Oncoprotein protein kinase

Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or... – Involving transferase

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435975, C12Q 148

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active

060015845

ABSTRACT:
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.

REFERENCES:
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Cano, E., et al., Parallel signal processing among mammalian MAPKs, TIBS, vol. 20, (1995), 117-122.
Hibi, M., et al.,Identification of an oncoprotein-and UV-responsive protein kinase that binds and potentiates the c-Jun activation domain, Genes and Development 7:2135-2148 (1993).
Minden, A., et al., c-Jun N-Terminal Phosphorylation Correlates with Activation of the JNK Subgroup but Not the ERK Subgroup of Mitogen-Activated Protein Kinase, Molecular and Cellular Biology, Oct. 1994, 14 (10), 6683-6688.
Adler et al., Phorbol esters stimulate the phosphorylation of c-Jun but not v-Jun: Regulation by the N-terminal .delta. domain, Proc. Natl. Acad. Sci. USA., vol. 89, pp. 5341-5345, Jun. 1992, Biochemistry.
Boulton, et al., ERKs: A Family of Protein-Serine/Threonine Kinases That Are Activated and Tyrosine Phosphorylated in Response to Insulin and NGF, Cell, vol. 65, pp. 663-675, May 17, 1991.
Boulton, T.G., et al., An insulin-Stimulated Protein Kinase Similar to Yeast Kinases Involved in Cell Cycle Control, Science, vol. 249, Jul. 6, 1990, pp. 64-67.
Anderson et al., Requirement for integration of signals from two distinct phosphorylation pathways for activation of MAP kinase, Nature, vol. 343, Feb. 15, 1990, pp. 651-653.
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Kyriakis et al., pp.54, Microtubule-associated Protein 2 Kinase, The Journal of Biological Chemistry, vol. 265, No. 28, Oct. pp. 17355-17363.

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