Human erythroid p55 nucleic acids

Organic compounds -- part of the class 532-570 series – Organic compounds – Carbohydrates or derivatives

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536 235, 536 2435, 435 6, C07H 2102, C07H 2104

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054018358

ABSTRACT:
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.

REFERENCES:
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Chishti, A. et al., "Human Erythroid P55: Homolog of Drosophila Tumor Suppressor Factor is Highly Conserved X-Linked Gene Product with Guanylate Kinase Activity", Blood 80(10):586 (1992).
Bryant, P. J. et al., "A Major Palmitoylated Membrane Protein of Human Erythrocytes Shows Homolog to Yeast Guanylate Kinase and to the Product of a Drosophila Tumor Suppressor Gene", Cell 68:621-622 (1992).
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Woods, D. F. et al., "The Discs-Large Tumor Suppressor Gene of Drosophila Encodes a Guanylate Kinase Homolog Localized at Septate Junctions", Cell 66:451-464 (1991).
Chishti, A. et al., "Purification of Erythrocyte Dematin (Protein 4.9) Reveals in an Endogenous Protein Kinase that Modulates Actin-Bunding Activity", J. Biol. Chem. 264(15):8985-8991 (1989).
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