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rdf:type |
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lifeskim:mentions |
umls-concept:C0009015,
umls-concept:C0017262,
umls-concept:C0021358,
umls-concept:C0039584,
umls-concept:C0085983,
umls-concept:C1171362,
umls-concept:C1368683,
umls-concept:C1511636,
umls-concept:C1515670,
umls-concept:C1540041,
umls-concept:C1880022
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pubmed:issue |
47
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pubmed:dateCreated |
2001-11-19
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pubmed:databankReference |
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pubmed:abstractText |
A human protein kinase, p53-related protein kinase (PRPK), was cloned from an interleukin-2-activated cytotoxic T-cell subtraction library. PRPK appears to be a homologue of a growth-related yeast serine/threonine protein kinase, YGR262c. However, a complementation assay using YGR262c-disrupted yeast indicated that PRPK is not functionally identical to the yeast enzyme. PRPK expression was observed in interleukin-2-activated cytotoxic T-cells, some human epithelial tumor cell lines, and the testes. The intrinsic transcriptional activity of p53 was up-regulated by a transient transfection of PRPK to COS-7 cells. PRPK was shown to bind to p53 and to phosphorylate p53 at Ser-15. These results indicate that PRPK may play an important role in the cell cycle and cell apoptosis through phosphorylation of p53.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0021-9258
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pubmed:author |
pubmed-author:AbeYY,
pubmed-author:EnomotoYY,
pubmed-author:HitsumotoYY,
pubmed-author:KitaYY,
pubmed-author:MatsumotoSS,
pubmed-author:MiyoshiAA,
pubmed-author:NezuKK,
pubmed-author:NikawaJJ,
pubmed-author:ShigemotoKK,
pubmed-author:UedaNN,
pubmed-author:WeiSS
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pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
276
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
44003-11
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:11546806-Amino Acid Sequence,
pubmed-meshheading:11546806-Animals,
pubmed-meshheading:11546806-Base Sequence,
pubmed-meshheading:11546806-Blotting, Northern,
pubmed-meshheading:11546806-Chromosome Mapping,
pubmed-meshheading:11546806-Cloning, Molecular,
pubmed-meshheading:11546806-DNA, Complementary,
pubmed-meshheading:11546806-DNA Primers,
pubmed-meshheading:11546806-Humans,
pubmed-meshheading:11546806-Immunohistochemistry,
pubmed-meshheading:11546806-In Situ Hybridization, Fluorescence,
pubmed-meshheading:11546806-Interleukin-2,
pubmed-meshheading:11546806-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:11546806-Lymphocyte Activation,
pubmed-meshheading:11546806-Male,
pubmed-meshheading:11546806-Molecular Sequence Data,
pubmed-meshheading:11546806-Phosphorylation,
pubmed-meshheading:11546806-Phylogeny,
pubmed-meshheading:11546806-Polymerase Chain Reaction,
pubmed-meshheading:11546806-Protein Kinases,
pubmed-meshheading:11546806-Protein-Serine-Threonine Kinases,
pubmed-meshheading:11546806-Sequence Homology, Amino Acid,
pubmed-meshheading:11546806-T-Lymphocytes, Cytotoxic,
pubmed-meshheading:11546806-Testis,
pubmed-meshheading:11546806-Transcription, Genetic,
pubmed-meshheading:11546806-Tumor Cells, Cultured,
pubmed-meshheading:11546806-Tumor Suppressor Protein p53
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pubmed:year |
2001
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pubmed:articleTitle |
Cloning and characterization of a p53-related protein kinase expressed in interleukin-2-activated cytotoxic T-cells, epithelial tumor cell lines, and the testes.
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pubmed:affiliation |
First Department of Pathology and Hygiene, Ehime University School of Medicine, Shigenobu, Ehime 791-0295, Japan. yasuhito@m.ehime-u.ac.jp
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pubmed:publicationType |
Journal Article
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