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Protein Page:
Pim1 (human)

Overview
Pim1 a proto-oncogene serine/threonine kinase involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression and by phosphorylation and inhibition of proapoptotic proteins (BAD, MAP3K5, FOXO3). Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase of transcriptional activity. The stabilization of MYC exerced by PIM1 might explain partly the strong synergism between these two oncogenes in tumorigenesis. Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl- X(L)/BCL2L1. Phosphorylation of ASK1 an other proapoptotic protein, by PIM1, significantly decreases ASK1 kinase activity and inhibits MAP3K5-mediated phosphorylation of JNK and JNK/p38MAPK subsequently reducing caspase-3 activation and cell apoptosis. Stimulates cell cycle progression at the G1-S and G2-M transitions by phosphorylation of CDC25A and CDC25C. Phosphorylation of p21Cip1, a regulator of cell cycle progression at G1, results in the relocation of p21Cip1 to the cytoplasm and enhanced p21Cip1 protein stability. Promote cell cycle progression and tumorigenesis by down-regulating expression of a regulator of cell cycle progression, p27Kip1, at both transcriptional and post- translational levels. Phosphorylation of p27Kip1,induces 14-3-3- proteins binding, nuclear export and proteasome-dependent degradation. May affect the structure or silencing of chromatin by phosphorylating HP1 gamma/CBX3. Acts also as a regulator of homing and migration of bone marrow cells involving functional interaction with the CXCL12-CXCR4 signaling axis. Isoform 2 is isolated as a monomer whereas isoform 1 complexes with other proteins. Binds to RP9. Isoform 1, but not isoform 2, binds BMX. Isoform 2 interacts with p27Kip1 and FOXO3. Interacts with BAD. Interacts with PPP2CA; this interaction promotes dephosphorylation of PIM1, ubiquitination and proteasomal degradation. Interacts with HSP90, this interaction stabilizes PIM1 protein levels. Ubiquitinated form interacts with HSP70 and promotes its proteosomal degradation. Strongly induced in leukocytes by the JAK/STAT pathway in response to cytokines. Induced by different cellular stresses, heat shock and cytotoxic agents. Expressed primarily in cells of the hematopoietic and germline lineages. 2 isoforms of the human protein are produced by alternative initiation. Both isoforms are expressed in prostate cancer cell lines. Note: This description may include information from UniProtKB.
Protein type: CAMK group; EC 2.7.11.1; Kinase, protein; Oncoprotein; PIM family; Protein kinase, CAMK; Protein kinase, Ser/Thr (non-receptor)
Chromosomal Location of Human Ortholog: 6p21.2
Cellular Component: cytoplasm
Molecular Function: ATP binding; manganese ion binding; protein binding; protein serine/threonine kinase activity; ribosomal small subunit binding; transcription factor binding
Biological Process: cell proliferation; multicellular organismal development; negative regulation of apoptosis; negative regulation of transcription factor activity; protein amino acid autophosphorylation; protein amino acid phosphorylation
Reference #:  P11309 (UniProtKB)
Alt. Names/Synonyms: Oncogene PIM1; PIM; pim-1 kinase 44 kDa isoform; pim-1 oncogene; pim-1 oncogene (proviral integration site 1); PIM1; Proto-oncogene serine/threonine-protein kinase pim-1
Gene Symbols: PIM1
Molecular weight: 45,412 Da
Basal Isoelectric point: 6.52  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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Pim1

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