Abstract:
:We have isolated cDNA molecules encoding a protein with the characteristic sequence elements that are conserved between the catalytic domains of protein kinases. This protein is apparently a serine/threonine kinase and is most closely related to the amino-terminal half of the ribosomal protein S6 kinase II first characterized in Xenopus eggs (42% overall identity and 56% identity in the predicted catalytic domain). However, it clearly differs from S6 kinase II in that it has only one, rather than two predicted catalytic domains and a deduced molecular mass of 59,109 Da. We propose that is may be more related to, or identical, with, the mitogen-inducible S6 kinase of molecular mass 65-70 kDa described in mammalian liver, mouse 3T3 cells and chicken embryos. Remarkable structural features of the cDNA-encoded polypeptide are a section rich in proline, serine and threonine residues that resemble the multiphosphorylation domains of glycogen synthase and phosphorylase kinase alpha subunit, and a characteristic tyrosine residue in the putative nucleotide-binding glycine cluster which, by analogy to cdc2 kinase, is a potential tyrosine phosphorylation site.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Harmann B,Kilimann MWdoi
10.1016/0014-5793(90)81096-7subject
Has Abstractpub_date
1990-10-29 00:00:00pages
248-52issue
1-2eissn
0014-5793issn
1873-3468pii
0014-5793(90)81096-7journal_volume
273pub_type
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