Insulin-like growth factor 1 receptor (Protein name
), IGF1R_HUMAN from NCBI database.
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General Annotation
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Antigen Annotation
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Gene name:
IGF1R;
Protein name:
Insulin-like growth factor 1 receptor;
Alternative:
Insulin-like growth factor I receptor(IGF-I receptor);
CD:
CD221;
Organism:
Human (Homo sapiens).
General Annotation
Sub Unit:
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 GNB2L1/RACK1.
Function:
This receptor binds insulin-like growth factor 1 (IGF1) with a high affinity and IGF2 with a lower affinity. It has a tyrosine-protein kinase activity, which is necessary for the activation of the IGF1-stimulated downstream signaling cascade. 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.
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Cited for: NUCLEOTIDE SEQUENCE [MRNA];PROTEIN SEQUENCE OF 31-56; 446-453; 503-524; 561-579; 668-672 AND 721-729
NIEHS SNPs program
Submitted (2003-06) to the EMBL/GenBank/DDBJ databases
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Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA];VARIANTS MET-388 AND HIS-605
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Cited for: PROTEIN SEQUENCE OF 31-45 AND 741-750;FUNCTION;FORMATION OF A HYBRID RECEPTOR WITH INSR
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1137-1193;TISSUE SPECIFICITY
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Cited for: FUNCTION;FORMATION OF A HYBRID RECEPTOR WITH INSR
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Cited for: FUNCTION;CATALYTIC ACTIVITY;AUTOPHOSPHORYLATION
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Cited for: INTERACTION WITH IRS1; SHC1 AND PIK3R1;MUTAGENESIS OF TYR-980 AND LYS-1033;PHOSPHORYLATION AT TYR-980
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Cited for: FORMATION OF A HYBRID RECEPTOR WITH INSR;TISSUE SPECIFICITY
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Cited for: FORMATION OF A HYBRID RECEPTOR WITH INSR;TISSUE SPECIFICITY
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Cited for: INTERACTION WITH GRB10;MUTAGENESIS OF TYR-980; TYR-1280; TYR-1281 AND TYR-1346
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Cited for: FUNCTION;FORMATION OF A HYBRID RECEPTOR WITH INSR
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Cited for: FUNCTION;FORMATION OF A HYBRID RECEPTOR WITH INSR
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Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 31-492;DISULFIDE BONDS;GLYCOSYLATION AT ASN-51; ASN-135; ASN-244 AND ASN-314
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Cited for: 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;PHOSPHORYLATION AT TYR-1161; TYR-1165 AND TYR-1166
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Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 981-1286 IN COMPLEX WITH ANP;AUTOPHOSPHORYLATION;ACTIVE SITE;IDENTIFICATION BY MASS SPECTROMETRY
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Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 974-1294
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Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 974-1294
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Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 982-1286 IN COMPLEX WITH BENZIMIDAZOLE PYRIDINONE INHIBITOR;CATALYTIC ACTIVITY;ENZYME REGULATION
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Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 981-1286;PHOSPHORYLATION AT TYR-1161; TYR-1165 AND TYR-1166
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Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 986-1286 IN COMPLEX WITH INHIBITOR PQIP;SUBUNIT;AUTOPHOSPHORYLATION;CATALYTIC ACTIVITY;ACTIVE SITE;ENZYME REGULATION
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Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 981-1286 IN COMPLEX WITH 3-CYANOQUINOLINE INHIBITOR;CATALYTIC ACTIVITY;ENZYME REGULATION;PHOSPHORYLATION AT TYR-1161; TYR-1165 AND TYR-1166
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Cited for: X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 982-1286 IN COMPLEX WITH BMS-754807;CATALYTIC ACTIVITY;ENZYME REGULATION
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Cited for: X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 983-1286 IN COMPLEX WITH MSC1609119A-1;CATALYTIC ACTIVITY;ENZYME REGULATION
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Cited for: X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) OF 982-1286 IN COMPLEXES WITH INHIBITORS;CATALYTIC ACTIVITY;ENZYME REGULATION
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Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 951-1286 IN COMPLEX WITH BIS-AZAINDOLE INHIBITOR;AUTOPHOSPHORYLATION;ENZYME REGULATION
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Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 982-1286 IN COMPLEX WITH HYDANTOIN DERIVATIVE;CATALYTIC ACTIVITY;ENZYME REGULATION
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Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 988-1286 IN COMPLEX WITH 2,4-BIS-ARYLAMINO-1,3-PYRIMIDINE INHIBITOR;CATALYTIC ACTIVITY;ENZYME REGULATION
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Cited for: VARIANTS IGF1RES GLN-138 AND ASN-145;CHARACTERIZATION OF VARIANTS IGF1RES GLN-138 AND ASN-145
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Cited for: VARIANT IGF1RES GLN-739;CHARACTERIZATION OF VARIANT IGF1RES GLN-739
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Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-105; HIS-437; HIS-595; SER-857; THR-1338 AND VAL-1347