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P54252 (ATX3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ataxin-3

EC=3.4.19.12
Alternative name(s):
Machado-Joseph disease protein 1
Spinocerebellar ataxia type 3 protein
Gene names
Name:ATXN3
Synonyms:ATX3, MJD, MJD1, SCA3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length364 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Deubiquitinating enzyme involved in protein homeostasis maintenance, transcription, cytoskeleton regulation, myogenesis and degradation of misfolded chaperone substrates. Binds long polyubiquitin chains and trims them, while it has weak or no activity against chains of 4 or less ubiquitins. 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. In response to misfolded substrate ubiquitination, mediates deubiquitination of monoubiquitinated STUB1/CHIP. Interacts with key regulators of transcription and represses transcription: acts as a histone-binding protein that regulates transcription. Ref.9 Ref.10 Ref.12 Ref.16

Catalytic activity

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). Ref.10

Subunit structure

Interacts with STUB1/CHIP (when monoubiquitinated) By similarity. Interacts with DNA repair proteins RAD23A and RAD23B.

Subcellular location

Nucleus matrix. Note: Predominantly nuclear, but not exclusively, inner nuclear matrix. Ref.8

Tissue specificity

Ubiquitous.

Domain

The UIM domains bind ubiquitin and interact with various E3 ubiquitin-protein ligase, such as STUB1/CHIP. They are essential to limit the length of ubiquitin chains By similarity.

Post-translational modification

Monoubiquitinated N-terminally by UBE2W, possibly leading to activate the deubiquitinating enzyme activity.

Polymorphism

The poly-Gln region of ATXN3 is highly polymorphic (14 to 41 repeats) in the normal population and is expanded to about 55-82 repeats in spinocerebellar ataxia 3 (SCA3) patients.

The MJD1a allele carries a single nucleotide substitution in codon 349 generating a stop codon instead of a Tyr. In the Japanese population, the MJD1a allele seems to be significantly associated with Gln expansion.

Involvement in 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1

Sequence similarities

Contains 1 Josephin domain.

Contains 3 UIM (ubiquitin-interacting motif) repeats.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
Ubl conjugation pathway
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
Triplet repeat expansion
   DiseaseNeurodegeneration
Spinocerebellar ataxia
   DomainRepeat
   Molecular functionHydrolase
Protease
Thiol protease
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton organization

Inferred from mutant phenotype PubMed 20637808. Source: MGI

cell death

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to misfolded protein

Inferred from sequence or structural similarity. Source: UniProtKB

intermediate filament cytoskeleton organization

Inferred from mutant phenotype PubMed 20637808. Source: MGI

microtubule cytoskeleton organization

Inferred from mutant phenotype PubMed 20637808. Source: MGI

misfolded or incompletely synthesized protein catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

monoubiquitinated protein deubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

nervous system development

Traceable author statement PubMed 9124802. Source: ProtInc

nucleotide-excision repair

Traceable author statement PubMed 10915768. Source: ProtInc

proteasome-mediated ubiquitin-dependent protein catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

protein K48-linked deubiquitination

Inferred from direct assay PubMed 22970133. Source: ParkinsonsUK-UCL

protein K63-linked deubiquitination

Inferred from direct assay PubMed 22970133. Source: ParkinsonsUK-UCL

regulation of cell-substrate adhesion

Inferred from mutant phenotype PubMed 20637808. Source: MGI

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

synaptic transmission

Traceable author statement PubMed 7655453. Source: ProtInc

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Traceable author statement PubMed 9124802. Source: ProtInc

nuclear matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement Ref.8. Source: ProtInc

   Molecular_functionATPase binding

Inferred from physical interaction PubMed 22970133. Source: ParkinsonsUK-UCL

Lys48-specific deubiquitinase activity

Inferred from direct assay PubMed 22970133. Source: ParkinsonsUK-UCL

Lys63-specific deubiquitinase activity

Inferred from direct assay PubMed 22970133. Source: ParkinsonsUK-UCL

identical protein binding

Inferred from physical interaction PubMed 22129356. Source: IntAct

omega peptidase activity

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction PubMed 16525503PubMed 16712842PubMed 16713569PubMed 19153604PubMed 20414249PubMed 16525503. Source: IntAct

ubiquitin protein ligase binding

Inferred from sequence or structural similarity. Source: UniProtKB

ubiquitin thiolesterase activity

Inferred from sequence or structural similarity. Source: UniProtKB

ubiquitin-specific protease activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P54252-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P54252-2)

The sequence of this isoform differs from the canonical sequence as follows:
     332-364: KACSPFIMFATFTLYLTYELHVIFALHYSSFPL → DAMSEEDMLQAAVTMSLETVRNDLKTEGKK
Isoform 3 (identifier: P54252-3)

The sequence of this isoform differs from the canonical sequence as follows:
     10-64: Missing.
     332-364: KACSPFIMFATFTLYLTYELHVIFALHYSSFPL → DAMSEEDMLQAAVTMSLETVRNDLKTEGKK
Isoform 4 (identifier: P54252-4)

The sequence of this isoform differs from the canonical sequence as follows:
     63-77: Missing.
     332-364: KACSPFIMFATFTLYLTYELHVIFALHYSSFPL → DAMSEEDMLQAAVTMSLETVRNDLKTEGKK
Note: Gene prediction based on EST data.
Isoform 5 (identifier: P54252-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-179: Missing.
     332-364: KACSPFIMFATFTLYLTYELHVIFALHYSSFPL → DAMSEEDMLQAAVTMSLETVRNDLKTEGKK
Note: Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 364364Ataxin-3
PRO_0000053831

Regions

Domain1 – 180180Josephin
Repeat224 – 24320UIM 1
Repeat244 – 26320UIM 2
Repeat331 – 34818UIM 3
Compositional bias292 – 30514Poly-Gln

Sites

Active site141Nucleophile
Active site1191Proton acceptor Probable
Active site1341 Probable

Amino acid modifications

Modified residue2191Phosphoserine By similarity
Cross-link1Peptide (Met-Gly) (interchain with G-Cter in ubiquitin)
Cross-link200Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.13

Natural variations

Alternative sequence1 – 179179Missing in isoform 5.
VSP_047085
Alternative sequence10 – 6455Missing in isoform 3.
VSP_002783
Alternative sequence63 – 7715Missing in isoform 4.
VSP_047086
Alternative sequence332 – 36433KACSP…SSFPL → DAMSEEDMLQAAVTMSLETV RNDLKTEGKK in isoform 2, isoform 3, isoform 4 and isoform 5.
VSP_002784
Natural variant2121V → M. Ref.1 Ref.2 Ref.4
Corresponds to variant rs1048755 [ dbSNP | Ensembl ].
VAR_013688
Natural variant3061G → QQQQQQQQQQQQR.
VAR_013689
Natural variant349 – 36416Missing in allele MJD1a.
VAR_013690

Experimental info

Mutagenesis141C → A: Loss of deubiquitination activity. Ref.12 Ref.16
Mutagenesis2361S → A: Inhibits substrate trapping. Ref.16
Mutagenesis2561S → A: Inhibits substrate trapping. Ref.16
Mutagenesis3351S → A: No effect on ubiquitination. Ref.16
Sequence conflict2521A → T in AAB63352. Ref.2
Sequence conflict2521A → T in AAB63353. Ref.2
Sequence conflict2521A → T in AAB63354. Ref.2

Secondary structure

........................................ 364
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 2, 2010. Version 4.
Checksum: 4B2477EB67C30EFF

FASTA36441,781
        10         20         30         40         50         60 
MESIFHEKQE GSLCAQHCLN NLLQGEYFSP VELSSIAHQL DEEERMRMAE GGVTSEDYRT 

        70         80         90        100        110        120 
FLQQPSGNMD DSGFFSIQVI SNALKVWGLE LILFNSPEYQ RLRIDPINER SFICNYKEHW 

       130        140        150        160        170        180 
FTVRKLGKQW FNLNSLLTGP ELISDTYLAL FLAQLQQEGY SIFVVKGDLP DCEADQLLQM 

       190        200        210        220        230        240 
IRVQQMHRPK LIGEELAQLK EQRVHKTDLE RVLEANDGSG MLDEDEEDLQ RALALSRQEI 

       250        260        270        280        290        300 
DMEDEEADLR RAIQLSMQGS SRNISQDMTQ TSGTNLTSEE LRKRREAYFE KQQQKQQQQQ 

       310        320        330        340        350        360 
QQQQQGDLSG QSSHPCERPA TSSGALGSDL GKACSPFIMF ATFTLYLTYE LHVIFALHYS 


SFPL 

« Hide

Isoform 2 [UniParc].

Checksum: 90C3EF73BB26CAFD
Show »

FASTA36141,250
Isoform 3 [UniParc].

Checksum: D2103044A948A525
Show »

FASTA30635,006
Isoform 4 [UniParc].

Checksum: D4DE7B21BDE6C4F1
Show »

FASTA34639,638
Isoform 5 [UniParc].

Checksum: F6BDA4CEE7251228
Show »

FASTA18220,633

References

« Hide 'large scale' references
[1]"CAG expansions in a novel gene for Machado-Joseph disease at chromosome 14q32.1."
Kawaguchi Y., Okamoto T., Taniwaki M., Aizawa M., Inoue M., Katayama S., Kawakami H., Nakamura S., Nishimura M., Akiguchi I., Kimura J., Narumiya S., Kakizuka A.
Nat. Genet. 8:221-228(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS MET-212; GLY-306 DELINS GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-ARG AND 349-TYR--LEU-364 DEL, INVOLVEMENT IN SCA3.
Tissue: Brain.
[2]"Machado-Joseph disease gene products carrying different carboxyl termini."
Goto J., Watanabe M., Ichikawa Y., Yee S.-B., Ihara N., Endo K., Igarashi S., Takiyama Y., Gaspar C., Maciel P., Tsuji S., Rouleau G.A., Kanazawa I.
Neurosci. Res. 28:373-377(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANTS MET-212; GLY-306 DELINS GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-ARG AND 349-TYR--LEU-364 DEL.
[3]"The genomic structure and expression of MJD, the Machado-Joseph disease gene."
Ichikawa Y., Goto J., Hattori M., Toyoda A., Ishii K., Jeong S.-Y., Hashida H., Masuda N., Ogata K., Kasai F., Hirai M., Maciel P., Rouleau G.A., Sakaki Y., Kanazawa I.
J. Hum. Genet. 46:413-422(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3), VARIANT 349-TYR--LEU-364 DEL.
[4]NIEHS SNPs program
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT MET-212.
[5]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT GLY-306 DELINS GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-ARG.
Tissue: Mammary gland.
[8]"Ataxin-3 is transported into the nucleus and associates with the nuclear matrix."
Tait D., Riccio M., Sittler A., Scherzinger E., Santi S., Ognibene A., Maraldi N.M., Lehrach H., Wanker E.E.
Hum. Mol. Genet. 7:991-997(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[9]"Ataxin-3 is a histone-binding protein with two independent transcriptional corepressor activities."
Li F., Macfarlan T., Pittman R.N., Chakravarti D.
J. Biol. Chem. 277:45004-45012(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"Josephin domain-containing proteins from a variety of species are active de-ubiquitination enzymes."
Tzvetkov N., Breuer P.
Biol. Chem. 388:973-978(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, FUNCTION.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"JosD1, a membrane-targeted deubiquitinating enzyme, is activated by ubiquitination and regulates membrane dynamics, cell motility, and endocytosis."
Seki T., Gong L., Williams A.J., Sakai N., Todi S.V., Paulson H.L.
J. Biol. Chem. 288:17145-17155(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF CYS-14.
[13]"The ubiquitin-conjugating enzyme (E2) Ube2w ubiquitinates the N terminus of substrates."
Scaglione K.M., Basrur V., Ashraf N.S., Konen J.R., Elenitoba-Johnson K.S., Todi S.V., Paulson H.L.
J. Biol. Chem. 288:18784-18788(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION AT MET-1 AND LYS-200.
[14]"Structural modeling of ataxin-3 reveals distant homology to adaptins."
Albrecht M., Hoffmann D., Evert B.O., Schmitt I., Wuellner U., Lengauer T.
Proteins 50:355-370(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
[15]"The solution structure of the Josephin domain of ataxin-3: structural determinants for molecular recognition."
Nicastro G., Menon R.P., Masino L., Knowles P.P., McDonald N.Q., Pastore A.
Proc. Natl. Acad. Sci. U.S.A. 102:10493-10498(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-182.
[16]"Deubiquitinating function of ataxin-3: insights from the solution structure of the Josephin domain."
Mao Y., Senic-Matuglia F., Di Fiore P.P., Polo S., Hodsdon M.E., De Camilli P.
Proc. Natl. Acad. Sci. U.S.A. 102:12700-12705(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-185, FUNCTION, MUTAGENESIS OF CYS-14; SER-236; SER-256 AND SER-335.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S75313 mRNA. Translation: AAB33571.1.
U64820 mRNA. Translation: AAB63352.1.
U64821 mRNA. Translation: AAB63353.1.
U64822 mRNA. Translation: AAB63354.1.
AB050194 mRNA. Translation: BAB18798.1.
AB038653 Genomic DNA. Translation: BAB55645.1.
AB038653 Genomic DNA. Translation: BAB55646.1.
EU009923 Genomic DNA. Translation: ABS29269.1.
AL049872 Genomic DNA. No translation available.
AL121773 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW81472.1.
BC033711 mRNA. Translation: AAH33711.1.
CCDSCCDS32143.1. [P54252-3]
CCDS45154.1. [P54252-4]
CCDS53908.1. [P54252-5]
CCDS9900.1. [P54252-2]
PIRS50830.
RefSeqNP_001121168.1. NM_001127696.1. [P54252-4]
NP_001158252.1. NM_001164780.1. [P54252-5]
NP_004984.2. NM_004993.5. [P54252-2]
NP_109376.1. NM_030660.4. [P54252-3]
UniGeneHs.532632.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YZBNMR-A1-182[»]
2AGANMR-A1-185[»]
2DOSNMR-A1-171[»]
2JRINMR-A1-182[»]
2KLZNMR-A222-263[»]
DisProtDP00576.
ProteinModelPortalP54252.
SMRP54252. Positions 1-185, 220-264.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110433. 74 interactions.
IntActP54252. 22 interactions.
MINTMINT-272839.

Protein family/group databases

MEROPSC86.001.

PTM databases

PhosphoSiteP54252.

Polymorphism databases

DMDM290457685.

Proteomic databases

MaxQBP54252.
PaxDbP54252.
PRIDEP54252.

Protocols and materials databases

DNASU4287.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000340660; ENSP00000339110; ENSG00000066427. [P54252-3]
ENST00000393287; ENSP00000376965; ENSG00000066427. [P54252-2]
ENST00000502250; ENSP00000425322; ENSG00000066427. [P54252-5]
ENST00000503767; ENSP00000426697; ENSG00000066427. [P54252-4]
ENST00000532032; ENSP00000437157; ENSG00000066427. [P54252-1]
GeneID4287.
KEGGhsa:4287.
UCSCuc001yac.4. human. [P54252-2]
uc001yad.4. human. [P54252-3]
uc021rzo.1. human. [P54252-1]

Organism-specific databases

CTD4287.
GeneCardsGC14M092524.
GeneReviewsATXN3.
HGNCHGNC:7106. ATXN3.
HPACAB021976.
HPA024123.
MIM109150. phenotype.
607047. gene.
neXtProtNX_P54252.
Orphanet276238. Machado-Joseph disease type 1.
276241. Machado-Joseph disease type 2.
276244. Machado-Joseph disease type 3.
PharmGKBPA134971833.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG327234.
HOVERGENHBG025648.
KOK11863.
OrthoDBEOG779NZ3.
PhylomeDBP54252.
TreeFamTF314228.

Gene expression databases

ArrayExpressP54252.
BgeeP54252.
GenevestigatorP54252.

Family and domain databases

InterProIPR006155. Josephin.
IPR003903. Ubiquitin-int_motif.
[Graphical view]
PfamPF02099. Josephin. 1 hit.
PF02809. UIM. 2 hits.
[Graphical view]
PRINTSPR01233. JOSEPHIN.
SMARTSM00726. UIM. 2 hits.
[Graphical view]
PROSITEPS50957. JOSEPHIN. 1 hit.
PS50330. UIM. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP54252.
GeneWikiAtaxin_3.
GenomeRNAi4287.
NextBio16875.
PMAP-CutDBA7LFZ5.
PROP54252.
SOURCESearch...

Entry information

Entry nameATX3_HUMAN
AccessionPrimary (citable) accession number: P54252
Secondary accession number(s): A7LFZ5 expand/collapse secondary AC list , D6RDL9, E9PB63, O15284, O15285, O15286, Q8N189, Q96TC3, Q96TC4, Q9H3N0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: March 2, 2010
Last modified: July 9, 2014
This is version 150 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM