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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_HUMAN             Reviewed;        1367 AA.
P08069; B1B5Y2; Q14CV2; Q9UCC0;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-AUG-1988, sequence version 1.
17-JUN-2020, entry version 232.
RecName: Full=Insulin-like growth factor 1 receptor;
EC=2.7.10.1;
AltName: Full=Insulin-like growth factor I receptor;
Short=IGF-I receptor;
AltName: CD_antigen=CD221;
Contains:
RecName: Full=Insulin-like growth factor 1 receptor alpha chain;
Contains:
RecName: Full=Insulin-like growth factor 1 receptor beta chain;
Flags: Precursor;
Name=IGF1R;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 31-56; 446-453;
503-524; 561-579; 668-672 AND 721-729.
TISSUE=Placenta;
PubMed=2877871; DOI=10.1002/j.1460-2075.1986.tb04528.x;
Ullrich A., Gray A., Tam A.W., Yang-Feng T., Tsubokawa M., Collins C.,
Henzel W., Bon T.L., Kathuria S., Chen E., Jacobs S., Francke U.,
Ramachandran J., Fujita-Yamaguchi Y.;
"Insulin-like growth factor I receptor primary structure: comparison with
insulin receptor suggests structural determinants that define functional
specificity.";
EMBO J. 5:2503-2512(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1316909;
Abbot A.M., Bueno R., Pedrini M.T., Murray J.M., Smith R.J.;
"Insulin-like growth factor I receptor gene structure.";
J. Biol. Chem. 267:10759-10763(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Fetal brain;
Nagase T., Kikuno R.F., Yamakawa H., Ohara O.;
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS MET-388 AND HIS-605.
NIEHS SNPs program;
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human chromosome
15.";
Nature 440:671-675(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31.
PubMed=1711844; DOI=10.1016/0006-291x(91)90654-p;
Cooke D.W., Bankert L.A., Roberts C.T. Jr., Leroith D., Casella S.J.;
"Analysis of the human type I insulin-like growth factor receptor promoter
region.";
Biochem. Biophys. Res. Commun. 177:1113-1120(1991).
[8]
PROTEIN SEQUENCE OF 31-45 AND 741-750, FUNCTION, AND FORMATION OF A HYBRID
RECEPTOR WITH INSR.
TISSUE=Placenta;
PubMed=8257688; DOI=10.1021/bi00212a019;
Kasuya J., Paz I.B., Maddux B.A., Goldfine I.D., Hefta S.A.,
Fujita-Yamaguchi Y.;
"Characterization of human placental insulin-like growth factor-I/insulin
hybrid receptors by protein microsequencing and purification.";
Biochemistry 32:13531-13536(1993).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 1137-1193, AND TISSUE SPECIFICITY.
TISSUE=Melanocyte;
PubMed=8247543;
Lee S.-T., Strunk K.M., Spritz R.A.;
"A survey of protein tyrosine kinase mRNAs expressed in normal human
melanocytes.";
Oncogene 8:3403-3410(1993).
[10]
FUNCTION, SUBUNIT, AND AUTOPHOSPHORYLATION.
PubMed=1846292; DOI=10.1021/bi00215a008;
Tollefsen S.E., Stoszek R.M., Thompson K.;
"Interaction of the alpha beta dimers of the insulin-like growth factor I
receptor is required for receptor autophosphorylation.";
Biochemistry 30:48-54(1991).
[11]
FUNCTION, AND FORMATION OF A HYBRID RECEPTOR WITH INSR.
PubMed=8452530; DOI=10.1042/bj2900419;
Soos M.A., Field C.E., Siddle K.;
"Purified hybrid insulin/insulin-like growth factor-I receptors bind
insulin-like growth factor-I, but not insulin, with high affinity.";
Biochem. J. 290:419-426(1993).
[12]
FUNCTION, CATALYTIC ACTIVITY, AND AUTOPHOSPHORYLATION.
PubMed=7679099;
Kato H., Faria T.N., Stannard B., Roberts C.T. Jr., LeRoith D.;
"Role of tyrosine kinase activity in signal transduction by the insulin-
like growth factor-I (IGF-I) receptor. Characterization of kinase-deficient
IGF-I receptors and the action of an IGF-I-mimetic antibody (alpha IR-3).";
J. Biol. Chem. 268:2655-2661(1993).
[13]
INTERACTION WITH IRS1; SHC1 AND PIK3R1, MUTAGENESIS OF TYR-980 AND
LYS-1033, AND PHOSPHORYLATION AT TYR-980.
PubMed=7541045; DOI=10.1074/jbc.270.26.15639;
Craparo A., O'Neill T.J., Gustafson T.A.;
"Non-SH2 domains within insulin receptor substrate-1 and SHC mediate their
phosphotyrosine-dependent interaction with the NPEY motif of the insulin-
like growth factor I receptor.";
J. Biol. Chem. 270:15639-15643(1995).
[14]
FORMATION OF A HYBRID RECEPTOR WITH INSR, AND TISSUE SPECIFICITY.
PubMed=9355755; DOI=10.1042/bj3270209;
Bailyes E.M., Nave B.T., Soos M.A., Orr S.R., Hayward A.C., Siddle K.;
"Insulin receptor/IGF-I receptor hybrids are widely distributed in
mammalian tissues: quantification of individual receptor species by
selective immunoprecipitation and immunoblotting.";
Biochem. J. 327:209-215(1997).
[15]
INTERACTION WITH 14-3-3 PROTEINS.
PubMed=9581554; DOI=10.1042/bj3270765;
Furlanetto R.W., Dey B.R., Lopaczynski W., Nissley S.P.;
"14-3-3 proteins interact with the insulin-like growth factor receptor but
not the insulin receptor.";
Biochem. J. 327:765-771(1997).
[16]
FORMATION OF A HYBRID RECEPTOR WITH INSR, AND TISSUE SPECIFICITY.
PubMed=9202395; DOI=10.1016/s0303-7207(97)04050-1;
Federici M., Porzio O., Zucaro L., Fusco A., Borboni P., Lauro D.,
Sesti G.;
"Distribution of insulin/insulin-like growth factor-I hybrid receptors in
human tissues.";
Mol. Cell. Endocrinol. 129:121-126(1997).
[17]
INTERACTION WITH SOCS1 AND SOCS2.
PubMed=9727029; DOI=10.1074/jbc.273.37.24095;
Dey B.R., Spence S.L., Nissley P., Furlanetto R.W.;
"Interaction of human suppressor of cytokine signaling (SOCS)-2 with the
insulin-like growth factor-I receptor.";
J. Biol. Chem. 273:24095-24101(1998).
[18]
INTERACTION WITH ARRB1 AND ARRB2.
PubMed=9822622; DOI=10.1074/jbc.273.48.31640;
Lin F.-T., Daaka Y., Lefkowitz R.J.;
"beta-arrestins regulate mitogenic signaling and clathrin-mediated
endocytosis of the insulin-like growth factor I receptor.";
J. Biol. Chem. 273:31640-31643(1998).
[19]
FUNCTION IN CANCER.
PubMed=10579905; DOI=10.1006/excr.1999.4667;
Baserga R.;
"The IGF-I receptor in cancer research.";
Exp. Cell Res. 253:1-6(1999).
[20]
INTERACTION WITH GRB10, AND MUTAGENESIS OF TYR-980; TYR-1280; TYR-1281 AND
TYR-1346.
PubMed=10454568; DOI=10.1128/mcb.19.9.6217;
Wang J., Dai H., Yousaf N., Moussaif M., Deng Y., Boufelliga A.,
Swamy O.R., Leone M.E., Riedel H.;
"Grb10, a positive, stimulatory signaling adapter in platelet-derived
growth factor BB-, insulin-like growth factor I-, and insulin-mediated
mitogenesis.";
Mol. Cell. Biol. 19:6217-6228(1999).
[21]
INTERACTION WITH SOCS3.
PubMed=11071852; DOI=10.1006/bbrc.2000.3762;
Dey B.R., Furlanetto R.W., Nissley P.;
"Suppressor of cytokine signaling (SOCS)-3 protein interacts with the
insulin-like growth factor-I receptor.";
Biochem. Biophys. Res. Commun. 278:38-43(2000).
[22]
AUTOPHOSPHORYLATION.
PubMed=11162456; DOI=10.1006/bbrc.2000.4046;
Lopaczynski W., Terry C., Nissley P.;
"Autophosphorylation of the insulin-like growth factor I receptor
cytoplasmic domain.";
Biochem. Biophys. Res. Commun. 279:955-960(2000).
[23]
FUNCTION IN ACTIVATION OF STAT3.
PubMed=10747872; DOI=10.1074/jbc.m000089200;
Zong C.S., Chan J., Levy D.E., Horvath C., Sadowski H.B., Wang L.H.;
"Mechanism of STAT3 activation by insulin-like growth factor I receptor.";
J. Biol. Chem. 275:15099-15105(2000).
[24]
TISSUE SPECIFICITY.
PubMed=12019176;
Hellawell G.O., Turner G.D., Davies D.R., Poulsom R., Brewster S.F.,
Macaulay V.M.;
"Expression of the type 1 insulin-like growth factor receptor is up-
regulated in primary prostate cancer and commonly persists in metastatic
disease.";
Cancer Res. 62:2942-2950(2002).
[25]
FUNCTION, AND FORMATION OF A HYBRID RECEPTOR WITH INSR.
PubMed=12138094; DOI=10.1074/jbc.m202766200;
Pandini G., Frasca F., Mineo R., Sciacca L., Vigneri R., Belfiore A.;
"Insulin/insulin-like growth factor I hybrid receptors have different
biological characteristics depending on the insulin receptor isoform
involved.";
J. Biol. Chem. 277:39684-39695(2002).
[26]
INTERACTION WITH RACK1.
PubMed=11884618; DOI=10.1128/mcb.22.7.2345-2365.2002;
Hermanto U., Zong C.S., Li W., Wang L.H.;
"RACK1, an insulin-like growth factor I (IGF-I) receptor-interacting
protein, modulates IGF-I-dependent integrin signaling and promotes cell
spreading and contact with extracellular matrix.";
Mol. Cell. Biol. 22:2345-2365(2002).
[27]
FUNCTION, AND INTERACTION WITH MAP3K5.
PubMed=12556535; DOI=10.1074/jbc.m211398200;
Galvan V., Logvinova A., Sperandio S., Ichijo H., Bredesen D.E.;
"Type 1 insulin-like growth factor receptor (IGF-IR) signaling inhibits
apoptosis signal-regulating kinase 1 (ASK1).";
J. Biol. Chem. 278:13325-13332(2003).
[28]
UBIQUITINATION BY MDM2, AND INTERACTION WITH MDM2.
PubMed=12821780; DOI=10.1073/pnas.1431613100;
Girnita L., Girnita A., Larsson O.;
"Mdm2-dependent ubiquitination and degradation of the insulin-like growth
factor 1 receptor.";
Proc. Natl. Acad. Sci. U.S.A. 100:8247-8252(2003).
[29]
ACTIVITY REGULATION.
PubMed=14729630; DOI=10.1158/0008-5472.can-03-2522;
Girnita A., Girnita L., del Prete F., Bartolazzi A., Larsson O.,
Axelson M.;
"Cyclolignans as inhibitors of the insulin-like growth factor-1 receptor
and malignant cell growth.";
Cancer Res. 64:236-242(2004).
[30]
INTERACTION WITH ARRB1 AND ARRB2.
PubMed=15878855; DOI=10.1074/jbc.m501129200;
Girnita L., Shenoy S.K., Sehat B., Vasilcanu R., Girnita A.,
Lefkowitz R.J., Larsson O.;
"{beta}-Arrestin is crucial for ubiquitination and down-regulation of the
insulin-like growth factor-1 receptor by acting as adaptor for the MDM2 E3
ligase.";
J. Biol. Chem. 280:24412-24419(2005).
[31]
INTERACTION WITH STAT3.
PubMed=15998644; DOI=10.1074/jbc.m501316200;
Yadav A., Kalita A., Dhillon S., Banerjee K.;
"JAK/STAT3 pathway is involved in survival of neurons in response to
insulin-like growth factor and negatively regulated by suppressor of
cytokine signaling-3.";
J. Biol. Chem. 280:31830-31840(2005).
[32]
FUNCTION, AND FORMATION OF A HYBRID RECEPTOR WITH INSR.
PubMed=16831875; DOI=10.1074/jbc.m605189200;
Slaaby R., Schaeffer L., Lautrup-Larsen I., Andersen A.S., Shaw A.C.,
Mathiasen I.S., Brandt J.;
"Hybrid receptors formed by insulin receptor (IR) and insulin-like growth
factor I receptor (IGF-IR) have low insulin and high IGF-1 affinity
irrespective of the IR splice variant.";
J. Biol. Chem. 281:25869-25874(2006).
[33]
SUBCELLULAR LOCATION, AND PROTEOLYTIC PROCESSING.
PubMed=17524361; DOI=10.1016/j.bbrc.2007.05.062;
McElroy B., Powell J.C., McCarthy J.V.;
"The insulin-like growth factor 1 (IGF-1) receptor is a substrate for
gamma-secretase-mediated intramembrane proteolysis.";
Biochem. Biophys. Res. Commun. 358:1136-1141(2007).
[34]
REVIEW ON IGF1R IN CANCER.
PubMed=17624760; DOI=10.1016/j.ejca.2007.05.021;
Hartog H., Wesseling J., Boezen H.M., van der Graaf W.T.;
"The insulin-like growth factor 1 receptor in cancer: old focus, new
future.";
Eur. J. Cancer 43:1895-1904(2007).
[35]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the
kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[36]
BINDING TO IGF1, AND IDENTIFICATION IN A COMPLEX WITH INTEGRIN AND IGF1.
PubMed=19578119; DOI=10.1074/jbc.m109.013201;
Saegusa J., Yamaji S., Ieguchi K., Wu C.Y., Lam K.S., Liu F.T.,
Takada Y.K., Takada Y.;
"The direct binding of insulin-like growth factor-1 (IGF-1) to integrin
alphavbeta3 is involved in IGF-1 signaling.";
J. Biol. Chem. 284:24106-24114(2009).
[37]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[38]
SUMOYLATION.
PubMed=20596523; DOI=10.1371/journal.pone.0011332;
Del Rincon S.V., Rogers J., Widschwendter M., Sun D., Sieburg H.B.,
Spruck C.;
"Development and validation of a method for profiling post-translational
modification activities using protein microarrays.";
PLoS ONE 5:E11332-E11332(2010).
[39]
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).
[40]
UBIQUITINATION AT LYS-1168 AND LYS-1171.
PubMed=21994939; DOI=10.1074/jbc.m111.288514;
Mao Y., Shang Y., Pham V.C., Ernst J.A., Lill J.R., Scales S.J., Zha J.;
"Polyubiquitination of insulin-like growth factor I receptor (IGF-IR)
activation loop promotes antibody-induced receptor internalization and
down-regulation.";
J. Biol. Chem. 286:41852-41861(2011).
[41]
BINDING TO IGF1, AND IDENTIFICATION IN A COMPLEX WITH INTEGRIN AND IGF1.
PubMed=22351760; DOI=10.1074/jbc.m111.304170;
Fujita M., Ieguchi K., Davari P., Yamaji S., Taniguchi Y., Sekiguchi K.,
Takada Y.K., Takada Y.;
"Cross-talk between integrin alpha6beta4 and insulin-like growth factor-1
receptor (IGF1R) through direct alpha6beta4 binding to IGF1 and subsequent
alpha6beta4-IGF1-IGF1R ternary complex formation in anchorage-independent
conditions.";
J. Biol. Chem. 287:12491-12500(2012).
[42]
INTERACTION WITH ZFAND2B.
PubMed=26692333; DOI=10.1038/nm.4013;
Osorio F.G., Soria-Valles C., Santiago-Fernandez O., Bernal T.,
Mittelbrunn M., Colado E., Rodriguez F., Bonzon-Kulichenko E., Vazquez J.,
Porta-de-la-Riva M., Ceron J., Fueyo A., Li J., Green A.R., Freije J.M.,
Lopez-Otin C.;
"Loss of the proteostasis factor AIRAPL causes myeloid transformation by
deregulating IGF-1 signaling.";
Nat. Med. 22:91-96(2016).
[43]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 31-492, DISULFIDE BONDS, AND
GLYCOSYLATION AT ASN-51; ASN-135; ASN-244 AND ASN-314.
PubMed=9690478; DOI=10.1038/28668;
Garrett T.P., McKern N.M., Lou M., Frenkel M.J., Bentley J.D.,
Lovrecz G.O., Elleman T.C., Cosgrove L.J., Ward C.W.;
"Crystal structure of the first three domains of the type-1 insulin-like
growth factor receptor.";
Nature 394:395-399(1998).
[44]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 988-1286 IN COMPLEX WITH AMP-PCP
AND PEPTIDE SUBSTRATE, CATALYTIC ACTIVITY, ACTIVE SITE, ACTIVITY
REGULATION, IDENTIFICATION BY MASS SPECTROMETRY, AND PHOSPHORYLATION AT
TYR-1161; TYR-1165 AND TYR-1166.
PubMed=11694888; DOI=10.1038/nsb721;
Favelyukis S., Till J.H., Hubbard S.R., Miller W.T.;
"Structure and autoregulation of the insulin-like growth factor 1 receptor
kinase.";
Nat. Struct. Biol. 8:1058-1063(2001).
[45]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 981-1286 IN COMPLEX WITH ANP,
AUTOPHOSPHORYLATION, ACTIVE SITE, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=11591350; DOI=10.1016/s0969-2126(01)00655-4;
Pautsch A., Zoephel A., Ahorn H., Spevak W., Hauptmann R., Nar H.;
"Crystal structure of bisphosphorylated IGF-1 receptor kinase: insight into
domain movements upon kinase activation.";
Structure 9:955-965(2001).
[46]
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 974-1294.
PubMed=12138114; DOI=10.1074/jbc.m205580200;
Munshi S., Kornienko M., Hall D.L., Reid J.C., Waxman L., Stirdivant S.M.,
Darke P.L., Kuo L.C.;
"Crystal structure of the Apo, unactivated insulin-like growth factor-1
receptor kinase. Implication for inhibitor specificity.";
J. Biol. Chem. 277:38797-38802(2002).
[47]
X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 974-1294.
PubMed=14501110; DOI=10.1107/s0907444903015415;
Munshi S., Hall D.L., Kornienko M., Darke P.L., Kuo L.C.;
"Structure of apo, unactivated insulin-like growth factor-1 receptor kinase
at 1.5 A resolution.";
Acta Crystallogr. D 59:1725-1730(2003).
[48]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 982-1286 IN COMPLEX WITH
BENZIMIDAZOLE PYRIDINONE INHIBITOR, CATALYTIC ACTIVITY, AND ACTIVITY
REGULATION.
PubMed=17317169; DOI=10.1016/j.bmcl.2007.01.102;
Velaparthi U., Wittman M., Liu P., Stoffan K., Zimmermann K., Sang X.,
Carboni J., Li A., Attar R., Gottardis M., Greer A., Chang C.Y.,
Jacobsen B.L., Sack J.S., Sun Y., Langley D.R., Balasubramanian B.,
Vyas D.;
"Discovery and initial SAR of 3-(1H-benzo[d]imidazol-2-yl)pyridin-2(1H)-
ones as inhibitors of insulin-like growth factor 1-receptor (IGF-1R).";
Bioorg. Med. Chem. Lett. 17:2317-2321(2007).
[49]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 981-1286, AND PHOSPHORYLATION AT
TYR-1161; TYR-1165 AND TYR-1166.
PubMed=18501599; DOI=10.1016/j.bmcl.2008.04.044;
Mayer S.C., Banker A.L., Boschelli F., Di L., Johnson M., Kenny C.H.,
Krishnamurthy G., Kutterer K., Moy F., Petusky S., Ravi M., Tkach D.,
Tsou H.R., Xu W.;
"Lead identification to generate isoquinolinedione inhibitors of insulin-
like growth factor receptor (IGF-1R) for potential use in cancer
treatment.";
Bioorg. Med. Chem. Lett. 18:3641-3645(2008).
[50]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 986-1286 IN COMPLEX WITH
INHIBITOR PQIP, SUBUNIT, AUTOPHOSPHORYLATION, CATALYTIC ACTIVITY, ACTIVE
SITE, AND ACTIVITY REGULATION.
PubMed=18566589; DOI=10.1038/emboj.2008.116;
Wu J., Li W., Craddock B.P., Foreman K.W., Mulvihill M.J., Ji Q.S.,
Miller W.T., Hubbard S.R.;
"Small-molecule inhibition and activation-loop trans-phosphorylation of the
IGF1 receptor.";
EMBO J. 27:1985-1994(2008).
[51]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 981-1286 IN COMPLEX WITH
3-CYANOQUINOLINE INHIBITOR, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND
PHOSPHORYLATION AT TYR-1161; TYR-1165 AND TYR-1166.
PubMed=19041240; DOI=10.1016/j.bmcl.2008.11.037;
Miller L.M., Mayer S.C., Berger D.M., Boschelli D.H., Boschelli F., Di L.,
Du X., Dutia M., Floyd M.B., Johnson M., Kenny C.H., Krishnamurthy G.,
Moy F., Petusky S., Tkach D., Torres N., Wu B., Xu W.;
"Lead identification to generate 3-cyanoquinoline inhibitors of insulin-
like growth factor receptor (IGF-1R) for potential use in cancer
treatment.";
Bioorg. Med. Chem. Lett. 19:62-66(2009).
[52]
X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 982-1286 IN COMPLEX WITH
BMS-754807, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
PubMed=19778024; DOI=10.1021/jm900786r;
Wittman M.D., Carboni J.M., Yang Z., Lee F.Y., Antman M., Attar R.,
Balimane P., Chang C., Chen C., Discenza L., Frennesson D., Gottardis M.M.,
Greer A., Hurlburt W., Johnson W., Langley D.R., Li A., Li J., Liu P.,
Mastalerz H., Mathur A., Menard K., Patel K., Sack J., Sang X.,
Saulnier M., Smith D., Stefanski K., Trainor G., Velaparthi U., Zhang G.,
Zimmermann K., Vyas D.M.;
"Discovery of a 2,4-disubstituted pyrrolo[1,2-f][1,2,4]triazine inhibitor
(BMS-754807) of insulin-like growth factor receptor (IGF-1R) kinase in
clinical development.";
J. Med. Chem. 52:7360-7363(2009).
[53]
X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 983-1286 IN COMPLEX WITH
MSC1609119A-1, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
DOI=10.1021/ml100044h;
Heinrich T., Graedler U., Boettcher H., Blaukat A., Shutes A.;
"Allosteric IGF-1R Inhibitors.";
ACS Med. Chem. Lett. 1:199-203(2010).
[54]
X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) OF 982-1286 IN COMPLEXES WITH
INHIBITORS, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
PubMed=20675137; DOI=10.1016/j.bmcl.2010.07.045;
Sampognaro A.J., Wittman M.D., Carboni J.M., Chang C., Greer A.F.,
Hurlburt W.W., Sack J.S., Vyas D.M.;
"Proline isosteres in a series of 2,4-disubstituted pyrrolo[1,2-
f][1,2,4]triazine inhibitors of IGF-1R kinase and IR kinase.";
Bioorg. Med. Chem. Lett. 20:5027-5030(2010).
[55]
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 951-1286 IN COMPLEX WITH
BIS-AZAINDOLE INHIBITOR, AUTOPHOSPHORYLATION, AND ACTIVITY REGULATION.
PubMed=20545947; DOI=10.1111/j.1747-0285.2010.00991.x;
Nemecek C., Metz W.A., Wentzler S., Ding F.X., Venot C., Souaille C.,
Dagallier A., Maignan S., Guilloteau J.P., Bernard F., Henry A.,
Grapinet S., Lesuisse D.;
"Design of potent IGF1-R inhibitors related to bis-azaindoles.";
Chem. Biol. Drug Des. 76:100-106(2010).
[56]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 982-1286 IN COMPLEX WITH
HYDANTOIN DERIVATIVE, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
PubMed=21441024; DOI=10.1016/j.bmcl.2011.03.003;
Lesuisse D., Mauger J., Nemecek C., Maignan S., Boiziau J., Harlow G.,
Hittinger A., Ruf S., Strobel H., Nair A., Ritter K., Malleron J.L.,
Dagallier A., El-Ahmad Y., Guilloteau J.P., Guizani H., Bouchard H.,
Venot C.;
"Discovery of the first non-ATP competitive IGF-1R kinase inhibitors:
advantages in comparison with competitive inhibitors.";
Bioorg. Med. Chem. Lett. 21:2224-2228(2011).
[57]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 988-1286 IN COMPLEX WITH
2,4-BIS-ARYLAMINO-1,3-PYRIMIDINE INHIBITOR, CATALYTIC ACTIVITY, AND
ACTIVITY REGULATION.
PubMed=21414779; DOI=10.1016/j.bmcl.2011.02.075;
Buchanan J.L., Newcomb J.R., Carney D.P., Chaffee S.C., Chai L.,
Cupples R., Epstein L.F., Gallant P., Gu Y., Harmange J.C., Hodge K.,
Houk B.E., Huang X., Jona J., Joseph S., Jun H.T., Kumar R., Li C., Lu J.,
Menges T., Morrison M.J., Novak P.M., van der Plas S., Radinsky R.,
Rose P.E., Sawant S., Sun J.R., Surapaneni S., Turci S.M., Xu K., Yanez E.,
Zhao H., Zhu X.;
"Discovery of 2,4-bis-arylamino-1,3-pyrimidines as insulin-like growth
factor-1 receptor (IGF-1R) inhibitors.";
Bioorg. Med. Chem. Lett. 21:2394-2399(2011).
[58]
VARIANTS IGF1RES GLN-138 AND ASN-145, AND CHARACTERIZATION OF VARIANTS
IGF1RES GLN-138 AND ASN-145.
PubMed=14657428; DOI=10.1056/nejmoa010107;
The intrauterine growth retardation (IUGR) study group;
Abuzzahab M.J., Schneider A., Goddard A., Grigorescu F., Lautier C.,
Keller E., Kiess W., Klammt J., Kratzsch J., Osgood D., Pfaeffle R.,
Raile K., Seidel B., Smith R.J., Chernausek S.D.;
"IGF-I receptor mutations resulting in intrauterine and postnatal growth
retardation.";
N. Engl. J. Med. 349:2211-2222(2003).
[59]
VARIANT IGF1RES GLN-739, AND CHARACTERIZATION OF VARIANT IGF1RES GLN-739.
PubMed=15928254; DOI=10.1210/jc.2004-1947;
Kawashima Y., Kanzaki S., Yang F., Kinoshita T., Hanaki K., Nagaishi J.,
Ohtsuka Y., Hisatome I., Ninomoya H., Nanba E., Fukushima T., Takahashi S.;
"Mutation at cleavage site of insulin-like growth factor receptor in a
short-stature child born with intrauterine growth retardation.";
J. Clin. Endocrinol. Metab. 90:4679-4687(2005).
[60]
VARIANTS [LARGE SCALE ANALYSIS] LEU-105; HIS-437; HIS-595; SER-857;
THR-1338 AND VAL-1347.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
[61]
VARIANTS IGF1RES TYR-359; CYS-865; SER-1256 AND CYS-1337, AND
CHARACTERIZATION OF VARIANTS IGF1RES TYR-359; CYS-865; SER-1256 AND
CYS-1337.
PubMed=25040157; DOI=10.1111/cen.12555;
Juanes M., Guercio G., Marino R., Berensztein E., Warman D.M., Ciaccio M.,
Gil S., Bailez M., Rivarola M.A., Belgorosky A.;
"Three novel IGF1R mutations in microcephalic patients with prenatal and
postnatal growth impairment.";
Clin. Endocrinol. (Oxf.) 82:704-711(2015).
-!- FUNCTION: Receptor tyrosine kinase which mediates actions of insulin-
like growth factor 1 (IGF1). Binds IGF1 with high affinity and IGF2 and
insulin (INS) with a lower affinity. The activated IGF1R is involved in
cell growth and survival control. IGF1R is crucial for tumor
transformation and survival of malignant cell. Ligand binding activates
the receptor kinase, leading to receptor autophosphorylation, and
tyrosines phosphorylation of multiple substrates, that function as
signaling adapter proteins including, the insulin-receptor substrates
(IRS1/2), Shc and 14-3-3 proteins. Phosphorylation of IRSs proteins
lead to the activation of two main signaling pathways: the PI3K-AKT/PKB
pathway and the Ras-MAPK pathway. The result of activating the MAPK
pathway is increased cellular proliferation, whereas activating the
PI3K pathway inhibits apoptosis and stimulates protein synthesis.
Phosphorylated IRS1 can activate the 85 kDa regulatory subunit of PI3K
(PIK3R1), leading to activation of several downstream substrates,
including protein AKT/PKB. AKT phosphorylation, in turn, enhances
protein synthesis through mTOR activation and triggers the
antiapoptotic effects of IGFIR through phosphorylation and inactivation
of BAD. In parallel to PI3K-driven signaling, recruitment of Grb2/SOS
by phosphorylated IRS1 or Shc leads to recruitment of Ras and
activation of the ras-MAPK pathway. In addition to these two main
signaling pathways IGF1R signals also through the Janus kinase/signal
transducer and activator of transcription pathway (JAK/STAT).
Phosphorylation of JAK proteins can lead to phosphorylation/activation
of signal transducers and activators of transcription (STAT) proteins.
In particular activation of STAT3, may be essential for the
transforming activity of IGF1R. The JAK/STAT pathway activates gene
transcription and may be responsible for the transforming activity. JNK
kinases can also be activated by the IGF1R. IGF1 exerts inhibiting
activities on JNK activation via phosphorylation and inhibition of
MAP3K5/ASK1, which is able to directly associate with the IGF1R.
-!- FUNCTION: When present in a hybrid receptor with INSR, binds IGF1.
PubMed:12138094 shows that hybrid receptors composed of IGF1R and INSR
isoform Long are activated with a high affinity by IGF1, with low
affinity by IGF2 and not significantly activated by insulin, and that
hybrid receptors composed of IGF1R and INSR isoform Short are activated
by IGF1, IGF2 and insulin. In contrast, PubMed:16831875 shows that
hybrid receptors composed of IGF1R and INSR isoform Long and hybrid
receptors composed of IGF1R and INSR isoform Short have similar binding
characteristics, both bind IGF1 and have a low affinity for insulin.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
Evidence={ECO:0000255|PROSITE-ProRule:PRU10028,
ECO:0000269|PubMed:11694888, ECO:0000269|PubMed:17317169,
ECO:0000269|PubMed:18566589, ECO:0000269|PubMed:19041240,
ECO:0000269|PubMed:19778024, ECO:0000269|PubMed:20675137,
ECO:0000269|PubMed:21414779, ECO:0000269|PubMed:21441024,
ECO:0000269|PubMed:7679099, ECO:0000269|Ref.53};
-!- ACTIVITY REGULATION: Activated by autophosphorylation at Tyr-1165, Tyr-
1161 and Tyr-1166 on the kinase activation loop; phosphorylation at all
three tyrosine residues is required for optimal kinase activity.
Inhibited by MSC1609119A-1, BMS-754807, PQIP, benzimidazole pyridinone,
isoquinolinedione, bis-azaindole, 3-cyanoquinoline, 2,4-bis-arylamino-
1,3-pyrimidine, pyrrolopyrimidine, pyrrole-5-carboxaldehyde,
picropodophyllin (PPP), tyrphostin derivatives. While most inhibitors
bind to the ATP binding pocket, MSC1609119A-1 functions as allosteric
inhibitor and binds close to the DFG motif and the activation loop.
{ECO:0000269|PubMed:11694888, ECO:0000269|PubMed:14729630,
ECO:0000269|PubMed:17317169, ECO:0000269|PubMed:18566589,
ECO:0000269|PubMed:19041240, ECO:0000269|PubMed:19778024,
ECO:0000269|PubMed:20545947, ECO:0000269|PubMed:20675137,
ECO:0000269|PubMed:21414779, ECO:0000269|PubMed:21441024,
ECO:0000269|Ref.53}.
-!- SUBUNIT: Tetramer of 2 alpha and 2 beta chains linked by disulfide
bonds. The alpha chains contribute to the formation of the ligand-
binding domain, while the beta chain carries the kinase domain.
Interacts with PIK3R1 and with the PTB/PID domains of IRS1 and SHC1 in
vitro when autophosphorylated on tyrosine residues. Forms a hybrid
receptor with INSR, the hybrid is a tetramer consisting of 1 alpha
chain and 1 beta chain of INSR and 1 alpha chain and 1 beta chain of
IGF1R. Interacts with ARRB1 and ARRB2. Interacts with GRB10. Interacts
with RACK1. Interacts with SOCS1, SOCS2 and SOCS3. Interacts with 14-3-
3 proteins. Interacts with NMD2. Interacts with MAP3K5. Interacts with
STAT3. Found in a ternary complex with IGF1 and ITGAV:ITGB3 or
ITGA6:ITGB4 (PubMed:19578119, PubMed:22351760). Interacts (nascent
precursor form) with ZFAND2B (PubMed:26692333).
{ECO:0000269|PubMed:10454568, ECO:0000269|PubMed:11071852,
ECO:0000269|PubMed:11591350, ECO:0000269|PubMed:11694888,
ECO:0000269|PubMed:11884618, ECO:0000269|PubMed:12556535,
ECO:0000269|PubMed:12821780, ECO:0000269|PubMed:15878855,
ECO:0000269|PubMed:15998644, ECO:0000269|PubMed:17317169,
ECO:0000269|PubMed:1846292, ECO:0000269|PubMed:18566589,
ECO:0000269|PubMed:19041240, ECO:0000269|PubMed:19578119,
ECO:0000269|PubMed:19778024, ECO:0000269|PubMed:20545947,
ECO:0000269|PubMed:21414779, ECO:0000269|PubMed:21441024,
ECO:0000269|PubMed:22351760, ECO:0000269|PubMed:26692333,
ECO:0000269|PubMed:7541045, ECO:0000269|PubMed:9581554,
ECO:0000269|PubMed:9727029, ECO:0000269|PubMed:9822622,
ECO:0000269|Ref.53}.
-!- INTERACTION:
P08069; Q9NZN5: ARHGEF12; NbExp=7; IntAct=EBI-475981, EBI-821440;
P08069; PRO_0000004724 [P49913]: CAMP; NbExp=3; IntAct=EBI-475981, EBI-6378485;
P08069; P41240: CSK; NbExp=5; IntAct=EBI-475981, EBI-1380630;
P08069; P35222: CTNNB1; NbExp=3; IntAct=EBI-475981, EBI-491549;
P08069; P05019: IGF1; NbExp=8; IntAct=EBI-475981, EBI-7902275;
P08069; P08069: IGF1R; NbExp=6; IntAct=EBI-475981, EBI-475981;
P08069; Q9Y2W7: KCNIP3; NbExp=6; IntAct=EBI-475981, EBI-751501;
P08069; Q9UJU2: LEF1; NbExp=5; IntAct=EBI-475981, EBI-926131;
P08069; Q00987: MDM2; NbExp=2; IntAct=EBI-475981, EBI-389668;
P08069; P27986: PIK3R1; NbExp=4; IntAct=EBI-475981, EBI-79464;
P08069; Q92569: PIK3R3; NbExp=2; IntAct=EBI-475981, EBI-79893;
P08069; P35813: PPM1A; NbExp=2; IntAct=EBI-475981, EBI-989143;
P08069; P18031: PTPN1; NbExp=3; IntAct=EBI-475981, EBI-968788;
P08069; Q06124: PTPN11; NbExp=4; IntAct=EBI-475981, EBI-297779;
P08069; P29350: PTPN6; NbExp=3; IntAct=EBI-475981, EBI-78260;
P08069; P29353-2: SHC1; NbExp=2; IntAct=EBI-475981, EBI-1000553;
P08069; Q01995: TAGLN; NbExp=2; IntAct=EBI-475981, EBI-1054248;
P08069; Q64010: Crk; Xeno; NbExp=3; IntAct=EBI-475981, EBI-2906540;
P08069; P01317: INS; Xeno; NbExp=4; IntAct=EBI-475981, EBI-3989070;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17524361};
Single-pass type I membrane protein {ECO:0000269|PubMed:17524361}.
-!- TISSUE SPECIFICITY: Found as a hybrid receptor with INSR in muscle,
heart, kidney, adipose tissue, skeletal muscle, hepatoma, fibroblasts,
spleen and placenta (at protein level). Expressed in a variety of
tissues. Overexpressed in tumors, including melanomas, cancers of the
colon, pancreas prostate and kidney. {ECO:0000269|PubMed:12019176,
ECO:0000269|PubMed:8247543, ECO:0000269|PubMed:9202395,
ECO:0000269|PubMed:9355755}.
-!- PTM: Autophosphorylated on tyrosine residues in response to ligand
binding. Autophosphorylation occurs in trans, i.e. one subunit of the
dimeric receptor phosphorylates tyrosine residues on the other subunit.
Autophosphorylation occurs in a sequential manner; Tyr-1165 is
predominantly phosphorylated first, followed by phosphorylation of Tyr-
1161 and Tyr-1166. While every single phosphorylation increases kinase
activity, all three tyrosine residues in the kinase activation loop
(Tyr-1165, Tyr-1161 and Tyr-1166) have to be phosphorylated for optimal
activity. Can be autophosphorylated at additional tyrosine residues (in
vitro). Autophosphorylated is followed by phosphorylation of
juxtamembrane tyrosines and C-terminal serines. Phosphorylation of Tyr-
980 is required for IRS1- and SHC1-binding. Phosphorylation of Ser-1278
by GSK-3beta restrains kinase activity and promotes cell surface
expression, it requires a priming phosphorylation at Ser-1282.
Dephosphorylated by PTPN1 (By similarity). {ECO:0000250}.
-!- PTM: Polyubiquitinated at Lys-1168 and Lys-1171 through both 'Lys-48'
and 'Lys-29' linkages, promoting receptor endocytosis and subsequent
degradation by the proteasome. Ubiquitination is facilitated by pre-
existing phosphorylation. {ECO:0000269|PubMed:11694888,
ECO:0000269|PubMed:12821780, ECO:0000269|PubMed:18501599,
ECO:0000269|PubMed:19041240, ECO:0000269|PubMed:21994939,
ECO:0000269|PubMed:7541045}.
-!- PTM: Sumoylated with SUMO1. {ECO:0000269|PubMed:20596523}.
-!- PTM: Controlled by regulated intramembrane proteolysis (RIP). Undergoes
metalloprotease-dependent constitutive ectodomain shedding to produce a
membrane-anchored 52 kDa C-Terminal fragment which is further processed
by presenilin gamma-secretase to yield an intracellular 50 kDa
fragment. {ECO:0000269|PubMed:17524361}.
-!- DISEASE: Insulin-like growth factor 1 resistance (IGF1RES)
[MIM:270450]: A disorder characterized by intrauterine growth
retardation, poor postnatal growth and increased plasma IGF1 levels.
{ECO:0000269|PubMed:14657428, ECO:0000269|PubMed:15928254,
ECO:0000269|PubMed:25040157}. Note=The disease is caused by mutations
affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-!- SEQUENCE CAUTION:
Sequence=BAG11657.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
Haematology;
URL="http://atlasgeneticsoncology.org/Genes/IGF1RID40928ch15q26.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/igf1r/";
-!- WEB RESOURCE: Name=Wikipedia; Note=IGF-1 receptor entry;
URL="https://en.wikipedia.org/wiki/IGF-1_receptor";
---------------------------------------------------------------------------
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EMBL; X04434; CAA28030.1; -; mRNA.
EMBL; AB425196; BAG11657.1; ALT_INIT; mRNA.
EMBL; AY332722; AAP81165.1; -; Genomic_DNA.
EMBL; AC055807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC069029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC118658; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC118660; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC113610; AAI13611.1; -; mRNA.
EMBL; BC113612; AAI13613.1; -; mRNA.
EMBL; M69229; AAB59399.1; -; Genomic_DNA.
CCDS; CCDS10378.1; -.
PIR; A25690; IGHUR1.
RefSeq; NP_000866.1; NM_000875.4.
RefSeq; NP_001278787.1; NM_001291858.1.
PDB; 1IGR; X-ray; 2.60 A; A=31-492.
PDB; 1JQH; X-ray; 2.10 A; A/B/C=979-1286.
PDB; 1K3A; X-ray; 2.10 A; A=988-1286.
PDB; 1M7N; X-ray; 2.70 A; A/B=974-1294.
PDB; 1P4O; X-ray; 1.50 A; A/B=974-1294.
PDB; 2OJ9; X-ray; 2.00 A; A=982-1286.
PDB; 2ZM3; X-ray; 2.50 A; A/B/C/D=981-1286.
PDB; 3D94; X-ray; 2.30 A; A=986-1286.
PDB; 3F5P; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/R/S/T=981-1286.
PDB; 3I81; X-ray; 2.08 A; A=982-1286.
PDB; 3LVP; X-ray; 3.00 A; A/B/C/D=951-1286.
PDB; 3LW0; X-ray; 1.79 A; A/B/C/D=983-1286.
PDB; 3NW5; X-ray; 2.14 A; A=982-1286.
PDB; 3NW6; X-ray; 2.20 A; A=982-1286.
PDB; 3NW7; X-ray; 2.11 A; A=982-1286.
PDB; 3O23; X-ray; 2.10 A; A=982-1286.
PDB; 3QQU; X-ray; 2.90 A; A/B/C/D=988-1286.
PDB; 4D2R; X-ray; 2.10 A; A=985-1286.
PDB; 4XSS; X-ray; 3.00 A; F=721-736.
PDB; 5FXQ; X-ray; 2.30 A; A=980-1286.
PDB; 5FXR; X-ray; 2.40 A; A=980-1286.
PDB; 5FXS; X-ray; 1.90 A; A=980-1286.
PDB; 5HZN; X-ray; 2.20 A; A/B/C/D/E/F/G/H=983-1286.
PDB; 5U8Q; X-ray; 3.27 A; A=31-935.
PDB; 5U8R; X-ray; 3.00 A; A=31-935.
PDB; 6JK8; EM; 4.70 A; A/B=1-1367.
PDBsum; 1IGR; -.
PDBsum; 1JQH; -.
PDBsum; 1K3A; -.
PDBsum; 1M7N; -.
PDBsum; 1P4O; -.
PDBsum; 2OJ9; -.
PDBsum; 2ZM3; -.
PDBsum; 3D94; -.
PDBsum; 3F5P; -.
PDBsum; 3I81; -.
PDBsum; 3LVP; -.
PDBsum; 3LW0; -.
PDBsum; 3NW5; -.
PDBsum; 3NW6; -.
PDBsum; 3NW7; -.
PDBsum; 3O23; -.
PDBsum; 3QQU; -.
PDBsum; 4D2R; -.
PDBsum; 4XSS; -.
PDBsum; 5FXQ; -.
PDBsum; 5FXR; -.
PDBsum; 5FXS; -.
PDBsum; 5HZN; -.
PDBsum; 5U8Q; -.
PDBsum; 5U8R; -.
PDBsum; 6JK8; -.
SMR; P08069; -.
BioGRID; 109701; 194.
CORUM; P08069; -.
DIP; DIP-476N; -.
IntAct; P08069; 134.
MINT; P08069; -.
STRING; 9606.ENSP00000268035; -.
BindingDB; P08069; -.
ChEMBL; CHEMBL1957; -.
DrugBank; DB07156; (4Z)-6-bromo-4-({[4-(pyrrolidin-1-ylmethyl)phenyl]amino}methylidene)isoquinoline-1,3(2H,4H)-dione.
DrugBank; DB07474; 3-[5-(1H-IMIDAZOL-1-YL)-7-METHYL-1H-BENZIMIDAZOL-2-YL]-4-[(PYRIDIN-2-YLMETHYL)AMINO]PYRIDIN-2(1H)-ONE.
DrugBank; DB05023; ATL1101.
DrugBank; DB12267; Brigatinib.
DrugBank; DB12250; Cixutumumab.
DrugBank; DB01306; Insulin aspart.
DrugBank; DB09564; Insulin degludec.
DrugBank; DB01307; Insulin detemir.
DrugBank; DB00047; Insulin glargine.
DrugBank; DB01309; Insulin glulisine.
DrugBank; DB00030; Insulin human.
DrugBank; DB00046; Insulin lispro.
DrugBank; DB00071; Insulin pork.
DrugBank; DB06075; Linsitinib.
DrugBank; DB01277; Mecasermin.
DrugBank; DB14751; Mecasermin rinfabate.
DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
DrugBank; DB05897; rhIGFBP-3.
DrugBank; DB09098; Somatrem.
DrugBank; DB06343; Teprotumumab.
DrugBank; DB05184; XL228.
DrugCentral; P08069; -.
GuidetoPHARMACOLOGY; 1801; -.
iPTMnet; P08069; -.
PhosphoSitePlus; P08069; -.
BioMuta; IGF1R; -.
DMDM; 124240; -.
EPD; P08069; -.
jPOST; P08069; -.
MassIVE; P08069; -.
MaxQB; P08069; -.
PaxDb; P08069; -.
PeptideAtlas; P08069; -.
PRIDE; P08069; -.
ProteomicsDB; 52065; -.
ABCD; P08069; 13 sequenced antibodies.
Antibodypedia; 4140; 2278 antibodies.
DNASU; 3480; -.
Ensembl; ENST00000650285; ENSP00000497069; ENSG00000140443.
GeneID; 3480; -.
KEGG; hsa:3480; -.
UCSC; uc002bul.4; human.
CTD; 3480; -.
DisGeNET; 3480; -.
EuPathDB; HostDB:ENSG00000140443.13; -.
GeneCards; IGF1R; -.
HGNC; HGNC:5465; IGF1R.
HPA; ENSG00000140443; Low tissue specificity.
MalaCards; IGF1R; -.
MIM; 147370; gene.
MIM; 270450; phenotype.
neXtProt; NX_P08069; -.
OpenTargets; ENSG00000140443; -.
Orphanet; 73273; Growth delay due to insulin-like growth factor I resistance.
PharmGKB; PA29698; -.
eggNOG; KOG4258; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00940000156682; -.
InParanoid; P08069; -.
KO; K05087; -.
OMA; PAKTTYE; -.
OrthoDB; 223327at2759; -.
PhylomeDB; P08069; -.
TreeFam; TF351636; -.
BRENDA; 2.7.10.1; 2681.
Reactome; R-HSA-2404192; Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R).
Reactome; R-HSA-2428928; IRS-related events triggered by IGF1R.
Reactome; R-HSA-2428933; SHC-related events triggered by IGF1R.
Reactome; R-HSA-9009391; Extra-nuclear estrogen signaling.
SignaLink; P08069; -.
SIGNOR; P08069; -.
BioGRID-ORCS; 3480; 161 hits in 817 CRISPR screens.
ChiTaRS; IGF1R; human.
EvolutionaryTrace; P08069; -.
GeneWiki; Insulin-like_growth_factor_1_receptor; -.
GenomeRNAi; 3480; -.
Pharos; P08069; Tclin.
PRO; PR:P08069; -.
Proteomes; UP000005640; Chromosome 15.
RNAct; P08069; protein.
Bgee; ENSG00000140443; Expressed in caput epididymis and 232 other tissues.
ExpressionAtlas; P08069; baseline and differential.
Genevisible; P08069; HS.
GO; GO:0035867; C:alphav-beta3 integrin-IGF-1-IGF1R complex; IDA:UniProtKB.
GO; GO:0030424; C:axon; IBA:GO_Central.
GO; GO:0005623; C:cell; IEA:GOC.
GO; GO:0005899; C:insulin receptor complex; IBA:GO_Central.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:BHF-UCL.
GO; GO:0016020; C:membrane; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; ISS:AgBase.
GO; GO:1902911; C:protein kinase complex; IDA:UniProtKB.
GO; GO:0043235; C:receptor complex; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0043559; F:insulin binding; IPI:BHF-UCL.
GO; GO:0005158; F:insulin receptor binding; IDA:BHF-UCL.
GO; GO:0043560; F:insulin receptor substrate binding; IPI:UniProtKB.
GO; GO:0005009; F:insulin-activated receptor activity; IBA:GO_Central.
GO; GO:0005520; F:insulin-like growth factor binding; IDA:UniProtKB.
GO; GO:0031994; F:insulin-like growth factor I binding; IDA:UniProtKB.
GO; GO:0005010; F:insulin-like growth factor-activated receptor activity; IDA:UniProtKB.
GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IPI:UniProtKB.
GO; GO:0140318; F:protein transporter activity; IMP:ARUK-UCL.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0005198; F:structural molecule activity; IDA:UniProtKB.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
GO; GO:0097242; P:amyloid-beta clearance; IMP:ARUK-UCL.
GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
GO; GO:1904646; P:cellular response to amyloid-beta; IGI:ARUK-UCL.
GO; GO:0071333; P:cellular response to glucose stimulus; IBA:GO_Central.
GO; GO:0097062; P:dendritic spine maintenance; ISS:ARUK-UCL.
GO; GO:0042593; P:glucose homeostasis; IBA:GO_Central.
GO; GO:0006955; P:immune response; IMP:BHF-UCL.
GO; GO:0051389; P:inactivation of MAPKK activity; IDA:UniProtKB.
GO; GO:0008286; P:insulin receptor signaling pathway; ISS:ARUK-UCL.
GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; IDA:UniProtKB.
GO; GO:0007275; P:multicellular organism development; IBA:GO_Central.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IMP:MGI.
GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IC:BHF-UCL.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IDA:BHF-UCL.
GO; GO:0030335; P:positive regulation of cell migration; IMP:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:BHF-UCL.
GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
GO; GO:0043410; P:positive regulation of MAPK cascade; IBA:GO_Central.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IBA:GO_Central.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IBA:GO_Central.
GO; GO:0043243; P:positive regulation of protein-containing complex disassembly; ISS:ARUK-UCL.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0046328; P:regulation of JNK cascade; IDA:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0045056; P:transcytosis; IMP:ARUK-UCL.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
CDD; cd00063; FN3; 3.
CDD; cd00064; FU; 1.
Gene3D; 2.60.40.10; -; 2.
Gene3D; 3.80.20.20; -; 2.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR006211; Furin-like_Cys-rich_dom.
InterPro; IPR006212; Furin_repeat.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR000494; Rcpt_L-dom.
InterPro; IPR036941; Rcpt_L-dom_sf.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR016246; Tyr_kinase_insulin-like_rcpt.
InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
Pfam; PF00757; Furin-like; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF01030; Recep_L_domain; 2.
PIRSF; PIRSF000620; Insulin_receptor; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00060; FN3; 3.
SMART; SM00261; FU; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF49265; SSF49265; 3.
SUPFAM; SSF56112; SSF56112; 1.
SUPFAM; SSF57184; SSF57184; 1.
PROSITE; PS50853; FN3; 4.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Cell membrane;
Cleavage on pair of basic residues; Direct protein sequencing;
Disease mutation; Disulfide bond; Glycoprotein; Isopeptide bond; Kinase;
Membrane; Nucleotide-binding; Phosphoprotein; Polymorphism; Receptor;
Reference proteome; Repeat; Signal; Transferase; Transmembrane;
Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation.
SIGNAL 1..30
/evidence="ECO:0000269|PubMed:2877871,
ECO:0000269|PubMed:8257688"
CHAIN 31..736
/note="Insulin-like growth factor 1 receptor alpha chain"
/id="PRO_0000016681"
CHAIN 741..1367
/note="Insulin-like growth factor 1 receptor beta chain"
/id="PRO_0000016682"
TOPO_DOM 741..935
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 936..959
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 960..1367
/note="Cytoplasmic"
/evidence="ECO:0000255"
DOMAIN 491..609
/note="Fibronectin type-III 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 610..708
/note="Fibronectin type-III 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 735..828
/note="Fibronectin type-III 3"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 834..927
/note="Fibronectin type-III 4"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 999..1274
/note="Protein kinase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 1005..1013
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
MOTIF 977..980
/note="IRS1- and SHC1-binding"
ACT_SITE 1135
/note="Proton acceptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10028"
BINDING 1033
/note="ATP"
MOD_RES 980
/note="Phosphotyrosine"
/evidence="ECO:0000305|PubMed:7541045"
MOD_RES 1161
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000269|PubMed:11694888,
ECO:0000269|PubMed:18501599, ECO:0000269|PubMed:19041240"
MOD_RES 1165
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000269|PubMed:11694888,
ECO:0000269|PubMed:18501599, ECO:0000269|PubMed:19041240"
MOD_RES 1166
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000269|PubMed:11694888,
ECO:0000269|PubMed:18501599, ECO:0000269|PubMed:19041240"
MOD_RES 1278
/note="Phosphoserine; by GSK3-beta"
/evidence="ECO:0000250|UniProtKB:Q60751"
MOD_RES 1282
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q60751"
CARBOHYD 51
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:9690478"
CARBOHYD 102
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 135
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:9690478"
CARBOHYD 244
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:9690478"
CARBOHYD 314
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:9690478"
CARBOHYD 417
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 438
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 534
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 607
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 622
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 640
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 747
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 756
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 764
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 900
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 913
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 33..52
/evidence="ECO:0000269|PubMed:9690478"
DISULFID 150..178
/evidence="ECO:0000269|PubMed:9690478"
DISULFID 182..205
/evidence="ECO:0000269|PubMed:9690478"
DISULFID 192..211
/evidence="ECO:0000269|PubMed:9690478"
DISULFID 215..224
/evidence="ECO:0000269|PubMed:9690478"
DISULFID 219..230
/evidence="ECO:0000269|PubMed:9690478"
DISULFID 231..239
/evidence="ECO:0000269|PubMed:9690478"
DISULFID 235..248
/evidence="ECO:0000269|PubMed:9690478"
DISULFID 251..260
/evidence="ECO:0000269|PubMed:9690478"
DISULFID 264..276
/evidence="ECO:0000269|PubMed:9690478"
DISULFID 282..303
/evidence="ECO:0000269|PubMed:9690478"
DISULFID 307..321
/evidence="ECO:0000269|PubMed:9690478"
DISULFID 324..328
/evidence="ECO:0000269|PubMed:9690478"
DISULFID 332..353
/evidence="ECO:0000269|PubMed:9690478"
DISULFID 455..488
/evidence="ECO:0000269|PubMed:9690478"
CROSSLNK 1168
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000269|PubMed:21994939"
CROSSLNK 1171
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000269|PubMed:21994939"
VARIANT 105
/note="V -> L (in a renal chromophobe sample; somatic
mutation)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_041424"
VARIANT 138
/note="R -> Q (in IGF1RES; has decreased IGF1R function;
dbSNP:rs121912426)"
/evidence="ECO:0000269|PubMed:14657428"
/id="VAR_034891"
VARIANT 145
/note="K -> N (in IGF1RES; has decreased IGF1R function;
dbSNP:rs121912427)"
/evidence="ECO:0000269|PubMed:14657428"
/id="VAR_034892"
VARIANT 359
/note="N -> Y (in IGF1RES; significant decrease in IGF1-
induced DNA synthesis and AKT1 phosphorylation in patient
fibroblasts)"
/evidence="ECO:0000269|PubMed:25040157"
/id="VAR_076247"
VARIANT 388
/note="V -> M (in dbSNP:rs45445894)"
/evidence="ECO:0000269|Ref.4"
/id="VAR_018855"
VARIANT 437
/note="R -> H (in dbSNP:rs34516635)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_034893"
VARIANT 511
/note="R -> Q (in dbSNP:rs33958176)"
/id="VAR_034894"
VARIANT 595
/note="R -> H (in dbSNP:rs56248469)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_041425"
VARIANT 605
/note="R -> H (in dbSNP:rs45553041)"
/evidence="ECO:0000269|Ref.4"
/id="VAR_018856"
VARIANT 739
/note="R -> Q (in IGF1RES; leads to failure of processing
of the IGF1R proreceptor to mature IGF1R;
dbSNP:rs121912429)"
/evidence="ECO:0000269|PubMed:15928254"
/id="VAR_034895"
VARIANT 808
/note="H -> R (in dbSNP:rs34061581)"
/id="VAR_034896"
VARIANT 828
/note="A -> T (in dbSNP:rs35224135)"
/id="VAR_034897"
VARIANT 857
/note="N -> S (in dbSNP:rs45611935)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_041426"
VARIANT 865
/note="Y -> C (in IGF1RES; significant decrease in IGF1-
induced DNA synthesis and AKT1 phosphorylation in patient
fibroblasts)"
/evidence="ECO:0000269|PubMed:25040157"
/id="VAR_076248"
VARIANT 1256
/note="R -> S (in IGF1RES; significant decrease in IGF1-
induced DNA synthesis and AKT1 phosphorylation in patient
fibroblasts)"
/evidence="ECO:0000269|PubMed:25040157"
/id="VAR_076249"
VARIANT 1337
/note="R -> C (in IGF1RES; a benign mutation or a rare
polymorphism, significant decrease in IGF1-induced DNA
synthesis; significant increase in IGF1-induced AKT1
phosphorylation in patient fibroblasts; dbSNP:rs141802822)"
/evidence="ECO:0000269|PubMed:25040157"
/id="VAR_076250"
VARIANT 1338
/note="A -> T (in dbSNP:rs34102392)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_041427"
VARIANT 1347
/note="A -> V (in a lung squamous cell carcinoma sample;
somatic mutation)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_041428"
MUTAGEN 980
/note="Y->F: Reduces tyrosine phosphorylation. Abolishes
interaction with IRS1 and SHC1. Does not abolish
interaction with PIK3R1, nor with GRB10."
/evidence="ECO:0000269|PubMed:10454568,
ECO:0000269|PubMed:7541045"
MUTAGEN 1033
/note="K->A: Kinase inactive. Abolishes tyrosine
phosphorylation and abolishes interaction with IRS1, SHC1
and PIK3R1."
/evidence="ECO:0000269|PubMed:7541045"
MUTAGEN 1280
/note="Y->F: No effect on GRB10-binding."
/evidence="ECO:0000269|PubMed:10454568"
MUTAGEN 1281
/note="Y->F: No effect on GRB10-binding."
/evidence="ECO:0000269|PubMed:10454568"
MUTAGEN 1346
/note="Y->F: Loss of GRB10-binding."
/evidence="ECO:0000269|PubMed:10454568"
CONFLICT 928..929
/note="TG -> R (in Ref. 3; BAG11657)"
/evidence="ECO:0000305"
STRAND 37..41
/evidence="ECO:0000244|PDB:1IGR"
HELIX 43..49
/evidence="ECO:0000244|PDB:1IGR"
STRAND 53..57
/evidence="ECO:0000244|PDB:1IGR"
STRAND 59..65
/evidence="ECO:0000244|PDB:1IGR"
STRAND 68..70
/evidence="ECO:0000244|PDB:1IGR"
STRAND 80..83
/evidence="ECO:0000244|PDB:1IGR"
STRAND 85..92
/evidence="ECO:0000244|PDB:1IGR"
HELIX 96..98
/evidence="ECO:0000244|PDB:1IGR"
STRAND 115..121
/evidence="ECO:0000244|PDB:1IGR"
STRAND 138..144
/evidence="ECO:0000244|PDB:1IGR"
HELIX 157..160
/evidence="ECO:0000244|PDB:1IGR"
HELIX 164..166
/evidence="ECO:0000244|PDB:1IGR"
STRAND 168..171
/evidence="ECO:0000244|PDB:1IGR"
HELIX 175..178
/evidence="ECO:0000244|PDB:1IGR"
TURN 183..188
/evidence="ECO:0000244|PDB:1IGR"
STRAND 194..199
/evidence="ECO:0000244|PDB:1IGR"
STRAND 201..203
/evidence="ECO:0000244|PDB:1IGR"
STRAND 205..209
/evidence="ECO:0000244|PDB:1IGR"
HELIX 217..219
/evidence="ECO:0000244|PDB:1IGR"
STRAND 222..224
/evidence="ECO:0000244|PDB:5U8R"
STRAND 226..228
/evidence="ECO:0000244|PDB:5U8Q"
STRAND 235..241
/evidence="ECO:0000244|PDB:1IGR"
STRAND 247..255
/evidence="ECO:0000244|PDB:1IGR"
STRAND 257..263
/evidence="ECO:0000244|PDB:1IGR"
STRAND 269..271
/evidence="ECO:0000244|PDB:1IGR"
TURN 272..274
/evidence="ECO:0000244|PDB:1IGR"
STRAND 275..277
/evidence="ECO:0000244|PDB:1IGR"
HELIX 279..283
/evidence="ECO:0000244|PDB:1IGR"
STRAND 297..299
/evidence="ECO:0000244|PDB:1IGR"
STRAND 302..306
/evidence="ECO:0000244|PDB:1IGR"
STRAND 311..315
/evidence="ECO:0000244|PDB:1IGR"
STRAND 321..323
/evidence="ECO:0000244|PDB:1IGR"
STRAND 325..327
/evidence="ECO:0000244|PDB:1IGR"
STRAND 331..341
/evidence="ECO:0000244|PDB:1IGR"
HELIX 345..347
/evidence="ECO:0000244|PDB:1IGR"
TURN 349..352
/evidence="ECO:0000244|PDB:1IGR"
STRAND 354..362
/evidence="ECO:0000244|PDB:1IGR"
HELIX 375..378
/evidence="ECO:0000244|PDB:1IGR"
STRAND 383..386
/evidence="ECO:0000244|PDB:1IGR"
STRAND 388..392
/evidence="ECO:0000244|PDB:1IGR"
TURN 415..417
/evidence="ECO:0000244|PDB:1IGR"
STRAND 418..423
/evidence="ECO:0000244|PDB:1IGR"
TURN 434..436
/evidence="ECO:0000244|PDB:1IGR"
STRAND 440..443
/evidence="ECO:0000244|PDB:1IGR"
STRAND 445..451
/evidence="ECO:0000244|PDB:1IGR"
STRAND 452..454
/evidence="ECO:0000244|PDB:5U8Q"
HELIX 456..466
/evidence="ECO:0000244|PDB:1IGR"
TURN 469..471
/evidence="ECO:0000244|PDB:5U8R"
STRAND 474..477
/evidence="ECO:0000244|PDB:1IGR"
TURN 479..481
/evidence="ECO:0000244|PDB:1IGR"
STRAND 482..485
/evidence="ECO:0000244|PDB:5U8R"
STRAND 491..493
/evidence="ECO:0000244|PDB:5U8R"
STRAND 495..500
/evidence="ECO:0000244|PDB:5U8R"
STRAND 505..509
/evidence="ECO:0000244|PDB:5U8R"
STRAND 515..518
/evidence="ECO:0000244|PDB:5U8Q"
STRAND 520..529
/evidence="ECO:0000244|PDB:5U8R"
STRAND 531..533
/evidence="ECO:0000244|PDB:5U8R"
TURN 542..544
/evidence="ECO:0000244|PDB:5U8Q"
STRAND 550..552
/evidence="ECO:0000244|PDB:5U8R"
STRAND 565..568
/evidence="ECO:0000244|PDB:5U8R"
STRAND 576..586
/evidence="ECO:0000244|PDB:5U8R"
STRAND 591..593
/evidence="ECO:0000244|PDB:5U8R"
STRAND 597..599
/evidence="ECO:0000244|PDB:5U8R"
STRAND 602..605
/evidence="ECO:0000244|PDB:5U8R"
STRAND 615..620
/evidence="ECO:0000244|PDB:5U8R"
STRAND 626..632
/evidence="ECO:0000244|PDB:5U8R"
STRAND 644..650
/evidence="ECO:0000244|PDB:5U8R"
STRAND 655..660
/evidence="ECO:0000244|PDB:5U8R"
TURN 662..664
/evidence="ECO:0000244|PDB:5U8R"
HELIX 724..730
/evidence="ECO:0000244|PDB:4XSS"
STRAND 777..782
/evidence="ECO:0000244|PDB:5U8R"
STRAND 786..792
/evidence="ECO:0000244|PDB:5U8R"
STRAND 798..805
/evidence="ECO:0000244|PDB:5U8R"
HELIX 810..813
/evidence="ECO:0000244|PDB:5U8R"
STRAND 821..824
/evidence="ECO:0000244|PDB:5U8R"
STRAND 839..843
/evidence="ECO:0000244|PDB:5U8R"
TURN 844..846
/evidence="ECO:0000244|PDB:5U8R"
STRAND 847..851
/evidence="ECO:0000244|PDB:5U8R"
STRAND 862..873
/evidence="ECO:0000244|PDB:5U8R"
STRAND 876..881
/evidence="ECO:0000244|PDB:5U8R"
HELIX 882..888
/evidence="ECO:0000244|PDB:5U8R"
STRAND 889..893
/evidence="ECO:0000244|PDB:5U8R"
STRAND 898..911
/evidence="ECO:0000244|PDB:5U8R"
STRAND 920..924
/evidence="ECO:0000244|PDB:5U8R"
STRAND 980..982
/evidence="ECO:0000244|PDB:1P4O"
HELIX 983..985
/evidence="ECO:0000244|PDB:2ZM3"
TURN 990..992
/evidence="ECO:0000244|PDB:2OJ9"
HELIX 996..998
/evidence="ECO:0000244|PDB:1P4O"
STRAND 999..1007
/evidence="ECO:0000244|PDB:1P4O"
STRAND 1009..1022
/evidence="ECO:0000244|PDB:1P4O"
STRAND 1025..1034
/evidence="ECO:0000244|PDB:1P4O"
STRAND 1037..1039
/evidence="ECO:0000244|PDB:3F5P"
HELIX 1041..1053
/evidence="ECO:0000244|PDB:1P4O"
HELIX 1054..1056
/evidence="ECO:0000244|PDB:1P4O"
STRAND 1065..1069
/evidence="ECO:0000244|PDB:1P4O"
STRAND 1071..1074
/evidence="ECO:0000244|PDB:1P4O"
STRAND 1076..1080
/evidence="ECO:0000244|PDB:1P4O"
HELIX 1087..1100
/evidence="ECO:0000244|PDB:1P4O"
HELIX 1109..1128
/evidence="ECO:0000244|PDB:1P4O"
HELIX 1138..1140
/evidence="ECO:0000244|PDB:1P4O"
STRAND 1141..1143
/evidence="ECO:0000244|PDB:1P4O"
STRAND 1149..1151
/evidence="ECO:0000244|PDB:1P4O"
HELIX 1155..1157
/evidence="ECO:0000244|PDB:3D94"
HELIX 1159..1164
/evidence="ECO:0000244|PDB:1P4O"
TURN 1165..1167
/evidence="ECO:0000244|PDB:3LVP"
HELIX 1168..1170
/evidence="ECO:0000244|PDB:1P4O"
STRAND 1171..1174
/evidence="ECO:0000244|PDB:1P4O"
HELIX 1176..1178
/evidence="ECO:0000244|PDB:1P4O"
HELIX 1181..1186
/evidence="ECO:0000244|PDB:1P4O"
HELIX 1191..1207
/evidence="ECO:0000244|PDB:1P4O"
TURN 1212..1215
/evidence="ECO:0000244|PDB:1P4O"
HELIX 1218..1226
/evidence="ECO:0000244|PDB:1P4O"
HELIX 1239..1248
/evidence="ECO:0000244|PDB:1P4O"
HELIX 1253..1255
/evidence="ECO:0000244|PDB:1P4O"
HELIX 1259..1266
/evidence="ECO:0000244|PDB:1P4O"
HELIX 1267..1269
/evidence="ECO:0000244|PDB:1P4O"
HELIX 1274..1277
/evidence="ECO:0000244|PDB:1P4O"
TURN 1279..1281
/evidence="ECO:0000244|PDB:3O23"
TURN 1283..1285
/evidence="ECO:0000244|PDB:3LVP"
STRAND 1286..1288
/evidence="ECO:0000244|PDB:1P4O"
SEQUENCE 1367 AA; 154793 MW; AE8A735F87F745C8 CRC64;
MKSGSGGGSP TSLWGLLFLS AALSLWPTSG EICGPGIDIR NDYQQLKRLE NCTVIEGYLH
ILLISKAEDY RSYRFPKLTV ITEYLLLFRV AGLESLGDLF PNLTVIRGWK LFYNYALVIF
EMTNLKDIGL YNLRNITRGA IRIEKNADLC YLSTVDWSLI LDAVSNNYIV GNKPPKECGD
LCPGTMEEKP MCEKTTINNE YNYRCWTTNR CQKMCPSTCG KRACTENNEC CHPECLGSCS
APDNDTACVA CRHYYYAGVC VPACPPNTYR FEGWRCVDRD FCANILSAES SDSEGFVIHD
GECMQECPSG FIRNGSQSMY CIPCEGPCPK VCEEEKKTKT IDSVTSAQML QGCTIFKGNL
LINIRRGNNI ASELENFMGL IEVVTGYVKI RHSHALVSLS FLKNLRLILG EEQLEGNYSF
YVLDNQNLQQ LWDWDHRNLT IKAGKMYFAF NPKLCVSEIY RMEEVTGTKG RQSKGDINTR
NNGERASCES DVLHFTSTTT SKNRIIITWH RYRPPDYRDL ISFTVYYKEA PFKNVTEYDG
QDACGSNSWN MVDVDLPPNK DVEPGILLHG LKPWTQYAVY VKAVTLTMVE NDHIRGAKSE
ILYIRTNASV PSIPLDVLSA SNSSSQLIVK WNPPSLPNGN LSYYIVRWQR QPQDGYLYRH
NYCSKDKIPI RKYADGTIDI EEVTENPKTE VCGGEKGPCC ACPKTEAEKQ AEKEEAEYRK
VFENFLHNSI FVPRPERKRR DVMQVANTTM SSRSRNTTAA DTYNITDPEE LETEYPFFES
RVDNKERTVI SNLRPFTLYR IDIHSCNHEA EKLGCSASNF VFARTMPAEG ADDIPGPVTW
EPRPENSIFL KWPEPENPNG LILMYEIKYG SQVEDQRECV SRQEYRKYGG AKLNRLNPGN
YTARIQATSL SGNGSWTDPV FFYVQAKTGY ENFIHLIIAL PVAVLLIVGG LVIMLYVFHR
KRNNSRLGNG VLYASVNPEY FSAADVYVPD EWEVAREKIT MSRELGQGSF GMVYEGVAKG
VVKDEPETRV AIKTVNEAAS MRERIEFLNE ASVMKEFNCH HVVRLLGVVS QGQPTLVIME
LMTRGDLKSY LRSLRPEMEN NPVLAPPSLS KMIQMAGEIA DGMAYLNANK FVHRDLAARN
CMVAEDFTVK IGDFGMTRDI YETDYYRKGG KGLLPVRWMS PESLKDGVFT TYSDVWSFGV
VLWEIATLAE QPYQGLSNEQ VLRFVMEGGL LDKPDNCPDM LFELMRMCWQ YNPKMRPSFL
EIISSIKEEM EPGFREVSFY YSEENKLPEP EELDLEPENM ESVPLDPSAS SSSLPLPDRH
SGHKAENGPG PGVLVLRASF DERQPYAHMN GGRKNERALP LPQSSTC


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Related Genes :
[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]
[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)
[IGF1R] Insulin-like growth factor 1 receptor (EC 2.7.10.1) (Insulin-like growth factor I receptor) (IGF-I receptor) (CD antigen CD221) (Fragments)
[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)
[INSR] Insulin receptor (IR) (EC 2.7.10.1) (CD antigen CD220) [Cleaved into: Insulin receptor subunit alpha; Insulin receptor subunit beta]
[Insr] Insulin receptor (IR) (EC 2.7.10.1) (CD antigen CD220) [Cleaved into: Insulin receptor subunit alpha; Insulin receptor subunit beta]
[Insr] Insulin receptor (IR) (EC 2.7.10.1) (CD antigen CD220) [Cleaved into: Insulin receptor subunit alpha; Insulin receptor subunit beta]
[IGF2 PP1446] Insulin-like growth factor II (IGF-II) (Somatomedin-A) (T3M-11-derived growth factor) [Cleaved into: Insulin-like growth factor II; Insulin-like growth factor II Ala-25 Del; Preptin]
[Fgfr4 Fgfr-4 Mpk-11] Fibroblast growth factor receptor 4 (FGFR-4) (EC 2.7.10.1) (Protein-tyrosine kinase receptor MPK-11) (CD antigen CD334)
[IGF2BP1 CRDBP VICKZ1 ZBP1] Insulin-like growth factor 2 mRNA-binding protein 1 (IGF2 mRNA-binding protein 1) (IMP-1) (IMP1) (Coding region determinant-binding protein) (CRD-BP) (IGF-II mRNA-binding protein 1) (VICKZ family member 1) (Zipcode-binding protein 1) (ZBP-1)
[Igf2bp1 Vickz1] Insulin-like growth factor 2 mRNA-binding protein 1 (IGF2 mRNA-binding protein 1) (IMP-1) (Coding region determinant-binding protein) (CRD-BP) (IGF-II mRNA-binding protein 1) (VICKZ family member 1) (Zipcode-binding protein 1) (ZBP-1)
[IGF2BP3 IMP3 KOC1 VICKZ3] Insulin-like growth factor 2 mRNA-binding protein 3 (IGF2 mRNA-binding protein 3) (IMP-3) (IGF-II mRNA-binding protein 3) (KH domain-containing protein overexpressed in cancer) (hKOC) (VICKZ family member 3)
[Igf1 Igf-1] Insulin-like growth factor I (IGF-I) (Somatomedin)
[Igf1 Igf-1] Insulin-like growth factor I (IGF-I) (Somatomedin)
[PDGFRA PDGFR2 RHEPDGFRA] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor) (CD140 antigen-like family member A) (CD140a antigen) (Platelet-derived growth factor alpha receptor) (Platelet-derived growth factor receptor 2) (PDGFR-2) (CD antigen CD140a)
[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)
[IGFBP1 IBP1] Insulin-like growth factor-binding protein 1 (IBP-1) (IGF-binding protein 1) (IGFBP-1) (Placental protein 12) (PP12)
[Igf2bp1 Imp1 Vickz1] Insulin-like growth factor 2 mRNA-binding protein 1 (IGF2 mRNA-binding protein 1) (IMP-1) (B-actin zipcode-binding protein 1) (ZBP1) (rZBP-1) (IGF-II mRNA-binding protein 1) (VICKZ family member 1)
[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)
[daf-2 Y55D5A.5] Insulin-like receptor (IR) (EC 2.7.10.1) (Abnormal dauer formation protein 2) [Cleaved into: Insulin-like receptor subunit alpha; Insulin-like receptor subunit beta]
[Pdgfra] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor) (CD140 antigen-like family member A) (Platelet-derived growth factor alpha receptor) (CD antigen CD140a)
[Pdgfra] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor) (CD140 antigen-like family member A) (Platelet-derived growth factor alpha receptor) (CD antigen CD140a)
[InR dinr Dir-a Inr-a CG18402] Insulin-like receptor (dIR) (dInr) (EC 2.7.10.1) (dIRH) [Cleaved into: Insulin-like receptor subunit alpha; Insulin-like receptor subunit beta 1; Insulin-like receptor subunit beta 2]
[BAIAP2] Brain-specific angiogenesis inhibitor 1-associated protein 2 (BAI-associated protein 2) (BAI1-associated protein 2) (Protein BAP2) (Fas ligand-associated factor 3) (FLAF3) (Insulin receptor substrate p53/p58) (IRS-58) (IRSp53/58) (Insulin receptor substrate protein of 53 kDa) (IRSp53) (Insulin receptor substrate p53)
[IGF2BP2 IMP2 VICKZ2] Insulin-like growth factor 2 mRNA-binding protein 2 (IGF2 mRNA-binding protein 2) (IMP-2) (Hepatocellular carcinoma autoantigen p62) (IGF-II mRNA-binding protein 2) (VICKZ family member 2)
[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 :
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