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The protooncogene product Myc associates with many proteins. The isolation of the mouse MM-1; c-Myc binding protein (Myc-Modulator 1) cDNA is described. The cDNA contains a 462 bp open reading frame that encodes a polypeptide of 154 amino acid residues. The deduced amino acid sequence indicates that mouse MM-1 has a 99% identity with the sequence of human MM-1. The expression of mouse MM-1 mRNA was detected in the fetal liver, but its level was 3-fold higher than that in the normal adult liver, and was slightly increased after a partial hepatectomy. It is expressed widely in a variety of adult mouse tissues. Thus, MM-1 may play a role in liver development and growth. A bioinformatics analysis indicates that mouse MM-1 gene consists of 6 exons. Furthermore, the chromosomal location of the mouse MM-1 gene was on the F2-F3 band of chromosome 15, as determined by fluorescence in situ hybridization.

We report the isolation of human pleckstrin 2 cDNA. The cDNA contains a 1059 bp open reading frame encoding a polypeptide of 353 amino acid residues. The deduced amino acid sequence indicates that pleckstrin 2 contains two pleckstrin homology domains and a DEP (dishvelled, egl-10, and pleckstrin) domain and had a 95% identity with the sequence of mouse pleckstrin 2. Northern blot and a reverse transcription-coupled polymerase chain reaction analysis revealed that pleckstrin 2 mRNA is widely expressed in a variety of cell lines. The chromosomal location of the mouse pleckstrin 2 gene was on the D3 band of chromosome 12, as determined by fluorescence in situ hybridization and the human pleckstrin 2 gene was mapped to chromosome 14q24.1 by a bioinformatics analysis.