Q28F89
SS
Gene name |
ube2s (TEgg003m12.1, TEgg028l19.1) |
Protein name |
Ubiquitin-conjugating enzyme E2 S |
Names |
EC 2.3.2.23 , E2 ubiquitin-conjugating enzyme S , Ubiquitin carrier protein S , Ubiquitin-protein ligase S |
Species |
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
KEGG Pathway |
xtr:549192 |
EC number |
2.3.2.23: Aminoacyltransferases |
Protein Class |
|
Descriptions
Ubiquitin conjugating enzyme E2 S (UBE2S) is a protein that plays a key role in accepting ubiquitin from the E1 complex and catalyzing its covalent attachment to other proteins. Dimerization regulates UBE2S by preventing autoubiquitination, thus stabilizing the protein and allowing it to inhibit premature ubiquitin chain elongation during the cell cycle. The autoinhibition is mediated by blocking the ubiquitin-binding sites in UBC domain, which are essential for its E2 activity. The C-helix of UBE2S engages the APC/C for chain elongation, blocking the promotion of UBE2S autoinhibition through dimerization achieved by C-helix.
Autoinhibitory domains (AIDs)
Target domain |
1-156 (UBC domain) |
Relief mechanism |
PTM |
Assay |
|
Accessory elements
No accessory elements
References
- Holliday MJ et al. (2019) "Structures of autoinhibited and polymerized forms of CARD9 reveal mechanisms of CARD9 and CARD11 activation", Nature communications, 10, 3070
- Liess AKL et al. (2020) "Dimerization regulates the human APC/C-associated ubiquitin-conjugating enzyme UBE2S", Science signaling, 13,
- Bremm A (2020) "Hug and hold tight: Dimerization controls the turnover of the ubiquitin-conjugating enzyme UBE2S", Science signaling, 13,
Autoinhibited structure
Activated structure
1 structures for Q28F89
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q28F89-F1 | Predicted | AlphaFoldDB |
No variants for Q28F89
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q28F89 | |||||
No associated diseases with Q28F89
7 regional properties for Q28F89
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | High mobility group box domain | 111 - 181 | IPR009071-1 |
| domain | High mobility group box domain | 195 - 265 | IPR009071-2 |
| domain | High mobility group box domain | 297 - 363 | IPR009071-3 |
| domain | High mobility group box domain | 406 - 476 | IPR009071-4 |
| domain | High mobility group box domain | 481 - 550 | IPR009071-5 |
| domain | High mobility group box domain | 567 - 635 | IPR009071-6 |
| domain | High mobility group box domain 5 | 479 - 563 | IPR029215 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.3.2.23 | Aminoacyltransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| anaphase-promoting complex | A ubiquitin ligase complex that degrades mitotic cyclins and anaphase inhibitory protein, thereby triggering sister chromatid separation and exit from mitosis. Substrate recognition by APC occurs through degradation signals, the most common of which is termed the Dbox degradation motif, originally discovered in cyclin B. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| endoplasmic reticulum | The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| ubiquitin conjugating enzyme activity | Isoenergetic transfer of ubiquitin from one protein to another via the reaction X-ubiquitin + Y -> Y-ubiquitin + X, where both the X-ubiquitin and Y-ubiquitin linkages are thioester bonds between the C-terminal glycine of ubiquitin and a sulfhydryl side group of a cysteine residue. |
6 GO annotations of biological process
| Name | Definition |
|---|---|
| anaphase-promoting complex-dependent catabolic process | The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, with ubiquitin-protein ligation catalyzed by the anaphase-promoting complex, and mediated by the proteasome. |
| cell division | The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells. |
| 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. |
| free ubiquitin chain polymerization | The process of creating free ubiquitin chains, compounds composed of a large number of ubiquitin monomers. These chains are not conjugated to a protein. |
| positive regulation of ubiquitin protein ligase activity | Any process that activates or increases the frequency, rate or extent of ubiquitin protein ligase activity. |
| protein K11-linked ubiquitination | A protein ubiquitination process in which ubiquitin monomers are attached to a protein, and then ubiquitin polymers are formed by linkages between lysine residues at position 11 of the ubiquitin monomers. K11-linked polyubiquitination targets the substrate protein for degradation. The anaphase-promoting complex promotes the degradation of mitotic regulators by assembling K11-linked polyubiquitin chains. |
7 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q1RML1 | UBE2S | Ubiquitin-conjugating enzyme E2 S | Bos taurus (Bovine) | SS |
| Q9VX25 | CG8188 | Ubiquitin-conjugating enzyme E2 S | Drosophila melanogaster (Fruit fly) | SS |
| Q16763 | UBE2S | Ubiquitin-conjugating enzyme E2 S | Homo sapiens (Human) | EV |
| Q921J4 | Ube2s | Ubiquitin-conjugating enzyme E2 S | Mus musculus (Mouse) | SS |
| B5DFI8 | Ube2s | Ubiquitin-conjugating enzyme E2 S | Rattus norvegicus (Rat) | SS |
| Q9FF66 | UBC22 | Ubiquitin-conjugating enzyme E2 22 | Arabidopsis thaliana (Mouse-ear cress) | SS |
| Q4V908 | ube2s | Ubiquitin-conjugating enzyme E2 S | Danio rerio (Zebrafish) (Brachydanio rerio) | SS |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MNSNVENLPP | HIIRQVYKEV | STLTSDPPEG | IKIIPNEEDI | TDVQVNIEGP | EGTPYAGGIF |
| 70 | 80 | 90 | 100 | 110 | 120 |
| RMKLILGKDF | PAAPPKGYFL | TKIFHPNVST | NGEICVNVLK | KDWKAELGIR | HVLLTIKCLL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| IHPNPESALN | EEAGRLLLEN | YEEYASRARL | MTEIHAQGSS | LRGKDPTDPC | SSASATLVSG |
| 190 | 200 | 210 | |||
| DGPMAKKHAG | DRDKKLAAKK | KTDKKRALRR | L |