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Citation
Ponting, C.P. (1995). SAM: A novel motif in yeast sterile and Drosophila polyhomeotic proteins.  Protein Sci. 4(9): 1928--1930.
FlyBase ID
FBrf0084275
Publication Type
Research paper
Abstract
Single copies of an approximately 65-70 residue domain are shown to be present in the sequences of 14 eukaryotic proteins, including yeast byr2, STE11, ste4, and STE50, which are essential participants in sexual differentiation. This domain, named SAM (sterile alpha motif), appears to participate in other developmental processes because it is also present in Drosophila polyhomeotic gene product and related homologues, which are thought to regulate determination of segmental specification in early embryogenesis. Its appearance in byr2 and STE11, which are MEK kinases, and in proteins containing pleckstrain homology, src homology 3, and discs-large homologous region domains, suggests possible participation in signal transduction pathways.
PubMed ID
PubMed Central ID
PMC2143222 (PMC) (EuropePMC)
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Secondary IDs
    Language of Publication
    English
    Additional Languages of Abstract
    Parent Publication
    Publication Type
    Journal
    Abbreviation
    Protein Sci.
    Title
    Protein Science
    Publication Year
    1992-
    ISBN/ISSN
    0961-8368
    Data From Reference
    Genes (3)