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

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.

journal_name

Cell

journal_title

Cell

authors

Selten G,Cuypers HT,Boelens W,Robanus-Maandag E,Verbeek J,Domen J,van Beveren C,Berns A

doi

10.1016/0092-8674(86)90886-x

subject

Has Abstract

pub_date

1986-08-15 00:00:00

pages

603-11

issue

4

eissn

0092-8674

issn

1097-4172

pii

0092-8674(86)90886-X

journal_volume

46

pub_type

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