| Post Translational Modifications | ISGylated in a CHMP5-dependent manner. Isgylation weakens its interaction with VPS4A. |
| Function | Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. In the ESCRT-III complex, it probably serves as an acceptor for the ESCRT-II complex on endosomal membranes. |
| Protein Name | Charged Multivesicular Body Protein 6Chromatin-Modifying Protein 6Vacuolar Protein Sorting-Associated Protein 20Vps20Hvps20 |
| Database Links | Reactome: R-HSA-162588Reactome: R-HSA-1632852Reactome: R-HSA-5620971Reactome: R-HSA-917729Reactome: R-HSA-9610379Reactome: R-HSA-9615710Reactome: R-HSA-9668328Reactome: R-HSA-9679504Reactome: R-HSA-9694676 |
| Cellular Localisation | Endomembrane SystemEndosome MembraneLipid-AnchorLate Endosome MembraneMembraneLocalizes To Endosomal Membranes |
| Alternative Protein Names | Charged Multivesicular Body Protein 6 proteinChromatin-Modifying Protein 6 proteinVacuolar Protein Sorting-Associated Protein 20 proteinVps20 proteinHvps20 proteinCHMP6 proteinVPS20 protein |
Information sourced from Uniprot.org
