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Primary Information | |
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| BoMiProt ID | Bomi2828 |
| Protein Name | Ubiquitin carboxyl-terminal hydrolase 12 |
| Organism | Bos taurus |
| Uniprot ID | A5D9H7 |
| Milk Fraction | Exosome |
| Ref Sequence ID | NP_001091528.1 |
| Aminoacid Length | 369 |
| Molecular Weight | 42683 |
| FASTA Sequence | Download |
| Gene Name | USP12 |
| Gene ID | 525655 |
| Protein Existence Status | Reviewed: Experimental evidence at transcript level |
Secondary Information | |
| Protein Function | important regulators of the ubiquitin system; responsible for processing inactive ubiquitin precursors, proofreading ubiquitin–protein conjugates, removing ubiquitin from cellular adducts, and keeping the 26S proteasome free of inhibitory ubiquitin chains; essential for preventing all of the cellular ubiquitin from being rapidly titrated by these compounds; act as negative regulators of proteolysis by counteracting against the action of the ubiquitination machinery on specific substrates; modulate nonproteolytic ubiquitin-dependent processes such as membrane protein trafficking decisions and certain signal transduction mechanisms; Ubiquitin carboxyl-terminal hydrolase 14 play an important role in removing the ubiquitin moiety from polyubiquitinated substrates; |
| Biochemical Properties | specifically cleave ubiquitin-linked molecules after the terminal carbonyl of the last residue of ubiquitin (Gly76); can hydrolyze different kinds of chemical bonds, although not necessarily with equal efficiency - many members of this family of enzymes can cleave ester, peptide and isopeptide bonds to ubiquitin at high rates; cysteine proteases contain two short but well-conserved motifs, named the Cys and His boxes, which include all the catalytic triad residues as well as other residues in the active site pocket; Ubiquitin carboxyl-terminal hydrolase 14 isactivated catalytically upon specific association with the 26S proteasome; prefers to cleave ubiquitin from the distal end of a Lys48-linked polyubiquitin chain; alternatively cleave linked ubiquitin oligomers such as Lys63-linked diubiquitin but the cleavage is slow; proteasome association promotes displacement of two polypeptide loops in USP14 that otherwise block access of substrates to the active site |
| Linking IDs | Bomi57 |
| Bibliography | 1. Hu, M., Li, P., Song, L., Jeffrey, P. D., Chenova, T. A., Wilkinson, K. D., … Shi, Y. (2005). Structure and mechanisms of the proteasome-associated deubiquitinating enzyme USP14. The EMBO Journal, 24(21), 3747–3756. https://doi.org/10.1038/sj.emboj.7600832. 2. Wilkinson, K. D., Deshpande, S., & Larsen, C. N. (1992). Comparisons of neuronal (PGP 9.5) and non-neuronal ubiquitin C-terminal hydrolases. Biochemical Society Transactions, 20(3), 631–637. https://doi.org/10.1042/bst0200631. 3. Koegl, M., Hoppe, T., Schlenker, S., Ulrich, H. D., Mayer, T. U., & Jentsch, S. (1999). A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly. Cell, 96(5), 635–644. https://doi.org/10.1016/s0092-8674(00)80574-7. 4. Mayer, A. N., & Wilkinson, K. D. (1989). Detection, resolution, and nomenclature of multiple ubiquitin carboxyl-terminal esterases from bovine calf thymus. Biochemistry, 28(1), 166–172. https://doi.org/10.1021/bi00427a024. |
| Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation | |
| Predicted Disorder Regions | (145-165) |
| DisProt Annotation | |
| TM Helix Prediction | No TM helices |