The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

PIM2  -  Pim-2 proto-oncogene, serine/threonine kinase

Homo sapiens

Synonyms: Pim-2h, Serine/threonine-protein kinase pim-2
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of PIM2

  • This was further confirmed using purified PIM2 and PIM6 from M. bovis BCG that decreased by half the internalization of M. smegmatis [1].
  • Disease progression may be related to proangiogenic processes and strong Pim2 expression [2].

High impact information on PIM2

  • Targeted down-regulation of PIM-2 by RNA interference (RNAi) selectively abrogated survival of Ba/F3 cells transformed by various Fms-like tyrosine kinase 3 (FLT3)-activating mutants [internal tandem duplication (ITD) and kinase domain] and attenuated growth of human cell lines containing FLT3 mutations [3].
  • Our observations indicate that combined inactivation of PIM-1 and PIM-2 interferes with oncogenic PTKs and suggest that PIMs are alternative therapeutic targets in PTK-mediated leukemia [3].
  • Cells expressing activated forms of KIT or platelet-derived growth factor receptor (PDGFR), two additional targets of imatinib, were unaffected by SKI-606, whereas activity was found against PIM2 [4].
  • Three of 15 genes up-regulated in the cDNA microarray were involved in the apoptosis signaling pathway (NFkappaB), and its downstream targets defender against cell death 1 and PIM-2 [5].
  • The additional two mannoses in PIM4, relative to PIM2, are located at the distal 6' carbon of the alpha1-alpha6-linked mannose and would project away from the CD1d binding groove for interaction with the TCR [6].

Biological context of PIM2


Associations of PIM2 with chemical compounds

  • Quercetagetin was a highly selective inhibitor of PIM1 compared with PIM2 and seven other serine-threonine kinases [8].
  • When coated on latex beads, PIM2 and polar GPL (GPL III) favored the particle entry through complement receptor 3 [1].
  • Inhibition was essentially attributable to phosphatidylinositol mannosides (PIMs), namely PIM2 and PIM6, because the purified phosphatidylethanolamine, phosphatidylglycerol, and phosphatidylinositol were inactive [1].
  • Addition of genistein and BAY 11-7085 resulted in a decrease in NFkappaB, PIM-2 and defender against cell death 1 as well as a reversal of the inhibition of apoptosis [5].

Other interactions of PIM2

  • RT-PCR was performed, and we found that MDM2, BCL2, PKCZ and PIM2 expression levels were increased in A549 cells and decreased in NCI-H446 cells after irradiation [9].

Analytical, diagnostic and therapeutic context of PIM2


  1. Mycobacteria use their surface-exposed glycolipids to infect human macrophages through a receptor-dependent process. Villeneuve, C., Gilleron, M., Maridonneau-Parini, I., Daffé, M., Astarie-Dequeker, C., Etienne, G. J. Lipid Res. (2005) [Pubmed]
  2. Gene expression signatures separate B-cell chronic lymphocytic leukaemia prognostic subgroups defined by ZAP-70 and CD38 expression status. H??ttmann, A., Klein-Hitpass, L., Thomale, J., Deenen, R., Carpinteiro, A., N??ckel, H., Ebeling, P., F??hrer, A., Edelmann, J., Sellmann, L., D??hrsen, U., D??rig, J. Leukemia (2006) [Pubmed]
  3. Targeting PIM kinases impairs survival of hematopoietic cells transformed by kinase inhibitor-sensitive and kinase inhibitor-resistant forms of Fms-like tyrosine kinase 3 and BCR/ABL. Adam, M., Pogacic, V., Bendit, M., Chappuis, R., Nawijn, M.C., Duyster, J., Fox, C.J., Thompson, C.B., Cools, J., Schwaller, J. Cancer Res. (2006) [Pubmed]
  4. In vitro and In vivo Activity of SKI-606, a Novel Src-Abl Inhibitor, against Imatinib-Resistant Bcr-Abl+ Neoplastic Cells. Puttini, M., Coluccia, A.M., Boschelli, F., Cleris, L., Marchesi, E., Donella-Deana, A., Ahmed, S., Redaelli, S., Piazza, R., Magistroni, V., Andreoni, F., Scapozza, L., Formelli, F., Gambacorti-Passerini, C. Cancer Res. (2006) [Pubmed]
  5. Growth and survival mechanisms associated with perineural invasion in prostate cancer. Ayala, G.E., Dai, H., Ittmann, M., Li, R., Powell, M., Frolov, A., Wheeler, T.M., Thompson, T.C., Rowley, D. Cancer Res. (2004) [Pubmed]
  6. Structural characterization of mycobacterial phosphatidylinositol mannoside binding to mouse CD1d. Zajonc, D.M., Ainge, G.D., Painter, G.F., Severn, W.B., Wilson, I.A. J. Immunol. (2006) [Pubmed]
  7. The PIM-2 kinase phosphorylates BAD on serine 112 and reverses BAD-induced cell death. Yan, B., Zemskova, M., Holder, S., Chin, V., Kraft, A., Koskinen, P.J., Lilly, M. J. Biol. Chem. (2003) [Pubmed]
  8. 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]
  9. Identification of differentially expressed genes contributing to radioresistance in lung cancer cells using microarray analysis. Guo, W.F., Lin, R.X., Huang, J., Zhou, Z., Yang, J., Guo, G.Z., Wang, S.Q. Radiat. Res. (2005) [Pubmed]
  10. PIM2: a revised version of the Paediatric Index of Mortality. Slater, A., Shann, F., Pearson, G. Intensive care medicine. (2003) [Pubmed]
  11. Use of protein C concentrate in pediatric patients with sepsis. Silvani, P., Camporesi, A., Licari, E., Wolfler, A. Minerva anestesiologica. (2005) [Pubmed]
WikiGenes - Universities