Human erythroid p55, an abundantly palmitoylated erythrocyte membrane protein, has been identified, cloned and sequenced. p55 appears to be ubiquitously expressed in human tissues and contains both an SH3 motif and an enzymatically active guanylate kinase domain. The presence of the SH3 motif indicates a possible role in the suppression of tyrosine kinase activity and the guanylate kinase domain may play a role in signal transduction and tissue proliferation by modulating guanine nucleotide levels. Localized to the Xq24-qter region of the X chromosome, abnormalities in p55 appear in patients suffering from hemolytic anemia and Dyskeratosis congenita. With the identification and sequencing of p55, nucleic acid probes and anti-p55 antibodies can be used in a variety of hybridization and immunological assays to screen for and detect p55 defects. Conventional and gene techniques can also be developed to treat p55 deficiencies and abnormalities.

dyskeratosis congenita/tyrosine

Human erythroid p55 nucleic acids

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