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Primary structure of the chicken c-mil protein:identification of domains shared with or absent from the retroviral v-mil protein

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Koenen,  Michael
Molecular anatomy of the neuromuscular junction, Max Planck Institute for Medical Research, Max Planck Society;
Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society;
Working Group Witzemann / Koenen, Max Planck Institute for Medical Research, Max Planck Society;
Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Koenen, M., Sippel, A. E., Trachmann, C., & Bister, K. (1988). Primary structure of the chicken c-mil protein:identification of domains shared with or absent from the retroviral v-mil protein. Oncogene, 2(2), 179-185. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/3285296.


Cite as: http://hdl.handle.net/21.11116/0000-0000-B18D-9
Abstract
The complete primary structure of the protein product of the proto−oncogene c−mil was deduced from the nucleotide sequence of chicken c−mil cDNA clones. The c−mil protein contains 647 amino acid residues and has a calculated molecular weight of 73,132. Based on sequence comparisons with proteins of known or presumed biochemical function, two domains were recognized on the c−mil protein. In the carboxyl−terminal half of the protein, a 250−amino acid segment displays significant homology to the protein kinase domains of the src oncogene protein or of protein kinase C. In the amino−terminal half, a cysteine−rich segment (Cys−X2−Cys−X9−Cys−X2−Cys−X7−Cys−X7−Cys) of the c−mil protein shares significant homology with two similar repetitive domains of protein kinase C. Of the two structural and presumably functional domains of the c−mil protein, only the kinase domain is contained within the carboxyl−terminal 379−amino acid polypeptide encoded by the transduced v−mil allele of avian oncogenic retrovirus MH2. Hence, truncation of the 5' coding region in the course of the transduction and the resulting lack of the authentic amino−terminal domain in the protein product of the transduced allele may be a critical event in changing mil function from physiologic to oncogenic