The primary structure of the putative oncogene pim-1 shows extensive homology with protein kinases.
We have shown previously that the putative oncogene pim-1 is frequently activated by provirus insertion in murine leukemia virus-induced T cell lymphomas. Here we describe the structure of the pim-1 gene as determined by sequencing genomic and cDNA clones. The gene has an open reading frame, encoding a protein of 313 amino acids, extending over six exons and preceded and followed by stop codons in all reading frames. Proviruses always integrate outside the protein-encoding domain, showing a high preference for a small region in the 3'-terminal exon; integration in the 3' exon results in relatively high levels of pim-1 mRNA. Computer search reveals homology between pim-1 and protein kinases: all the domains characteristic of protein kinases are conserved in the pim-1 amino acid sequence. The highest homologies were observed with the protein-serine kinases.
D000595:Amino Acid Sequence; D002472:Cell Transformation, Viral; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics; D009052:Leukemia Virus, Murine / Q000235:genetics; D008223:Lymphoma / Q000235:genetics*; D009856:Oncogene Proteins, Viral / Q000235:genetics*; D009857:Oncogenes; D012323:RNA Processing, Post-Transcriptional; D012333:RNA, Messenger / Q000235:genetics; D012689:Sequence Homology, Nucleic Acid; D014158:Transcription, Genetic
D009856:Oncogene Proteins, Viral; D012333:RNA, Messenger; D004247:DNA