Q9FF66
SS
Gene name |
UBC22 (At5g05080, MUG13.6) |
Protein name |
Ubiquitin-conjugating enzyme E2 22 |
Names |
EC 2.3.2.23 , E2 ubiquitin-conjugating enzyme 22 , Ubiquitin carrier protein 22 |
Species |
Arabidopsis thaliana (Mouse-ear cress) |
KEGG Pathway |
ath:AT5G05080 |
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 |
0-185 (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 Q9FF66
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9FF66-F1 | Predicted | AlphaFoldDB |
14 variants for Q9FF66
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| tmp_5_1499407_C_T | 87 | V>I | No | 1000Genomes | |
| tmp_5_1499400_G_A | 89 | S>F | No | 1000Genomes | |
| ENSVATH13927671 | 106 | L>V | No | 1000Genomes | |
| tmp_5_1499014_G_A | 157 | P>S | No | 1000Genomes | |
| ENSVATH00607221 | 176 | G>S | No | 1000Genomes | |
| tmp_5_1498938_G_A | 182 | T>M | No | 1000Genomes | |
| ENSVATH00607220 | 188 | A>V | No | 1000Genomes | |
| ENSVATH13927642 | 190 | P>A | No | 1000Genomes | |
| tmp_5_1498904_C_A | 193 | M>I | No | 1000Genomes | |
| ENSVATH06924713 | 203 | A>S | No | 1000Genomes | |
| ENSVATH10580645 | 206 | Q>L | No | 1000Genomes | |
| ENSVATH00607219 | 219 | S>N | No | 1000Genomes | |
| ENSVATH06924712 | 224 | T>M | No | 1000Genomes | |
| ENSVATH06924711 | 235 | Q>H | No | 1000Genomes |
No associated diseases with Q9FF66
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 | |
2 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. |
| 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). |
3 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. |
| ubiquitin-protein transferase activity | Catalysis of the transfer of ubiquitin from one protein to another via the reaction X-Ub + Y --> Y-Ub + X, where both X-Ub and Y-Ub are covalent linkages. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| protein ubiquitination | The process in which one or more ubiquitin groups are added to a protein. |
| ubiquitin-dependent protein 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 a ubiquitin group, or multiple ubiquitin groups, to the protein. |
11 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 |
| Q9C8X7 | UBC31 | Probable ubiquitin-conjugating enzyme E2 31 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q9SLE4 | UBC29 | Ubiquitin-conjugating enzyme E2 29 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q9LSP7 | UBC32 | Ubiquitin-conjugating enzyme E2 32 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q9LJD7 | COP10 | Constitutive photomorphogenesis protein 10 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q28F89 | ube2s | Ubiquitin-conjugating enzyme E2 S | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) | SS |
| Q4V908 | ube2s | Ubiquitin-conjugating enzyme E2 S | Danio rerio (Zebrafish) (Brachydanio rerio) | SS |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MASNENLPPN | VIKQLAKELK | SLDESPPDGI | KVVVNDEDFS | QICADIEGPV | GTPYENGLFR |
| 70 | 80 | 90 | 100 | 110 | 120 |
| MKLALSHDFP | HSPPKGYFMT | KIFHPNVASN | GEICVNTLKK | DWNPSLGLRH | VLSVVRCLLI |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EPFPESALNE | QAGKMLLENY | DEYARHARLY | TGIHAKPKPK | FKTGAISEST | TALNVGQTNN |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ETPGAATAIP | SSMTDIKRVT | TSAQDQQHVA | NVVVAASASV | VTTTQKREAG | LAKVQADKKK |
| 250 | |||||
| VDARKKSLKR | L |