Insulin receptor (Protein name
), INSR_HUMAN from NCBI database.
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General Annotation
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Gene name:
INSR;
Protein name:
Insulin receptor(IR);
Alternative:
CD:
CD220;
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 chains carry the kinase domain. Interacts with SORBS1 but dissociates from it following insulin stimulation. Binds SH2B2. Interacts with the PTB/PID domains of IRS1 and SHC1 in vitro when autophosphorylated on tyrosine residues. The sequences surrounding the phosphorylated NPXY motif contribute differentially to either IRS1 or SHC1 recognition. Interacts with the SH2 domains of the 85 kDa regulatory subunit of PI3K (PIK3R1) in vitro, when autophosphorylated on tyrosine residues. Interacts with SOCS7. Forms a hybrid receptor with IGF1R, 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 CAV2 (tyrosine-phosphorylated form); the interaction is increased with 'Tyr-27'phosphorylation of CAV2. Interacts with ARRB2 (By similarity). Interacts with GRB10; this interaction blocks the association between IRS1/IRS2 and INSR, significantly reduces insulin-stimulated tyrosine phosphorylation of IRS1 and IRS2 and thus decreases insulin signaling. Interacts with GRB7.
Function:
This receptor binds insulin and has a tyrosine-protein kinase activity. Isoform Short has a higher affinity for insulin. Mediates the metabolic functions of insulin. Binding to insulin stimulates association of the receptor with downstream mediators including IRS1 and phosphatidylinositol 3'-kinase (PI3K). Can activate PI3K either directly by binding to the p85 regulatory subunit, or indirectly via IRS1. When present in a hybrid receptor with IGF1R, 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] (ISOFORM LONG);VARIANTS GLY-2; HIS-171; THR-448 AND LYS-492
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT);PROTEIN SEQUENCE OF 28-49 AND 763-782;GLYCOSYLATION AT ASN-43 AND ASN-769;VARIANT GLY-2
3.
Chen E.Y.
Submitted (1985-07) to the EMBL/GenBank/DDBJ databases
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Cited for: SEQUENCE REVISION TO 899-900
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Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA];VARIANT GLY-2
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT);VARIANT GLY-2
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Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33;VARIANT GLY-2
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Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33;VARIANT GLY-2
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Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33;VARIANT GLY-2
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Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33;VARIANT GLY-2
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Cited for: PROTEIN SEQUENCE OF 28-44; 192-205; 299-314; 610-627 AND 763-780;ENZYME REGULATION;SUBUNIT
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Cited for: PROTEIN SEQUENCE OF 28-45 AND 763-782;FUNCTION;FORMATION OF A HYBRID RECEPTOR WITH IGF1R
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 538-1382 (ISOFORM SHORT)
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 728-772 (ISOFORM LONG);ALTERNATIVE SPLICING
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 744-823 (ISOFORM LONG);TISSUE SPECIFICITY;LIGAND-BINDING;AUTOPHOSPHORYLATION
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Cited for: PROTEIN SEQUENCE OF 927-956; 981-1019; 1182-1194 AND 1352-1369;PHOSPHORYLATION AT TYR-999; TYR-1355 AND TYR-1361
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Cited for: FUNCTION;FORMATION OF A HYBRID RECEPTOR WITH IGF1R
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Cited for: INTERACTION WITH IRS1 AND SHC1;MUTAGENESIS OF LEU-991; TYR-992; ASN-996; 996-ASN-PRO-997; PRO-997; TYR-999; LEU-1000 AND ALA-1002
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Cited for: INTERACTION WITH IRS1; SHC1 AND PIK3R1;MUTAGENESIS OF ASN-996; PRO-997; GLU-998; TYR-999 AND LYS-1057
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Cited for: FORMATION OF A HYBRID RECEPTOR WITH IGF1R;TISSUE SPECIFICITY
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Cited for: FUNCTION IN PHOSPHORYLATION OF STAT5B;MUTAGENESIS OF TYR-999;INTERACTION WITH STAT5B; IRS1 AND IRS2
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Cited for: INTERACTION WITH PTPRE;DEPHOSPHORYLATION BY PTPRE
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Cited for: FORMATION OF A HYBRID RECEPTOR WITH IGF1R;TISSUE SPECIFICITY
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Cited for: TISSUE SPECIFICITY;FUNCTION AS RECEPTOR FOR IGFII (ISOFORM SHORT)
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Cited for: PHOSPHORYLATION;DEPHOSPHORYLATION BY PTPN1 AND PTPN2
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Cited for: INTERACTION WITH GRB7;MUTAGENESIS OF LYS-1057; TYR-1189 AND TYR-1190
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Cited for: CATALYTIC ACTIVITY;MUTAGENESIS OF ASP-1159 AND ARG-1163;ENZYME REGULATION
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Cited for: FUNCTION;FORMATION OF A HYBRID RECEPTOR WITH IGF1R
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Cited for: FUNCTION IN PHOSPHORYLATION OF PDPK1;INTERACTION WITH PDPK1
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Cited for: FUNCTION;FORMATION OF A HYBRID RECEPTOR WITH IGF1R
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-400; TYR-401 AND SER-407;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-242 AND ASN-541
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Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-445 AND ASN-920
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Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1005-1310
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Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1005-1310 IN COMPLEX WITH ATP ANALOG AND IRS1 PEPTIDE;CATALYTIC ACTIVITY;ACTIVE SITE;AUTOPHOSPHORYLATION;PHOSPHORYLATION AT TYR-1185; TYR-1189 AND TYR-1190
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Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1005-1310 IN COMPLEX WITH ATP ANALOG;CATALYTIC ACTIVITY
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Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1005-1298 OF MUTANT ASN-1159;CATALYTIC ACTIVITY;AUTOPHOSPHORYLATION;MUTAGENESIS OF TYR-1011
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Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1005-1310 IN COMPLEX WITH ATP ANALOG AND SH2B2;PHOSPHORYLATION AT TYR-1185; TYR-1189 AND TYR-1190
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Cited for: X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 1005-1310 IN COMPLEX WITH GRB14;INTERACTION WITH GRB14;AUTOPHOSPHORYLATION;PHOSPHORYLATION AT TYR-1185; TYR-1189 AND TYR-1190
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Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1005-1310 IN COMPLEX WITH PTPN1;PHOSPHORYLATION AT TYR-1185; TYR-1189 AND TYR-1190
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Cited for: X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF 28-943 IN COMPLEX WITH INSULIN ANALOG;DOMAIN;DISULFIDE BONDS
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Cited for: X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS) OF 28-512;GLYCOSYLATION AT ASN-43; ASN-52; ASN-138; ASN-242; ASN-282; ASN-364; ASN-424 AND ASN-445;DISULFIDE BONDS
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Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 1005-1310 IN COMPLEX WITH ATP AND IRS2;CATALYTIC ACTIVITY;PHOSPHORYLATION AT TYR-1185; TYR-1189 AND TYR-1190;INTERACTION WITH IRS2
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Cited for: X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 1009-1310 IN COMPLEX WITH INHIBITORY PEPTIDE;PHOSPHORYLATION AT TYR-1185; TYR-1189 AND TYR-1190
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Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1005-1310 IN COMPLEX WITH SYNTHETIC INHIBITOR;CATALYTIC ACTIVITY
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Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1005-1310 IN COMPLEX WITH SYNTHETIC INHIBITOR;CATALYTIC ACTIVITY
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Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1017-1322 IN COMPLEX WITH SYNTHETIC INHIBITOR;CATALYTIC ACTIVITY
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Cited for: X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS) OF 28-956;INSULIN-BINDING REGION;DISULFIDE BONDS
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Cited for: X-RAY CRYSTALLOGRAPHY (3.9 ANGSTROMS) OF 28-620 IN COMPLEX WITH INSULIN;DOMAIN;GLYCOSYLATION AT ASN-43; ASN-52; ASN-138; ASN-242 AND ASN-282;DISULFIDE BONDS
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Cited for: VARIANT RMS LYS-42;VARIANT LEPRCH ARG-236;VARIANT IRAN TYPE A SER-489
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Cited for: CHARACTERIZATION OF VARIANT IRAN TYPE A GLU-1162
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Cited for: VARIANT RMS SYNDROME LEU-350;VARIANTS IRAN TYPE A LEU-1205 AND GLN-1378;VARIANT MET-1012
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Cited for: CHARACTERIZATION OF VARIANT IRAN TYPE A GLN-1201
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Cited for: CHARACTERIZATION OF VARIANTS IRAN TYPE A ASP-1206 AND LEU-1220
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Cited for: CHARACTERIZATION OF VARIANTS LEPRCH PRO-113; VAL-119; ASN-308 DEL; THR-925 AND TRP-926;VARIANTS RMS THR-997; THR-1143; TRP-1158 AND TRP-1201
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Cited for: VARIANT IRAN TYPE A HIS-279;VARIANTS LEPRCH GLN-120; LEU-350; ASP-458 AND TRP-1119;CHARACTERIZATION OF VARIANT IRAN TYPE A HIS-279;CHARACTERIZATION OF VARIANTS LEPRCH GLN-120 AND ASP-458
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Cited for: VARIANTS RMS ARG-236 AND SER-386;CHARACTERIZATION OF VARIANTS RMS ARG-236 AND SER-386
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Cited for: VARIANTS [LARGE SCALE ANALYSIS] ARG-228; ARG-695; SER-811; MET-1012; VAL-1065 AND ALA-1282