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

Marco Muda, Elise R. Manning, Kim Orth, Jack E. Dixon

Research output: Contribution to journalArticle

38 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)23991-23995
Number of pages5
JournalJournal of Biological Chemistry
Volume274
Issue number34
DOIs
Publication statusPublished - Aug 20 1999

    Fingerprint

ASJC Scopus subject areas

  • Biochemistry

Cite this