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: | SERPINA1 |
| Gene Name: | SERPINA1 |
| Protein Full Name: | Alpha-1-antitrypsin |
| Alias: | A1A; A1AT; AAT; Alpha-1 protease inhibitor; Alpha-1-antiproteinase; Alpha-1-antitrypsin; PI; PI1; Protease inhibitor 1 (anti-elastase), alpha-1-antitrypsin; Serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin) member 1 |
| Mass (Da): | 46737 |
| Number AA: | 418 |
| UniProt ID: | P01009 |
| Locus ID: | 5265 |
| COSMIC ID: | SERPINA1 |
| Gene location on chromosome: | 14q32.1 |
| Number of cancer specimens: | 19718 |
| Percent of cancer specimens with mutations: | 0.61 |
| Normal role description: | Protease inhibitor. Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. The aberrant form inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin. Short peptide from AAT (SPAAT) is a reversible chymotrypsin inhibitor. It also inhibits elastase, but not trypsin. Its major physiological function is the protection of the lower respiratory tract against proteolytic destruction by human leukocyte elastase (HLE). |
| Commentary on involvement of protein in cancer: | Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. The aberrant form inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin. |