OTUD7B
entrez
56957
canonical
uniprot
Q6GQQ9
canonical
ensembl
ENSG00000264522
resolver
ensp
ENSP00000462729
resolver
ensp
ENSP00000577967
resolver
ensp
ENSP00000577970
resolver
genesymbol
OTUD7B
resolver
genesymbol_syn
ZA20D1
resolver
hgnc
HGNC:16683
resolver
uniprot
B7Z643
resolver
uniprot
D3DUZ8
resolver
uniprot
Q5SZ60
resolver
uniprot
Q8WWA7
resolver
uniprot
Q9NQ53
resolver
uniprot
Q9UFF4
resolver
uniprot_entry
OTU7B_HUMAN
resolver
uniprot_sec
B7Z643
resolver
uniprot_sec
D3DUZ8
resolver
uniprot_sec
Q5SZ60
resolver
uniprot_sec
Q8WWA7
resolver
uniprot_sec
Q9NQ53
resolver
uniprot_sec
Q9UFF4
resolver
activity_regulation
ACTIVITY REGULATION: Deubiquitinase activity is inhibited following interaction with PARK7. {ECO:0000269|PubMed:21097510}.
uniprot
proteins
amino_acid_sequence
MTLDMDAVLSDFVRSTGAEPGLARDLLEGKNWDVNAALSDFEQLRQVHAGNLPPSFSEGSGGSRTPEKGFSDREPTRPPRPILQRQDDIVQEKRLSRGISHASSSIVSLARSHVSSNGGGGGSNEHPLEMPICAFQLPDLTVYNEDFRSFIERDLIEQSMLVALEQAGRLNWWVSVDPTSQRLLPLATTGDGNCLLHAASLGMWGFHDRDLMLRKALYALMEKGVEKEALKRRWRWQQTQQNKESGLVYTEDEWQKEWNELIKLASSEPRMHLGTNGANCGGVESSEEPVYESLEEFHVFVLAHVLRRPIVVVADTMLRDSGGEAFAPIPFGGIYLPLEVPASQCHRSPLVLAYDQAHFSALVSMEQKENTKEQAVIPLTDSEYKLLPLHFAVDPGKGWEWGKDDSDNVRLASVILSLEVKLHLLHSYMNVKWIPLSSDAQAPLAQPESPTASAGDEPRSTPESGDSDKESVGSSSTSNEGGRRKEKSKRDREKDKKRADSVANKLGSFGKTLGSKLKKNMGGLMHSKGSKPGGVGTGLGGSSGTETLEKKKKNSLKSWKGGKEEAAGDGPVSEKPPAESVGNGGSKYSQEVMQSLSILRTAMQGEGKFIFVGTLKMGHRHQYQEEMIQRYLSDAEERFLAEQKQKEAERKIMNGGIGGGPPPAKKPEPDAREEQPTGPPAESRAMAFSTGYPGDFTIPRPSGGGVHCQEPRRQLAGGPCVGGLPPYATFPRQCPPGRPYPHQDSIPSLEPGSHSKDGLHRGALLPPPYRVADSYSNGYREPPEPDGWAGGLRGLPPTQTKCKQPNCSFYGHPETNNFCSCCYREELRRREREPDGELLVHRF
uniprot
proteins
ec_number
3.4.19.12
uniprot
proteins
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 (PubMed:18178551). 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 (By similarity). 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:11463333, PubMed:20622874, PubMed:23827681, 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 (PubMed:12682062). Acts as a regulator of mTORC1 and mTORC2 assembly by mediating 'Lys-63'-linked deubiquitination of MLST8, thereby promoting assembly of the mTORC2 complex, while inhibiting formation of the mTORC1 complex (PubMed:28489822). {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:26903241, ECO:0000269|PubMed:27732584, ECO:0000269|PubMed:28489822}.
uniprot
proteins
mass_dalton
92526
uniprot
proteins
mutagenesis
MUTAGEN 155..156; /note="LI->GG: Reduces deubiquitinating activity."; /evidence="ECO:0000269|PubMed:27732584"; MUTAGEN 157; /note="E->K: Reduces deubiquitinating activity with 'Lys-11'-linked ubiquitin chains; no effect on cleavage of 'Lys-48'-linked and 'Lys-63'-linked ubiquitin chains."; /evidence="ECO:0000269|PubMed:27732584"; MUTAGEN 193; /note="N->L,M: Loss of deubiquitinating activity due to stabilization of the autoinhibited conformation."; /evidence="ECO:0000269|PubMed:27732584"; MUTAGEN 194; /note="C->A: Loss of deubiquitinating activity. Increased ability to interact with polyubiquitin."; /evidence="ECO:0000269|PubMed:12682062, ECO:0000269|PubMed:14748687, ECO:0000269|PubMed:22179831, ECO:0000269|PubMed:27732584"; MUTAGEN 194; /note="C->S: Loss of deubiquitinating activity."; /evidence="ECO:0000269|PubMed:12682062, ECO:0000269|PubMed:14748687, ECO:0000269|PubMed:22179831"; MUTAGEN 194; /note="C->S: Loss of deubiquitinating activity; when associated with N-358."; /evidence="ECO:0000269|PubMed:26903241"; MUTAGEN 197; /note="H->A,E: Strongly reduces deubiquitinating activity."; /evidence="ECO:0000269|PubMed:27732584"; MUTAGEN 197; /note="H->D,N: Reduces deubiquitinating activity."; /evidence="ECO:0000269|PubMed:27732584"; MUTAGEN 210; /note="D->A: Reduces deubiquitinating activity."; /evidence="ECO:0000269|PubMed:27732584"; MUTAGEN 295; /note="E->K: Loss of deubiquitinating activity."; /evidence="ECO:0000269|PubMed:27732584"; MUTAGEN 358; /note="H->A: Loss of deubiquitinating activity."; /evidence="ECO:0000269|PubMed:27732584"; MUTAGEN 358; /note="H->N: Loss of deubiquitinating activity; when associated with S-194."; /evidence="ECO:0000269|PubMed:26903241"; MUTAGEN 809; /note="F->A: Does not affect interaction with EGFR."; /evidence="ECO:0000269|PubMed:22179831"; MUTAGEN 810; /note="Y->A: Impairs interaction with EGFR."; /evidence="ECO:0000269|PubMed:22179831
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by EGFR. {ECO:0000269|PubMed:22179831}.
uniprot
proteins
protein_family
Peptidase C64 family
uniprot
proteins
pubmed
11463333
uniprot
proteins
pubmed
12682062
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14748687
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18178551
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20622874
uniprot
proteins
pubmed
21097510
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21888622
uniprot
proteins
pubmed
22179831
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23827681
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
26903241
uniprot
proteins
pubmed
27732584
uniprot
proteins
pubmed
28489822
uniprot
proteins
sequence_length
843
uniprot
proteins
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}.
uniprot
proteins