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Title: Oncoprotein protein kinase

Patent ·
OSTI ID:872710
 [1];  [2]
  1. San Diego, CA
  2. La Jolla, CA
+ Show Author Affiliations

An isolated polypeptide (JNK) characterized by having a molecular weight of 46 kD or 55 kD as determined by reducing SDS-PAGE, having serine and theonine kinase activity, phosphorylating the c-Jun N-terminal activation domain and polynucleotide sequences and method of detection of JNK are provided herein. JNK phosphorylates c-Jun N-terminal activation domain which affects gene expression from AP-1 sites.

Research Organization:
Univ. of California (United States)
DOE Contract Number:
FG03-86ER60429
Assignee:
University of California (Oakland, CA)
Patent Number(s):
US 5994513
Application Number:
09/150,200
OSTI ID:
872710
Country of Publication:
United States
Language:
English

References (10)

c-Jun N-terminal phosphorylation correlates with activation of the JNK subgroup but not the ERK subgroup of mitogen-activated protein kinases. journal October 1994
pp54 microtubule-associated protein 2 kinase. A novel serine/threonine protein kinase regulated by phosphorylation and stimulated by poly-L-lysine. journal October 1990
An insulin-stimulated protein kinase similar to yeast kinases involved in cell cycle control journal July 1990
Requirement for integration of signals from two distinct phosphorylation pathways for activation of MAP kinase journal February 1990
Identification of an oncoprotein- and UV-responsive protein kinase that binds and potentiates the c-Jun activation domain. journal November 1993
Phorbol esters stimulate the phosphorylation of c-Jun but not v-Jun: regulation by the N-terminal delta domain. journal June 1992
ERKs: A family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGF journal May 1991
Parallel signal processing among mammalian MAPKs journal March 1995
JNK1: A protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain journal March 1994
Phosphorylation of c-jun mediated by MAP kinases journal October 1991

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Related Subjects

oncoprotein
protein
kinase
isolated
polypeptide
jnk
characterized
molecular
weight
46
kd
55
determined
reducing
sds-page
serine
theonine
activity
phosphorylating
c-jun
n-terminal
activation
domain
polynucleotide
sequences
method
detection
provided
phosphorylates
affects
expression
ap-1
sites
phosphorylates c-jun
oncoprotein protein
ap-1 sites
protein kinase
reducing sds-page
kinase activity
jnk phosphorylates
activation domain
nucleotide sequences
nucleotide sequence
n-terminal activation
c-jun n-terminal
molecular weight
isolated polypeptide
polynucleotide sequences
theonine kinase
protein protein
/530/