| IED ID | IndEnz0002009253 |
| Enzyme Type ID | protease009253 |
| Protein Name |
OTU domain-containing protein 7B EC 3.4.19.12 Cellular zinc finger anti-NF-kappa-B protein Cezanne Zinc finger A20 domain-containing protein 1 Zinc finger protein Cezanne |
| Gene Name | OTUD7B ZA20D1 |
| 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 | MTLDMDAVLSDFVRSTGAEPGLARDLLEGKNWDVNAALSDFEQLRQVHAGNLPPSFSEGSGGSRTPEKGFSDREPTRPPRPILQRQDDIVQEKRLSRGISHASSSIVSLARSHVSSNGGGGGSNEHPLEMPICAFQLPDLTVYNEDFRSFIERDLIEQSMLVALEQAGRLNWWVSVDPTSQRLLPLATTGDGNCLLHAASLGMWGFHDRDLMLRKALYALMEKGVEKEALKRRWRWQQTQQNKESGLVYTEDEWQKEWNELIKLASSEPRMHLGTNGANCGGVESSEEPVYESLEEFHVFVLAHVLRRPIVVVADTMLRDSGGEAFAPIPFGGIYLPLEVPASQCHRSPLVLAYDQAHFSALVSMEQKENTKEQAVIPLTDSEYKLLPLHFAVDPGKGWEWGKDDSDNVRLASVILSLEVKLHLLHSYMNVKWIPLSSDAQAPLAQPESPTASAGDEPRSTPESGDSDKESVGSSSTSNEGGRRKEKSKRDREKDKKRADSVANKLGSFGKTLGSKLKKNMGGLMHSKGSKPGGVGTGLGGSSGTETLEKKKKNSLKSWKGGKEEAAGDGPVSEKPPAESVGNGGSKYSQEVMQSLSILRTAMQGEGKFIFVGTLKMGHRHQYQEEMIQRYLSDAEERFLAEQKQKEAERKIMNGGIGGGPPPAKKPEPDAREEQPTGPPAESRAMAFSTGYPGDFTIPRPSGGGVHCQEPRRQLAGGPCVGGLPPYATFPRQCPPGRPYPHQDSIPSLEPGSHSKDGLHRGALLPPPYRVADSYSNGYREPPEPDGWAGGLRGLPPTQTKCKQPNCSFYGHPETNNFCSCCYREELRRREREPDGELLVHRF |
| Enzyme Length | 843 |
| Uniprot Accession Number | Q6GQQ9 |
| Absorption | |
| Active Site | ACT_SITE 191; /evidence="ECO:0000250"; ACT_SITE 194; /note="Nucleophile"; /evidence="ECO:0000269|PubMed:12682062, ECO:0000269|PubMed:14748687, ECO:0000269|PubMed:22179831, ECO:0000269|PubMed:27732584"; ACT_SITE 358; /note="Proton acceptor"; /evidence="ECO:0000269|PubMed:27732584" |
| Activity Regulation | ACTIVITY REGULATION: Deubiquitinase activity is inhibited following interaction with PARK7. {ECO:0000269|PubMed:21097510}. |
| 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:12682062, ECO:0000269|PubMed:14748687, ECO:0000269|PubMed:22179831, ECO:0000269|PubMed:23827681, ECO:0000269|PubMed:26903241, ECO:0000269|PubMed:27732584}; |
| DNA Binding | |
| EC Number | 3.4.19.12 |
| Enzyme Function | FUNCTION: Negative regulator of the non-canonical NF-kappa-B pathway that acts by mediating deubiquitination of TRAF3, an inhibitor of the NF-kappa-B pathway, thereby acting as a negative regulator of B-cell responses. In response to non-canonical NF-kappa-B stimuli, deubiquitinates 'Lys-48'-linked polyubiquitin chains of TRAF3, preventing TRAF3 proteolysis and over-activation of non-canonical NF-kappa-B. Negatively regulates mucosal immunity against infections (By similarity). Deubiquitinates ZAP70, and thereby regulates T cell receptor (TCR) signaling that leads to the activation of NF-kappa-B (PubMed:26903241). Plays a role in T cell homeostasis and is required for normal T cell responses, including production of IFNG and IL2 (By similarity). Mediates deubiquitination of EGFR (PubMed:22179831). Has deubiquitinating activity toward 'Lys-11', 'Lys-48' and 'Lys-63'-linked polyubiquitin chains (PubMed:27732584). Has a much higher catalytic rate with 'Lys-11'-linked polyubiquitin chains (in vitro); however the physiological significance of these data are unsure (PubMed:27732584). Hydrolyzes both linear and branched forms of polyubiquitin. {ECO:0000250|UniProtKB:B2RUR8, ECO:0000269|PubMed:11463333, ECO:0000269|PubMed:12682062, ECO:0000269|PubMed:18178551, ECO:0000269|PubMed:20622874, ECO:0000269|PubMed:22179831, ECO:0000269|PubMed:23827681, ECO:0000269|PubMed:27732584}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (1); Beta strand (14); Chain (1); Compositional bias (4); Domain (1); Erroneous initiation (1); Helix (14); Metal binding (4); Modified residue (5); Motif (1); Mutagenesis (14); Region (7); Sequence conflict (3); Site (1); Turn (2); Zinc finger (1) |
| Keywords | 3D-structure;Adaptive immunity;Alternative splicing;Cytoplasm;Hydrolase;Immunity;Metal-binding;Nucleus;Phosphoprotein;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway;Zinc;Zinc-finger |
| Interact With | Q8IVM0; Q9H305; Q15038; Q7L775; Q96LI6; Q96BN8; Q99497; Q92569; Q7Z5V6-2; P20618; Q8N0X7; P01023; P02768-3; P54253; P46379-2; P55212; P09172; Q14203-5; G5E9A7; O14645; P41091; O75460-2; P22607; Q0VDC6; P14136; Q14957; P06396; P54652; P04792; O43464; Q8WXH2; O60333-2; O14901; P13473-2; P27361; P51608; P19404; P35240-4; Q9BVL2; O14832; D3DTS7; O60260-5; O75400-2; P60891; P62826; Q9Y3C5; P37840; P00441; Q7Z699; Q13148; Q86WV8; P02766; P0CG47; Q9UMX0; O76024; Q9Y649 |
| Induction | INDUCTION: By TNF-alpha. {ECO:0000269|PubMed:18178551}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11463333, ECO:0000269|PubMed:21888622}. Nucleus {ECO:0000269|PubMed:21888622}. Note=Shuttles be cytoplasm and the nucleus in a XPO1/CRM1-dependent manner. {ECO:0000269|PubMed:21888622}. |
| Modified Residue | MOD_RES 100; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"; MOD_RES 464; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:B2RUR8"; MOD_RES 467; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 471; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:B2RUR8"; MOD_RES 729; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:B2RUR8" |
| Post Translational Modification | PTM: Phosphorylated by EGFR. {ECO:0000269|PubMed:22179831}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 5LRU; 5LRV; 5LRW; |
| Mapped Pubmed ID | 12887920; 15334086; 16260783; 16603398; 16953224; 18029035; 18474597; 19427028; 19615732; 19910467; 21624200; 22179575; 22435550; 22848449; 23313255; 23564640; 24098568; 24705354; 25353672; 25355043; 25638165; 25814554; 26112491; 26148512; 27499151; 28365890; 28489822; 28817177; 28880268; 29973362; 31747939; 31937588; 34035221; |
| Motif | MOTIF 483..498; /note=Nuclear localization signal; /evidence=ECO:0000255 |
| Gene Encoded By | |
| Mass | 92,526 |
| Kinetics | |
| Metal Binding | METAL 802; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00451; METAL 807; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00451; METAL 819; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00451; METAL 822; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00451 |
| Rhea ID | |
| Cross Reference Brenda |