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PMID:11546806

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Citation

Abe, Y, Matsumoto, S, Wei, S, Nezu, K, Miyoshi, A, Kito, K, Ueda, N, Shigemoto, K, Hitsumoto, Y, Nikawa, J and Enomoto, Y (2001) Cloning and characterization of a p53-related protein kinase expressed in interleukin-2-activated cytotoxic T-cells, epithelial tumor cell lines, and the testes. J. Biol. Chem. 276:44003-11

Abstract

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.

Links

PubMed Online version:10.1074/jbc.M105669200

Keywords

Amino Acid Sequence; Animals; Base Sequence; Blotting, Northern; Chromosome Mapping; Cloning, Molecular; DNA Primers; DNA, Complementary; Humans; Immunohistochemistry; In Situ Hybridization, Fluorescence; Interleukin-2/pharmacology; Intracellular Signaling Peptides and Proteins; Lymphocyte Activation; Male; Molecular Sequence Data; Phosphorylation; Phylogeny; Polymerase Chain Reaction; Protein Kinases/chemistry; Protein Kinases/genetics; Protein Kinases/metabolism; Protein-Serine-Threonine Kinases; Sequence Homology, Amino Acid; T-Lymphocytes, Cytotoxic/drug effects; T-Lymphocytes, Cytotoxic/metabolism; Testis/cytology; Testis/drug effects; Testis/metabolism; Transcription, Genetic; Tumor Cells, Cultured; Tumor Suppressor Protein p53/metabolism

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

HUMAN:PRPK

enables

GO:0002039: p53 binding

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

HUMAN:PRPK

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P04637

F

Seeded From UniProt

complete

HUMAN:PRPK

located_in

GO:0005634: nucleus

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

HUMAN:PRPK

involved_in

GO:0006468: protein phosphorylation

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

HUMAN:PRPK

enables

GO:0004674: protein serine/threonine kinase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

MOUSE:PRPK

located_in

GO:0005634: nucleus

ECO:0000266: sequence orthology evidence used in manual assertion

EMBL:AB017505

C

Seeded From UniProt

complete

MOUSE:PRPK

enables

GO:0004674: protein serine/threonine kinase activity

ECO:0000266: sequence orthology evidence used in manual assertion

EMBL:AB017505

F

Seeded From UniProt

complete

MOUSE:PRPK

located_in

GO:0005634: nucleus

ECO:0000250: sequence similarity evidence used in manual assertion

UniProtKB:Q96S44

C

Seeded From UniProt

complete

MOUSE:PRPK

enables

GO:0004674: protein serine/threonine kinase activity

ECO:0000250: sequence similarity evidence used in manual assertion

UniProtKB:Q96S44

F

Seeded From UniProt

complete

MOUSE:PRPK

involved_in

GO:0006468: protein phosphorylation

ECO:0000250: sequence similarity evidence used in manual assertion

UniProtKB:Q96S44

P

Seeded From UniProt

complete

HUMAN:P53

enables

GO:0019901: protein kinase binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q96S44

F

Seeded From UniProt

complete


See also

References

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