Phosphorylation of Ser-42 and Ser-59 in the N-terminal region of the tyrosine kinase p56(lck)

In vitro kinase assays show that Ser-59 can be uniquely phosphorylated by mitogen-activated protein kinase and that Ser-42 can be phosphorylated by either protein kinase A or protein kinase C.

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1993-06, Vol.90 (11), p.5176
Main Authors: Winkler, David G, Park, Indal, Kim, TaeUe, Payne, Nicola S
Format: Article
Language:English
Subjects:
Cellular biology
Enzymes
Proteins
Online Access:Get full text
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Description
Summary:In vitro kinase assays show that Ser-59 can be uniquely phosphorylated by mitogen-activated protein kinase and that Ser-42 can be phosphorylated by either protein kinase A or protein kinase C.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.90.11.5176