Abstract
A novel protein kinase named BRPK was isolated and partially characterized. BRPK was expressed at a higher level in three carcinoma cell lines with higher metastatic potential. Mouse and human BRPK cDNAs are well conserved and encode 580 and 581 amino acids, respectively. BRPK has a serine/threonine-type protein kinase domain, and the recombinant proteins of BRPK were capable of autophosphorylation. The results of a comparative sequence analysis indicated a possible link of BRPK to BRAP2. BRAP2 is known to bind the nuclear localization signal of BRCA1. We cloned mouse BRAP2 cDNA and showed the presence of isoforms.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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BRCA1 Protein / chemistry
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Carrier Proteins / chemistry
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Cell Line
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Cloning, Molecular
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Colonic Neoplasms / enzymology*
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Colonic Neoplasms / genetics
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Colonic Neoplasms / secondary
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DNA, Complementary
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Gene Expression Regulation, Enzymologic
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Humans
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Melanoma / enzymology*
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Melanoma / genetics
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Melanoma / secondary
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Mice
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Molecular Sequence Data
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Phosphorylation
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Protein Kinases / genetics*
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Protein Kinases / metabolism
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Sequence Homology, Amino Acid
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Skin Neoplasms / enzymology*
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Skin Neoplasms / genetics
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Skin Neoplasms / secondary
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Transfection
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Tumor Cells, Cultured
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Ubiquitin-Protein Ligases
Substances
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BRCA1 Protein
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Carrier Proteins
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DNA, Complementary
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BRAP protein, human
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Ubiquitin-Protein Ligases
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Protein Kinases