Oncoprotein protein kinase
AssigneeThe Regents of the University of California
InventorsMichael Karin, Masahiko Hibi, Anning Lin
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Abstract
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.
Claims27
An isolated polynucleotide encoding a c-Jun N-terminal kinase, wherein said polynucleotide hybridizes to SEQ ID No. 13 and SEQ ID No. 14 under stringent conditions and wherein said polynucleotide encodes a polypeptide that phosphorylates the c-Jun N-terminal activation domain.
An isolated polynucleotide encoding a c-Jun N-terminal kinase, wherein said polynucleotide hybridizes to the complement of SEQ ID No. 11 under stringent conditions and wherein said polynucleotide encodes a polypeptide that phosphorylates the c-Jun N-terminal activation domain.
An isolated nucleic acid encoding a c-Jun N-terminal kinase wherein said nucleic acid hybridizes to the complement of SEQ ID No. 11 under stringent conditions and wherein said nucleic acid encodes a polypeptide that phosphorylates the c-Jun N-terminal activation domain.
An isolated nucleic acid encoding a c-Jun N-terminal Kinase wherein said nucleic acid hybridizes to the complement of SEQ ID No. 17 under stringent conditions and wherein said nucleic acid encodes a polypeptide that phosphorylates the c-Jun N-terminal activation domain.
An isolated polypeptide with serine threonine kinase activity that binds to residues 33-79 of c-Jun (SEQ ID No. 1) and is capable of phosphorylating the c-Jun N-terminal activation domain.
Dependencies are inferred from the claim text.