The primary structure of the putative oncogene pim-1 shows extensive homology with protein kinases

Cell. 1986 Aug 15;46(4):603-11. doi: 10.1016/0092-8674(86)90886-x.

Abstract

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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Cell Transformation, Viral
  • Cloning, Molecular
  • DNA / genetics
  • Leukemia Virus, Murine / genetics
  • Lymphoma / genetics*
  • Oncogene Proteins, Viral / genetics*
  • Oncogenes
  • RNA Processing, Post-Transcriptional
  • RNA, Messenger / genetics
  • Sequence Homology, Nucleic Acid
  • Transcription, Genetic

Substances

  • Oncogene Proteins, Viral
  • RNA, Messenger
  • DNA

Associated data

  • GENBANK/M13945
  • GENBANK/M13946