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Department of Hematology, Section of Molecular Hematology, The University of Texas M. D. Anderson Cancer Center, Houston, Texas 77030
The human PIM-1 gene, a homologue of murine retroviral insertion site mpim-1, is overexpressed in a subset of hematolymphoid malignancies. Deduced amino acid sequence of PIM-1 complementary DNA predicts it to be a protein kinase. In vitro transcription coupled translation of the putative 313-amino acid open reading frame yields a Mr 34,000 protein; an immune complex kinase assay of the wild-type PIM-1 and not a site-directed mutant, in which the invariant Lys67 has been changed to Arg, demonstrates autophosphorylating activity on serine residues. Thus, PIM-1 is a protein serine kinase with a possible role in neoplastic transformation.
1 This work was supported by NIH Grant CA-49765A.
2 To whom requests for reprints should be addressed, at Department of Hematology, Box 24, M. D. Anderson Cancer Center, 1515 Holcombe Blvd., Houston, TX 77030.
Received 1/28/91. Accepted 3/11/91.
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