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

Pub. Date : 1997 Jan 2

PMID : 9000514






8 Functional Relationships(s)
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1 Identification of Ser-1275 and Ser-1309 as autophosphorylation sites of the insulin receptor. Serine insulin receptor Homo sapiens
2 Identification of Ser-1275 and Ser-1309 as autophosphorylation sites of the insulin receptor. Serine insulin receptor Homo sapiens
3 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. Serine insulin receptor Homo sapiens
4 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. Serine insulin receptor Homo sapiens
5 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. Serine insulin receptor Homo sapiens
6 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. Serine insulin receptor Homo sapiens
7 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. Serine insulin receptor Homo sapiens
8 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. Serine insulin receptor Homo sapiens