STY, a tyrosine-phosphorylating enzyme with sequence homology to serine/threonine kinases. | Zendy

Brian W. Howell | Zendy; Daniel Afar | Zendy; John I. Lew | Zendy; Elizabeth Douville | Zendy; Pamela L. Icely | Zendy; Douglas A. Gray | Zendy; John C. Bell | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

STY, a tyrosine-phosphorylating enzyme with sequence homology to serine/threonine kinases.

Author(s) -

Brian W. Howell,

Daniel Afar,

John I. Lew,

Elizabeth Douville,

Pamela L. Icely,

Douglas A. Gray,

John C. Bell

Publication year - 1991

Publication title -

molecular and cellular biology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.14

H-Index - 327

eISSN - 1067-8824

pISSN - 0270-7306

DOI - 10.1128/mcb.11.1.568

Subject(s) - biology , serine , phosphorylation , akt3 , complementary dna , threonine , kinase , biochemistry , microbiology and biotechnology , akt2 , protein serine threonine kinases , protein phosphorylation , map2k7 , protein kinase a , akt1 , cyclin dependent kinase 2 , gene , protein kinase b

We have cloned a novel kinase (STY) from an embryonal carcinoma cell line. Sequence analysis of the STY cDNA reveals that it shares sequence homology with serine/threonine-type kinases and yet the bacterial expression product of the STY cDNA appears to have serine-, threonine-, and tyrosine-phosphorylating activities. The predicted STY protein is highly basic and contains a putative nuclear localization signal. During differentiation, two new mRNAs were detected in addition to the embryonic transcript.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research