OTUD3
entrez
23252
canonical
uniprot
Q5T2D3
canonical
ensembl
ENSG00000169914
resolver
ensp
ENSP00000364261
resolver
ensp
ENSP00000550313
resolver
enst
ENST00000375120
resolver
genesymbol
OTUD3
resolver
genesymbol_syn
KIAA0459
resolver
hgnc
HGNC:29038
resolver
uniprot
O75047
resolver
uniprot_entry
OTUD3_HUMAN
resolver
uniprot_sec
O75047
resolver
amino_acid_sequence
MSRKQAAKSRPGSGSRKAEAERKRDERAARRALAKERRNRPESGGGGGCEEEFVSFANQLQALGLKLREVPGDGNCLFRALGDQLEGHSRNHLKHRQETVDYMIKQREDFEPFVEDDIPFEKHVASLAKPGTFAGNDAIVAFARNHQLNVVIHQLNAPLWQIRGTEKSSVRELHIAYRYGEHYDSVRRINDNSEAPAHLQTDFQMLHQDESNKREKIKTKGMDSEDDLRDEVEDAVQKVCNATGCSDFNLIVQNLEAENYNIESAIIAVLRMNQGKRNNAEENLEPSGRVLKQCGPLWEEGGSGARIFGNQGLNEGRTENNKAQASPSEENKANKNQLAKVTNKQRREQQWMEKKKRQEERHRHKALESRGSHRDNNRSEAEANTQVTLVKTFAALNI
uniprot
proteins
ec_number
3.4.19.12
uniprot
proteins
function
FUNCTION: Deubiquitinating enzyme that hydrolyzes 'Lys-6'- and 'Lys-11'-linked polyubiquitin. Also hydrolyzes heterotypic (mixed and branched) and homotypic chains (PubMed:23827681, PubMed:32011234, PubMed:35675826). Important regulator of energy metabolism (PubMed:35675826). Glucose and fatty acids trigger its nuclear translocation by CBP-dependent acetylation (PubMed:35675826). In the nucleus, deubiquitinates and stabilizes the nuclear receptor PPARD regulating the expression of various genes involved in glucose and lipid metabolism and oxidative phosphorylation (PubMed:35675826). Also acts as a negative regulator of the ribosome quality control (RQC) by mediating deubiquitination of 40S ribosomal proteins RPS10/eS10 and RPS20/uS10, thereby antagonizing ZNF598-mediated 40S ubiquitination (PubMed:32011234). {ECO:0000269|PubMed:23827681, ECO:0000269|PubMed:32011234, ECO:0000269|PubMed:35675826}.
uniprot
proteins
mass_dalton
45124
uniprot
proteins
mutagenesis
MUTAGEN 76; /note="C->S: Abolished deubiquitinase activity."; /evidence="ECO:0000269|PubMed:32011234"; MUTAGEN 178..181; /note="RYGE->LSNG: Impaired activity."; /evidence="ECO:0000269|PubMed:23827681
uniprot
proteins
post_translational_modification
PTM: Glucose and fatty acids stimulate CREBBP-dependent acetylation, promoting its nuclear translocation. {ECO:0000269|PubMed:35675826}.
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23827681
uniprot
proteins
pubmed
32011234
uniprot
proteins
pubmed
35675826
uniprot
proteins
pubmed
9455484
uniprot
proteins
sequence_length
398
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:35675826}. Nucleus {ECO:0000269|PubMed:35675826}. Note=Glucose or fatty acid promote nuclear translocation upon acetylation. {ECO:0000269|PubMed:35675826}.
uniprot
proteins