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Growth factor receptor-bound protein 10 (GRB10 adapter protein) (Insulin receptor-binding protein Grb-IR)

 GRB10_HUMAN             Reviewed;         594 AA.
Q13322; A4D258; A7VJ95; A8K0E6; D3DVM9; O00427; O00701; O75222; Q92606;
Q92907; Q92948;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
15-JUL-1999, sequence version 2.
10-FEB-2021, entry version 213.
RecName: Full=Growth factor receptor-bound protein 10;
AltName: Full=GRB10 adapter protein;
AltName: Full=Insulin receptor-binding protein Grb-IR;
Name=GRB10; Synonyms=GRBIR, KIAA0207;
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).
TISSUE=Skeletal muscle;
PubMed=7479769; DOI=10.1073/pnas.92.22.10287;
Liu F., Roth R.A.;
"Grb-IR: a SH2-domain-containing protein that binds to the insulin receptor
and inhibits its function.";
Proc. Natl. Acad. Sci. U.S.A. 92:10287-10291(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Skeletal muscle;
PubMed=8798417; DOI=10.1074/jbc.271.37.22506;
O'Neill T.J., Rose D.W., Pillay T.S., Hotta K., Olefsky J.M.,
Gustafson T.A.;
"Interaction of a GRB-IR splice variant (a human GRB10 homolog) with the
insulin and insulin-like growth factor I receptors. Evidence for a role in
mitogenic signaling.";
J. Biol. Chem. 271:22506-22513(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Cerebellum, and Skeletal muscle;
PubMed=9006901; DOI=10.1074/jbc.272.5.2659;
Frantz J.D., Giorgetti-Peraldi S., Ottinger E.A., Shoelson S.E.;
"Human GRB-IR-beta/GRB10: splice variants of an insulin and growth factor
receptor-binding protein with PH and SH2 domains.";
J. Biol. Chem. 272:2659-2667(1997).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
PubMed=9360986; DOI=10.1074/jbc.272.46.29104;
Dong L.Q., Du H., Porter S.G., Kolakowski L.F. Jr., Lee A.V.,
Mandarino L.J., Fan J., Yee D., Liu F.;
"Cloning, chromosome localization, expression, and characterization of an
Src homology 2 and pleckstrin homology domain-containing insulin receptor
binding protein hGrb10gamma.";
J. Biol. Chem. 272:29104-29112(1997).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
TISSUE=Brain;
PubMed=9553107; DOI=10.1074/jbc.273.17.10475;
Nantel A., Mohammad-Ali K., Sherk J., Posner B.I., Thomas D.Y.;
"Interaction of the Grb10 adapter protein with the Raf1 and MEK1 kinases.";
J. Biol. Chem. 273:10475-10484(1998).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PHOSPHORYLATION AT TYR-67.
PubMed=9753425; DOI=10.1046/j.1365-2443.1998.00201.x;
Mano H., Ohya K., Miyazato A., Yamashita Y., Ogawa W., Inazawa J.,
Ikeda U., Shimada K., Hatake K., Kasuga M., Ozawa K., Kajigaya S.;
"Grb10/GrbIR as an in vivo substrate of Tec tyrosine kinase.";
Genes Cells 3:431-441(1998).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM 3).
PubMed=9881709; DOI=10.1038/sj.onc.1202226;
Angrist M., Bolk S., Bentley K., Nallasamy S., Halushka M.K.,
Chakravarti A.;
"Genomic structure of the gene for the SH2 and pleckstrin homology domain-
containing protein GRB10 and evaluation of its role in Hirschsprung
disease.";
Oncogene 17:3065-3070(1998).
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), ALTERNATIVE SPLICING, AND
IMPRINTING.
TISSUE=Testis;
PubMed=10861285; DOI=10.1093/hmg/9.11.1587;
Blagitko N., Mergenthaler S., Schulz U., Wollmann H.A., Craigen W.,
Eggermann T., Ropers H.-H., Kalscheuer V.M.;
"Human GRB10 is imprinted and expressed from the paternal and maternal
allele in a highly tissue- and isoform-specific fashion.";
Hum. Mol. Genet. 9:1587-1595(2000).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Bone marrow;
PubMed=9039502; DOI=10.1093/dnares/3.5.321;
Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
Tanaka A., Kotani H., Miyajima N., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. VI. The
coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of
cDNA clones from cell line KG-1 and brain.";
DNA Res. 3:321-329(1996).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Cerebellum;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[14]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Kidney;
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).
[15]
PROTEIN SEQUENCE OF 415-425, PHOSPHORYLATION AT SER-150; SER-418 AND
SER-476, AND MUTAGENESIS OF SER-104; SER-150; SER-418 AND SER-476.
PubMed=15952796; DOI=10.1021/bi050413i;
Langlais P., Wang C., Dong L.Q., Carroll C.A., Weintraub S.T., Liu F.;
"Phosphorylation of Grb10 by mitogen-activated protein kinase:
identification of Ser150 and Ser476 of human Grb10zeta as major
phosphorylation sites.";
Biochemistry 44:8890-8897(2005).
[16]
TISSUE SPECIFICITY, AND IMPRINTING.
PubMed=11527390; DOI=10.1006/bbrc.2001.5500;
McCann J.A., Zheng H., Islam A., Goodyer C.G., Polychronakos C.;
"Evidence against GRB10 as the gene responsible for Silver-Russell
syndrome.";
Biochem. Biophys. Res. Commun. 286:943-948(2001).
[17]
FUNCTION, INTERACTION WITH INSR, AND MUTAGENESIS OF ARG-520.
PubMed=12493740; DOI=10.1074/jbc.m208518200;
Wick K.R., Werner E.D., Langlais P., Ramos F.J., Dong L.Q., Shoelson S.E.,
Liu F.;
"Grb10 inhibits insulin-stimulated insulin receptor substrate (IRS)-
phosphatidylinositol 3-kinase/Akt signaling pathway by disrupting the
association of IRS-1/IRS-2 with the insulin receptor.";
J. Biol. Chem. 278:8460-8467(2003).
[18]
INTERACTION WITH MAP3K14, AND IDENTIFICATION IN A COMPLEX WITH EGFR AND
ERBB2.
PubMed=12853971; DOI=10.1038/sj.onc.1206532;
Chen D., Xu L.G., Chen L., Li L., Zhai Z., Shu H.B.;
"NIK is a component of the EGF/heregulin receptor signaling complexes.";
Oncogene 22:4348-4355(2003).
[19]
FUNCTION, INTERACTION WITH NEDD4, AND MUTAGENESIS OF PRO-136; PRO-139;
PRO-141 AND ARG-520.
PubMed=15060076; DOI=10.1074/jbc.m311802200;
Murdaca J., Treins C., Monthouel-Kartmann M.N., Pontier-Bres R., Kumar S.,
Van Obberghen E., Giorgetti-Peraldi S.;
"Grb10 prevents Nedd4-mediated vascular endothelial growth factor receptor-
2 degradation.";
J. Biol. Chem. 279:26754-26761(2004).
[20]
INTERACTION WITH YWHAE, PHOSPHORYLATION AT SER-428, AND MUTAGENESIS OF
SER-134 AND SER-428.
PubMed=15722337; DOI=10.1074/jbc.m501477200;
Urschel S., Bassermann F., Bai R.Y., Munch S., Peschel C., Duyster J.;
"Phosphorylation of grb10 regulates its interaction with 14-3-3.";
J. Biol. Chem. 280:16987-16993(2005).
[21]
ROLE IN THE UBIQUITINATION OF INSR.
PubMed=16434550; DOI=10.1152/ajpendo.00609.2005;
Ramos F.J., Langlais P.R., Hu D., Dong L.Q., Liu F.;
"Grb10 mediates insulin-stimulated degradation of the insulin receptor: a
mechanism of negative regulation.";
Am. J. Physiol. 290:E1262-E1266(2006).
[22]
FUNCTION.
PubMed=17376403; DOI=10.1016/j.bbrc.2007.03.019;
Tezuka N., Brown A.M., Yanagawa S.;
"GRB10 binds to LRP6, the Wnt co-receptor and inhibits canonical Wnt
signaling pathway.";
Biochem. Biophys. Res. Commun. 356:648-654(2007).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-418, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104 AND SER-418, 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).
[25]
IMPRINTING.
PubMed=19487367; DOI=10.1093/hmg/ddp248;
Monk D., Arnaud P., Frost J., Hills F.A., Stanier P., Feil R., Moore G.E.;
"Reciprocal imprinting of human GRB10 in placental trophoblast and brain:
evolutionary conservation of reversed allelic expression.";
Hum. Mol. Genet. 18:3066-3074(2009).
[26]
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).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
"Quantitative phosphoproteomics reveals widespread full phosphorylation
site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[28]
PHOSPHORYLATION AT SER-150; SER-428 AND SER-476 BY MTOR, AND ACTIVITY
REGULATION.
PubMed=21659604; DOI=10.1126/science.1199498;
Hsu P.P., Kang S.A., Rameseder J., Zhang Y., Ottina K.A., Lim D.,
Peterson T.R., Choi Y., Gray N.S., Yaffe M.B., Marto J.A., Sabatini D.M.;
"The mTOR-regulated phosphoproteome reveals a mechanism of mTORC1-mediated
inhibition of growth factor signaling.";
Science 332:1317-1322(2011).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104 AND SER-418, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and 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).
[30]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 487-591.
PubMed=12551896; DOI=10.1074/jbc.m212026200;
Stein E.G., Ghirlando R., Hubbard S.R.;
"Structural basis for dimerization of the Grb10 Src homology 2 domain.
Implications for ligand specificity.";
J. Biol. Chem. 278:13257-13264(2003).
[31]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 164-415, INTERACTION WITH NRAS AND
PHOSPHOINOSITIDES, AND MUTAGENESIS OF LYS-300; LYS-305; LYS-308 AND
ASN-355.
PubMed=19648926; DOI=10.1038/nsmb.1642;
Depetris R.S., Wu J., Hubbard S.R.;
"Structural and functional studies of the Ras-associating and pleckstrin-
homology domains of Grb10 and Grb14.";
Nat. Struct. Mol. Biol. 16:833-839(2009).
[32]
ERRATUM OF PUBMED:19648926.
Depetris R.S., Wu J., Hubbard S.R.;
Nat. Struct. Mol. Biol. 16:1331-1331(2009).
[33]
VARIANT SER-95, AND IMPRINTING.
PubMed=10856193; DOI=10.1086/302997;
Yoshihashi H., Maeyama K., Kosaki R., Ogata T., Tsukahara M., Goto Y.,
Hata J., Matsuo N., Smith R.J., Kosaki K.;
"Imprinting of human GRB10 and its mutations in two patients with Russell-
Silver syndrome.";
Am. J. Hum. Genet. 67:476-482(2000).
-!- FUNCTION: Adapter protein which modulates coupling of a number of cell
surface receptor kinases with specific signaling pathways. Binds to,
and suppress signals from, activated receptors tyrosine kinases,
including the insulin (INSR) and insulin-like growth factor (IGF1R)
receptors. The inhibitory effect can be achieved by 2 mechanisms:
interference with the signaling pathway and increased receptor
degradation. Delays and reduces AKT1 phosphorylation in response to
insulin stimulation. Blocks association between INSR and IRS1 and IRS2
and prevents insulin-stimulated IRS1 and IRS2 tyrosine phosphorylation.
Recruits NEDD4 to IGF1R, leading to IGF1R ubiquitination, increased
internalization and degradation by both the proteasomal and lysosomal
pathways. May play a role in mediating insulin-stimulated
ubiquitination of INSR, leading to proteasomal degradation. Negatively
regulates Wnt signaling by interacting with LRP6 intracellular portion
and interfering with the binding of AXIN1 to LRP6. Positive regulator
of the KDR/VEGFR-2 signaling pathway. May inhibit NEDD4-mediated
degradation of KDR/VEGFR-2. {ECO:0000269|PubMed:12493740,
ECO:0000269|PubMed:15060076, ECO:0000269|PubMed:16434550,
ECO:0000269|PubMed:17376403}.
-!- ACTIVITY REGULATION: Phosphorylation by mTORC1 stabilizes and activates
GRB10 constituting a feedback pathway by which mTORC1 inhibits INSR-
dependent signaling. {ECO:0000269|PubMed:21659604}.
-!- SUBUNIT: Interacts with ligand-activated tyrosine kinase receptors,
including FGFR1, INSR, IGF1R, MET and PDGFRB in a phosphotyrosine-
dependent manner through the SH2 domain (By similarity). Poorly binds
to the EGFR (By similarity). Directly interacts with MAP3K14/NIK and is
recruited to the EGFR-ERBB2 complex. Interacts with GIGYF1/PERQ1 and
GIGYF2/TNRC15 (By similarity). When unphosphorylated, interacts with
AKT1 and when phosphorylated with YWHAE/14-3-3 epsilon. Interacts with
NEDD4. Interacts with LRP6, thus interfering with the binding of AXIN1
to LRP6 (By similarity). Binds to activated NRAS. {ECO:0000250,
ECO:0000269|PubMed:12493740, ECO:0000269|PubMed:12853971,
ECO:0000269|PubMed:15060076, ECO:0000269|PubMed:15722337,
ECO:0000269|PubMed:19648926}.
-!- INTERACTION:
Q13322; P00533: EGFR; NbExp=3; IntAct=EBI-80275, EBI-297353;
Q13322; P54762: EPHB1; NbExp=2; IntAct=EBI-80275, EBI-80252;
Q13322; P36888: FLT3; NbExp=6; IntAct=EBI-80275, EBI-3946257;
Q13322; P06213: INSR; NbExp=3; IntAct=EBI-80275, EBI-475899;
Q13322; P27986: PIK3R1; NbExp=2; IntAct=EBI-80275, EBI-79464;
Q13322; Q9UKA8: RCAN3; NbExp=3; IntAct=EBI-80275, EBI-9091952;
Q13322-3; Q13322-3: GRB10; NbExp=2; IntAct=EBI-15796145, EBI-15796145;
Q13322-4; Q16613: AANAT; NbExp=3; IntAct=EBI-12353035, EBI-7451846;
Q13322-4; Q86V38: ATN1; NbExp=3; IntAct=EBI-12353035, EBI-11954292;
Q13322-4; P51451: BLK; NbExp=3; IntAct=EBI-12353035, EBI-2105445;
Q13322-4; A0A140G945: CRYAA2; NbExp=3; IntAct=EBI-12353035, EBI-25838900;
Q13322-4; O95363: FARS2; NbExp=3; IntAct=EBI-12353035, EBI-2513774;
Q13322-4; P01100: FOS; NbExp=3; IntAct=EBI-12353035, EBI-852851;
Q13322-4; P50440: GATM; NbExp=3; IntAct=EBI-12353035, EBI-2552594;
Q13322-4; P14136: GFAP; NbExp=3; IntAct=EBI-12353035, EBI-744302;
Q13322-4; Q13322-4: GRB10; NbExp=3; IntAct=EBI-12353035, EBI-12353035;
Q13322-4; P62993: GRB2; NbExp=3; IntAct=EBI-12353035, EBI-401755;
Q13322-4; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-12353035, EBI-1055254;
Q13322-4; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-12353035, EBI-2556193;
Q13322-4; O00505: KPNA3; NbExp=3; IntAct=EBI-12353035, EBI-358297;
Q13322-4; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-12353035, EBI-11742507;
Q13322-4; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-12353035, EBI-10271199;
Q13322-4; Q13153: PAK1; NbExp=3; IntAct=EBI-12353035, EBI-1307;
Q13322-4; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-12353035, EBI-79165;
Q13322-4; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-12353035, EBI-9090795;
Q13322-4; P12931: SRC; NbExp=3; IntAct=EBI-12353035, EBI-621482;
Q13322-4; Q8WW24: TEKT4; NbExp=3; IntAct=EBI-12353035, EBI-750487;
Q13322-4; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-12353035, EBI-11139477;
Q13322-4; Q13470-2: TNK1; NbExp=3; IntAct=EBI-12353035, EBI-11018037;
Q13322-4; P42681: TXK; NbExp=3; IntAct=EBI-12353035, EBI-7877438;
Q13322-4; P61981: YWHAG; NbExp=3; IntAct=EBI-12353035, EBI-359832;
Q13322-4; Q96E35: ZMYND19; NbExp=3; IntAct=EBI-12353035, EBI-746595;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=When complexed with
NEDD4 and IGF1R, follows IGF1R internalization, remaining associated
with early endosomes. Uncouples from IGF1R-containing endosomes before
the sorting of the receptor to the lysosomal compartment (By
similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Comment=Additional isoforms seem to exist, many of which involve
splicing of 5' non-coding exons.;
Name=3; Synonyms=Zeta;
IsoId=Q13322-1; Sequence=Displayed;
Name=1; Synonyms=Beta;
IsoId=Q13322-2; Sequence=VSP_001843;
Name=2; Synonyms=Gamma, Beta, SV-1;
IsoId=Q13322-3; Sequence=VSP_001842;
Name=4; Synonyms=Epsilon;
IsoId=Q13322-4; Sequence=VSP_038784;
-!- TISSUE SPECIFICITY: Widely expressed in fetal and adult tissues,
including fetal and postnatal liver, lung, kidney, skeletal muscle,
heart, spleen, skin and brain. {ECO:0000269|PubMed:11527390}.
-!- DOMAIN: The PH domain binds relatively non-specifically to several
phosphoinositides, including PI(5)P, PI(4,5)P2, PI(3,4)P2 and
PI(3,4,5)P3, with modest affinities.
-!- PTM: Phosphorylated on serine residues upon EGF, FGF and PDGF
stimulation (By similarity). Phosphorylated at Tyr-67 by TEC.
{ECO:0000250, ECO:0000269|PubMed:15722337, ECO:0000269|PubMed:15952796,
ECO:0000269|PubMed:21659604, ECO:0000269|PubMed:9753425}.
-!- MISCELLANEOUS: The GRB10 locus is imprinted. During embryonic
development, the expression in the brain and spinal cord is from the
paternal allele, while in placental villous trophoblasts and skeletal
muscle, it is from the maternal one. Expression is biallelic in most
other tissues. Paternal expression in the brain is maintained
throughout adulthood. Imprinting often is isoform-specific.
-!- MISCELLANEOUS: GRB10 is unlikely to be responsible for Silver-Russell
syndrome (SRS).
-!- SIMILARITY: Belongs to the GRB7/10/14 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA13198.2; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
Haematology;
URL="http://atlasgeneticsoncology.org/Genes/GRB10ID278.html";
---------------------------------------------------------------------------
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EMBL; U34355; AAA88819.1; -; mRNA.
EMBL; U66065; AAC50671.1; -; mRNA.
EMBL; U69276; AAB08431.1; -; mRNA.
EMBL; AF001534; AAB81134.1; -; mRNA.
EMBL; AF000017; AAC19748.1; -; mRNA.
EMBL; AB000731; BAF76353.1; -; mRNA.
EMBL; AJ271366; CAB96542.1; -; mRNA.
EMBL; D86962; BAA13198.2; ALT_INIT; mRNA.
EMBL; AK289511; BAF82200.1; -; mRNA.
EMBL; AF073378; AAC83655.1; -; Genomic_DNA.
EMBL; AF073363; AAC83655.1; JOINED; Genomic_DNA.
EMBL; AF073364; AAC83655.1; JOINED; Genomic_DNA.
EMBL; AF073365; AAC83655.1; JOINED; Genomic_DNA.
EMBL; AF073366; AAC83655.1; JOINED; Genomic_DNA.
EMBL; AF073367; AAC83655.1; JOINED; Genomic_DNA.
EMBL; AF073368; AAC83655.1; JOINED; Genomic_DNA.
EMBL; AF073369; AAC83655.1; JOINED; Genomic_DNA.
EMBL; AF073370; AAC83655.1; JOINED; Genomic_DNA.
EMBL; AF073371; AAC83655.1; JOINED; Genomic_DNA.
EMBL; AF073372; AAC83655.1; JOINED; Genomic_DNA.
EMBL; AF073373; AAC83655.1; JOINED; Genomic_DNA.
EMBL; AF073374; AAC83655.1; JOINED; Genomic_DNA.
EMBL; AF073375; AAC83655.1; JOINED; Genomic_DNA.
EMBL; AF073376; AAC83655.1; JOINED; Genomic_DNA.
EMBL; AF073377; AAC83655.1; JOINED; Genomic_DNA.
EMBL; AF073378; AAC83654.1; -; Genomic_DNA.
EMBL; AF073363; AAC83654.1; JOINED; Genomic_DNA.
EMBL; AF073364; AAC83654.1; JOINED; Genomic_DNA.
EMBL; AF073365; AAC83654.1; JOINED; Genomic_DNA.
EMBL; AF073366; AAC83654.1; JOINED; Genomic_DNA.
EMBL; AF073367; AAC83654.1; JOINED; Genomic_DNA.
EMBL; AF073368; AAC83654.1; JOINED; Genomic_DNA.
EMBL; AF073369; AAC83654.1; JOINED; Genomic_DNA.
EMBL; AF073371; AAC83654.1; JOINED; Genomic_DNA.
EMBL; AF073372; AAC83654.1; JOINED; Genomic_DNA.
EMBL; AF073373; AAC83654.1; JOINED; Genomic_DNA.
EMBL; AF073374; AAC83654.1; JOINED; Genomic_DNA.
EMBL; AF073375; AAC83654.1; JOINED; Genomic_DNA.
EMBL; AF073376; AAC83654.1; JOINED; Genomic_DNA.
EMBL; AF073377; AAC83654.1; JOINED; Genomic_DNA.
EMBL; AC005153; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH236955; EAL23897.1; -; Genomic_DNA.
EMBL; CH471128; EAW60964.1; -; Genomic_DNA.
EMBL; CH471128; EAW60965.1; -; Genomic_DNA.
EMBL; CH471128; EAW60967.1; -; Genomic_DNA.
EMBL; BC024285; AAH24285.1; -; mRNA.
CCDS; CCDS43582.1; -. [Q13322-1]
CCDS; CCDS43583.1; -. [Q13322-3]
CCDS; CCDS47586.1; -. [Q13322-2]
CCDS; CCDS87503.1; -. [Q13322-3]
PIR; I39175; I39175.
RefSeq; NP_001001549.1; NM_001001549.2. [Q13322-2]
RefSeq; NP_001001550.1; NM_001001550.2. [Q13322-3]
RefSeq; NP_001001555.1; NM_001001555.2. [Q13322-3]
RefSeq; NP_005302.3; NM_005311.4.
RefSeq; XP_011513606.1; XM_011515304.1.
RefSeq; XP_011513614.1; XM_011515312.2.
RefSeq; XP_011513618.1; XM_011515316.1. [Q13322-3]
RefSeq; XP_016867534.1; XM_017012045.1. [Q13322-3]
RefSeq; XP_016867535.1; XM_017012046.1. [Q13322-1]
RefSeq; XP_016867552.1; XM_017012063.1. [Q13322-3]
RefSeq; XP_016867553.1; XM_017012064.1. [Q13322-3]
RefSeq; XP_016867554.1; XM_017012065.1. [Q13322-3]
RefSeq; XP_016867555.1; XM_017012066.1.
RefSeq; XP_016867556.1; XM_017012067.1. [Q13322-3]
RefSeq; XP_016867557.1; XM_017012068.1. [Q13322-3]
PDB; 1NRV; X-ray; 1.65 A; A/B=487-591.
PDB; 3HK0; X-ray; 2.60 A; A/B=164-415.
PDBsum; 1NRV; -.
PDBsum; 3HK0; -.
SMR; Q13322; -.
BioGRID; 109144; 135.
DIP; DIP-31657N; -.
ELM; Q13322; -.
IntAct; Q13322; 123.
MINT; Q13322; -.
STRING; 9606.ENSP00000381793; -.
BindingDB; Q13322; -.
ChEMBL; CHEMBL3621028; -.
iPTMnet; Q13322; -.
PhosphoSitePlus; Q13322; -.
BioMuta; GRB10; -.
DMDM; 6166186; -.
CPTAC; CPTAC-1247; -.
EPD; Q13322; -.
jPOST; Q13322; -.
MassIVE; Q13322; -.
MaxQB; Q13322; -.
PaxDb; Q13322; -.
PeptideAtlas; Q13322; -.
PRIDE; Q13322; -.
ProteomicsDB; 59307; -. [Q13322-1]
ProteomicsDB; 59308; -. [Q13322-2]
ProteomicsDB; 59309; -. [Q13322-3]
ProteomicsDB; 59310; -. [Q13322-4]
Antibodypedia; 27751; 449 antibodies.
DNASU; 2887; -.
Ensembl; ENST00000335866; ENSP00000338543; ENSG00000106070. [Q13322-3]
Ensembl; ENST00000357271; ENSP00000349818; ENSG00000106070. [Q13322-2]
Ensembl; ENST00000398810; ENSP00000381790; ENSG00000106070. [Q13322-3]
Ensembl; ENST00000398812; ENSP00000381793; ENSG00000106070. [Q13322-1]
Ensembl; ENST00000401949; ENSP00000385770; ENSG00000106070. [Q13322-1]
Ensembl; ENST00000402497; ENSP00000385748; ENSG00000106070. [Q13322-3]
Ensembl; ENST00000402578; ENSP00000385189; ENSG00000106070. [Q13322-3]
Ensembl; ENST00000403097; ENSP00000385544; ENSG00000106070. [Q13322-3]
Ensembl; ENST00000406641; ENSP00000385366; ENSG00000106070. [Q13322-3]
Ensembl; ENST00000407526; ENSP00000385046; ENSG00000106070. [Q13322-3]
Ensembl; ENST00000643299; ENSP00000496245; ENSG00000106070. [Q13322-3]
Ensembl; ENST00000645075; ENSP00000495341; ENSG00000106070. [Q13322-3]
GeneID; 2887; -.
KEGG; hsa:2887; -.
UCSC; uc003tph.4; human. [Q13322-1]
CTD; 2887; -.
DisGeNET; 2887; -.
GeneCards; GRB10; -.
HGNC; HGNC:4564; GRB10.
HPA; ENSG00000106070; Tissue enhanced (pancreas).
MIM; 601523; gene.
neXtProt; NX_Q13322; -.
OpenTargets; ENSG00000106070; -.
PharmGKB; PA28960; -.
VEuPathDB; HostDB:ENSG00000106070.17; -.
eggNOG; KOG3751; Eukaryota.
GeneTree; ENSGT00940000155909; -.
HOGENOM; CLU_023207_0_1_1; -.
InParanoid; Q13322; -.
OMA; NGSHTQL; -.
OrthoDB; 497681at2759; -.
PhylomeDB; Q13322; -.
TreeFam; TF317511; -.
PathwayCommons; Q13322; -.
Reactome; R-HSA-1433557; Signaling by SCF-KIT.
Reactome; R-HSA-74713; IRS activation.
Reactome; R-HSA-74749; Signal attenuation.
Reactome; R-HSA-74751; Insulin receptor signalling cascade.
Reactome; R-HSA-8853659; RET signaling.
Reactome; R-HSA-9648895; Response of EIF2AK1 (HRI) to heme deficiency.
SignaLink; Q13322; -.
SIGNOR; Q13322; -.
BioGRID-ORCS; 2887; 6 hits in 878 CRISPR screens.
ChiTaRS; GRB10; human.
EvolutionaryTrace; Q13322; -.
GeneWiki; GRB10; -.
GenomeRNAi; 2887; -.
Pharos; Q13322; Tbio.
PRO; PR:Q13322; -.
Proteomes; UP000005640; Chromosome 7.
RNAct; Q13322; protein.
Bgee; ENSG00000106070; Expressed in body of pancreas and 243 other tissues.
ExpressionAtlas; Q13322; baseline and differential.
Genevisible; Q13322; HS.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005158; F:insulin receptor binding; ISS:BHF-UCL.
GO; GO:0007411; P:axon guidance; TAS:Reactome.
GO; GO:0008286; P:insulin receptor signaling pathway; ISS:BHF-UCL.
GO; GO:0046325; P:negative regulation of glucose import; ISS:BHF-UCL.
GO; GO:0045719; P:negative regulation of glycogen biosynthetic process; ISS:BHF-UCL.
GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; ISS:BHF-UCL.
GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IDA:UniProtKB.
GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
GO; GO:0042327; P:positive regulation of phosphorylation; ISS:BHF-UCL.
GO; GO:0030949; P:positive regulation of vascular endothelial growth factor receptor signaling pathway; IDA:UniProtKB.
GO; GO:0032868; P:response to insulin; ISS:BHF-UCL.
CDD; cd01259; PH_APBB1IP; 1.
CDD; cd10415; SH2_Grb10; 1.
Gene3D; 2.30.29.30; -; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR015042; BPS-dom.
InterPro; IPR039664; GRB/APBB1IP.
InterPro; IPR035036; Grb10.
InterPro; IPR035037; Grb10_SH2.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR039665; PH_APBB1IP.
InterPro; IPR001849; PH_domain.
InterPro; IPR000159; RA_dom.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR029071; Ubiquitin-like_domsf.
PANTHER; PTHR11243; PTHR11243; 1.
PANTHER; PTHR11243:SF4; PTHR11243:SF4; 1.
Pfam; PF08947; BPS; 1.
Pfam; PF00169; PH; 1.
Pfam; PF00788; RA; 1.
Pfam; PF00017; SH2; 1.
PRINTS; PR00401; SH2DOMAIN.
SMART; SM00233; PH; 1.
SMART; SM00314; RA; 1.
SMART; SM00252; SH2; 1.
SUPFAM; SSF54236; SSF54236; 1.
SUPFAM; SSF55550; SSF55550; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS50200; RA; 1.
PROSITE; PS50001; SH2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cytoplasm; Direct protein sequencing;
Phosphoprotein; Reference proteome; SH2 domain.
CHAIN 1..594
/note="Growth factor receptor-bound protein 10"
/id="PRO_0000150346"
DOMAIN 166..250
/note="Ras-associating"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
DOMAIN 290..399
/note="PH"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
DOMAIN 493..574
/note="SH2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
MOD_RES 67
/note="Phosphotyrosine; by TEC"
/evidence="ECO:0000269|PubMed:9753425"
MOD_RES 104
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163"
MOD_RES 150
/note="Phosphoserine; by MTOR, MAPK1 and MAPK3"
/evidence="ECO:0000269|PubMed:15952796,
ECO:0000269|PubMed:21659604"
MOD_RES 418
/note="Phosphoserine; by MAPK1 and MAPK3; in vitro"
/evidence="ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:15952796"
MOD_RES 428
/note="Phosphoserine; by MTOR and PKB/AKT1"
/evidence="ECO:0000269|PubMed:15722337,
ECO:0000269|PubMed:21659604"
MOD_RES 431
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q60760"
MOD_RES 476
/note="Phosphoserine; by MTOR, MAPK1 and MAPK3"
/evidence="ECO:0000269|PubMed:15952796,
ECO:0000269|PubMed:21659604"
VAR_SEQ 1..58
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8798417,
ECO:0000303|PubMed:9006901"
/id="VSP_001842"
VAR_SEQ 1..17
/note="MALAGCPDSFLHHPYYQ -> MQAAGPLFRSK (in isoform 4)"
/evidence="ECO:0000303|PubMed:9039502"
/id="VSP_038784"
VAR_SEQ 283..328
/note="Missing (in isoform 1)"
/evidence="ECO:0000303|PubMed:7479769,
ECO:0000303|PubMed:9753425"
/id="VSP_001843"
VARIANT 36
/note="P -> L (in dbSNP:rs35647889)"
/id="VAR_053112"
VARIANT 95
/note="P -> S (in dbSNP:rs80244589)"
/evidence="ECO:0000269|PubMed:10856193"
/id="VAR_062864"
VARIANT 558
/note="D -> H (in dbSNP:rs11768472)"
/id="VAR_053113"
MUTAGEN 104
/note="S->G: No effect on phosphorylation."
/evidence="ECO:0000269|PubMed:15952796"
MUTAGEN 134
/note="S->A: No effect on YWHAE-binding."
/evidence="ECO:0000269|PubMed:15722337"
MUTAGEN 136
/note="P->A: No effect on NEDD4-binding; when associated
with A-139 and A-141."
/evidence="ECO:0000269|PubMed:15060076"
MUTAGEN 139
/note="P->A: No effect on NEDD4-binding; when associated
with A-136 and A-141."
/evidence="ECO:0000269|PubMed:15060076"
MUTAGEN 141
/note="P->S: No effect on NEDD4-binding; when associated
with A-136 and A-139."
/evidence="ECO:0000269|PubMed:15060076"
MUTAGEN 150
/note="S->I: Loss of phosphorylation."
/evidence="ECO:0000269|PubMed:15952796"
MUTAGEN 300
/note="K->A: 2-fold loss of inositide-binding."
/evidence="ECO:0000269|PubMed:19648926"
MUTAGEN 305
/note="K->A: 5-fold loss of inositide-binding."
/evidence="ECO:0000269|PubMed:19648926"
MUTAGEN 308
/note="K->A: 5-fold loss of inositide-binding."
/evidence="ECO:0000269|PubMed:19648926"
MUTAGEN 355
/note="N->G: 5-fold loss of inositide-binding."
/evidence="ECO:0000269|PubMed:19648926"
MUTAGEN 418
/note="S->A: No net loss of phosphorylation, this may be
due to a compensatory phosphorylation of T-422 in vitro."
/evidence="ECO:0000269|PubMed:15952796"
MUTAGEN 428
/note="S->A: Impairs YWHAE-binding."
/evidence="ECO:0000269|PubMed:15722337"
MUTAGEN 476
/note="S->A: Loss of phosphorylation."
/evidence="ECO:0000269|PubMed:15952796"
MUTAGEN 520
/note="R->K: No effect on NEDD4-binding. No effect on the
disruption of the interaction between INSR and IRS1 and
IRS2."
/evidence="ECO:0000269|PubMed:12493740,
ECO:0000269|PubMed:15060076"
CONFLICT 152
/note="P -> A (in Ref. 9; BAA13198)"
/evidence="ECO:0000305"
CONFLICT 400
/note="G -> E (in Ref. 3; AAB08431)"
/evidence="ECO:0000305"
CONFLICT 428
/note="S -> F (in Ref. 10; BAF82200)"
/evidence="ECO:0000305"
CONFLICT 498
/note="I -> F (in Ref. 3; AAB08431)"
/evidence="ECO:0000305"
CONFLICT 541
/note="N -> I (in Ref. 2; AAC50671)"
/evidence="ECO:0000305"
STRAND 168..174
/evidence="ECO:0000244|PDB:3HK0"
STRAND 179..184
/evidence="ECO:0000244|PDB:3HK0"
HELIX 190..198
/evidence="ECO:0000244|PDB:3HK0"
STRAND 209..215
/evidence="ECO:0000244|PDB:3HK0"
TURN 216..219
/evidence="ECO:0000244|PDB:3HK0"
STRAND 220..223
/evidence="ECO:0000244|PDB:3HK0"
HELIX 230..235
/evidence="ECO:0000244|PDB:3HK0"
STRAND 242..247
/evidence="ECO:0000244|PDB:3HK0"
TURN 249..252
/evidence="ECO:0000244|PDB:3HK0"
HELIX 253..256
/evidence="ECO:0000244|PDB:3HK0"
HELIX 258..260
/evidence="ECO:0000244|PDB:3HK0"
STRAND 266..269
/evidence="ECO:0000244|PDB:3HK0"
HELIX 281..285
/evidence="ECO:0000244|PDB:3HK0"
STRAND 291..300
/evidence="ECO:0000244|PDB:3HK0"
STRAND 307..315
/evidence="ECO:0000244|PDB:3HK0"
STRAND 318..324
/evidence="ECO:0000244|PDB:3HK0"
HELIX 330..332
/evidence="ECO:0000244|PDB:3HK0"
STRAND 333..337
/evidence="ECO:0000244|PDB:3HK0"
STRAND 342..349
/evidence="ECO:0000244|PDB:3HK0"
HELIX 351..354
/evidence="ECO:0000244|PDB:3HK0"
STRAND 357..366
/evidence="ECO:0000244|PDB:3HK0"
STRAND 377..383
/evidence="ECO:0000244|PDB:3HK0"
HELIX 384..399
/evidence="ECO:0000244|PDB:3HK0"
HELIX 401..407
/evidence="ECO:0000244|PDB:3HK0"
HELIX 500..509
/evidence="ECO:0000244|PDB:1NRV"
STRAND 516..521
/evidence="ECO:0000244|PDB:1NRV"
STRAND 529..535
/evidence="ECO:0000244|PDB:1NRV"
STRAND 538..546
/evidence="ECO:0000244|PDB:1NRV"
STRAND 555..558
/evidence="ECO:0000244|PDB:1NRV"
STRAND 564..566
/evidence="ECO:0000244|PDB:1NRV"
HELIX 567..574
/evidence="ECO:0000244|PDB:1NRV"
STRAND 581..583
/evidence="ECO:0000244|PDB:1NRV"
SEQUENCE 594 AA; 67231 MW; 53A5F885E17C6C6B CRC64;
MALAGCPDSF LHHPYYQDKV EQTPRSQQDP AGPGLPAQSD RLANHQEDDV DLEALVNDMN
ASLESLYSAC SMQSDTVPLL QNGQHARSQP RASGPPRSIQ PQVSPRQRVQ RSQPVHILAV
RRLQEEDQQF RTSSLPAIPN PFPELCGPGS PPVLTPGSLP PSQAAAKQDV KVFSEDGTSK
VVEILADMTA RDLCQLLVYK SHCVDDNSWT LVEHHPHLGL ERCLEDHELV VQVESTMASE
SKFLFRKNYA KYEFFKNPMN FFPEQMVTWC QQSNGSQTQL LQNFLNSSSC PEIQGFLHVK
ELGKKSWKKL YVCLRRSGLY CSTKGTSKEP RHLQLLADLE DSNIFSLIAG RKQYNAPTDH
GLCIKPNKVR NETKELRLLC AEDEQTRTCW MTAFRLLKYG MLLYQNYRIP QQRKALLSPF
STPVRSVSEN SLVAMDFSGQ TGRVIENPAE AQSAALEEGH AWRKRSTRMN ILGSQSPLHP
STLSTVIHRT QHWFHGRISR EESHRIIKQQ GLVDGLFLLR DSQSNPKAFV LTLCHHQKIK
NFQILPCEDD GQTFFSLDDG NTKFSDLIQL VDFYQLNKGV LPCKLKHHCI RVAL


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Pathways :
WP2292: Chemokine signaling pathway
WP2272: Pathogenic Escherichia coli infection
WP731: Sterol regulatory element binding protein related
WP444: Signaling of Hepatocyte Growth Factor Receptor
WP1899: Regulation of Insulin-like Growth Factor (IGF) Activity by Insulin-like Growth Factor Binding Proteins (IGFBPs)
WP1235: Signaling of Hepatocyte Growth Factor Receptor
WP927: Signaling of Hepatocyte Growth Factor Receptor
WP313: Signaling of Hepatocyte Growth Factor Receptor
WP810: Signaling of Hepatocyte Growth Factor Receptor
WP1789: Binding of RNA by Insulin-like Growth Factor-2 mRNA Binding Proteins (IGF2BPs/IMPs/VICKZs)
WP1046: Signaling of Hepatocyte Growth Factor Receptor
WP1206: Signaling of Hepatocyte Growth Factor Receptor
WP94: Signaling of Hepatocyte Growth Factor Receptor
WP1531: Vitamin D synthesis
WP1162: Signaling of Hepatocyte Growth Factor Receptor
WP1616: ABC transporters
WP193: Signaling of Hepatocyte Growth Factor Receptor
WP1613: 1,4-Dichlorobenzene degradation
WP1869: Neuroransmitter Receptor Binding And Downstream Transmission In The Postsynaptic Cell
WP2371: Parkinsons Disease Pathway
WP1004: Kit Receptor Signaling Pathway
WP1678: Nucleotide excision repair
WP211: BMP signaling pathway
WP1690: Propanoate metabolism
WP1625: Base excision repair

Related Genes :
[GRB2 ASH] Growth factor receptor-bound protein 2 (Adapter protein GRB2) (Protein Ash) (SH2/SH3 adapter GRB2)
[IGF1R] Insulin-like growth factor 1 receptor (EC 2.7.10.1) (Insulin-like growth factor I receptor) (IGF-I receptor) (CD antigen CD221) [Cleaved into: Insulin-like growth factor 1 receptor alpha chain; Insulin-like growth factor 1 receptor beta chain]
[INSR] Insulin receptor (IR) (EC 2.7.10.1) (CD antigen CD220) [Cleaved into: Insulin receptor subunit alpha; Insulin receptor subunit beta]
[Igf1r] Insulin-like growth factor 1 receptor (EC 2.7.10.1) (Insulin-like growth factor I receptor) (IGF-I receptor) (CD antigen CD221) [Cleaved into: Insulin-like growth factor 1 receptor alpha chain; Insulin-like growth factor 1 receptor beta chain]
[Igf1r] Insulin-like growth factor 1 receptor (EC 2.7.10.1) (Insulin-like growth factor I receptor) (IGF-I receptor) (CD antigen CD221) [Cleaved into: Insulin-like growth factor 1 receptor alpha chain; Insulin-like growth factor 1 receptor beta chain]
[IGF1R] Insulin-like growth factor 1 receptor (EC 2.7.10.1) (Insulin-like growth factor I receptor) (IGF-I receptor) (CD antigen CD221) [Cleaved into: Insulin-like growth factor 1 receptor alpha chain; Insulin-like growth factor 1 receptor beta chain] (Fragment)
[GRB7] Growth factor receptor-bound protein 7 (B47) (Epidermal growth factor receptor GRB-7) (GRB7 adapter protein)
[Gigyf2 Kiaa0642 Perq2 Tnrc15] GRB10-interacting GYF protein 2 (PERQ amino acid-rich with GYF domain-containing protein 2) (Trinucleotide repeat-containing gene 15 protein)
[Grb2] Growth factor receptor-bound protein 2 (Adapter protein GRB2) (SH2/SH3 adapter GRB2)
[Grb2 Ash] Growth factor receptor-bound protein 2 (Adapter protein GRB2) (Protein Ash) (SH2/SH3 adapter GRB2)
[GRB2] Growth factor receptor-bound protein 2 (Adapter protein GRB2) (SH2/SH3 adapter GRB2)
[Insr] Insulin receptor (IR) (EC 2.7.10.1) (CD antigen CD220) [Cleaved into: Insulin receptor subunit alpha; Insulin receptor subunit beta]
[Grb7] Growth factor receptor-bound protein 7 (Epidermal growth factor receptor GRB-7) (GRB7 adapter protein)
[PDGFRB PDGFR PDGFR1] Platelet-derived growth factor receptor beta (PDGF-R-beta) (PDGFR-beta) (EC 2.7.10.1) (Beta platelet-derived growth factor receptor) (Beta-type platelet-derived growth factor receptor) (CD140 antigen-like family member B) (Platelet-derived growth factor receptor 1) (PDGFR-1) (CD antigen CD140b)
[Insr] Insulin receptor (IR) (EC 2.7.10.1) (CD antigen CD220) [Cleaved into: Insulin receptor subunit alpha; Insulin receptor subunit beta]
[Pdgfrb Pdgfr Pdgfr1] Platelet-derived growth factor receptor beta (PDGF-R-beta) (PDGFR-beta) (EC 2.7.10.1) (Beta platelet-derived growth factor receptor) (Beta-type platelet-derived growth factor receptor) (CD140 antigen-like family member B) (Platelet-derived growth factor receptor 1) (PDGFR-1) (CD antigen CD140b)
[FGFR1 BFGFR CEK FGFBR FLG FLT2 HBGFR] Fibroblast growth factor receptor 1 (FGFR-1) (EC 2.7.10.1) (Basic fibroblast growth factor receptor 1) (BFGFR) (bFGF-R-1) (Fms-like tyrosine kinase 2) (FLT-2) (N-sam) (Proto-oncogene c-Fgr) (CD antigen CD331)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[GAB1] GRB2-associated-binding protein 1 (GRB2-associated binder 1) (Growth factor receptor bound protein 2-associated protein 1)
[NCK2 GRB4] Cytoplasmic protein NCK2 (Growth factor receptor-bound protein 4) (NCK adaptor protein 2) (Nck-2) (SH2/SH3 adaptor protein NCK-beta)
[EGFR ERBB ERBB1 HER1] Epidermal growth factor receptor (EC 2.7.10.1) (Proto-oncogene c-ErbB-1) (Receptor tyrosine-protein kinase erbB-1)
[Fgfr1 Flg] Fibroblast growth factor receptor 1 (FGFR-1) (bFGF-R-1) (EC 2.7.10.1) (Basic fibroblast growth factor receptor 1) (MFR) (Proto-oncogene c-Fgr) (CD antigen CD331)
[Pdgfrb Pdgfr Pdgfr1] Platelet-derived growth factor receptor beta (PDGF-R-beta) (PDGFR-beta) (EC 2.7.10.1) (Beta platelet-derived growth factor receptor) (Beta-type platelet-derived growth factor receptor) (CD140 antigen-like family member B) (Platelet-derived growth factor receptor 1) (PDGFR-1) (CD antigen CD140b)
[PDGFRB PDGFR PDGFR1] Platelet-derived growth factor receptor beta (PDGF-R-beta) (PDGFR-beta) (EC 2.7.10.1) (Beta platelet-derived growth factor receptor) (Beta-type platelet-derived growth factor receptor) (CD140 antigen-like family member B) (Platelet-derived growth factor receptor 1) (PDGFR-1) (CD antigen CD140b)
[Met] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[Met] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)

Bibliography :
[9360986] Cloning, chromosome localization, expression, and characterization of an Src homology 2 and pleckstrin homology domain-containing insulin receptor binding protein hGrb10gamma.
[9006901] Human GRB-IRbeta/GRB10. Splice variants of an insulin and growth factor receptor-binding protein with PH and SH2 domains.