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: | APPL1 |
| Gene Name: | APPL1 |
| Protein Full Name: | DCC-interacting protein 13-alpha |
| Alias: | Adapter protein containing PH domain, PTB domain and leucine zipper motif 1; Adaptor protein APPL; Adaptor protein containing pH domain, PTB domain and leucine zipper motif; Adaptor protein, phosphotyrosine interaction, PH domain and leucine zipper containing 1; DIP13 alpha; DP13A; KIAA1428; Signaling adaptor protein DIP13alpha |
| Mass (Da): | 79663 |
| Number AA: | 709 |
| UniProt ID: | Q9UKG1 |
| Locus ID: | 26060 |
| COSMIC ID: | APPL1 |
| Gene location on chromosome: | 3p21.1-p14.3 |
| Number of cancer specimens: | 19688 |
| Percent of cancer specimens with mutations: | 0.55 |
| Commentary on involvement of protein in cancer: | The protein encoded by this gene has been shown to be involved in the regulation of cell proliferation, and in the crosstalk between the adiponectin signalling and insulin signalling pathways. The encoded protein binds many other proteins, including RAB5A, DCC, AKT2, PIK3CA, adiponectin receptors, and proteins of the NuRD/MeCP1 complex. This protein is found associated with endosomal membranes, but can be released by EGF and translocated to the nucleus. It is required for the regulation of cell proliferation in response to extracellular signals from an early endosomal compartment. Links Rab5 to nuclear signal transduction. Binds RAB5A/Rab5 through an N-terminal domain. This interaction is essential for its recruitment to endosomal membranes as well as its role in cell proliferation. Binds DCC and the catalytic domain of the inactive form of AKT2 through its PID domain. Binds PIK3CA and subunits of the NuRD/MeCP1 complex. Interacts with OCRL. Early endosomal membrane-bound and nuclear. Translocated into the nucleus upon release from endosomal membranes following internalization of EGF. |