IED ID | IndEnz0002011551 |
Enzyme Type ID | protease011551 |
Protein Name |
Ubiquitin carboxyl-terminal hydrolase 12 EC 3.4.19.12 Deubiquitinating enzyme 12 Ubiquitin thioesterase 12 Ubiquitin-hydrolyzing enzyme 1 Ubiquitin-specific-processing protease 12 |
Gene Name | USP12 UBH1 USP12L1 |
Organism | Homo sapiens (Human) |
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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
Enzyme Sequence | MEILMTVSKFASICTMGANASALEKEIGPEQFPVNEHYFGLVNFGNTCYCNSVLQALYFCRPFREKVLAYKSQPRKKESLLTCLADLFHSIATQKKKVGVIPPKKFITRLRKENELFDNYMQQDAHEFLNYLLNTIADILQEERKQEKQNGRLPNGNIDNENNNSTPDPTWVHEIFQGTLTNETRCLTCETISSKDEDFLDLSVDVEQNTSITHCLRGFSNTETLCSEYKYYCEECRSKQEAHKRMKVKKLPMILALHLKRFKYMDQLHRYTKLSYRVVFPLELRLFNTSGDATNPDRMYDLVAVVVHCGSGPNRGHYIAIVKSHDFWLLFDDDIVEKIDAQAIEEFYGLTSDISKNSESGYILFYQSRD |
Enzyme Length | 370 |
Uniprot Accession Number | O75317 |
Absorption | |
Active Site | ACT_SITE 48; /note="Nucleophile"; /evidence="ECO:0000269|PubMed:27373336"; ACT_SITE 317; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093" |
Activity Regulation | ACTIVITY REGULATION: Activated by interaction with WDR20 and WDR48 through different allosteric mechanisms. {ECO:0000269|PubMed:20147737, ECO:0000269|PubMed:27373336}. |
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:0000269|PubMed:19075014}; |
DNA Binding | |
EC Number | 3.4.19.12 |
Enzyme Function | FUNCTION: Deubiquitinating enzyme. Has almost no deubiquitinating activity by itself and requires the interaction with WDR20 and WDR48 to have a high activity (PubMed:19075014, PubMed:27373336). Not involved in deubiquitination of monoubiquitinated FANCD2 (PubMed:19075014). In complex with WDR48, acts as a potential tumor suppressor by positively regulating PHLPP1 stability (PubMed:24145035). {ECO:0000269|PubMed:19075014, ECO:0000269|PubMed:24145035, ECO:0000269|PubMed:27373336}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Beta strand (21); Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Helix (13); Metal binding (4); Mutagenesis (10); Region (1); Sequence conflict (1); Turn (5) |
Keywords | 3D-structure;Hydrolase;Metal-binding;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway;Zinc |
Interact With | P27797; P36957; Q8TDX7; Q8TBZ3 |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | X-ray crystallography (5) |
Cross Reference PDB | 5K16; 5K1A; 5K1B; 5K1C; 5L8W; |
Mapped Pubmed ID | 19615732; 19915573; 20501646; 22778262; 24056413; 24850727; 25216524; 25855980; 26811477; 29755129; 30266909; 30466959; 33174033; 34381028; |
Motif | |
Gene Encoded By | |
Mass | 42,858 |
Kinetics | |
Metal Binding | METAL 186; /note="Zinc"; /evidence="ECO:0007744|PDB:5K16, ECO:0007744|PDB:5K1A, ECO:0007744|PDB:5K1B, ECO:0007744|PDB:5L8W"; METAL 189; /note="Zinc"; /evidence="ECO:0007744|PDB:5K16, ECO:0007744|PDB:5K1A, ECO:0007744|PDB:5K1B, ECO:0007744|PDB:5K1C, ECO:0007744|PDB:5L8W"; METAL 233; /note="Zinc"; /evidence="ECO:0007744|PDB:5K16, ECO:0007744|PDB:5K1A, ECO:0007744|PDB:5K1B, ECO:0007744|PDB:5K1C, ECO:0007744|PDB:5L8W"; METAL 236; /note="Zinc"; /evidence="ECO:0007744|PDB:5K16, ECO:0007744|PDB:5K1A, ECO:0007744|PDB:5K1B, ECO:0007744|PDB:5K1C, ECO:0007744|PDB:5L8W" |
Rhea ID | |
Cross Reference Brenda |