The SHB adaptor protein maps to human chromosome 9
- Imperial College, London (United Kingdom)
Many proteins involved in the regulation of cellular proliferation contain sequence motifs named SH2 and SH3. These domains mediate interaction with other proteins: the SH2 domain interacts with tyrosine phosphorylation sites, while SH3 domains interact with proline-rich sequences. Many signal transduction pathways involve the induction of the formation of complexes of proteins such as growth factor receptors, adaptor proteins, and target enzymes through SH2 and SH3 interactions. Adaptor proteins are molecules with multiple protein interaction motifs that do not appear to have any catalytic activity of their own but mediate the interaction of other proteins. The recently identified SHB gene encodes two such adaptor proteins (from two different start methionines) of 67 and 56 kDa. Both proteins possess one SH2 domain at the carboxy terminus and a proline-rich motif that is likely to be a site that binds to SH3 domains in other proteins. While the exact function of the SHB proteins has not been determined yet, it is likely that they play an important role in the transduction of signals from a tyrosine kinase receptor to an unknown cytoplasmic enzyme. As the proteins of signal transduction pathways can be involved in human pathology, particularly oncogenesis, it is important to map their genes to determine proximity to known sites of mutation, such as loss of heterozygosity or chromosomal translocation. Therefore, we have resolved the mapping position of the SHB gene in the human genome to the proximal short arm of chromosome 9. 9 refs., 2 figs.
- OSTI ID:
- 241058
- Journal Information:
- Genomics, Journal Name: Genomics Journal Issue: 3 Vol. 24; ISSN 0888-7543; ISSN GNMCEP
- Country of Publication:
- United States
- Language:
- English
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