Review Article

Expression of Tra2β in Cancer Cells as a Potential Contributory Factor to Neoplasia and Metastasis

Figure 3

Protein domain architecture of known Tra2β splicing targets which are expressed in cancer cells. (a) Modular structure of NASP protein assembled from the UniProt database (http://www.uniprot.org/uniprot/P49321) [46], showing the position of the peptide insert encoded by the Tra2β-target exon NASP-T. (b) Modular structure of CD44 protein assembled using information from the UniProt database (http://www.uniprot.org/uniprot/P16070#P16070-6) [46], showing the position of peptide sequences encoded by the Tra2β-target exons CD44 v4 and v5. The CD44 antigen is displayed on the cell surface, and the protein is anchored on the cell surface by a single trans-membrane domain. Alternative isoforms are made through alternative splicing of 10 exons out of 19 encoding amino acids in the extracellular domain and also 2 exons which encode peptide sequence in the cytoplasmic domain. The two exons reported CD44 v4 and v5 exons correspond to amino acids 386–428 and 429–472, respectively, in the encoded protein. The protein domain structures are not drawn to scale.
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