Identification of Ser-1275 and Ser-1309 as autophosphorylation sites of the insulin receptor

Autor:	H, Al-Hasani, B, Eisermann, N, Tennagels, C, Magg, W, Passlack, M, Koenen, D, Müller-Wieland, H E, Meyer, H W, Klein
Rok vydání:	1997
Předmět:	Phosphopeptides Threonine Molecular Sequence Data Spodoptera Peptide Mapping Receptor Insulin Recombinant Proteins Cell Line Solubility Mutation Serine Animals Humans Amino Acid Sequence Phosphorylation
Zdroj:	FEBS letters. 400(1)
ISSN:	0014-5793
Popis:	We have identified Ser-1275 and Ser-1309 as novel serine autophosphorylation sites by direct sequencing of HPLC-purified tryptic phosphopeptides of the histidine-tagged insulin receptor kinase IRKD-HIS. The corresponding peptides (Ser-1275, amino acids 1272-1292; Ser-1309, amino acids 1305-1313) have been detected in the HPLC profiles of both the soluble kinase IRKD, which contains the entire cytoplasmic domain of the insulin receptor beta-subunit, and the insulin receptor purified from human placenta. In contrast, a kinase negative mutant, IRKD-K1018A, did not undergo phosphorylation at either the tyrosine or serine residues, strongly suggesting that insulin receptor kinase has an intrinsic activity to autophosphorylate serine residues.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::653b34a3638fff631e7c005d24ddb114 https://pubmed.ncbi.nlm.nih.gov/9000514 Zobrazit plný text záznamu Plný text