Q6DFS6
Gene name |
chmp2a (TNeu078g14.1) |
Protein name |
Charged multivesicular body protein 2a |
Names |
Chromatin-modifying protein 2a , CHMP2a |
Species |
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
KEGG Pathway |
xtr:448496 |
EC number |
|
Protein Class |
|

Descriptions
Autoinhibitory domains (AIDs)
Target domain |
1-144 (N-terminal α1-α4 domains) |
Relief mechanism |
Partner binding |
Assay |
|
Accessory elements
No accessory elements
Autoinhibited structure

Activated structure

1 structures for Q6DFS6
Entry ID | Method | Resolution | Chain | Position | Source |
---|---|---|---|---|---|
AF-Q6DFS6-F1 | Predicted | AlphaFoldDB |
No variants for Q6DFS6
Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
---|---|---|---|---|---|
No variants for Q6DFS6 |
No associated diseases with Q6DFS6
1 regional properties for Q6DFS6
Type | Name | Position | InterPro Accession |
---|---|---|---|
domain | Small GTP-binding protein domain | 16 - 141 | IPR005225 |
4 GO annotations of cellular component
Name | Definition |
---|---|
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. |
nuclear envelope | The double lipid bilayer enclosing the nucleus and separating its contents from the rest of the cytoplasm; includes the intermembrane space, a gap of width 20-40 nm (also called the perinuclear space). |
No GO annotations of molecular function
Name | Definition |
---|---|
No GO annotations for molecular function |
5 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. |
exit from mitosis | The cell cycle transition where a cell leaves M phase and enters a new G1 phase. M phase is the part of the mitotic cell cycle during which mitosis and cytokinesis take place. |
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. |
nuclear membrane reassembly | The reformation of the nuclear membranes following their breakdown in the context of a normal process. |
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 |
---|---|---|---|---|
Q5ZHN1 | CHMP2A | Charged multivesicular body protein 2a | Gallus gallus (Chicken) | SS |
O43633 | CHMP2A | Charged multivesicular body protein 2a | Homo sapiens (Human) | EV |
Q9DB34 | Chmp2a | Charged multivesicular body protein 2a | Mus musculus (Mouse) | SS |
Q9SKI2 | VPS2.1 | Vacuolar protein sorting-associated protein 2 homolog 1 | Arabidopsis thaliana (Mouse-ear cress) | SS |
Q5BKM3 | chmp3 | Charged multivesicular body protein 3 | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) | SS |
Q6DF27 | chmp1b | Charged multivesicular body protein 1b | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) | PR |
Q7ZW25 | chmp2a | Charged multivesicular body protein 2a | Danio rerio (Zebrafish) (Brachydanio rerio) | SS |
10 | 20 | 30 | 40 | 50 | 60 |
MEFLFGRRKT | PEEMLRQNQR | ALNKAMREMD | RERQKLEQQE | KKIIADIKKM | AKQGQMDAVK |
70 | 80 | 90 | 100 | 110 | 120 |
IMAKDLVRTR | RYVKKFIMMR | ANIQAVSLKI | QTLKSNNSMA | QAMKGVTKAM | ATMNRQLKLP |
130 | 140 | 150 | 160 | 170 | 180 |
QIQKIMMEFE | KQSEIMDMKE | EMMNDAIDDA | MGDEDDEEES | DAVVSQVLDE | LGLTLTDELS |
190 | 200 | 210 | |||
NLPSTGGSLS | VAGAKKGEPS | AALADADADL | EERLNNLRRD |