A basic problem of proteomics is identifying the subcellular locations of a protein. One factor making the problem more complicated is that some proteins may simultaneously exist in two or more than two subcellular locations. To improve multisite prediction quality, it is necessary to use effective feature extraction methods. Here, we developed a new feature extraction method based on the pK value and frequencies of amino acids to represent a protein as a real values vector.
GRAS proteins are plant-specific transcription factors that are involved in the regulation of root and shoot growth. Here, we cloned BkGRAS2 from Betula kirghisorum (abbreviated to Bk) and analyzed the physicochemical properties and expression pattern of the encoded protein. BkGRAS2 had an open reading frame of 1614 bp encoding 537 amino acid residues. The deduced BkGRAS2 protein was hydrophilic, and it contained highly conserved VHIID and SAW motifs. BkGRAS1 and BkGRAS2 showed considerable sequence similarities.