Detail Information for IndEnz0002009260
IED ID IndEnz0002009260
Enzyme Type ID protease009260
Protein Name Ubiquitin thioesterase OTUB2
EC 3.4.19.12
Deubiquitinating enzyme OTUB2
OTU domain-containing ubiquitin aldehyde-binding protein 2
Otubain-2
Ubiquitin-specific-processing protease OTUB2
Gene Name OTUB2 C14orf137 OTB2 OTU2
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 MSETSFNLISEKCDILSILRDHPENRIYRRKIEELSKRFTAIRKTKGDGNCFYRALGYSYLESLLGKSREIFKFKERVLQTPNDLLAAGFEEHKFRNFFNAFYSVVELVEKDGSVSSLLKVFNDQSASDHIVQFLRLLTSAFIRNRADFFRHFIDEEMDIKDFCTHEVEPMATECDHIQITALSQALSIALQVEYVDEMDTALNHHVFPEAATPSVYLLYKTSHYNILYAADKH
Enzyme Length 234
Uniprot Accession Number Q96DC9
Absorption
Active Site ACT_SITE 48; /evidence="ECO:0000305|PubMed:15258613"; ACT_SITE 51; /note="Nucleophile"; /evidence="ECO:0000305|PubMed:12704427, ECO:0000305|PubMed:15258613"; ACT_SITE 224; /evidence="ECO:0000305|PubMed:15258613"
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:0000269|PubMed:23827681};
DNA Binding
EC Number 3.4.19.12
Enzyme Function FUNCTION: Hydrolase that can remove conjugated ubiquitin from proteins in vitro and may therefore play an important regulatory role at the level of protein turnover by preventing degradation. Mediates deubiquitination of 'Lys-11'-,'Lys-48'- and 'Lys-63'-linked polyubiquitin chains, with a preference for 'Lys-63'-linked polyubiquitin chains. {ECO:0000269|PubMed:12704427, ECO:0000269|PubMed:18954305, ECO:0000269|PubMed:23827681}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Alternative sequence (1); Beta strand (8); Chain (1); Domain (1); Helix (10); Mutagenesis (3); Site (1); Turn (2)
Keywords 3D-structure;Alternative splicing;Hydrolase;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway
Interact With Q96B67; P54252; Q9H305; Q16630; Q15038; Q92567; Q92567-2; Q9BRK4; O15344; Q9UJV3-2; Q9UHC7; Q53GA4; Q96CS7; Q969W9-2; Q04864; Q04864-2; Q8IUQ4; Q8N0X7; Q05BL1; Q13625-3; Q9Y4K3; Q9BYV2; Q9BZR9; P54252
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (14)
Cross Reference PDB 1TFF; 4FJV; 5QIO; 5QIP; 5QIQ; 5QIR; 5QIS; 5QIT; 5QIU; 5QIV; 5QIW; 5QIX; 5QIY; 5QIZ;
Mapped Pubmed ID 14661020; 16189514; 19383985; 19615732; 19996094; 20553488; 22124327; 23515685; 24560272; 25416956; 25590432; 30241937; 30472188; 30662561; 32003539; 32265297; 32830515;
Motif
Gene Encoded By
Mass 27,213
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda