| IED ID | IndEnz0002008340 |
| Enzyme Type ID | protease008340 |
| Protein Name |
OTU domain-containing protein 5 EC 3.4.19.12 Deubiquitinating enzyme A DUBA |
| Gene Name | OTUD5 |
| 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 | MTILPKKKPPPPDADPANEPPPPGPMPPAPRRGGGVGVGGGGTGVGGGDRDRDSGVVGARPRASPPPQGPLPGPPGALHRWALAVPPGAVAGPRPQQASPPPCGGPGGPGGGPGDALGAAAAGVGAAGVVVGVGGAVGVGGCCSGPGHSKRRRQAPGVGAVGGGSPEREEVGAGYNSEDEYEAAAARIEAMDPATVEQQEHWFEKALRDKKGFIIKQMKEDGACLFRAVADQVYGDQDMHEVVRKHCMDYLMKNADYFSNYVTEDFTTYINRKRKNNCHGNHIEMQAMAEMYNRPVEVYQYSTGTSAVEPINTFHGIHQNEDEPIRVSYHRNIHYNSVVNPNKATIGVGLGLPSFKPGFAEQSLMKNAIKTSEESWIEQQMLEDKKRATDWEATNEAIEEQVARESYLQWLRDQEKQARQVRGPSQPRKASATCSSATAAASSGLEEWTSRSPRQRSSASSPEHPELHAELGMKPPSPGTVLALAKPPSPCAPGTSSQFSAGADRATSPLVSLYPALECRALIQQMSPSAFGLNDWDDDEILASVLAVSQQEYLDSMKKNKVHRDPPPDKS |
| Enzyme Length | 571 |
| Uniprot Accession Number | Q96G74 |
| Absorption | |
| Active Site | ACT_SITE 221; /evidence=ECO:0000255; ACT_SITE 224; /note=Nucleophile; /evidence=ECO:0000269|PubMed:22245969; ACT_SITE 334; /evidence=ECO:0000305|PubMed:22245969 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by N-ethyl-maleimide (NEM). |
| 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:22245969}; |
| DNA Binding | |
| EC Number | 3.4.19.12 |
| Enzyme Function | FUNCTION: Deubiquitinating enzyme that functions as negative regulator of the innate immune system. Acts via TRAF3 deubiquitination and subsequent suppression of type I interferon (IFN) production. Has peptidase activity towards 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. Can also cleave 'Lys-11'-linked ubiquitin chains (in vitro). Controls neuroectodermal differentiation through cleaving 'Lys-48'-linked ubiquitin chains to counteract degradation of select chromatin regulators such as ARID1A, HDAC2 and HCF1 (PubMed:33523931). {ECO:0000269|PubMed:17991829, ECO:0000269|PubMed:22245969, ECO:0000269|PubMed:23827681, ECO:0000269|PubMed:33523931}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (5); Beta strand (6); Chain (1); Compositional bias (3); Domain (1); Erroneous initiation (2); Helix (10); Modified residue (6); Mutagenesis (4); Natural variant (7); Region (6); Turn (1) |
| Keywords | 3D-structure;Alternative splicing;Disease variant;Hydrolase;Mental retardation;Nucleus;Phosphoprotein;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway |
| Interact With | |
| Induction | INDUCTION: Up-regulated by bacterial lipopolysaccharide (LPS) in bone marrow-derived macrophages. {ECO:0000269|PubMed:22245969}. |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:33523931}. |
| Modified Residue | MOD_RES 64; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:22245969, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"; MOD_RES 165; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:22245969, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"; MOD_RES 175; /note="Phosphotyrosine"; /evidence="ECO:0000269|PubMed:22245969"; MOD_RES 177; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:22245969, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"; MOD_RES 452; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648"; MOD_RES 507; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:22245969" |
| Post Translational Modification | PTM: Phosphorylation at Ser-177 is required for deubiquitinating activity. {ECO:0000269|PubMed:22245969, ECO:0000269|PubMed:33523931}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 3PFY; 3TMO; 3TMP; |
| Mapped Pubmed ID | 16169070; 19615732; 20711500; 24143256; 25499082; 30232733; 30508113; 30980112; 32071088; 32655987; 32826889; 33110214; 33131077; 33417762; 33587979; 33748114; |
| Motif | |
| Gene Encoded By | |
| Mass | 60,626 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |