P52483
PR
Gene name |
Ube2e3 (Ubce4, Ubcm2) |
Protein name |
Ubiquitin-conjugating enzyme E2 E3 |
Names |
E2 ubiquitin-conjugating enzyme E3, UbcM2, Ubiquitin carrier protein E3, Ubiquitin-conjugating enzyme E2-23 kDa, Ubiquitin-protein ligase E3 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:22193 |
EC number |
2.3.2.23: Aminoacyltransferases |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for P52483
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P52483-F1 | Predicted | AlphaFoldDB |
3 variants for P52483
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs1131896554 | 77 | P>T | No | EVA | |
| rs3388564100 | 103 | S>F | No | EVA | |
| rs3388560363 | 205 | Y>H | No | EVA |
No associated diseases with P52483
3 regional properties for P52483
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Cyclin, N-terminal | 37 - 148 | IPR006671 |
| domain | Cyclin-like domain | 46 - 144 | IPR013763-1 |
| domain | Cyclin-like domain | 161 - 236 | IPR013763-2 |
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 |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
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. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| 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. |
| protein K48-linked ubiquitination | A protein ubiquitination process in which a polymer of ubiquitin, formed by linkages between lysine residues at position 48 of the ubiquitin monomers, is added to a protein. K48-linked ubiquitination targets the substrate protein for degradation. |
| protein K63-linked ubiquitination | A protein ubiquitination process in which a polymer of ubiquitin, formed by linkages between lysine residues at position 63 of the ubiquitin monomers, is added to a protein. K63-linked ubiquitination does not target the substrate protein for degradation, but is involved in several pathways, notably as a signal to promote error-free DNA postreplication repair. |
| protein polyubiquitination | Addition of multiple ubiquitin groups to a protein, forming a ubiquitin chain. |
19 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q32LD2 | UBE2T | Ubiquitin-conjugating enzyme E2 T | Bos taurus (Bovine) | PR |
| P35128 | ben | Ubiquitin-conjugating enzyme E2 N | Drosophila melanogaster (Fruit fly) | PR |
| P25867 | eff | Ubiquitin-conjugating enzyme E2-17 kDa | Drosophila melanogaster (Fruit fly) | PR |
| Q9NPD8 | UBE2T | Ubiquitin-conjugating enzyme E2 T | Homo sapiens (Human) | PR |
| Q969T4 | UBE2E3 | Ubiquitin-conjugating enzyme E2 E3 | Homo sapiens (Human) | PR |
| Q96LR5 | UBE2E2 | Ubiquitin-conjugating enzyme E2 E2 | Homo sapiens (Human) | PR |
| P61079 | Ube2d3 | Ubiquitin-conjugating enzyme E2 D3 | Mus musculus (Mouse) | PR |
| Q9CQ37 | Ube2t | Ubiquitin-conjugating enzyme E2 T | Mus musculus (Mouse) | PR |
| Q921J4 | Ube2s | Ubiquitin-conjugating enzyme E2 S | Mus musculus (Mouse) | SS |
| Q9D1C1 | Ube2c | Ubiquitin-conjugating enzyme E2 C | Mus musculus (Mouse) | PR |
| Q9JJZ4 | Ube2j1 | Ubiquitin-conjugating enzyme E2 J1 | Mus musculus (Mouse) | PR |
| P61087 | Ube2k | Ubiquitin-conjugating enzyme E2 K | Mus musculus (Mouse) | PR |
| Q64362 | Aktip | AKT-interacting protein | Mus musculus (Mouse) | PR |
| Q7TSS2 | Ube2q1 | Ubiquitin-conjugating enzyme E2 Q1 | Mus musculus (Mouse) | PR |
| A0PJN4 | Ube2ql1 | Ubiquitin-conjugating enzyme E2Q-like protein 1 | Mus musculus (Mouse) | PR |
| P35129 | let-70 | Ubiquitin-conjugating enzyme E2 2 | Caenorhabditis elegans | PR |
| 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 |
| Q9LJD7 | COP10 | Constitutive photomorphogenesis protein 10 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSSDRQRSDD | ESPSTSSGSS | DADQRDPAAP | EPEEQEERKP | SATQQKKNTK | LSSKTTAKLS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| TSAKRIQKEL | AEITLDPPPN | CSAGPKGDNI | YEWRSTILGP | PGSVYEGGVF | FLDITFSSDY |
| 130 | 140 | 150 | 160 | 170 | 180 |
| PFKPPKVTFR | TRIYHCNINS | QGVICLDILK | DNWSPALTIS | KVLLSICSLL | TDCNPADPLV |
| 190 | 200 | ||||
| GSIATQYLTN | RAEHDRIARQ | WTKRYAT |