| UniProt functional annotation for P61085 | |||
| UniProt code: P61085. |
| Organism: | Bos taurus (Bovine). | |
| Taxonomy: | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos. | |
| Function: | Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro, in the presence or in the absence of BRCA1-BARD1 E3 ubiquitin-protein ligase complex, catalyzes the synthesis of 'Lys-48'-linked polyubiquitin chains. Does not transfer ubiquitin directly to but elongates monoubiquitinated substrate protein. Mediates the selective degradation of short-lived and abnormal proteins, such as the endoplasmic reticulum-associated degradation (ERAD) of misfolded lumenal proteins. Ubiquitinates huntingtin. May mediate foam cell formation by the suppression of apoptosis of lipid-bearing macrophages through ubiquitination and subsequence degradation of p53/TP53 (By similarity). Proposed to be involved in ubiquitination and proteolytic processing of NF-kappa-B; in vitro supports ubiquitination of NFKB1. {ECO:0000250|UniProtKB:P61086, ECO:0000269|PubMed:9535861}. | |
| Catalytic activity: | Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin- activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin- conjugating enzyme]-L-cysteine.; EC=2.3.2.23; Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE- ProRule:PRU10133}; | |
| Pathway: | Protein modification; protein ubiquitination. {ECO:0000255|PROSITE-ProRule:PRU00388}. | |
| Subunit: | Interacts with RNF138/NARF. Interacts with BRCA1. {ECO:0000250|UniProtKB:P61086}. | |
| Subcellular location: | Cytoplasm. | |
| Ptm: | Sumoylation at Lys-14 impairs catalytic activity. {ECO:0000269|PubMed:15723079}. | |
| Similarity: | Belongs to the ubiquitin-conjugating enzyme family. {ECO:0000255|PROSITE-ProRule:PRU00388}. | |
Annotations taken from UniProtKB at the EBI.