Background：

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]