Molecular cloning and characterization of a novel cbl-family gene, cbl-c.

We have cloned a novel gene, cbl-c, of mammalian cbl-family. The cbl-c gene is predicted to encode a protein of 52 kDa that has a phosphotyrosine-binding domain, a RING finger and a proline-rich region. Cbl-c shows 50% homology to the amino-terminal sequences of Cbl and Cbl-b, but a sequence corresponding ...
to the carboxy-terminal half of Cbl and Cbl-b is largely missing in Cbl-c. The expression of cbl-c mRNA is distinct from that of cbl and cbl-b mRNAs, being high in the colon and small intestine, but undetectable in brain and lymphoid tissues. The cbl-c gene is mapped in 19q13.2-13.3. Finally, the 52 kDa Cbl-c protein binds to the EGF receptor and Fyn tyrosine kinase. We conclude that Cbl-c is a novel Cbl-family adaptor protein that would regulate intracellular signaling mediated by various tyrosine kinases.
Mesh Terms:
Amino Acid Sequence, Base Sequence, Chromosome Mapping, Chromosomes, Human, Pair 19, Cloning, Molecular, DNA, Complementary, Female, Gene Expression, Humans, In Situ Hybridization, Fluorescence, Male, Molecular Sequence Data, Protein Binding, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-cbl, Proto-Oncogene Proteins c-fyn, RNA, Messenger, Receptor, Epidermal Growth Factor, Sequence Alignment, Sequence Analysis, DNA, Sequence Homology, Amino Acid, Tissue Distribution, Ubiquitin-Protein Ligases
Gene
Date: Oct. 18, 1999
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