Q5BKM3
Gene name |
chmp3 (vps24, TEgg091h16.1) |
Protein name |
Charged multivesicular body protein 3 |
Names |
Chromatin-modifying protein 3 , Vacuolar protein-sorting-associated protein 24 |
Species |
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
KEGG Pathway |
xtr:548983 |
EC number |
|
Protein Class |
|

Descriptions
Autoinhibitory domains (AIDs)
Target domain |
1-150 (N-terminal domain) |
Relief mechanism |
Partner binding |
Assay |
|
Accessory elements
No accessory elements
References
- Zamborlini A et al. (2006) "Release of autoinhibition converts ESCRT-III components into potent inhibitors of HIV-1 budding", Proceedings of the National Academy of Sciences of the United States of America, 103, 19140-5
- Bajorek M et al. (2009) "Structural basis for ESCRT-III protein autoinhibition", Nature structural & molecular biology, 16, 754-62
Autoinhibited structure

Activated structure

1 structures for Q5BKM3
Entry ID | Method | Resolution | Chain | Position | Source |
---|---|---|---|---|---|
AF-Q5BKM3-F1 | Predicted | AlphaFoldDB |
No variants for Q5BKM3
Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
---|---|---|---|---|---|
No variants for Q5BKM3 |
No associated diseases with Q5BKM3
No regional properties for Q5BKM3
Type | Name | Position | InterPro Accession |
---|---|---|---|
No domain, repeats, and functional sites for Q5BKM3 |
4 GO annotations of cellular component
Name | Definition |
---|---|
cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
ESCRT III complex | A complex with membrane scission activity that plays a major role in many processes where membranes are remodelled - including endosomal transport (vesicle budding), nuclear envelope organisation (membrane closure, mitotic bridge cleavage), and cytokinesis (abscission). |
late endosome membrane | The lipid bilayer surrounding a late endosome. |
multivesicular body | A type of endosome in which regions of the limiting endosomal membrane invaginate to form internal vesicles; membrane proteins that enter the internal vesicles are sequestered from the cytoplasm. |
No GO annotations of molecular function
Name | Definition |
---|---|
No GO annotations for molecular function |
3 GO annotations of biological process
Name | Definition |
---|---|
endosome transport via multivesicular body sorting pathway | The directed movement of substances from endosomes to lysosomes or vacuoles by a pathway in which molecules are sorted into multivesicular bodies, which then fuse with the target compartment. |
late endosome to vacuole transport | The directed movement of substances from late endosomes to the vacuole. In yeast, after transport to the prevacuolar compartment, endocytic content is delivered to the late endosome and on to the vacuole. This pathway is analogous to endosome to lysosome transport. |
protein transport | The directed movement of proteins into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. |
7 homologous proteins in AiPD
UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
---|---|---|---|---|
Q58CS7 | CHMP3 | Charged multivesicular body protein 3 | Bos taurus (Bovine) | SS |
Q9Y3E7 | CHMP3 | Charged multivesicular body protein 3 | Homo sapiens (Human) | EV |
Q9CQ10 | Chmp3 | Charged multivesicular body protein 3 | Mus musculus (Mouse) | SS |
Q8CGS4 | Chmp3 | Charged multivesicular body protein 3 | Rattus norvegicus (Rat) | SS |
Q6DFS6 | chmp2a | Charged multivesicular body protein 2a | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) | SS |
Q6DF27 | chmp1b | Charged multivesicular body protein 1b | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) | PR |
Q6NY88 | chmp3 | Charged multivesicular body protein 3 | Danio rerio (Zebrafish) (Brachydanio rerio) | SS |
10 | 20 | 30 | 40 | 50 | 60 |
MGLFGKTQER | PPKDLVNEWS | LKIRKEMRVI | DRQIRDIQRE | QEKVKRSIKE | SAKKGNREAC |
70 | 80 | 90 | 100 | 110 | 120 |
VILAKEVVHS | KKAVNKLYAS | KAHMNSVLMS | MKNQLAVLRV | SGSLQKSTEV | MKAMQNLVKI |
130 | 140 | 150 | 160 | 170 | 180 |
PEIQATMRDL | SKEMMKAGII | EEMLEDTFEG | MEDQDEMEEQ | AEMEIDRILF | EITAGALGKA |
190 | 200 | 210 | |||
PSKVTDALPE | PEITGAMAAS | DEEEEEDLEA | MQSRLAALRS |