Identification of the Human YVH1 Protein-tyrosine Phosphatase Orthologue Reveals a Novel Zinc Binding Domain Essential for in Vivo Function
A human orthologue of the Saccharomyces cerevisiae YVH1 protein-tyrosine phosphatase is able to rescue the slow growth defect caused by the disruption of the S. cerevisiae YVH1 gene. The human YVH1 gene is located on chromosome 1q21-q22, which falls in a region amplified in human liposarcomas. The e...
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Veröffentlicht in: | The Journal of biological chemistry 1999-08, Vol.274 (34), p.23991-23995 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | A human orthologue of the Saccharomyces cerevisiae YVH1 protein-tyrosine phosphatase is able to rescue the slow growth defect caused by the disruption of the S. cerevisiae YVH1 gene. The human YVH1 gene is located on chromosome 1q21-q22, which falls in a region amplified in human liposarcomas. The evolutionary conserved COOH-terminal noncatalytic domain of human YVH1 is essential for in vivo function. The cysteine-rich COOH-terminal domain is capable of coordinating 2 mol of zinc/mol of protein, defining it as a novel zinc finger domain. Human YVH1 is the first protein-tyrosine phosphatase that contains and is regulated by a zinc finger domain. |
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ISSN: | 0021-9258 1083-351X |
DOI: | 10.1074/jbc.274.34.23991 |