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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.
22-NOV-2017, entry version 210.
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;
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]
ENZYME 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]
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).
[43]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 988-1286 IN COMPLEX WITH
AMP-PCP AND PEPTIDE SUBSTRATE, CATALYTIC ACTIVITY, ACTIVE SITE, ENZYME
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).
[44]
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).
[45]
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).
[46]
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).
[47]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 982-1286 IN COMPLEX WITH
BENZIMIDAZOLE PYRIDINONE INHIBITOR, CATALYTIC ACTIVITY, AND ENZYME
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).
[48]
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).
[49]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 986-1286 IN COMPLEX WITH
INHIBITOR PQIP, SUBUNIT, AUTOPHOSPHORYLATION, CATALYTIC ACTIVITY,
ACTIVE SITE, AND ENZYME 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).
[50]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 981-1286 IN COMPLEX WITH
3-CYANOQUINOLINE INHIBITOR, CATALYTIC ACTIVITY, ENZYME 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).
[51]
X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 982-1286 IN COMPLEX WITH
BMS-754807, CATALYTIC ACTIVITY, AND ENZYME 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).
[52]
X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 983-1286 IN COMPLEX WITH
MSC1609119A-1, CATALYTIC ACTIVITY, AND ENZYME 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).
[53]
X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) OF 982-1286 IN COMPLEXES WITH
INHIBITORS, CATALYTIC ACTIVITY, AND ENZYME 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).
[54]
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 951-1286 IN COMPLEX WITH
BIS-AZAINDOLE INHIBITOR, AUTOPHOSPHORYLATION, AND ENZYME 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).
[55]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 982-1286 IN COMPLEX WITH
HYDANTOIN DERIVATIVE, CATALYTIC ACTIVITY, AND ENZYME 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).
[56]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 988-1286 IN COMPLEX WITH
2,4-BIS-ARYLAMINO-1,3-PYRIMIDINE INHIBITOR, CATALYTIC ACTIVITY, AND
ENZYME 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).
[57]
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).
[58]
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).
[59]
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).
[60]
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: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {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.52}.
-!- ENZYME 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.52}.
-!- 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). {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:7541045, ECO:0000269|PubMed:9581554,
ECO:0000269|PubMed:9727029, ECO:0000269|PubMed:9822622,
ECO:0000269|Ref.52}.
-!- INTERACTION:
Self; NbExp=6; IntAct=EBI-475981, EBI-475981;
Q9NZN5:ARHGEF12; NbExp=7; IntAct=EBI-475981, EBI-821440;
P49913:CAMP; NbExp=3; IntAct=EBI-475981, EBI-6378485;
Q64010:Crk (xeno); NbExp=3; IntAct=EBI-475981, EBI-2906540;
P41240:CSK; NbExp=5; IntAct=EBI-475981, EBI-1380630;
P35222:CTNNB1; NbExp=3; IntAct=EBI-475981, EBI-491549;
P05019:IGF1; NbExp=8; IntAct=EBI-475981, EBI-7902275;
P01317:INS (xeno); NbExp=4; IntAct=EBI-475981, EBI-3989070;
Q9Y2W7:KCNIP3; NbExp=5; IntAct=EBI-475981, EBI-751501;
Q9UJU2:LEF1; NbExp=5; IntAct=EBI-475981, EBI-926131;
Q00987:MDM2; NbExp=2; IntAct=EBI-475981, EBI-389668;
P27986:PIK3R1; NbExp=4; IntAct=EBI-475981, EBI-79464;
Q92569:PIK3R3; NbExp=2; IntAct=EBI-475981, EBI-79893;
P18031:PTPN1; NbExp=3; IntAct=EBI-475981, EBI-968788;
Q06124:PTPN11; NbExp=3; IntAct=EBI-475981, EBI-297779;
P29353-2:SHC1; NbExp=2; IntAct=EBI-475981, EBI-1000553;
Q01995:TAGLN; NbExp=2; IntAct=EBI-475981, EBI-1054248;
-!- 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=Translation N-terminally shortened.; 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.
UniGene; Hs.643120; -.
UniGene; Hs.714012; -.
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.
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; -.
ProteinModelPortal; P08069; -.
SMR; P08069; -.
BioGrid; 109701; 99.
CORUM; P08069; -.
DIP; DIP-476N; -.
IntAct; P08069; 55.
MINT; MINT-85902; -.
STRING; 9606.ENSP00000268035; -.
BindingDB; P08069; -.
ChEMBL; CHEMBL1957; -.
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; DB05759; IMC-A12.
DrugBank; DB05900; INSM-18.
DrugBank; DB00047; Insulin Glargine.
DrugBank; DB00030; Insulin Human.
DrugBank; DB00046; Insulin Lispro.
DrugBank; DB00071; Insulin Pork.
DrugBank; DB01277; Mecasermin.
DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
DrugBank; DB05897; rhIGFBP-3.
DrugBank; DB05184; XL228.
GuidetoPHARMACOLOGY; 1801; -.
iPTMnet; P08069; -.
PhosphoSitePlus; P08069; -.
BioMuta; IGF1R; -.
DMDM; 124240; -.
EPD; P08069; -.
MaxQB; P08069; -.
PaxDb; P08069; -.
PeptideAtlas; P08069; -.
PRIDE; P08069; -.
DNASU; 3480; -.
Ensembl; ENST00000268035; ENSP00000268035; 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; CAB010268; -.
HPA; HPA045563; -.
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; ENSGT00760000118818; -.
HOGENOM; HOG000038045; -.
HOVERGEN; HBG006134; -.
InParanoid; P08069; -.
KO; K05087; -.
OMA; GYLYRHN; -.
OrthoDB; EOG091G00GE; -.
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.
SignaLink; P08069; -.
SIGNOR; P08069; -.
ChiTaRS; IGF1R; human.
EvolutionaryTrace; P08069; -.
GeneWiki; Insulin-like_growth_factor_1_receptor; -.
GenomeRNAi; 3480; -.
PRO; PR:P08069; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000140443; -.
CleanEx; HS_IGF1R; -.
ExpressionAtlas; P08069; baseline and differential.
Genevisible; P08069; HS.
GO; GO:0035867; C:alphav-beta3 integrin-IGF-1-IGF1R complex; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IC:UniProtKB.
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: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: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:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0097242; P:amyloid-beta clearance; IMP:ARUK-UCL.
GO; GO:1904646; P:cellular response to amyloid-beta; IGI:ARUK-UCL.
GO; GO:0097062; P:dendritic spine maintenance; ISS:ARUK-UCL.
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: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 proliferation; TAS:ProtInc.
GO; GO:0045740; P:positive regulation of DNA replication; IMP:BHF-UCL.
GO; GO:0043243; P:positive regulation of protein complex disassembly; ISS:ARUK-UCL.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0051262; P:protein tetramerization; IDA:UniProtKB.
GO; GO:0046328; P:regulation of JNK cascade; IDA:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
CDD; cd00063; FN3; 3.
Gene3D; 2.60.40.10; -; 3.
Gene3D; 3.80.20.20; -; 3.
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; IPR032675; LRR_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; 4.
SUPFAM; SSF52058; SSF52058; 2.
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; Complete proteome;
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 {ECO:0000269|PubMed:2877871,
ECO:0000269|PubMed:8257688}.
CHAIN 31 736 Insulin-like growth factor 1 receptor
alpha chain.
/FTId=PRO_0000016681.
CHAIN 741 1367 Insulin-like growth factor 1 receptor
beta chain.
/FTId=PRO_0000016682.
TOPO_DOM 741 935 Extracellular. {ECO:0000255}.
TRANSMEM 936 959 Helical. {ECO:0000255}.
TOPO_DOM 960 1367 Cytoplasmic. {ECO:0000255}.
DOMAIN 491 609 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 610 708 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 735 828 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 834 927 Fibronectin type-III 4.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 999 1274 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 1005 1013 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 977 980 IRS1- and SHC1-binding.
ACT_SITE 1135 1135 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 1033 1033 ATP.
MOD_RES 980 980 Phosphotyrosine.
{ECO:0000305|PubMed:7541045}.
MOD_RES 1161 1161 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:11694888,
ECO:0000269|PubMed:18501599,
ECO:0000269|PubMed:19041240}.
MOD_RES 1165 1165 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:11694888,
ECO:0000269|PubMed:18501599,
ECO:0000269|PubMed:19041240}.
MOD_RES 1166 1166 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:11694888,
ECO:0000269|PubMed:18501599,
ECO:0000269|PubMed:19041240}.
MOD_RES 1278 1278 Phosphoserine; by GSK3-beta.
{ECO:0000250|UniProtKB:Q60751}.
MOD_RES 1282 1282 Phosphoserine.
{ECO:0000250|UniProtKB:Q60751}.
CARBOHYD 51 51 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:9690478}.
CARBOHYD 102 102 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 135 135 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:9690478}.
CARBOHYD 244 244 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:9690478}.
CARBOHYD 314 314 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:9690478}.
CARBOHYD 417 417 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 438 438 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 534 534 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 607 607 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 622 622 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 640 640 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 747 747 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 756 756 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 764 764 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 900 900 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 913 913 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 33 52 {ECO:0000269|PubMed:9690478}.
DISULFID 150 178 {ECO:0000269|PubMed:9690478}.
DISULFID 182 205 {ECO:0000269|PubMed:9690478}.
DISULFID 192 211 {ECO:0000269|PubMed:9690478}.
DISULFID 215 224 {ECO:0000269|PubMed:9690478}.
DISULFID 219 230 {ECO:0000269|PubMed:9690478}.
DISULFID 231 239 {ECO:0000269|PubMed:9690478}.
DISULFID 235 248 {ECO:0000269|PubMed:9690478}.
DISULFID 251 260 {ECO:0000269|PubMed:9690478}.
DISULFID 264 276 {ECO:0000269|PubMed:9690478}.
DISULFID 282 303 {ECO:0000269|PubMed:9690478}.
DISULFID 307 321 {ECO:0000269|PubMed:9690478}.
DISULFID 324 328 {ECO:0000269|PubMed:9690478}.
DISULFID 332 353 {ECO:0000269|PubMed:9690478}.
DISULFID 455 488 {ECO:0000269|PubMed:9690478}.
CROSSLNK 1168 1168 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:21994939}.
CROSSLNK 1171 1171 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:21994939}.
VARIANT 105 105 V -> L (in a renal chromophobe sample;
somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041424.
VARIANT 138 138 R -> Q (in IGF1RES; has decreased IGF1R
function; dbSNP:rs121912426).
{ECO:0000269|PubMed:14657428}.
/FTId=VAR_034891.
VARIANT 145 145 K -> N (in IGF1RES; has decreased IGF1R
function; dbSNP:rs121912427).
{ECO:0000269|PubMed:14657428}.
/FTId=VAR_034892.
VARIANT 359 359 N -> Y (in IGF1RES; significant decrease
in IGF1-induced DNA synthesis and AKT1
phosphorylation in patient fibroblasts).
{ECO:0000269|PubMed:25040157}.
/FTId=VAR_076247.
VARIANT 388 388 V -> M (in dbSNP:rs45445894).
{ECO:0000269|Ref.4}.
/FTId=VAR_018855.
VARIANT 437 437 R -> H (in dbSNP:rs34516635).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_034893.
VARIANT 511 511 R -> Q (in dbSNP:rs33958176).
/FTId=VAR_034894.
VARIANT 595 595 R -> H (in dbSNP:rs56248469).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041425.
VARIANT 605 605 R -> H (in dbSNP:rs45553041).
{ECO:0000269|Ref.4}.
/FTId=VAR_018856.
VARIANT 739 739 R -> Q (in IGF1RES; leads to failure of
processing of the IGF1R proreceptor to
mature IGF1R; dbSNP:rs121912429).
{ECO:0000269|PubMed:15928254}.
/FTId=VAR_034895.
VARIANT 808 808 H -> R (in dbSNP:rs34061581).
/FTId=VAR_034896.
VARIANT 828 828 A -> T (in dbSNP:rs35224135).
/FTId=VAR_034897.
VARIANT 857 857 N -> S (in dbSNP:rs45611935).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041426.
VARIANT 865 865 Y -> C (in IGF1RES; significant decrease
in IGF1-induced DNA synthesis and AKT1
phosphorylation in patient fibroblasts).
{ECO:0000269|PubMed:25040157}.
/FTId=VAR_076248.
VARIANT 1256 1256 R -> S (in IGF1RES; significant decrease
in IGF1-induced DNA synthesis and AKT1
phosphorylation in patient fibroblasts).
{ECO:0000269|PubMed:25040157}.
/FTId=VAR_076249.
VARIANT 1337 1337 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).
{ECO:0000269|PubMed:25040157}.
/FTId=VAR_076250.
VARIANT 1338 1338 A -> T (in dbSNP:rs34102392).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041427.
VARIANT 1347 1347 A -> V (in a lung squamous cell carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041428.
MUTAGEN 980 980 Y->F: Reduces tyrosine phosphorylation.
Abolishes interaction with IRS1 and SHC1.
Does not abolish interaction with PIK3R1,
nor with GRB10.
{ECO:0000269|PubMed:10454568,
ECO:0000269|PubMed:7541045}.
MUTAGEN 1033 1033 K->A: Kinase inactive. Abolishes tyrosine
phosphorylation and abolishes interaction
with IRS1, SHC1 and PIK3R1.
{ECO:0000269|PubMed:7541045}.
MUTAGEN 1280 1280 Y->F: No effect on GRB10-binding.
{ECO:0000269|PubMed:10454568}.
MUTAGEN 1281 1281 Y->F: No effect on GRB10-binding.
{ECO:0000269|PubMed:10454568}.
MUTAGEN 1346 1346 Y->F: Loss of GRB10-binding.
{ECO:0000269|PubMed:10454568}.
CONFLICT 928 929 TG -> R (in Ref. 3; BAG11657).
{ECO:0000305}.
STRAND 37 41 {ECO:0000244|PDB:1IGR}.
HELIX 43 49 {ECO:0000244|PDB:1IGR}.
STRAND 53 57 {ECO:0000244|PDB:1IGR}.
STRAND 59 65 {ECO:0000244|PDB:1IGR}.
STRAND 68 70 {ECO:0000244|PDB:1IGR}.
STRAND 80 83 {ECO:0000244|PDB:1IGR}.
STRAND 85 92 {ECO:0000244|PDB:1IGR}.
HELIX 96 98 {ECO:0000244|PDB:1IGR}.
STRAND 115 121 {ECO:0000244|PDB:1IGR}.
STRAND 138 144 {ECO:0000244|PDB:1IGR}.
HELIX 157 160 {ECO:0000244|PDB:1IGR}.
HELIX 164 166 {ECO:0000244|PDB:1IGR}.
STRAND 168 171 {ECO:0000244|PDB:1IGR}.
HELIX 175 178 {ECO:0000244|PDB:1IGR}.
TURN 183 188 {ECO:0000244|PDB:1IGR}.
STRAND 194 199 {ECO:0000244|PDB:1IGR}.
STRAND 201 203 {ECO:0000244|PDB:1IGR}.
STRAND 205 209 {ECO:0000244|PDB:1IGR}.
HELIX 217 219 {ECO:0000244|PDB:1IGR}.
STRAND 235 241 {ECO:0000244|PDB:1IGR}.
STRAND 247 255 {ECO:0000244|PDB:1IGR}.
STRAND 257 263 {ECO:0000244|PDB:1IGR}.
STRAND 269 271 {ECO:0000244|PDB:1IGR}.
TURN 272 274 {ECO:0000244|PDB:1IGR}.
STRAND 275 277 {ECO:0000244|PDB:1IGR}.
HELIX 279 283 {ECO:0000244|PDB:1IGR}.
STRAND 297 299 {ECO:0000244|PDB:1IGR}.
STRAND 302 306 {ECO:0000244|PDB:1IGR}.
STRAND 311 315 {ECO:0000244|PDB:1IGR}.
STRAND 321 323 {ECO:0000244|PDB:1IGR}.
STRAND 325 327 {ECO:0000244|PDB:1IGR}.
STRAND 331 341 {ECO:0000244|PDB:1IGR}.
HELIX 345 347 {ECO:0000244|PDB:1IGR}.
TURN 349 352 {ECO:0000244|PDB:1IGR}.
STRAND 354 362 {ECO:0000244|PDB:1IGR}.
HELIX 375 378 {ECO:0000244|PDB:1IGR}.
STRAND 383 386 {ECO:0000244|PDB:1IGR}.
STRAND 388 392 {ECO:0000244|PDB:1IGR}.
TURN 415 417 {ECO:0000244|PDB:1IGR}.
STRAND 418 423 {ECO:0000244|PDB:1IGR}.
TURN 434 436 {ECO:0000244|PDB:1IGR}.
STRAND 440 443 {ECO:0000244|PDB:1IGR}.
STRAND 445 451 {ECO:0000244|PDB:1IGR}.
HELIX 456 466 {ECO:0000244|PDB:1IGR}.
STRAND 474 477 {ECO:0000244|PDB:1IGR}.
TURN 479 481 {ECO:0000244|PDB:1IGR}.
HELIX 724 730 {ECO:0000244|PDB:4XSS}.
STRAND 980 982 {ECO:0000244|PDB:1P4O}.
HELIX 983 985 {ECO:0000244|PDB:2ZM3}.
TURN 990 992 {ECO:0000244|PDB:2OJ9}.
HELIX 996 998 {ECO:0000244|PDB:1P4O}.
STRAND 999 1007 {ECO:0000244|PDB:1P4O}.
STRAND 1009 1022 {ECO:0000244|PDB:1P4O}.
STRAND 1025 1034 {ECO:0000244|PDB:1P4O}.
STRAND 1037 1039 {ECO:0000244|PDB:3F5P}.
HELIX 1041 1053 {ECO:0000244|PDB:1P4O}.
HELIX 1054 1056 {ECO:0000244|PDB:1P4O}.
STRAND 1065 1069 {ECO:0000244|PDB:1P4O}.
STRAND 1071 1074 {ECO:0000244|PDB:1P4O}.
STRAND 1076 1080 {ECO:0000244|PDB:1P4O}.
HELIX 1087 1100 {ECO:0000244|PDB:1P4O}.
HELIX 1109 1128 {ECO:0000244|PDB:1P4O}.
HELIX 1138 1140 {ECO:0000244|PDB:1P4O}.
STRAND 1141 1143 {ECO:0000244|PDB:1P4O}.
STRAND 1149 1151 {ECO:0000244|PDB:1P4O}.
HELIX 1155 1157 {ECO:0000244|PDB:3D94}.
HELIX 1159 1164 {ECO:0000244|PDB:1P4O}.
TURN 1165 1167 {ECO:0000244|PDB:3LVP}.
HELIX 1168 1170 {ECO:0000244|PDB:1P4O}.
STRAND 1171 1174 {ECO:0000244|PDB:1P4O}.
HELIX 1176 1178 {ECO:0000244|PDB:1P4O}.
HELIX 1181 1186 {ECO:0000244|PDB:1P4O}.
HELIX 1191 1207 {ECO:0000244|PDB:1P4O}.
TURN 1212 1215 {ECO:0000244|PDB:1P4O}.
HELIX 1218 1226 {ECO:0000244|PDB:1P4O}.
HELIX 1239 1248 {ECO:0000244|PDB:1P4O}.
HELIX 1253 1255 {ECO:0000244|PDB:1P4O}.
HELIX 1259 1266 {ECO:0000244|PDB:1P4O}.
HELIX 1267 1269 {ECO:0000244|PDB:1P4O}.
HELIX 1274 1277 {ECO:0000244|PDB:1P4O}.
TURN 1279 1281 {ECO:0000244|PDB:3O23}.
TURN 1283 1285 {ECO:0000244|PDB:3LVP}.
STRAND 1286 1288 {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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16-8849-80 Anti-Human CD221 (Insulin-like Growth Factor-1 Receptor) Functional Grade Purified 25 ug
16-8849-82 Anti-Human CD221 (Insulin-like Growth Factor-1 Receptor) Functional Grade Purified 100 ug
orb82618 Human LR3IGF1 protein Insulin-like growth factor-1 (IGF1) is the principal hormonal mediator of statural growth. Under normal circumstances, growth hormone (GH) binds to its receptor in the liver, and 20
U1629h CLIA 300 kDa mannose 6-phosphate receptor,Cation-independent mannose-6-phosphate receptor,CI Man-6-P receptor,CI-MPR,Homo sapiens,Human,IGF2R,IGF-II receptor,Insulin-like growth factor 2 receptor,Insu 96T
E1629h ELISA 300 kDa mannose 6-phosphate receptor,Cation-independent mannose-6-phosphate receptor,CI Man-6-P receptor,CI-MPR,Homo sapiens,Human,IGF2R,IGF-II receptor,Insulin-like growth factor 2 receptor,Ins 96T
U1629b CLIA 300 kDa mannose 6-phosphate receptor,Bos taurus,Bovine,Cation-independent mannose-6-phosphate receptor,CI Man-6-P receptor,CI-MPR,IGF2R,IGF-II receptor,Insulin-like growth factor 2 receptor,Insul 96T
E1629b ELISA 300 kDa mannose 6-phosphate receptor,Bos taurus,Bovine,Cation-independent mannose-6-phosphate receptor,CI Man-6-P receptor,CI-MPR,IGF2R,IGF-II receptor,Insulin-like growth factor 2 receptor,Insu 96T
E1629b ELISA kit 300 kDa mannose 6-phosphate receptor,Bos taurus,Bovine,Cation-independent mannose-6-phosphate receptor,CI Man-6-P receptor,CI-MPR,IGF2R,IGF-II receptor,Insulin-like growth factor 2 receptor 96T
IQ391 Mouse Anti-Insulin-Like Growth Factor (IGF-1) Target Antigen Insulin-Like Growth Factor (IGF-1) Host Isotype Mouse IgG1 Application RIA or EIA assay development & studies of IGF-1 on frozen & paraf 0.1ml (1mg/ml)


 

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