INS

After removal of the precursor signal peptide, proinsulin is post-translationally cleaved into three peptides: the B chain and A chain peptides, which are covalently linked via two disulfide bonds to form insulin, and C-peptide. Binding of insulin to the insulin receptor (INSR) stimulates glucose uptake. A multitude of mutant alleles with phenotypic effects have been identified. There is a read-through gene, INS-IGF2, which overlaps with this gene at the 5 region and with the IGF2 gene at the 3 region. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jun 2010] After removal of the precursor signal peptide, proinsulin is post-translationally cleaved into three peptides: the B chain and A chain peptides, which are covalently linked via two disulfide bonds to form insulin, and C-peptide. Binding of insulin to the insulin receptor (INSR) stimulates glucose uptake. A multitude of mutant alleles with phenotypic effects have been identified. There is a read-through gene, INS-IGF2, which overlaps with this gene at the 5' region and with the IGF2 gene at the 3' region. Alternative splicing results in multiple transcript variants.

INS; insulin; ILPR; IRDN; IDDM1; IDDM2; MODY10; proinsulin; preproinsulin; insulin-dependent diabetes mellitus 2; OTTHUMP00000011161; OTTHUMP00000011162; OTTHUMP00000196036; OTTHUMP00000196038; OTTHUMP00000217519;