Insulin receptor information

INSR
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1GAG, 1I44, 1IR3, 1IRK, 1P14, 1RQQ, 2AUH, 2B4S, 2HR7, 3BU3, 3BU5, 3BU6, 3EKK, 3EKN, 3ETA, 3W11, 3W12, 3W13, 3W14, 2MFR, 2Z8C, 4IBM, 4OGA, 4XLV, 4XST, 5E1S, 4ZXB, 5J3H, 5HHW
Identifiers
Aliases	INSR, CD220, HHF5, insulin receptor
External IDs	OMIM: 147670 MGI: 96575 HomoloGene: 20090 GeneCards: INSR
Gene location (Human)
Chr.	Chromosome 19 (human)
End	7,294,414 bp
Gene location (Mouse)
Chr.	Chromosome 8 (mouse)
End	3,329,617 bp
RNA expression pattern
	Top expressed in
	palpebral conjunctiva; ; visceral pleura; ; middle temporal gyrus; ; kidney tubule; ; renal medulla; ; tibia; ; seminal vesicula; ; body of pancreas; ; internal globus pallidus; ; pylorus;
	Top expressed in
	retinal pigment epithelium; ; Paneth cell; ; ciliary body; ; lacrimal gland; ; left lobe of liver; ; parotid gland; ; substantia nigra; ; digastric muscle; ; triceps brachii muscle; ; sternocleidomastoid muscle;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	kinase activity; insulin-like growth factor II binding; transmembrane receptor protein tyrosine kinase activity; ATP binding; protein kinase activity; insulin-like growth factor receptor binding; insulin receptor substrate binding; transferase activity; protein binding; protein tyrosine kinase activity; nucleotide binding; insulin-like growth factor I binding; GTP binding; PTB domain binding; phosphatidylinositol 3-kinase binding; insulin binding; insulin-activated receptor activity; protein domain specific binding; amyloid-beta binding; cargo receptor activity; protein-containing complex binding;
Cellular component	membrane; caveola; insulin receptor complex; extracellular exosome; integral component of membrane; receptor complex; plasma membrane; endosome membrane; integral component of plasma membrane; intracellular anatomical structure; nuclear envelope; external side of plasma membrane; axon; nuclear lumen; dendrite membrane; neuronal cell body membrane;
Biological process	positive regulation of glucose import; insulin receptor signaling pathway; positive regulation of protein phosphorylation; regulation of embryonic development; positive regulation of developmental growth; protein phosphorylation; regulation of female gonad development; animal organ morphogenesis; transformation of host cell by virus; positive regulation of mitotic nuclear division; positive regulation of meiotic cell cycle; positive regulation of protein kinase B signaling; positive regulation of glycogen biosynthetic process; regulation of transcription, DNA-templated; transmembrane receptor protein tyrosine kinase signaling pathway; male sex determination; positive regulation of transcription, DNA-templated; epidermis development; cellular response to insulin stimulus; protein autophosphorylation; positive regulation of respiratory burst; positive regulation of MAPK cascade; exocrine pancreas development; G protein-coupled receptor signaling pathway; male gonad development; phosphorylation; carbohydrate metabolic process; positive regulation of DNA replication; peptidyl-tyrosine autophosphorylation; activation of protein kinase B activity; positive regulation of cell migration; positive regulation of nitric oxide biosynthetic process; cellular response to growth factor stimulus; heart morphogenesis; adrenal gland development; positive regulation of cell population proliferation; positive regulation of glycolytic process; activation of protein kinase activity; signal transduction; glucose homeostasis; peptidyl-tyrosine phosphorylation; protein heterotetramerization; intracellular signal transduction; receptor-mediated endocytosis; learning; memory; positive regulation of phosphatidylinositol 3-kinase signaling; positive regulation of protein-containing complex disassembly; anatomical structure development; dendritic spine maintenance; amyloid-beta clearance; neuron projection maintenance;
	Sources:Amigo / QuickGO
Orthologs
	3643
	16337
	ENSG00000171105
	ENSMUSG00000005534
	P06213
	P15208
	NM_000208; NM_001079817
	NM_010568; NM_001330056
	NP_000199; NP_001073285
	NP_001316985; NP_034698
	Wikidata
View/Edit Human	View/Edit Mouse

The insulin receptor (IR) is a transmembrane receptor that is activated by insulin, IGF-I, IGF-II and belongs to the large class of receptor tyrosine kinase.^[5] Metabolically, the insulin receptor plays a key role in the regulation of glucose homeostasis; a functional process that under degenerate conditions may result in a range of clinical manifestations including diabetes and cancer.^[6]^[7] Insulin signalling controls access to blood glucose in body cells. When insulin falls, especially in those with high insulin sensitivity, body cells begin only to have access to lipids that do not require transport across the membrane. So, in this way, insulin is the key regulator of fat metabolism as well. Biochemically, the insulin receptor is encoded by a single gene INSR, from which alternate splicing during transcription results in either IR-A or IR-B isoforms.^[8] Downstream post-translational events of either isoform result in the formation of a proteolytically cleaved α and β subunit, which upon combination are ultimately capable of homo or hetero-dimerisation to produce the ≈320 kDa disulfide-linked transmembrane insulin receptor.^[8]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000171105 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000005534 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Ward CW, Lawrence MC (April 2009). "Ligand-induced activation of the insulin receptor: a multi-step process involving structural changes in both the ligand and the receptor". BioEssays. 31 (4): 422–34. doi:10.1002/bies.200800210. PMID 19274663. S2CID 27645596.
^ Ebina Y, Ellis L, Jarnagin K, Edery M, Graf L, Clauser E, Ou JH, Masiarz F, Kan YW, Goldfine ID (April 1985). "The human insulin receptor cDNA: the structural basis for hormone-activated transmembrane signalling". Cell. 40 (4): 747–58. doi:10.1016/0092-8674(85)90334-4. PMID 2859121. S2CID 23230348.
^ Malaguarnera R, Sacco A, Voci C, Pandini G, Vigneri R, Belfiore A (May 2012). "Proinsulin binds with high affinity the insulin receptor isoform A and predominantly activates the mitogenic pathway". Endocrinology. 153 (5): 2152–63. doi:10.1210/en.2011-1843. PMID 22355074.
^ ^a ^b Belfiore A, Frasca F, Pandini G, Sciacca L, Vigneri R (October 2009). "Insulin receptor isoforms and insulin receptor/insulin-like growth factor receptor hybrids in physiology and disease". Endocrine Reviews. 30 (6): 586–623. doi:10.1210/er.2008-0047. PMID 19752219.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000171105 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000005534 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid19274663-5] Ward CW, Lawrence MC (April 2009). "Ligand-induced activation of the insulin receptor: a multi-step process involving structural changes in both the ligand and the receptor". BioEssays. 31 (4): 422–34. doi:10.1002/bies.200800210. PMID 19274663. S2CID 27645596.

[pmid2859121-6] Ebina Y, Ellis L, Jarnagin K, Edery M, Graf L, Clauser E, Ou JH, Masiarz F, Kan YW, Goldfine ID (April 1985). "The human insulin receptor cDNA: the structural basis for hormone-activated transmembrane signalling". Cell. 40 (4): 747–58. doi:10.1016/0092-8674(85)90334-4. PMID 2859121. S2CID 23230348.

[pmid22355074-7] Malaguarnera R, Sacco A, Voci C, Pandini G, Vigneri R, Belfiore A (May 2012). "Proinsulin binds with high affinity the insulin receptor isoform A and predominantly activates the mitogenic pathway". Endocrinology. 153 (5): 2152–63. doi:10.1210/en.2011-1843. PMID 22355074.

[pmid19752219-8] Belfiore A, Frasca F, Pandini G, Sciacca L, Vigneri R (October 2009). "Insulin receptor isoforms and insulin receptor/insulin-like growth factor receptor hybrids in physiology and disease". Endocrine Reviews. 30 (6): 586–623. doi:10.1210/er.2008-0047. PMID 19752219.

Insulin receptor information

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