1. Academic Validation
  2. Identification of the human YVH1 protein-tyrosine phosphatase orthologue reveals a novel zinc binding domain essential for in vivo function

Identification of the human YVH1 protein-tyrosine phosphatase orthologue reveals a novel zinc binding domain essential for in vivo function

  • J Biol Chem. 1999 Aug 20;274(34):23991-5. doi: 10.1074/jbc.274.34.23991.
M Muda 1 E R Manning K Orth J E Dixon
Affiliations

Affiliation

  • 1 Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor, Michigan 48109-0606, USA.
Abstract

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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