In:
FEBS Letters, Wiley, Vol. 400, No. 1 ( 1997-01-02), p. 65-70
Abstract:
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 β‐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.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/S0014-5793(96)01342-7
Language:
English
Publisher:
Wiley
Publication Date:
1997
detail.hit.zdb_id:
1460391-3
SSG:
12
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