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PIM1  -  Pim-1 proto-oncogene, serine/threonine kinase

Homo sapiens

Synonyms: Serine/threonine-protein kinase pim-1
 
 
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Disease relevance of PIM1

 

High impact information on PIM1

  • Diploid yeast that carry one wild-type and one disrupted copy of spi1 have multiple satellite nuclei, and mitotic haploidization occurs at very high frequency. spi1 appears to interact with pim1 in the maintenance of a coordinated cell cycle [6].
  • A fission yeast mutant is described in which the onset of mitosis is uncoupled from the completion of DNA replication. pim1 (premature initiation of mitosis) cells can undergo mitotic chromosome condensation and mitotic spindle formation without completion of S phase and without the cdc25 mitotic inducer [6].
  • The pim-1 oncogene is regulated by hematopoietic cytokine receptors, encodes a serine/threonine protein kinase, and cooperates with c-myc in lymphoid cell transformation [7].
  • The pim-1 oncogene encodes two related protein-serine/threonine kinases by alternative initiation at AUG and CUG [8].
  • In addition, a number of mutations in PIM-1 and c-MYC were found to affect coding exons, leading to amino acid substitutions with likely functional consequences [9].
 

Chemical compound and disease context of PIM1

 

Biological context of PIM1

 

Anatomical context of PIM1

  • Furthermore, the ability of quercetagetin to inhibit the growth of other prostate epithelial cell lines varied in proportion to their levels of PIM1 protein [14].
  • Additionally, PIM-1 expression provides supplementary information for distinguishing HGPIN from benign epithelium [4].
  • Subunits composing these proteases are evolutionarily conserved from yeast to humans and, in support of an endosymbiotic origin of mitochondria, evolved from prokaryotic ancestors: the PIM1/Lon protease is active in the matrix of mitochondria, while the i-AAA protease and the m-AAA protease mediate the turnover of inner membrane proteins [15].
  • Nuclear run on assays of nascent RNA from K562 cells revealed premature transcriptional termination within the PIM-1 gene [16].
  • We also showed that in human 293T cells PIM-1 interacts with ribosomes and may be involved in translational control [17].
 

Associations of PIM1 with chemical compounds

  • RWPE2 cells treated with quercetagetin showed pronounced growth inhibition at inhibitor concentrations that blocked PIM1 kinase activity [14].
  • Mutation of the conserved Tyrosine 218 in the activation loop results in reduced kinase activity of Pim1 [2].
  • One crystal structure reported here shows that changing P123 to methionine, a common residue that offers the backbone hydrogen bond to ATP, does not restore the ATP binding pocket of Pim1 to that of a typical kinase [3].
  • Pim1 is unique among protein kinases due to the presence of a proline residue at position 123 that precludes the formation of the canonical second hydrogen bond between the hinge backbone and the adenine moiety of ATP [3].
  • PAP-1 is an in vitro phosphorylation target of the Pim-1 oncogene [18].
 

Physical interactions of PIM1

 

Other interactions of PIM1

 

Analytical, diagnostic and therapeutic context of PIM1

References

  1. Gain of chromosome 6p is an infrequent cause of increased PIM1 expression in B-cell non-Hodgkin's lymphomas. Sivertsen, E.A., Galteland, E., Mu, D., Holte, H., Meza-Zepeda, L., Myklebost, O., Patzke, S., Smeland, E.B., Stokke, T. Leukemia (2006) [Pubmed]
  2. Synergism of cytoplasmic kinases in IL6-induced ligand-independent activation of androgen receptor in prostate cancer cells. Kim, O., Jiang, T., Xie, Y., Guo, Z., Chen, H., Qiu, Y. Oncogene (2004) [Pubmed]
  3. Crystal structures of proto-oncogene kinase Pim1: a target of aberrant somatic hypermutations in diffuse large cell lymphoma. Kumar, A., Mandiyan, V., Suzuki, Y., Zhang, C., Rice, J., Tsai, J., Artis, D.R., Ibrahim, P., Bremer, R. J. Mol. Biol. (2005) [Pubmed]
  4. Pim-1 expression in prostatic intraepithelial neoplasia and human prostate cancer. Valdman, A., Fang, X., Pang, S.T., Ekman, P., Egevad, L. Prostate (2004) [Pubmed]
  5. Regulated protein degradation in mitochondria. Langer, T., Neupert, W. Experientia (1996) [Pubmed]
  6. Premature initiation of mitosis in yeast lacking RCC1 or an interacting GTPase. Matsumoto, T., Beach, D. Cell (1991) [Pubmed]
  7. Pim-1 kinase and p100 cooperate to enhance c-Myb activity. Leverson, J.D., Koskinen, P.J., Orrico, F.C., Rainio, E.M., Jalkanen, K.J., Dash, A.B., Eisenman, R.N., Ness, S.A. Mol. Cell (1998) [Pubmed]
  8. The pim-1 oncogene encodes two related protein-serine/threonine kinases by alternative initiation at AUG and CUG. Saris, C.J., Domen, J., Berns, A. EMBO J. (1991) [Pubmed]
  9. Aberrant somatic hypermutation in multiple subtypes of AIDS-associated non-Hodgkin lymphoma. Gaidano, G., Pasqualucci, L., Capello, D., Berra, E., Deambrogi, C., Rossi, D., Maria Larocca, L., Gloghini, A., Carbone, A., Dalla-Favera, R. Blood (2003) [Pubmed]
  10. The YAL017 gene on the left arm of chromosome I of Saccharomyces cerevisiae encodes a putative serine/threonine protein kinase. Clark, M.W., Zhong, W.W., Keng, T., Storms, R.K., Ouellette, B.F., Barton, A., Kaback, D.B., Bussey, H. Yeast (1993) [Pubmed]
  11. The PIM1 kinase is a critical component of a survival pathway activated by docetaxel and promotes survival of docetaxel-treated prostate cancer cells. Zemskova, M., Sahakian, E., Bashkirova, S., Lilly, M. J. Biol. Chem. (2008) [Pubmed]
  12. Investigatory and analytical approaches to differential gene expression profiling in mantle cell lymphoma. Zhu, Y., Hollmén, J., Räty, R., Aalto, Y., Nagy, B., Elonen, E., Kere, J., Mannila, H., Franssila, K., Knuutila, S. Br. J. Haematol. (2002) [Pubmed]
  13. Cloning and characterization of the human PIM-1 gene: a putative oncogene related to the protein kinases. Meeker, T.C., Nagarajan, L., ar-Rushdi, A., Croce, C.M. J. Cell. Biochem. (1987) [Pubmed]
  14. Characterization of a potent and selective small-molecule inhibitor of the PIM1 kinase. Holder, S., Zemskova, M., Zhang, C., Tabrizizad, M., Bremer, R., Neidigh, J.W., Lilly, M.B. Mol. Cancer Ther. (2007) [Pubmed]
  15. ATP-dependent proteases controlling mitochondrial function in the yeast Saccharomyces cerevisiae. Van Dyck, L., Langer, T. Cell. Mol. Life Sci. (1999) [Pubmed]
  16. Transcriptional attenuation of PIM-1 gene. Nagarajan, L., Narayana, L. Biochem. Biophys. Res. Commun. (1993) [Pubmed]
  17. Interactions between RPS19, mutated in Diamond-Blackfan anemia, and the PIM-1 oncoprotein. Chiocchetti, A., Gibello, L., Carando, A., Aspesi, A., Secco, P., Garelli, E., Loreni, F., Angelini, M., Biava, A., Dahl, N., Dianzani, U., Ramenghi, U., Santoro, C., Dianzani, I. Haematologica (2005) [Pubmed]
  18. PAP-1, the mutated gene underlying the RP9 form of dominant retinitis pigmentosa, is a splicing factor. Maita, H., Kitaura, H., Keen, T.J., Inglehearn, C.F., Ariga, H., Iguchi-Ariga, S.M. Exp. Cell Res. (2004) [Pubmed]
  19. Translocation (1;6)(p12;p23) in ANLL. Jacob, A.K., Sreekantaiah, C., Baer, M.R., Sandberg, A.A. Cancer Genet. Cytogenet. (1990) [Pubmed]
  20. Gene expression profile predicts patient survival of gastric cancer after surgical resection. Chen, C.N., Lin, J.J., Chen, J.J., Lee, P.H., Yang, C.Y., Kuo, M.L., Chang, K.J., Hsieh, F.J. J. Clin. Oncol. (2005) [Pubmed]
  21. Molecular dynamics study of polarizable ion models for molten AgBr. Bitrian, V., Trullàs, J. The journal of physical chemistry. B, Condensed matter, materials, surfaces, interfaces & biophysical. (2006) [Pubmed]
  22. Ubiquitous expression and cell cycle regulation of the protein kinase PIM-1. Liang, H., Hittelman, W., Nagarajan, L. Arch. Biochem. Biophys. (1996) [Pubmed]
  23. Overexpression of PIM-1 is a potential biomarker in prostate carcinoma. Xu, Y., Zhang, T., Tang, H., Zhang, S., Liu, M., Ren, D., Niu, Y. Journal of surgical oncology. (2005) [Pubmed]
 
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