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Title: Oncoprotein protein kinase

Abstract

An isolated polypeptide (JNK) characterized by having a molecular weight of 46 kD as determined by reducing SDS-PAGE is disclosed. The polypeptide has serine and threonine kinase activity, phosphorylating the c-Jun N-terminal activation domain and polynucleotide sequences. The method of detection of JNK is also provided. JNK phosphorylates c-Jun N-terminal activation domain which affects gene expression from AP-1 sites. 44 figs.

Inventors:
; ;
Issue Date:
Research Org.:
University of California
OSTI Identifier:
441865
Patent Number(s):
5,605,808
Application Number:
PAN: 8-444,393; CNN: Grant CA-50528;Grant CA-58396
Assignee:
Univ. of California, Oakland, CA (United States)
DOE Contract Number:  
FG03-86ER60429
Resource Type:
Patent
Resource Relation:
Other Information: PBD: 25 Feb 1997
Country of Publication:
United States
Language:
English
Subject:
55 BIOLOGY AND MEDICINE, BASIC STUDIES; POLYPEPTIDES; PHOSPHOTRANSFERASES; ENZYME ACTIVITY; AMINO ACID SEQUENCE; PHOSPHORYLATION; GENE REGULATION; CHEMICAL COMPOSITION

Citation Formats

Karin, M, Hibi, M, and Lin, A. Oncoprotein protein kinase. United States: N. p., 1997. Web.
Karin, M, Hibi, M, & Lin, A. Oncoprotein protein kinase. United States.
Karin, M, Hibi, M, and Lin, A. Tue . "Oncoprotein protein kinase". United States.
@article{osti_441865,
title = {Oncoprotein protein kinase},
author = {Karin, M and Hibi, M and Lin, A},
abstractNote = {An isolated polypeptide (JNK) characterized by having a molecular weight of 46 kD as determined by reducing SDS-PAGE is disclosed. The polypeptide has serine and threonine kinase activity, phosphorylating the c-Jun N-terminal activation domain and polynucleotide sequences. The method of detection of JNK is also provided. JNK phosphorylates c-Jun N-terminal activation domain which affects gene expression from AP-1 sites. 44 figs.},
doi = {},
journal = {},
number = ,
volume = ,
place = {United States},
year = {1997},
month = {2}
}