| IED ID | IndEnz0002011763 |
| Enzyme Type ID | protease011763 |
| Protein Name |
Ubiquitin carboxyl-terminal hydrolase 10-B EC 3.4.19.12 Deubiquitinating enzyme 10-B Ubiquitin thioesterase 10-B Ubiquitin-specific-processing protease 10-B |
| Gene Name | usp10-b |
| Organism | Xenopus laevis (African clawed frog) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amphibia Batrachia Anura Pipoidea Pipidae Xenopodinae Xenopus Xenopus Xenopus laevis (African clawed frog) |
| Enzyme Sequence | MASPSGQYIFGEFSDDEFKQFFVTARCTVELPPYNEHFFPCGPQSSVDFQDDMHLKFSEVIHGISGEECPRIEFGIEQVVDRDTALNNNTDYSISSNLNPQAPEFILTCSSFPKTSNNVLHENNFDAINCQFSESAIPDGSGNADSDGTSGTGQRERKKKKKRPPGYYSYLEGVGDVPSETLVNGHANSTGLDSISTDDPDLADDIPISTTSPRTCTSPDNFVDLINEALSDEASMHNVLDNARTAGQPEECSVTSSEQSCIPSDNGSESPVRTAVVQPFAGTDTTENLGVTNGQTLESPEEDTVSNGVVLHPEVSSFSEEVKTEETSTAQALIHLSGSASSNPPAKSWASLFHTSKPSSSPQVAYVETKNAPTVVSPQVPEKQVEIKEEPVPVSDDPVAIEFAELLEEVKLVHKPVSLQPRGLINKGNWCYINATLQALVACPPMYHLMKSIPVYTKAQRPCTSTPMIDSFVRLMNEFTNMPILPKAKQAPGEKVIKDIRPGAPFEPTYIYRLLTVFKSSLSEKGRQEDAEEYLGFILNGLHEEMLALKKLLLPQNDQIHINNCPNPVSGVEEVNKEEQEGSDEEWEQVGPRNKSSVTRQADFVQTPITDIFGGHMRSVVYQQSSKESATLQPFFTLQLDIQSEKIRTVQDALESLVARESVQGYTTKTKQEVEICRRVTLEELPPVLVLHLKRFVFEKTGGCQKLIKNIEYPVDLEVSKDLLSPGVKSKIFKGQRTYRLFAVVYHHGNSATGGHYTTDVFQIGLNGWLRIDDQSVKVINQYQVVKQTVERTAYLLYYRRVDLL |
| Enzyme Length | 805 |
| Uniprot Accession Number | Q7ZXR7 |
| Absorption | |
| Active Site | ACT_SITE 431; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093"; ACT_SITE 756; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093" |
| 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:Q14694}; |
| DNA Binding | |
| EC Number | 3.4.19.12 |
| Enzyme Function | FUNCTION: Hydrolase that can remove conjugated ubiquitin from target proteins such as p53/tp53. Acts as an essential regulator of p53/tp53 stability: in unstressed cells, specifically deubiquitinates p53/tp53 in the cytoplasm, leading to counteracts MDM2 action and stabilize p53/tp53. Following DNA damage, translocates to the nucleus and deubiquitinates p53/tp53, leading to regulate the p53/TP53-dependent DNA damage response. Component of a regulatory loop that controls autophagy and p53/tp53 levels (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Compositional bias (2); Domain (1); Region (3) |
| Keywords | Autophagy;Cytoplasm;DNA damage;DNA repair;Hydrolase;Nucleus;Protease;Thiol protease;Ubl conjugation pathway |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14694}. Nucleus {ECO:0000250|UniProtKB:Q14694}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 89,197 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |