OTUD4
entrez
54726
canonical
uniprot
Q01804
canonical
ensembl
ENSG00000164164
resolver
ensp
ENSP00000395487
resolver
ensp
ENSP00000409279
resolver
ensp
ENSP00000424192
resolver
ensp
ENSP00000576736
resolver
ensp
ENSP00000594665
resolver
ensp
ENSP00000594667
resolver
ensp
ENSP00000743886
resolver
genesymbol
OTUD4
resolver
genesymbol_syn
HIN-1
resolver
genesymbol_syn
KIAA1046
resolver
hgnc
HGNC:24949
resolver
uniprot
B4DYS4
resolver
uniprot
Q147U2
resolver
uniprot
Q1ZYK1
resolver
uniprot
Q6PG39
resolver
uniprot
Q96MQ5
resolver
uniprot
Q9NT94
resolver
uniprot
Q9UPV6
resolver
uniprot_entry
OTUD4_HUMAN
resolver
uniprot_sec
B4DYS4
resolver
uniprot_sec
Q147U2
resolver
uniprot_sec
Q1ZYK1
resolver
uniprot_sec
Q6PG39
resolver
uniprot_sec
Q96MQ5
resolver
uniprot_sec
Q9NT94
resolver
uniprot_sec
Q9UPV6
resolver
activity_regulation
ACTIVITY REGULATION: Phosphorylation on Ser-202 and Ser-204 induces 'Lys-63'-specific deubiquitinase activity. {ECO:0000269|PubMed:29395066}.
uniprot
proteins
amino_acid_sequence
MEAAVGVPDGGDQGGAGPREDATPMDAYLRKLGLYRKLVAKDGSCLFRAVAEQVLHSQSRHVEVRMACIHYLRENREKFEAFIEGSFEEYLKRLENPQEWVGQVEISALSLMYRKDFIIYREPNVSPSQVTENNFPEKVLLCFSNGNHYDIVYPIKYKESSAMCQSLLYELLYEKVFKTDVSKIVMELDTLEVADEDNSEISDSEDDSCKSKTAAAAADVNGFKPLSGNEQLKNNGNSTSLPLSRKVLKSLNPAVYRNVEYEIWLKSKQAQQKRDYSIAAGLQYEVGDKCQVRLDHNGKFLNADVQGIHSENGPVLVEELGKKHTSKNLKAPPPESWNTVSGKKMKKPSTSGQNFHSDVDYRGPKNPSKPIKAPSALPPRLQHPSGVRQHAFSSHSSGSQSQKFSSEHKNLSRTPSQIIRKPDRERVEDFDHTSRESNYFGLSPEERREKQAIEESRLLYEIQNRDEQAFPALSSSSVNQSASQSSNPCVQRKSSHVGDRKGSRRRMDTEERKDKDSIHGHSQLDKRPEPSTLENITDDKYATVSSPSKSKKLECPSPAEQKPAEHVSLSNPAPLLVSPEVHLTPAVPSLPATVPAWPSEPTTFGPTGVPAPIPVLSVTQTLTTGPDSAVSQAHLTPSPVPVSIQAVNQPLMPLPQTLSLYQDPLYPGFPCNEKGDRAIVPPYSLCQTGEDLPKDKNILRFFFNLGVKAYSCPMWAPHSYLYPLHQAYLAACRMYPKVPVPVYPHNPWFQEAPAAQNESDCTCTDAHFPMQTEASVNGQMPQPEIGPPTFSSPLVIPPSQVSESHGQLSYQADLESETPGQLLHADYEESLSGKNMFPQPSFGPNPFLGPVPIAPPFFPHVWYGYPFQGFIENPVMRQNIVLPSDEKGELDLSLENLDLSKDCGSVSTVDEFPEARGEHVHSLPEASVSSKPDEGRTEQSSQTRKADTALASIPPVAEGKAHPPTQILNRERETVPVELEPKRTIQSLKEKTEKVKDPKTAADVVSPGANSVDSRVQRPKEESSEDENEVSNILRSGRSKQFYNQTYGSRKYKSDWGYSGRGGYQHVRSEESWKGQPSRSRDEGYQYHRNVRGRPFRGDRRRSGMGDGHRGQHT
uniprot
proteins
ec_number
3.4.19.12
uniprot
proteins
function
FUNCTION: Deubiquitinase which hydrolyzes the isopeptide bond between the ubiquitin C-terminus and the lysine epsilon-amino group of the target protein (PubMed:23827681, PubMed:25944111, PubMed:29395066). May negatively regulate inflammatory and pathogen recognition signaling in innate immune response. Upon phosphorylation at Ser-202 and Ser-204 residues, via IL-1 receptor and Toll-like receptor signaling pathway, specifically deubiquitinates 'Lys-63'-polyubiquitinated MYD88 adapter protein triggering down-regulation of NF-kappa-B-dependent transcription of inflammatory mediators (PubMed:29395066). Independently of the catalytic activity, acts as a scaffold for alternative deubiquitinases to assemble specific deubiquitinase-substrate complexes. Associates with USP7 and USP9X deubiquitinases to stabilize alkylation repair enzyme ALKBH3, thereby promoting the repair of alkylated DNA lesions (PubMed:25944111). {ECO:0000269|PubMed:23827681, ECO:0000269|PubMed:25944111, ECO:0000269|PubMed:29395066}.
uniprot
proteins
mass_dalton
124045
uniprot
proteins
mutagenesis
MUTAGEN 45; /note="C->A: Abolishes 'Lys-48'- and 'Lys-63'-specific deubiquitinase activity. Impairs 'Lys-63'-specific deubiquitinase activity toward MYD88 substrate."; /evidence="ECO:0000269|PubMed:23827681, ECO:0000269|PubMed:25944111, ECO:0000269|PubMed:29395066"; MUTAGEN 45; /note="C->S: Abolishes 'Lys-48'- and 'Lys-63'-specific deubiquitinase activity."; /evidence="ECO:0000269|PubMed:29395066"; MUTAGEN 181..550; /note="Missing: Abolishes interaction with USP7 and USP9X deubiquitinases."; /evidence="ECO:0000269|PubMed:25944111"; MUTAGEN 202; /note="S->A: Decreases 'Lys-63'-specific deubiquitinase activity. Loss of 'Lys-63'-specific deubiquitinase activity; when associated with A-204."; /evidence="ECO:0000269|PubMed:29395066"; MUTAGEN 204; /note="S->A: Loss of 'Lys-63'-specific deubiquitinase activity; when associated with A-204."; /evidence="ECO:0000269|PubMed:29395066"; MUTAGEN 273..275; /note="KRD->AAA: Abolishes 'Lys-63'-specific deubiquitinase activity by impairing the affinity for 'Lys-63'-linked ubiquitin chain substrate."; /evidence="ECO:0000269|PubMed:29395066"; MUTAGEN 279; /note="A->R: Abolishes 'Lys-63'-specific deubiquitinase activity by impairing the affinity for 'Lys-63'-linked ubiquitin chain substrate."; /evidence="ECO:0000269|PubMed:29395066
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on Ser-202 and Ser-204 likely by CSNK2A1-CSNK2A2 serine/threonine-protein kinase complex. Activates 'Lys-63'-specific deubiquitinase activity. {ECO:0000269|PubMed:29395066}.
uniprot
proteins
pubmed
10470851
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
1475186
uniprot
proteins
pubmed
15144186
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23656588
uniprot
proteins
pubmed
23827681
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944111
uniprot
proteins
pubmed
29395066
uniprot
proteins
pubmed
40215271
uniprot
proteins
sequence_length
1114
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25944111}. Nucleus {ECO:0000269|PubMed:25944111}. Note=Primarily cytoplasmic. {ECO:0000269|PubMed:25944111}.
uniprot
proteins