Cancer Protein Description
This report provides a detailed description of a selected cancer protein with information collected from various sources, including UniProt, the Wellcome Trust Sanger Institute’s Catalogue of Somatic Mutations in Cancer (COSMIC), and the Atlas of Genetics and Cytogenetics in Oncology and Haematology.
| Protein Name: | PTPN11 |
| Gene Name: | PTPN11 |
| Protein Full Name: | Tyrosine-protein phosphatase non-receptor type 11 |
| Alias: | BPTP3; EC 3.1.3.48; NS1; Protein-tyrosine phosphatase 1D; Protein-tyrosine phosphatase 2C; Protein-tyrosine phosphatase, non-receptor 11; PTN11; PTP1D; PTP-1D; PTP2C; PTP-2C; SHP2; SHPTP2; SH-PTP2; SH-PTP3; Syp |
| Mass (Da): | 68436 |
| Number AA: | 597 |
| UniProt ID: | Q06124 |
| Locus ID: | 5781 |
| COSMIC ID: | PTPN11 |
| Gene location on chromosome: | 12q24.1 |
| Cancer protein type: | UNCLEAR |
| Effect of cancer mutation on protein: | UNCLEAR |
| Effect of active protein on cancer: | UNCLEAR |
| Number of cancer specimens: | 33061 |
| Percent of cancer specimens with mutations: | 2.29 |
| General distribution of mutations: | Multi-site |
| Location of most mutations: | Two main clusters at AA 60-76 and AA 502-510 with point mutations. No complex mutations, deletions or insertions have been described. |
| Commonly recorded point mutations: | E76K (93); D61V (73); |
| Normal role description: | PTPN11 is a protein-tyrosine phosphatase. PTPN1 is broadly expressed in the majority of tissues, where it plays a regulatory role in various cell-signalling events that, in turn, impacts a diversity of cell functions, including: mitogenic activation, metabolic control, transcription regulation, and cell migration. Mutations in this gene are associated with acute myeloid leukemia. |
| Commentary on involvement of protein in cancer: | E76K in JMML. E76 is located in the first SH2 domain. The SH2 domains repress phosphatase activity. Binding of these domains to phosphotyrosine-containing proteins relieves this auto-inhibition, possibly by inducing a conformational change in the enzyme. Perhaps the E76 residue mediates the repressiv activity of the SH2 domain. Q510 is thought to be involved in substrate binding. |