Detail Information for IndEnz0002011551
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