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Literature summary for 6.2.1.45 extracted from
- LMO2 blocks the UBA6-USE1 interaction and downstream FAT10ylation by targeting the ubiquitin fold domain of UBA6 (2016), Biochem. Biophys. Res. Commun., 478, 1442-1448 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant transient overexpression of GST-tagged or Myc-tagged full-length wild-type enzyme and truncated mutant versions in HEK-293T cells, recombinant expression of UBA6 from pGEX-4T-1/pGEX4T-1-UBA6/pGEX4T-1-UFD plasmids in Escherichia coli | Homo sapiens |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| LMO2 | interaction between LMO2 and UBA6 blocks the recruitment of USE1 by UBA6 in a dose-dependent manner.. The LMO2 protein interacts with the E1 ubiquitin-activating enzyme UBA6 at the C-terminal ubiquitin fold domain (UFD), which mediates the recognition and recruitment of the E2-conjugating enzyme USE1. The LMO2-UBA6 interaction leads to the decline of the overall cellular FAT10ylation level as well as the FAT10ylation and degradation of a known FAT10 substrate p62. Interaction analysis of LMO2 with isolated UBA6 domains, LMO2 interacts with UBA6 at the ubiquitin-fold domain, overview. LMO2 co-localizes with UBA6 and USE1 primarily in the cytoplasm of epithelium-derived cells | Homo sapiens |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytoplasm | primarily | Homo sapiens | 5737 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Homo sapiens |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine | Homo sapiens | - |
AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine | - |
? | |
| additional information | Homo sapiens | E1 ubiquitin-activating enzyme UBA6 is the only E1 enzyme that can activate both ubiquitin and ubiquitin-like protein HLA-F adjacent transcript 10 (FAT10). FAT10 consists of two ubiquitin-like domains with 29% and 36% identity to ubiquitin, respectively, that are separated by a short linker region | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | A0AVT1 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant tagged full-length wild-type enzyme and truncated mutant versions from Escherichia coli by affinity chromatography | Homo sapiens |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| epithelial cell | - |
Homo sapiens | - |
| K-562 cell | - |
Homo sapiens | - |
| MDA-MB-231 cell | - |
Homo sapiens | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine | - |
Homo sapiens | AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine | - |
? | |
| additional information | E1 ubiquitin-activating enzyme UBA6 is the only E1 enzyme that can activate both ubiquitin and ubiquitin-like protein HLA-F adjacent transcript 10 (FAT10). FAT10 consists of two ubiquitin-like domains with 29% and 36% identity to ubiquitin, respectively, that are separated by a short linker region | Homo sapiens | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Uba6 | - |
Homo sapiens |
| UBE1L2 | - |
Homo sapiens |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Homo sapiens | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | the LMO2 protein interacts with the E1 ubiquitin-activating enzyme UBA6 at the C-terminal ubiquitin fold domain (UFD), which mediates the recognition and recruitment of the E2-conjugating enzyme USE1. Functionally, the LMO2-UBA6 interaction disturbes the interaction between UBA6 and USE1 and leads to the decline of the overall cellular FAT10ylation level as well as the FAT10ylation and degradation of a known FAT10 substrate p62 | Homo sapiens |
| physiological function | UBA6 is the specific E1 that activates FAT10 and USE1 (also known as UBE2Z), an E2-conjugating enzyme that interacts exclusively with UBA6, accepts both ubiquitin and FAT10 from UBA6. UBA6 is one of the eight known E1 ubiquitin-activating enzymes and is the only E1 enzyme that can activate both ubiquitin and ubiquitin-like protein HLA-F adjacent transcript 10 (FAT10). In eukaryotic cells, the post-translational modification of proteins by ubiquitin or ubiquitin-like proteins (UBLs) is the most common trigger for protein degradation and is involved in the regulation of a wide range of biological processes. FAT10 (HLA-F-adjacent transcript 10), which belongs to the UBL family, is activated specifically through the UBA6-USE1 cascade and targets substrates covalently for 26S proteasomal degradation. The E1 ubiquitin-activating enzyme interacts with LMO2, a well-recognized transcriptional regulator in hematopoietic and endothelial systems, that is involved in the regulatory hierarchy of UBA6-USE1-FAT10ylation pathway by targeting the E1 enzyme UBA6 | Homo sapiens |
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