ATXN3
entrez
4287
canonical
uniprot
P54252
canonical
ensembl
ENSG00000066427
resolver
ensp
ENSP00000339110
resolver
ensp
ENSP00000376965
resolver
ensp
ENSP00000389376
resolver
ensp
ENSP00000425322
resolver
ensp
ENSP00000426697
resolver
ensp
ENSP00000496695
resolver
ensp
ENSP00000768286
resolver
ensp
ENSP00000798625
resolver
enst
ENST00000393287
resolver
enst
ENST00000429774
resolver
genesymbol
ATXN3
resolver
genesymbol_syn
ATX3
resolver
genesymbol_syn
MJD
resolver
genesymbol_syn
MJD1
resolver
genesymbol_syn
SCA3
resolver
hgnc
HGNC:7106
resolver
uniprot
A0A0A0MS38
resolver
uniprot
A7LFZ5
resolver
uniprot
C9JQV6
resolver
uniprot
D6RDL9
resolver
uniprot
E9PB63
resolver
uniprot
O15284
resolver
uniprot
O15285
resolver
uniprot
O15286
resolver
uniprot
Q8N189
resolver
uniprot
Q96TC3
resolver
uniprot
Q96TC4
resolver
uniprot
Q9H3N0
resolver
uniprot_entry
A0A0A0MS38_HUMAN
resolver
uniprot_entry
ATX3_HUMAN
resolver
uniprot_entry
C9JQV6_HUMAN
resolver
uniprot_sec
A7LFZ5
resolver
uniprot_sec
D6RDL9
resolver
uniprot_sec
E9PB63
resolver
uniprot_sec
O15284
resolver
uniprot_sec
O15285
resolver
uniprot_sec
O15286
resolver
uniprot_sec
Q8N189
resolver
uniprot_sec
Q96TC3
resolver
uniprot_sec
Q96TC4
resolver
uniprot_sec
Q9H3N0
resolver
amino_acid_sequence
MESIFHEKQEGSLCAQHCLNNLLQGEYFSPVELSSIAHQLDEEERMRMAEGGVTSEDYRTFLQQPSGNMDDSGFFSIQVISNALKVWGLELILFNSPEYQRLRIDPINERSFICNYKEHWFTVRKLGKQWFNLNSLLTGPELISDTYLALFLAQLQQEGYSIFVVKGDLPDCEADQLLQMIRVQQMHRPKLIGEELAQLKEQRVHKTDLERVLEANDGSGMLDEDEEDLQRALALSRQEIDMEDEEADLRRAIQLSMQGSSRNISQDMTQTSGTNLTSEELRKRREAYFEKQQQKQQQQQQQQQQGDLSGQSSHPCERPATSSGALGSDLGDAMSEEDMLQAAVTMSLETVRNDLKTEGKK
uniprot
proteins
disease_involvement
DISEASE: Spinocerebellar ataxia 3 (SCA3) [MIM:109150]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to cerebellum degeneration with variable involvement of the brainstem and spinal cord. SCA3 belongs to the autosomal dominant cerebellar ataxias type I (ADCA I) which are characterized by cerebellar ataxia in combination with additional clinical features like optic atrophy, ophthalmoplegia, bulbar and extrapyramidal signs, peripheral neuropathy and dementia. The molecular defect in SCA3 is the a CAG repeat expansion in ATX3 coding region. Longer expansions result in earlier onset and more severe clinical manifestations of the disease. {ECO:0000269|PubMed:7874163}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.4.19.12
uniprot
proteins
function
FUNCTION: Deubiquitinating enzyme involved in protein homeostasis maintenance, transcription, cytoskeleton regulation, myogenesis and degradation of misfolded chaperone substrates (PubMed:12297501, PubMed:16118278, PubMed:17696782, PubMed:23625928, PubMed:28445460, PubMed:33157014). Binds long polyubiquitin chains and trims them, while it has weak or no activity against chains of 4 or less ubiquitins (PubMed:17696782). Involved in degradation of misfolded chaperone substrates via its interaction with STUB1/CHIP: recruited to monoubiquitinated STUB1/CHIP, and restricts the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension (By similarity). Interacts with key regulators of transcription and represses transcription: acts as a histone-binding protein that regulates transcription (PubMed:12297501). Acts as a negative regulator of mTORC1 signaling in response to amino acid deprivation by mediating deubiquitination of RHEB, thereby promoting RHEB inactivation by the TSC-TBC complex (PubMed:33157014). Regulates autophagy via the deubiquitination of 'Lys-402' of BECN1 leading to the stabilization of BECN1 (PubMed:28445460). {ECO:0000250|UniProtKB:Q9CVD2, ECO:0000269|PubMed:12297501, ECO:0000269|PubMed:16118278, ECO:0000269|PubMed:17696782, ECO:0000269|PubMed:23625928, ECO:0000269|PubMed:28445460, ECO:0000269|PubMed:33157014}.
uniprot
proteins
mass_dalton
41250
uniprot
proteins
mutagenesis
MUTAGEN 14; /note="C->A: Loss of deubiquitination activity."; /evidence="ECO:0000269|PubMed:16118278, ECO:0000269|PubMed:23625928, ECO:0000269|PubMed:33157014"; MUTAGEN 236; /note="S->A: Inhibits substrate trapping."; /evidence="ECO:0000269|PubMed:16118278"; MUTAGEN 256; /note="S->A: Inhibits substrate trapping."; /evidence="ECO:0000269|PubMed:16118278"; MUTAGEN 335; /note="S->A: No effect on ubiquitination."; /evidence="ECO:0000269|PubMed:16118278
uniprot
proteins
post_translational_modification
PTM: Monoubiquitinated N-terminally by UBE2W, possibly leading to activate the deubiquitinating enzyme activity (PubMed:23696636). {ECO:0000269|PubMed:23696636}.
uniprot
proteins
pubmed
11450850
uniprot
proteins
pubmed
12297501
uniprot
proteins
pubmed
12486728
uniprot
proteins
pubmed
12508121
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16020535
uniprot
proteins
pubmed
16118278
uniprot
proteins
pubmed
17696782
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23625928
uniprot
proteins
pubmed
23696636
uniprot
proteins
pubmed
28445460
uniprot
proteins
pubmed
30455355
uniprot
proteins
pubmed
33157014
uniprot
proteins
pubmed
7874163
uniprot
proteins
pubmed
9274833
uniprot
proteins
pubmed
9580663
uniprot
proteins
sequence_length
361
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000269|PubMed:9580663}. Nucleus {ECO:0000269|PubMed:30455355}. Lysosome membrane {ECO:0000269|PubMed:33157014}; Peripheral membrane protein {ECO:0000269|PubMed:33157014}. Note=Predominantly nuclear, but not exclusively, inner nuclear matrix (PubMed:9580663). Recruited to lysosomal membrane in response to amino acid deprivation by the RagA/RRAGA-RagB/RRAGB complex (PubMed:33157014). {ECO:0000269|PubMed:33157014, ECO:0000269|PubMed:9580663}.
uniprot
proteins