348,
ECO:0000269|PubMed:8798570, ECO:0000269|PubMed:9062191,
ECO:0000269|PubMed:9108392, ECO:0000269|PubMed:9148935,
ECO:0000269|PubMed:9178760, ECO:0000269|PubMed:9233773,
ECO:0000269|PubMed:9422736, ECO:0000269|PubMed:9484780,
ECO:0000269|PubMed:9489702, ECO:0000269|PubMed:9553137}.
-!- INTERACTION:
Self; NbExp=5; IntAct=EBI-401755, EBI-401755;
O92972:- (xeno); NbExp=2; IntAct=EBI-401755, EBI-710506;
P26662:- (xeno); NbExp=3; IntAct=EBI-401755, EBI-9099462;
P27958:- (xeno); NbExp=3; IntAct=EBI-401755, EBI-706378;
Q9P2A4:ABI3; NbExp=3; IntAct=EBI-401755, EBI-742038;
P42684:ABL2; NbExp=2; IntAct=EBI-401755, EBI-1102694;
Q15027:ACAP1; NbExp=3; IntAct=EBI-401755, EBI-751746;
Q13444:ADAM15; NbExp=3; IntAct=EBI-401755, EBI-77818;
Q08117:AES; NbExp=3; IntAct=EBI-401755, EBI-717810;
Q15109:AGER; NbExp=2; IntAct=EBI-401755, EBI-1646426;
Q01484:ANK2; NbExp=2; IntAct=EBI-401755, EBI-941975;
Q9BRR9:ARHGAP9; NbExp=3; IntAct=EBI-401755, EBI-750254;
Q12774:ARHGEF5; NbExp=4; IntAct=EBI-401755, EBI-602199;
Q66PJ3-4:ARL6IP4; NbExp=2; IntAct=EBI-401755, EBI-5280499;
Q9ULH1:ASAP1; NbExp=7; IntAct=EBI-401755, EBI-346622;
O43150:ASAP2; NbExp=3; IntAct=EBI-401755, EBI-310968;
P30530:AXL; NbExp=3; IntAct=EBI-401755, EBI-2850927;
P11274:BCR; NbExp=8; IntAct=EBI-401755, EBI-712838;
Q8WV28:BLNK; NbExp=4; IntAct=EBI-401755, EBI-2623522;
O60885:BRD4; NbExp=2; IntAct=EBI-401755, EBI-723869;
Q6P1W5:C1orf94; NbExp=3; IntAct=EBI-401755, EBI-946029;
P22681:CBL; NbExp=10; IntAct=EBI-401755, EBI-518228;
Q13191:CBLB; NbExp=10; IntAct=EBI-401755, EBI-744027;
Q9Y5K6:CD2AP; NbExp=3; IntAct=EBI-401755, EBI-298152;
P98082:DAB2; NbExp=2; IntAct=EBI-401755, EBI-1171238;
P98078:Dab2 (xeno); NbExp=4; IntAct=EBI-401755, EBI-1391846;
P14868:DARS; NbExp=2; IntAct=EBI-401755, EBI-358730;
Q16643:DBN1; NbExp=4; IntAct=EBI-401755, EBI-351394;
Q92841:DDX17; NbExp=3; IntAct=EBI-401755, EBI-746012;
O14490:DLGAP1; NbExp=3; IntAct=EBI-401755, EBI-1753207;
Q9P1A6:DLGAP2; NbExp=2; IntAct=EBI-401755, EBI-1753397;
Q9Y2H0:DLGAP4; NbExp=2; IntAct=EBI-401755, EBI-722139;
Q05193:DNM1; NbExp=3; IntAct=EBI-401755, EBI-713135;
P50570:DNM2; NbExp=6; IntAct=EBI-401755, EBI-346547;
Q14185:DOCK1; NbExp=2; IntAct=EBI-401755, EBI-446740;
Q7L190:DPPA4; NbExp=3; IntAct=EBI-401755, EBI-710457;
Q8N9I9:DTX3; NbExp=4; IntAct=EBI-401755, EBI-2340258;
P00533:EGFR; NbExp=36; IntAct=EBI-401755, EBI-297353;
P54762:EPHB1; NbExp=2; IntAct=EBI-401755, EBI-80252;
Q12929:EPS8; NbExp=3; IntAct=EBI-401755, EBI-375576;
P04626:ERBB2; NbExp=4; IntAct=EBI-401755, EBI-641062;
P21860:ERBB3; NbExp=3; IntAct=EBI-401755, EBI-720706;
Q9UJM3:ERRFI1; NbExp=12; IntAct=EBI-401755, EBI-2941912;
B7ZLH0:FAM22F; NbExp=5; IntAct=EBI-401755, EBI-10220102;
O15360:FANCA; NbExp=2; IntAct=EBI-401755, EBI-81570;
P21802:FGFR2; NbExp=5; IntAct=EBI-401755, EBI-1028658;
P21333:FLNA; NbExp=2; IntAct=EBI-401755, EBI-350432;
O75369:FLNB; NbExp=2; IntAct=EBI-401755, EBI-352089;
Q14315:FLNC; NbExp=2; IntAct=EBI-401755, EBI-489954;
Q13480:GAB1; NbExp=5; IntAct=EBI-401755, EBI-517684;
Q9UQC2:GAB2; NbExp=10; IntAct=EBI-401755, EBI-975200;
Q9UQC2-1:GAB2; NbExp=3; IntAct=EBI-15787932, EBI-15787947;
Q9H706:GAREM1; NbExp=8; IntAct=EBI-401755, EBI-3440103;
P61978:HNRNPK; NbExp=9; IntAct=EBI-401755, EBI-304185;
Q8IX15-3:HOMEZ; NbExp=3; IntAct=EBI-401755, EBI-10172004;
Q9UKT9:IKZF3; NbExp=7; IntAct=EBI-401755, EBI-747204;
Q0VD86:INCA1; NbExp=3; IntAct=EBI-401755, EBI-6509505;
P35570:Irs1 (xeno); NbExp=5; IntAct=EBI-401755, EBI-520230;
Q07666:KHDRBS1; NbExp=8; IntAct=EBI-401755, EBI-1364;
P10721:KIT; NbExp=6; IntAct=EBI-401755, EBI-1379503;
P05787:KRT8; NbExp=3; IntAct=EBI-401755, EBI-297852;
O43561:LAT; NbExp=7; IntAct=EBI-401755, EBI-1222766;
O43561-2:LAT; NbExp=3; IntAct=EBI-15787932, EBI-8070286;
Q13094:LCP2; NbExp=14; IntAct=EBI-401755, EBI-346946;
P48357:LEPR; NbExp=3; IntAct=EBI-401755, EBI-518596;
P25791:LMO2; NbExp=3; IntAct=EBI-401755, EBI-739696;
Q8TE12:LMX1A; NbExp=3; IntAct=EBI-401755, EBI-10692065;
Q8TBB1:LNX1; NbExp=3; IntAct=EBI-401755, EBI-739832;
Q9BRK4:LZTS2; NbExp=3; IntAct=EBI-401755, EBI-741037;
Q13163:MAP2K5; NbExp=2; IntAct=EBI-401755, EBI-307294;
Q92918:MAP4K1; NbExp=8; IntAct=EBI-401755, EBI-881;
Q8IVH8:MAP4K3; NbExp=2; IntAct=EBI-401755, EBI-1758170;
Q9Y4K4:MAP4K5; NbExp=4; IntAct=EBI-401755, EBI-1279;
Q9H204:MED28; NbExp=3; IntAct=EBI-401755, EBI-514199;
P35579:MYH9; NbExp=3; IntAct=EBI-401755, EBI-350338;
Q8WX92:NELFB; NbExp=2; IntAct=EBI-401755, EBI-347721;
Q9GZT8:NIF3L1; NbExp=3; IntAct=EBI-401755, EBI-740897;
Q13177:PAK2; NbExp=2; IntAct=EBI-401755, EBI-1045887;
Q9NPB6-2:PARD6A; NbExp=3; IntAct=EBI-401755, EBI-10693102;
O00750:PIK3C2B; NbExp=2; IntAct=EBI-401755, EBI-641107;
P27986:PIK3R1; NbExp=4; IntAct=EBI-401755, EBI-79464;
O00459:PIK3R2; NbExp=4; IntAct=EBI-401755, EBI-346930;
P19174:PLCG1; NbExp=2; IntAct=EBI-401755, EBI-79387;
O14939:PLD2; NbExp=4; IntAct=EBI-401755, EBI-1053996;
Q5SXH7:PLEKHS1; NbExp=3; IntAct=EBI-401755, EBI-10691507;
Q96PV4:PNMA5; NbExp=3; IntAct=EBI-401755, EBI-10171633;
Q07869:PPARA; NbExp=3; IntAct=EBI-401755, EBI-78615;
Q08209:PPP3CA; NbExp=3; IntAct=EBI-401755, EBI-352922;
Q9Y478:PRKAB1; NbExp=2; IntAct=EBI-401755, EBI-719769;
P34152:Ptk2 (xeno); NbExp=3; IntAct=EBI-401755, EBI-77070;
P18031:PTPN1; NbExp=2; IntAct=EBI-401755, EBI-968788;
Q06124:PTPN11; NbExp=6; IntAct=EBI-401755, EBI-297779;
P35235:Ptpn11 (xeno); NbExp=7; IntAct=EBI-401755, EBI-397236;
Q9Y2R2:PTPN22; NbExp=2; IntAct=EBI-401755, EBI-1211241;
Q9H3S7:PTPN23; NbExp=6; IntAct=EBI-401755, EBI-724478;
P29350:PTPN6; NbExp=3; IntAct=EBI-401755, EBI-78260;
P18433:PTPRA; NbExp=8; IntAct=EBI-401755, EBI-2609645;
O14522:PTPRT; NbExp=2; IntAct=EBI-401755, EBI-728180;
P06400:RB1; NbExp=4; IntAct=EBI-401755, EBI-491274;
Q04864:REL; NbExp=3; IntAct=EBI-401755, EBI-307352;
Q8NFH8-2:REPS2; NbExp=8; IntAct=EBI-401755, EBI-8029141;
Q15427:SF3B4; NbExp=2; IntAct=EBI-401755, EBI-348469;
Q9H788:SH2D4A; NbExp=3; IntAct=EBI-401755, EBI-747035;
Q9UPX8:SHANK2; NbExp=2; IntAct=EBI-401755, EBI-1570571;
Q9BYB0:SHANK3; NbExp=2; IntAct=EBI-401755, EBI-1752330;
P29353:SHC1; NbExp=23; IntAct=EBI-401755, EBI-78835;
P29353-1:SHC1; NbExp=3; IntAct=EBI-401755, EBI-8160716;
Q8WXH5:SOCS4; NbExp=3; IntAct=EBI-401755, EBI-3942425;
Q07889:SOS1; NbExp=22; IntAct=EBI-401755, EBI-297487;
Q62245:Sos1 (xeno); NbExp=4; IntAct=EBI-401755, EBI-1693;
Q07890:SOS2; NbExp=8; IntAct=EBI-401755, EBI-298181;
O43597:SPRY2; NbExp=3; IntAct=EBI-401755, EBI-742487;
O43295:SRGAP3; NbExp=2; IntAct=EBI-401755, EBI-368166;
O95630:STAMBP; NbExp=9; IntAct=EBI-401755, EBI-396676;
O15056:SYNJ2; NbExp=2; IntAct=EBI-401755, EBI-310513;
Q8N1K5-1:THEMIS; NbExp=10; IntAct=EBI-401755, EBI-15102259;
Q5BJH2-2:TMEM128; NbExp=3; IntAct=EBI-401755, EBI-10694905;
Q92973:TNPO1; NbExp=2; IntAct=EBI-401755, EBI-286693;
O75674:TOM1L1; NbExp=2; IntAct=EBI-401755, EBI-712991;
Q13625-3:TP53BP2; NbExp=3; IntAct=EBI-401755, EBI-10175039;
Q9ULW0:TPX2; NbExp=2; IntAct=EBI-401755, EBI-1037322;
P14373:TRIM27; NbExp=3; IntAct=EBI-401755, EBI-719493;
O60636:TSPAN2; NbExp=6; IntAct=EBI-401755, EBI-3914288;
Q16851:UGP2; NbExp=2; IntAct=EBI-401755, EBI-743729;
P15498:VAV1; NbExp=2; IntAct=EBI-401755, EBI-625518;
Q9UKW4:VAV3; NbExp=7; IntAct=EBI-401755, EBI-297568;
P55072:VCP; NbExp=3; IntAct=EBI-401755, EBI-355164;
O00401:WASL; NbExp=8; IntAct=EBI-401755, EBI-957615;
Q9Y2W2:WBP11; NbExp=4; IntAct=EBI-401755, EBI-714455;
O43516:WIPF1; NbExp=3; IntAct=EBI-401755, EBI-346356;
Q8TF74:WIPF2; NbExp=3; IntAct=EBI-401755, EBI-2850112;
O15156:ZBTB7B; NbExp=3; IntAct=EBI-401755, EBI-740434;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21179510}.
Cytoplasm {ECO:0000269|PubMed:21179510}. Endosome
{ECO:0000269|PubMed:21179510}. Golgi apparatus {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Comment=Additional isoforms seem to exist.;
Name=1; Synonyms=Ash-L;
IsoId=P62993-1, P29354-1;
Sequence=Displayed;
Name=2; Synonyms=GRB3-3;
IsoId=P62993-2, P29354-2;
Sequence=VSP_001839;
-!- DOMAIN: The SH3 domains mediate interaction with RALGPS1 and SHB.
-!- SIMILARITY: Belongs to the GRB2/sem-5/DRK family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/GRB2ID386ch17q25.html";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; M96995; AAA58448.1; -; mRNA.
EMBL; X62852; CAA44664.1; -; mRNA.
EMBL; L29511; AAC37549.1; -; mRNA.
EMBL; AF063618; AAC72075.1; -; Genomic_DNA.
EMBL; AF063614; AAC72075.1; JOINED; Genomic_DNA.
EMBL; AF063615; AAC72075.1; JOINED; Genomic_DNA.
EMBL; AF063616; AAC72075.1; JOINED; Genomic_DNA.
EMBL; AF063617; AAC72075.1; JOINED; Genomic_DNA.
EMBL; AF498925; AAM21073.1; -; mRNA.
EMBL; CR541942; CAG46740.1; -; mRNA.
EMBL; AC011933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC000631; AAH00631.1; -; mRNA.
CCDS; CCDS11721.1; -.
CCDS; CCDS11722.1; -. [P62993-2]
PIR; A43321; A43321.
RefSeq; NP_002077.1; NM_002086.4. [P62993-1]
RefSeq; NP_987102.1; NM_203506.2. [P62993-2]
UniGene; Hs.444356; -.
PDB; 1AZE; NMR; -; A=1-56.
PDB; 1BM2; X-ray; 2.10 A; A=49-163.
PDB; 1BMB; X-ray; 1.80 A; A=49-168.
PDB; 1CJ1; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L=57-152.
PDB; 1FHS; NMR; -; A=53-163.
PDB; 1FYR; X-ray; 2.40 A; A/B/C/D=50-161.
PDB; 1GCQ; X-ray; 1.68 A; A/B=159-217.
PDB; 1GFC; NMR; -; A=159-215.
PDB; 1GFD; NMR; -; A=159-215.
PDB; 1GHU; NMR; -; A=60-158.
PDB; 1GRI; X-ray; 3.10 A; A/B=1-217.
PDB; 1IO6; NMR; -; A=159-215.
PDB; 1JYQ; X-ray; 2.00 A; A/B=60-151.
PDB; 1JYR; X-ray; 1.55 A; A=60-151.
PDB; 1JYU; X-ray; 2.75 A; A=60-151.
PDB; 1QG1; NMR; -; E=58-159.
PDB; 1TZE; X-ray; 2.10 A; E=55-152.
PDB; 1X0N; NMR; -; A=58-159.
PDB; 1ZFP; X-ray; 1.80 A; E=56-153.
PDB; 2AOA; X-ray; 1.99 A; A/B=55-153.
PDB; 2AOB; X-ray; 1.80 A; A/B/C/D=55-153.
PDB; 2H46; X-ray; 1.90 A; E=53-162.
PDB; 2H5K; X-ray; 3.25 A; A/B=53-162.
PDB; 2HUW; X-ray; 1.90 A; A/B=53-162.
PDB; 2VVK; X-ray; 1.60 A; A=161-214.
PDB; 2VWF; X-ray; 1.58 A; A=159-214.
PDB; 2W0Z; X-ray; 1.70 A; A=159-214.
PDB; 3C7I; X-ray; 1.70 A; A=53-162.
PDB; 3IMD; X-ray; 2.00 A; A/B=53-163.
PDB; 3IMJ; X-ray; 2.02 A; A/B=53-163.
PDB; 3IN7; X-ray; 2.00 A; A/C=53-163.
PDB; 3IN8; X-ray; 1.70 A; A=53-163.
PDB; 3KFJ; X-ray; 2.02 A; A=53-163.
PDB; 3MXC; X-ray; 2.00 A; A=55-152.
PDB; 3MXY; X-ray; 2.30 A; A=55-152.
PDB; 3N7Y; X-ray; 2.02 A; A/B/C=55-152.
PDB; 3N84; X-ray; 2.00 A; A/B/C/D/E/F=53-163.
PDB; 3N8M; X-ray; 2.00 A; A=53-163.
PDB; 3OV1; X-ray; 1.60 A; A=53-163.
PDB; 3OVE; X-ray; 1.82 A; A=53-163.
PDB; 3S8L; X-ray; 1.71 A; A=53-163.
PDB; 3S8N; X-ray; 1.71 A; A=53-163.
PDB; 3S8O; X-ray; 1.85 A; A=53-163.
PDB; 3WA4; X-ray; 1.35 A; A=60-152.
PDB; 4P9V; X-ray; 1.64 A; A=53-163.
PDB; 4P9Z; X-ray; 1.80 A; A=53-163.
PDB; 5CDW; X-ray; 2.60 A; A/B/C/E/G/H/K/L/O/P/U/V/Y/Z/c/d=54-153.
PDBsum; 1AZE; -.
PDBsum; 1BM2; -.
PDBsum; 1BMB; -.
PDBsum; 1CJ1; -.
PDBsum; 1FHS; -.
PDBsum; 1FYR; -.
PDBsum; 1GCQ; -.
PDBsum; 1GFC; -.
PDBsum; 1GFD; -.
PDBsum; 1GHU; -.
PDBsum; 1GRI; -.
PDBsum; 1IO6; -.
PDBsum; 1JYQ; -.
PDBsum; 1JYR; -.
PDBsum; 1JYU; -.
PDBsum; 1QG1; -.
PDBsum; 1TZE; -.
PDBsum; 1X0N; -.
PDBsum; 1ZFP; -.
PDBsum; 2AOA; -.
PDBsum; 2AOB; -.
PDBsum; 2H46; -.
PDBsum; 2H5K; -.
PDBsum; 2HUW; -.
PDBsum; 2VVK; -.
PDBsum; 2VWF; -.
PDBsum; 2W0Z; -.
PDBsum; 3C7I; -.
PDBsum; 3IMD; -.
PDBsum; 3IMJ; -.
PDBsum; 3IN7; -.
PDBsum; 3IN8; -.
PDBsum; 3KFJ; -.
PDBsum; 3MXC; -.
PDBsum; 3MXY; -.
PDBsum; 3N7Y; -.
PDBsum; 3N84; -.
PDBsum; 3N8M; -.
PDBsum; 3OV1; -.
PDBsum; 3OVE; -.
PDBsum; 3S8L; -.
PDBsum; 3S8N; -.
PDBsum; 3S8O; -.
PDBsum; 3WA4; -.
PDBsum; 4P9V; -.
PDBsum; 4P9Z; -.
PDBsum; 5CDW; -.
DisProt; DP00210; -.
ProteinModelPortal; P62993; -.
SMR; P62993; -.
BioGrid; 109142; 539.
CORUM; P62993; -.
DIP; DIP-29229N; -.
ELM; P62993; -.
IntAct; P62993; 775.
MINT; MINT-91952; -.
STRING; 9606.ENSP00000339007; -.
BindingDB; P62993; -.
ChEMBL; CHEMBL3663; -.
DrugBank; DB00061; Pegademase bovine.
iPTMnet; P62993; -.
PhosphoSitePlus; P62993; -.
BioMuta; GRB2; -.
DMDM; 51702266; -.
OGP; P62993; -.
SWISS-2DPAGE; P62993; -.
EPD; P62993; -.
MaxQB; P62993; -.
PaxDb; P62993; -.
PeptideAtlas; P62993; -.
PRIDE; P62993; -.
TopDownProteomics; P62993-1; -. [P62993-1]
TopDownProteomics; P62993-2; -. [P62993-2]
DNASU; 2885; -.
Ensembl; ENST00000316615; ENSP00000317360; ENSG00000177885. [P62993-2]
Ensembl; ENST00000316804; ENSP00000339007; ENSG00000177885. [P62993-1]
Ensembl; ENST00000392562; ENSP00000376345; ENSG00000177885. [P62993-1]
Ensembl; ENST00000392563; ENSP00000376346; ENSG00000177885. [P62993-2]
Ensembl; ENST00000392564; ENSP00000376347; ENSG00000177885. [P62993-1]
GeneID; 2885; -.
KEGG; hsa:2885; -.
UCSC; uc002jnx.5; human.
CTD; 2885; -.
DisGeNET; 2885; -.
EuPathDB; HostDB:ENSG00000177885.13; -.
GeneCards; GRB2; -.
HGNC; HGNC:4566; GRB2.
HPA; CAB002589; -.
HPA; HPA030749; -.
HPA; HPA030750; -.
MIM; 108355; gene.
neXtProt; NX_P62993; -.
OpenTargets; ENSG00000177885; -.
PharmGKB; PA28962; -.
eggNOG; KOG3601; Eukaryota.
eggNOG; ENOG410XR1G; LUCA.
GeneTree; ENSGT00820000126999; -.
HOGENOM; HOG000251625; -.
HOVERGEN; HBG005404; -.
InParanoid; P62993; -.
KO; K04364; -.
OMA; HWWHGEI; -.
OrthoDB; EOG091G0HWS; -.
PhylomeDB; P62993; -.
TreeFam; TF354288; -.
Reactome; R-HSA-109704; PI3K Cascade.
Reactome; R-HSA-112412; SOS-mediated signalling.
Reactome; R-HSA-114604; GPVI-mediated activation cascade.
Reactome; R-HSA-1236382; Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants.
Reactome; R-HSA-1250196; SHC1 events in ERBB2 signaling.
Reactome; R-HSA-1250347; SHC1 events in ERBB4 signaling.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-1295596; Spry regulation of FGF signaling.
Reactome; R-HSA-1433557; Signaling by SCF-KIT.
Reactome; R-HSA-1433559; Regulation of KIT signaling.
Reactome; R-HSA-167044; Signalling to RAS.
Reactome; R-HSA-179812; GRB2 events in EGFR signaling.
Reactome; R-HSA-180292; GAB1 signalosome.
Reactome; R-HSA-180336; SHC1 events in EGFR signaling.
Reactome; R-HSA-182971; EGFR downregulation.
Reactome; R-HSA-1839117; Signaling by cytosolic FGFR1 fusion mutants.
Reactome; R-HSA-186763; Downstream signal transduction.
Reactome; R-HSA-1963640; GRB2 events in ERBB2 signaling.
Reactome; R-HSA-1963642; PI3K events in ERBB2 signaling.
Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-HSA-210993; Tie2 Signaling.
Reactome; R-HSA-2179392; EGFR Transactivation by Gastrin.
Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
Reactome; R-HSA-2424491; DAP12 signaling.
Reactome; R-HSA-2428933; SHC-related events triggered by IGF1R.
Reactome; R-HSA-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
Reactome; R-HSA-2871796; FCERI mediated MAPK activation.
Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization.
Reactome; R-HSA-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
Reactome; R-HSA-375165; NCAM signaling for neurite out-growth.
Reactome; R-HSA-388841; Costimulation by the CD28 family.
Reactome; R-HSA-389359; CD28 dependent Vav1 pathway.
Reactome; R-HSA-391160; Signal regulatory protein family interactions.
Reactome; R-HSA-392451; G beta:gamma signalling through PI3Kgamma.
Reactome; R-HSA-512988; Interleukin-3, 5 and GM-CSF signaling.
Reactome; R-HSA-5637810; Constitutive Signaling by EGFRvIII.
Reactome; R-HSA-5654688; SHC-mediated cascade:FGFR1.
Reactome; R-HSA-5654689; PI-3K cascade:FGFR1.
Reactome; R-HSA-5654693; FRS-mediated FGFR1 signaling.
Reactome; R-HSA-5654695; PI-3K cascade:FGFR2.
Reactome; R-HSA-5654699; SHC-mediated cascade:FGFR2.
Reactome; R-HSA-5654700; FRS-mediated FGFR2 signaling.
Reactome; R-HSA-5654704; SHC-mediated cascade:FGFR3.
Reactome; R-HSA-5654706; FRS-mediated FGFR3 signaling.
Reactome; R-HSA-5654710; PI-3K cascade:FGFR3.
Reactome; R-HSA-5654712; FRS-mediated FGFR4 signaling.
Reactome; R-HSA-5654719; SHC-mediated cascade:FGFR4.
Reactome; R-HSA-5654720; PI-3K cascade:FGFR4.
Reactome; R-HSA-5654726; Negative regulation of FGFR1 signaling.
Reactome; R-HSA-5654727; Negative regulation of FGFR2 signaling.
Reactome; R-HSA-5654732; Negative regulation of FGFR3 signaling.
Reactome; R-HSA-5654733; Negative regulation of FGFR4 signaling.
Reactome; R-HSA-5655253; Signaling by FGFR2 in disease.
Reactome; R-HSA-5655291; Signaling by FGFR4 in disease.
Reactome; R-HSA-5655302; Signaling by FGFR1 in disease.
Reactome; R-HSA-5663213; RHO GTPases Activate WASPs and WAVEs.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
Reactome; R-HSA-6807004; Negative regulation of MET activity.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-HSA-74749; Signal attenuation.
Reactome; R-HSA-74751; Insulin receptor signalling cascade.
Reactome; R-HSA-8851805; MET activates RAS signaling.
Reactome; R-HSA-8851907; MET activates PI3K/AKT signaling.
Reactome; R-HSA-8853334; Signaling by FGFR3 fusions in cancer.
Reactome; R-HSA-8853338; Signaling by FGFR3 point mutants in cancer.
Reactome; R-HSA-8853659; RET signaling.
Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
Reactome; R-HSA-8865999; MET activates PTPN11.
Reactome; R-HSA-8875360; InlB-mediated entry of Listeria monocytogenes into host cell.
Reactome; R-HSA-8875555; MET activates RAP1 and RAC1.
Reactome; R-HSA-8875656; MET receptor recycling.
Reactome; R-HSA-8983432; Interleukin-15 signaling.
Reactome; R-HSA-912526; Interleukin receptor SHC signaling.
Reactome; R-HSA-912631; Regulation of signaling by CBL.
Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
SignaLink; P62993; -.
SIGNOR; P62993; -.
ChiTaRS; GRB2; human.
EvolutionaryTrace; P62993; -.
GeneWiki; GRB2; -.
GenomeRNAi; 2885; -.
PRO; PR:P62993; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000177885; -.
CleanEx; HS_GRB2; -.
ExpressionAtlas; P62993; baseline and differential.
Genevisible; P62993; HS.
GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
GO; GO:0008180; C:COP9 signalosome; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:HGNC.
GO; GO:0005768; C:endosome; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
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; IDA:BHF-UCL.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0012506; C:vesicle membrane; IEA:Ensembl.
GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; TAS:Reactome.
GO; GO:0046875; F:ephrin receptor binding; IPI:UniProtKB.
GO; GO:0005154; F:epidermal growth factor receptor binding; IPI:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0043560; F:insulin receptor substrate binding; IPI:UniProtKB.
GO; GO:0005168; F:neurotrophin TRKA receptor binding; IPI:UniProtKB.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
GO; GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; TAS:Reactome.
GO; GO:0001784; F:phosphotyrosine residue binding; IPI:CAFA.
GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL.
GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0017124; F:SH3 domain binding; IDA:UniProtKB.
GO; GO:0005070; F:SH3/SH2 adaptor activity; TAS:UniProtKB.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0048646; P:anatomical structure formation involved in morphogenesis; IEA:Ensembl.
GO; GO:0007411; P:axon guidance; TAS:Reactome.
GO; GO:0060670; P:branching involved in labyrinthine layer morphogenesis; IEA:Ensembl.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0016477; P:cell migration; IBA:GO_Central.
GO; GO:0007267; P:cell-cell signaling; TAS:UniProtKB.
GO; GO:0071479; P:cellular response to ionizing radiation; IMP:BHF-UCL.
GO; GO:0035635; P:entry of bacterium into host cell; TAS:Reactome.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:UniProtKB.
GO; GO:0038128; P:ERBB2 signaling pathway; TAS:Reactome.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0008286; P:insulin receptor signaling pathway; IPI:UniProtKB.
GO; GO:0038111; P:interleukin-7-mediated signaling pathway; TAS:Reactome.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:Reactome.
GO; GO:0030838; P:positive regulation of actin filament polymerization; IEA:Ensembl.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IMP:BHF-UCL.
GO; GO:0051291; P:protein heterooligomerization; IEA:Ensembl.
GO; GO:0007265; P:Ras protein signal transduction; TAS:UniProtKB.
GO; GO:0031623; P:receptor internalization; IMP:BHF-UCL.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0043408; P:regulation of MAPK cascade; IEA:Ensembl.
GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; TAS:Reactome.
GO; GO:0042770; P:signal transduction in response to DNA damage; IMP:BHF-UCL.
GO; GO:0031295; P:T cell costimulation; TAS:Reactome.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
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_sf.
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; 2.
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;
Host-virus interaction; Nucleus; Phosphoprotein; Reference proteome;
Repeat; SH2 domain; SH3 domain.
CHAIN 1 217 Growth factor receptor-bound protein 2.
/FTId=PRO_0000088198.
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:0000244|PubMed:22814378}.
MOD_RES 6 6 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 50 50 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 109 109 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 211 211 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
VAR_SEQ 60 100 Missing (in isoform 2).
{ECO:0000303|PubMed:8178156}.
/FTId=VSP_001839.
MUTAGEN 49 49 P->L: Ineffective in DNA synthesis.
Abolishes interaction with SHB; when
associated with L-206. Abolishes
interaction with SOS1.
{ECO:0000269|PubMed:1322798,
ECO:0000269|PubMed:8493579,
ECO:0000269|PubMed:9484780}.
MUTAGEN 89 89 E->K: No effect on the interaction with
SOS1. {ECO:0000269|PubMed:8493579}.
MUTAGEN 90 90 S->N: No effect on the interaction with
SOS1. {ECO:0000269|PubMed:8493579}.
MUTAGEN 203 203 G->R: Ineffective in DNA synthesis.
Abolishes interaction with SOS1.
{ECO:0000269|PubMed:1322798,
ECO:0000269|PubMed:8493579}.
MUTAGEN 206 206 P->L: Abolishes interaction with SHB;
when associated with L-49.
{ECO:0000269|PubMed:9484780}.
STRAND 2 5 {ECO:0000244|PDB:1GRI}.
STRAND 13 15 {ECO:0000244|PDB:1GRI}.
STRAND 24 26 {ECO:0000244|PDB:1GRI}.
STRAND 36 43 {ECO:0000244|PDB:1GRI}.
STRAND 45 49 {ECO:0000244|PDB:1GRI}.
HELIX 50 52 {ECO:0000244|PDB:1GRI}.
STRAND 61 64 {ECO:0000244|PDB:3IMD}.
HELIX 67 75 {ECO:0000244|PDB:3WA4}.
STRAND 78 80 {ECO:0000244|PDB:1FHS}.
STRAND 82 87 {ECO:0000244|PDB:3WA4}.
TURN 89 93 {ECO:0000244|PDB:3WA4}.
STRAND 95 101 {ECO:0000244|PDB:3WA4}.
STRAND 104 112 {ECO:0000244|PDB:3WA4}.
STRAND 114 116 {ECO:0000244|PDB:1GRI}.
STRAND 118 122 {ECO:0000244|PDB:3WA4}.
STRAND 124 127 {ECO:0000244|PDB:3WA4}.
HELIX 128 134 {ECO:0000244|PDB:3WA4}.
TURN 135 137 {ECO:0000244|PDB:3WA4}.
STRAND 142 144 {ECO:0000244|PDB:3WA4}.
STRAND 149 152 {ECO:0000244|PDB:1FHS}.
STRAND 155 157 {ECO:0000244|PDB:1QG1}.
STRAND 160 165 {ECO:0000244|PDB:2VWF}.
STRAND 171 174 {ECO:0000244|PDB:1IO6}.
STRAND 182 187 {ECO:0000244|PDB:2VWF}.
STRAND 190 198 {ECO:0000244|PDB:2VWF}.
STRAND 201 206 {ECO:0000244|PDB:2VWF}.
HELIX 207 209 {ECO:0000244|PDB:2VWF}.
STRAND 210 212 {ECO:0000244|PDB:2VWF}.
SEQUENCE 217 AA; 25206 MW; 83A4B0BA1B248DC4 CRC64;
MEAIAKYDFK ATADDELSFK RGDILKVLNE ECDQNWYKAE LNGKDGFIPK NYIEMKPHPW
FFGKIPRAKA EEMLSKQRHD GAFLIRESES APGDFSLSVK FGNDVQHFKV LRDGAGKYFL
WVVKFNSLNE LVDYHRSTSV SRNQQIFLRD IEQVPQQPTY VQALFDFDPQ EDGELGFRRG
DFIHVMDNSD PNWWKGACHG QTGMFPRNYV TPVNRNV


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