| Post Translational Modifications | Heavily O-glycosylated.expresses both type 1 and type 2 core glycans. Heavily N-glycosylated.expresses primarily high mannose and complex bisecting type N-linked glycans. May be phosphorylated. Phosphorylation of the intracellular C-terminal domain may induce proteolytic cleavage and the liberation of the extracellular domain into the extracellular space. May contain numerous disulfide bridges. Association of several molecules of the secreted form may occur through interchain disulfide bridges providing an extraordinarily large gel-like matrix in the extracellular space or in the lumen of secretory ducts. |
| Function | Thought to provide a protective, lubricating barrier against particles and infectious agents at mucosal surfaces. |
| Protein Name | Mucin-16Muc-16Ovarian Cancer-Related Tumor Marker Ca125Ca-125Ovarian Carcinoma Antigen Ca125 |
| Database Links | Reactome: R-HSA-5083625Reactome: R-HSA-5083632Reactome: R-HSA-5083636Reactome: R-HSA-5621480Reactome: R-HSA-913709Reactome: R-HSA-977068 |
| Cellular Localisation | Cell MembraneSingle-Pass Type I Membrane ProteinSecretedExtracellular SpaceMay Be Liberated Into The Extracellular Space Following The Phosphorylation Of The Intracellular C-Terminus Which Induces The Proteolytic Cleavage And Liberation Of The Extracellular Domain |
| Alternative Protein Names | Mucin-16 proteinMuc-16 proteinOvarian Cancer-Related Tumor Marker Ca125 proteinCa-125 proteinOvarian Carcinoma Antigen Ca125 proteinMUC16 proteinCA125 protein |
Information sourced from Uniprot.org
