| http://purl.uniprot.org/citations/1323835 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/1323835 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/1323835 | http://www.w3.org/2000/01/rdf-schema#comment | "Protein-tyrosine-phosphatases (PTPases, EC 3.1.3.48) play a crucial role in the regulation of protein tyrosine phosphorylation. Recently, it was found that the PTPase gene family exhibits a large variety of different functional domains associated with the PTPase catalytic domains. In this paper, we report the complete cDNA sequence of a human transmembrane PTPase, PTP zeta, isolated from fetal brain cDNA libraries. The deduced amino acid sequence of human PTP zeta is composed of a putative signal peptide of 19 amino acids, a very large extracellular domain of 1616 amino acids, a transmembrane peptide of 26 amino acids, and a cytoplasmic domain of 653 amino acids. The extracellular portion of human PTP zeta contains two striking structural features: the N-terminal 280-amino acid sequence that is homologous to carbonic anhydrases (carbonate hydro-lyase, EC 4.2.1.1), and a sequence of 1048 amino acids without a cysteine residue. While it is unlikely that the carbonic anhydrase-like domain of PTP zeta has any carbonic anhydrase activity, its three-dimensional structure may be quite similar to that of carbonic anhydrases, a structure that appears ideal for binding a small soluble ligand. The cytoplasmic portion of human PTP zeta contains two repeated PTPase-like domains, which, when expressed in Escherichia coli, had PTPase activity in vitro. Mutational analyses indicate that only the membrane-proximal PTPase domain is catalytically active. Reverse transcription-polymerase chain reaction analyses indicate that human PTP zeta is highly expressed in a glioblastoma cell line."xsd:string |
| http://purl.uniprot.org/citations/1323835 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.89.16.7417"xsd:string |
| http://purl.uniprot.org/citations/1323835 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.89.16.7417"xsd:string |
| http://purl.uniprot.org/citations/1323835 | http://purl.uniprot.org/core/author | "Saito H."xsd:string |
| http://purl.uniprot.org/citations/1323835 | http://purl.uniprot.org/core/author | "Saito H."xsd:string |
| http://purl.uniprot.org/citations/1323835 | http://purl.uniprot.org/core/author | "Krueger N.X."xsd:string |
| http://purl.uniprot.org/citations/1323835 | http://purl.uniprot.org/core/author | "Krueger N.X."xsd:string |
| http://purl.uniprot.org/citations/1323835 | http://purl.uniprot.org/core/date | "1992"xsd:gYear |
| http://purl.uniprot.org/citations/1323835 | http://purl.uniprot.org/core/date | "1992"xsd:gYear |
| http://purl.uniprot.org/citations/1323835 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
| http://purl.uniprot.org/citations/1323835 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
| http://purl.uniprot.org/citations/1323835 | http://purl.uniprot.org/core/pages | "7417-7421"xsd:string |
| http://purl.uniprot.org/citations/1323835 | http://purl.uniprot.org/core/pages | "7417-7421"xsd:string |
| http://purl.uniprot.org/citations/1323835 | http://purl.uniprot.org/core/title | "A human transmembrane protein-tyrosine-phosphatase, PTP zeta, is expressed in brain and has an N-terminal receptor domain homologous to carbonic anhydrases."xsd:string |
| http://purl.uniprot.org/citations/1323835 | http://purl.uniprot.org/core/title | "A human transmembrane protein-tyrosine-phosphatase, PTP zeta, is expressed in brain and has an N-terminal receptor domain homologous to carbonic anhydrases."xsd:string |
| http://purl.uniprot.org/citations/1323835 | http://purl.uniprot.org/core/volume | "89"xsd:string |
| http://purl.uniprot.org/citations/1323835 | http://purl.uniprot.org/core/volume | "89"xsd:string |
| http://purl.uniprot.org/citations/1323835 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/1323835 |
| http://purl.uniprot.org/citations/1323835 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/1323835 |
| http://purl.uniprot.org/citations/1323835 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/1323835 |
| http://purl.uniprot.org/citations/1323835 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/1323835 |
| http://purl.uniprot.org/uniprot/P23471 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/1323835 |
| http://purl.uniprot.org/embl-cds/AAA60225.1 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/1323835 |