IED ID | IndEnz0002011364 |
Enzyme Type ID | protease011364 |
Protein Name |
Ubiquitin carboxyl-terminal hydrolase usp-48 EC 3.4.19.12 Ubiquitin-specific protease 48 |
Gene Name | usp-48 F30A10.10 |
Organism | Caenorhabditis elegans |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis elegans |
Enzyme Sequence | MTKETDKKPKERPNQRKVAFRNEAINALVNTDEDQVTFSKAMEVAKLDCQKCLLHDMHSSKSSNCRDNPFCIHRLGLEKFEKLITQEQETKEEAKKDQKRRDLNDQPAGLINGGNFCYVNSFLQVWFNVPEFRQLIYDFRPSENFVPPEAPRMNVQATMLALQDIFYTLQTTPFNETDKTSNLGKLLRLNSEQQDSQEFGLKFFNALERCLPDHPNGKETLKRLKDLFTGETCTRIVCKCGQRSEREETAISLTLNIEGYCTLLDALDAYFGEEHLDDFKCSKCNKTGDVSKQSDYVKLPPVIVIQLNRYKYTSKGRQKLKTPMAYPREIPAKAFQRTNNSIPPPAEMYDLFAVTIHEGNNAECGHYYDLIKSPLNQKWYRYNDEAIEAIPKPPGTEKPTTAKTEKSRKKDKEKYPTDQKACYGLLYRRRDAFKPLPHPKLPPEELIIDSKTEIEELFEGLTKKKIEKSEKRLYDLERRINKVKISYGKLETHSDKYKEANEVVFLPTTLLQDVLAQEYEVAKGEKKKKKKEASENEEKKKNEEDEALSAAIAASEADQRDKASSEPSTSAAATEAGDDEELRAESETPNPENAESTQVAIMETDEIMDTTPTKDIDILAKAMEDNALPTVEVPQPELKKRTRQQNGEVKYVYSQRTPRKSHNGTNGTNSSPQKQPVSSRVAALLSSHEIPTCGHGKMSIDPILYGDVKAVSRAPAIALLREYDFRVKIVYDNGENVFPENEKERDVFIFTAEDICMECVREMREEGNFNNQLEDDEKLVRRILKEEKQRCSVKCPSERPDGYLYVAKFALSNFKKSAMSARENRLAQSHNKQGTLHFDSHPMFQQKSNSGYLTLSLKRTRGKPRKSLSEIPEKMQKLDEIGSKELPDEIIADEEEISENMGSDIPTKPVESINPDALVPFEKIEFNSELRCSHGGINFNQFRLSVSPEEWAHLKVYFDECYEVKCSDDVCDQCRQMEVDAQNGSENMRGLVREMRKRISDTLKTVESRAESKEDGADIKYGICSVFIDKLRKLTSRQSTSPPSICQECLLCPHQQPFKGFLNEDNHKDSHVVGLTEEEWNTFLTEIRKLEEAGDDQSIAVDPCPIPIENGQIVDMCEKCFEQHIKFTEEQKYMFENENIYVKLVNLNVEEDIAKANGKARRGRAKNLYAIKMSSTNKLMELKVQLYDKTHQLPNDQLLYRTAGGEQFDVSNNQKTLFDLRLSPNNNDNPLILIAQQFSPSASQADETGDRAPERGFVDTALAH |
Enzyme Length | 1264 |
Uniprot Accession Number | G5ECC7 |
Absorption | |
Active Site | ACT_SITE 117; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01035; ACT_SITE 366; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01035 |
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:Q86UV5}; |
DNA Binding | |
EC Number | 3.4.19.12 |
Enzyme Function | FUNCTION: Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin (By similarity). Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins (By similarity). Required post-developmentally to restrict the plasticity of epidermal cells, probably by regulating gene expression (PubMed:31088904). {ECO:0000250|UniProtKB:Q86UV5, ECO:0000269|PubMed:31088904}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (4); Domain (1); Mutagenesis (3); Region (3) |
Keywords | Alternative splicing;Chromosome;Coiled coil;Hydrolase;Nucleus;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31088904}. Chromosome {ECO:0000269|PubMed:31088904}. Note=In pachytene germline cells and oocytes, localizes to chromosomes. {ECO:0000269|PubMed:31088904}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 12242227; 12445391; 14551910; 16710447; 18006689; 19165329; 20308279; 20439774; 21177967; 21343362; 21909284; 22286215; 22560298; 23800452; 25487147; |
Motif | |
Gene Encoded By | |
Mass | 144,457 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |