SCUBA

CHMP2B — Charged multivesicular body protein 2B

CHMP2B belongs to a gene co-expression module in 2 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.

CHMP2B's module in each cell type

Cell typeModuleShares the module with
CD4⁺ T cellsmRNA Processing
RNA processing
ABI1, AGFG1, CCND3, CD164, DBF4, GHITM, HNRNPL, LSM1 +9 moreView in SCUBA
MacrophagesAutophagy Lysosomal Regulation
Lysosomal & pahgocytosis
ADIPOR1, ARL8A, ATOSB, BCL10, BROX, CCR1, CEBPB, CHP1 +22 moreView in SCUBA

About the gene

SynonymsCHMP2.5, DKFZP564O123, VPS2B
Chromosome3: 87227271-87255556
Predicted locationIntracellular
Essential geneNo
Protein classDisease related genes, Human disease related genes, Predicted intracellular proteins
Biological processProtein transport, Transport

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

Human Protein Atlas · Open Targets · UniProt

Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.