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Oncoprotein protein kinase

Patent ·
OSTI ID:870843
 [1];  [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 as determined by reducing SDS-PAGE, having serine and threonine 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:
University of California
DOE Contract Number:
FG03-86ER60429
Assignee:
Regents of University of California (Oakland, CA)
Patent Number(s):
US 5605808
OSTI ID:
870843
Country of Publication:
United States
Language:
English

References (10)

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

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Related Subjects

/435/
46
activation
activation domain
activity
affects
ap-1
ap-1 sites
c-jun
c-jun n-terminal
characterized
detection
determined
domain
expression
isolated
isolated polypeptide
jnk
jnk phosphorylates
kd
kinase
kinase activity
method
molecular
molecular weight
n-terminal
n-terminal activation
nucleotide sequence
nucleotide sequences
oncoprotein
oncoprotein protein
phosphorylates
phosphorylates c-jun
phosphorylating
polynucleotide
polynucleotide sequences
polypeptide
protein
protein kinase
protein protein
provided
reducing
reducing sds-page
sds-page
sequences
serine
sites
threonine
threonine kinase
weight