Molecular cloning of a novel protein‐tyrosine phosphatase containing a membrane‐binding domain and GLGF repeats

A full‐length cDNA encoding a novel cytosolic protein‐tyrosine phosphatase (PTP), PTP‐BAS, was cloned from human basophils. Due to in‐frame deletions in the coding region, PTP‐BAS exists in three isoforms: 7,455 bp (2,485 aa) for type 1, 7,398 bp (2,466 aa) for type 2 and 6,882 bp (2,294 aa) for type 3. All three isoforms contain a single PTP catalytic domain at the carboxyl termini as well as two distinct structural sequences. Amino terminal sequences of 300 amino acids are homologous to membrane‐binding domains of eytoskeleton‐associated proteins. Three 90 amino acid internal repetitive sequences are homologous to the GLGF repeats found in guanylate kinase proteins. PTP‐BAS was expressed in various human tissues, especially highly in the kidney and lung. Interestingly, the BAS mRNA level in the fetal brain was remarkably high.

• Publication year

  1994

• Venue

  FEBS Letters

• Publication date

  1994-01-10

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/0014-5793(94)80273-4PMID 8287977
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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