IRS1 è un gene codificato dal simbolo IRS1. Comunemente indicato anche come: Insulin receptor substrate 1; IRS-1. IRS1 ha una massa di 131.59kDa, una lunghezza di amminoacidi di 1242, ed è implicato in Diabetes mellitus, non-insulin-dependent.
Offriamo 63 anticorpi contro IRS1, allevati nel Coniglio e Topo, che sono adatti per WB, IHC, ELISA e ICC/IF con campioni derivati da Umano, Topo, Ratto e Scimmia.
Informazioni su geni e proteine
Riepilogo UniProt
May mediate the control of various cellular processes by insulin. When phosphorylated by the insulin receptor binds specifically to various cellular proteins containing SH2 domains such as phosphatidylinositol 3-kinase p85 subunit or GRB2. Activates phosphatidylinositol 3-kinase when bound to the regulatory p85 subunit (By similarity).
Sommario di Entrez
This gene encodes a protein which is phosphorylated by insulin receptor tyrosine kinase. Mutations in this gene are associated with type II diabetes and susceptibility to insulin resistance.
Coinvolgimento nella malattia
Diabetes mellitus, non-insulin-dependent: A multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to the body's own insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels.
Modifica post-translazionale
Serine phosphorylation of IRS1 is a mechanism for insulin resistance. Ser-312 phosphorylation inhibits insulin action through disruption of IRS1 interaction with the insulin receptor (By similarity). Phosphorylation of Tyr-896 is required for GRB2-binding (By similarity). Phosphorylated by ALK. Phosphorylated at Ser-270, Ser-307, Ser-636 and Ser-1101 by RPS6KB1; phosphorylation induces accelerated degradation of IRS1 (PubMed:18952604). Phosphorylated on tyrosine residues in response to insulin (PubMed:23401856). In skeletal muscles, dephosphorylated on Tyr-612 by TNS2 under anabolic conditions; dephosphorylation results in the proteasomal degradation of IRS1 (PubMed:23401856).
