The reference OMIM entry for this protein is 600267

Protein-tyrosine phosphatase, nonreceptor-type, 13; ptpn13
Protein-tyrosine phosphatase ptpl1
Fas-associated protein-tyrosine phosphatase 1; fap1

CLONING

Using a PCR-based approach, Saras et al. (1994) cloned a cytoplasmic protein tyrosine phosphatase of nonreceptor type, which they designated PTPL1. Overlapping cDNA clones encompassed an open reading frame of 7,398 bp, predicting a 2,466-amino acid protein with a molecular mass of 275 kD. PTPL1 was found to have a wide tissue distribution, a 9.5-kb transcript being expressed in most tissues. PTPL1 has a protein-tyrosine phosphatase domain located in the C terminus. In the nonenzymatic part of PTPL1, 3 different structural motifs were identified; 2 of these are often found in proteins at the interface between the plasma membrane and the cytoskeleton, namely, a domain with similarity to the band 4.1 (130500) superfamily, and a region consisting of 5 copies of an 80-amino acid repeat found in a variety of cytoskeleton-associated proteins. In addition, PTPL1 has a leucine zipper motif. Saras et al. (1994) noted that PTPL1 was the largest known PTP and the only one known to contain a leucine zipper motif. Its structure suggests that it may be able to form dimers and may localize to the submembranous cytoskeleton. Both Banville et al. (1994) and Maekawa et al. (1994) isolated the same nonreceptor-type protein-tyrosine phosphatase, PTPN13, which they referred to as hPTP1E and PTP-BAS, respectively. Maekawa et al. (1994) originally isolated a PCR product from basophil mRNA using degenerate primers and RT-PCR. This was used as a probe to screen a basophil-enriched KU812E cell cDNA library. The fully characterized cDNA was over 8.1 kb and encoded a 2,485-amino acid predicted reading frame. The Banville et al. (1994) cDNA was isolated by screening a ZR-75-1 breast carcinoma cell line at low stringency with a probe for LAR cDNA (179590). The cDNA they identified was over 8.3 kb long and encoded a 2,490-amino acid reading frame. Both groups noted that the N-terminal region contains motifs showing similarity to the GLGF motifs found in guanylate kinase proteins that may play a role in the subcellular distribution of these proteins within specialized structures of the cell membrane where cell-cell interactions occur. Maekawa et al. (1994) presented evidence for alternative splicing producing at least 3 different isoforms of PTPN13. Banville et al. (1994) expressed the protein in E. coli and showed that the recombinant protein had the expected protein-tyrosine phosphatase activity. Northern blot analysis showed expression in a variety of tissues with especially high levels in the kidney, lung, and fetal brain. PTPN13 binds to a negative regulatory domain in Fas that inhibits Fas-induced apoptosis; it has therefore also been called Fas-associated protein-tyrosine-1 (FAP1) (Inazawa et al., 1996).

GENE STRUCTURE

Yoshida et al. (2002) determined that the PTPN13 gene is located only 633 bp upstream from JNK3 (602897) in a head-to-head orientation. A short G/C-rich region between the cap sites of the 2 genes suggested that they might share a bidirectional promoter region that appears to contain multiple cis elements. They found that the PTPN13 gene, which contains 48 exons, initiates transcription within exon 2 and terminates in exon 48.

MAPPING

Banville et al. (1994) assigned the PTPN13 gene to chromosome 11 by PCR of somatic cell hybrid DNAs. In an erratum, they stated that the gene had been assigned to chromosome 4 and not 11 as reported. Inazawa et al. (1996) localized the PTPN13 gene to 4q21.3 by both fluorescenc ... More on the omim web site

Subscribe to this protein entry history

July 1, 2020: Protein entry updated
Automatic update: OMIM entry 600267 was added.

Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).