| IED ID | IndEnz0002009247 |
| Enzyme Type ID | protease009247 |
| Protein Name |
Deubiquitinase OTUD6B OTU domain-containing protein 6B EC 3.4.19.12 |
| Gene Name | Otud6b |
| Organism | Mus musculus (Mouse) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MEEVVAEELDDEEQLVRRHRKEKKELQAKIQGMKNAVPKNDKKRRKQLTEDVAKLEREMEQKHREELEQLKQLTFKDSKIDSVAVNISNLVLENQPPRISKAQKRREKKAALEKEREERIAEAEIENLSGARHLESEKLAQILAARELEIKQIPSDGHCMYGALEDQLREQDCALTVASLRRQTAEYMQTHSDDFLPFLTNPSTGDMYTPEEFGKYCDDIVNTAAWGGQLELRALSHILQTPIEILQADAPPIIVGEEYPRNPLVLVYMRHAYGLGEHYNSVTRLVNSATENCS |
| Enzyme Length | 294 |
| Uniprot Accession Number | Q8K2H2 |
| Absorption | |
| Active Site | ACT_SITE 156; /evidence=ECO:0000250; ACT_SITE 159; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:Q8N6M0; ACT_SITE 278; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:Q8N6M0}; |
| DNA Binding | |
| EC Number | 3.4.19.12 |
| Enzyme Function | FUNCTION: Deubiquitinating enzyme that may play a role in the ubiquitin-dependent regulation of protein synthesis, downstream of mTORC1 (By similarity). May associate with the protein synthesis initiation complex and modify its ubiquitination to repress translation (By similarity). May also repress DNA synthesis and modify different cellular targets thereby regulating cell growth and proliferation (By similarity). May also play a role in proteasome assembly and function (By similarity). {ECO:0000250|UniProtKB:Q8N6M0}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Domain (1); Modified residue (1); Region (3); Sequence conflict (5) |
| Keywords | Acetylation;Hydrolase;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway |
| Interact With | |
| Induction | INDUCTION: Up-regulated by cytokines but followed by a rapid decline in B lymphocytes. {ECO:0000269|PubMed:21267069}. |
| Subcellular Location | |
| Modified Residue | MOD_RES 1; /note=N-acetylmethionine; /evidence=ECO:0000250|UniProtKB:Q8N6M0 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10725249; 11217851; 12466851; 12520002; 18799693; 21677750; 24194600; 27626380; |
| Motif | |
| Gene Encoded By | |
| Mass | 33,758 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |