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P54252

- ATX3_HUMAN

UniProt

P54252 - ATX3_HUMAN

Protein

Ataxin-3

Gene

ATXN3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 4 (02 Mar 2010)
      Previous versions | rss
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    Functioni

    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.4 Publications

    Catalytic activityi

    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).1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei14 – 141Nucleophile
    Active sitei119 – 1191Proton acceptorCurated
    Active sitei134 – 1341Curated

    GO - Molecular functioni

    1. ATPase binding Source: ParkinsonsUK-UCL
    2. identical protein binding Source: IntAct
    3. Lys48-specific deubiquitinase activity Source: ParkinsonsUK-UCL
    4. Lys63-specific deubiquitinase activity Source: ParkinsonsUK-UCL
    5. omega peptidase activity Source: InterPro
    6. protein binding Source: IntAct
    7. ubiquitin protein ligase binding Source: UniProtKB
    8. ubiquitin-specific protease activity Source: UniProtKB
    9. ubiquitin thiolesterase activity Source: UniProtKB

    GO - Biological processi

    1. actin cytoskeleton organization Source: MGI
    2. cell death Source: UniProtKB-KW
    3. cellular response to misfolded protein Source: UniProtKB
    4. intermediate filament cytoskeleton organization Source: MGI
    5. microtubule cytoskeleton organization Source: MGI
    6. misfolded or incompletely synthesized protein catabolic process Source: UniProtKB
    7. monoubiquitinated protein deubiquitination Source: UniProtKB
    8. nervous system development Source: ProtInc
    9. nucleotide-excision repair Source: ProtInc
    10. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
    11. protein K48-linked deubiquitination Source: ParkinsonsUK-UCL
    12. protein K63-linked deubiquitination Source: ParkinsonsUK-UCL
    13. regulation of cell-substrate adhesion Source: MGI
    14. regulation of transcription, DNA-templated Source: UniProtKB-KW
    15. synaptic transmission Source: ProtInc
    16. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Transcription, Transcription regulation, Ubl conjugation pathway

    Protein family/group databases

    MEROPSiC86.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ataxin-3 (EC:3.4.19.12)
    Alternative name(s):
    Machado-Joseph disease protein 1
    Spinocerebellar ataxia type 3 protein
    Gene namesi
    Name:ATXN3
    Synonyms:ATX3, MJD, MJD1, SCA3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:7106. ATXN3.

    Subcellular locationi

    Nucleus matrix 1 Publication
    Note: Predominantly nuclear, but not exclusively, inner nuclear matrix.

    GO - Cellular componenti

    1. cytoplasm Source: ProtInc
    2. cytosol Source: ParkinsonsUK-UCL
    3. nuclear matrix Source: UniProtKB-SubCell
    4. nucleoplasm Source: ProtInc
    5. nucleus Source: ParkinsonsUK-UCL

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

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

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi14 – 141C → A: Loss of deubiquitination activity. 2 Publications
    Mutagenesisi236 – 2361S → A: Inhibits substrate trapping. 1 Publication
    Mutagenesisi256 – 2561S → A: Inhibits substrate trapping. 1 Publication
    Mutagenesisi335 – 3351S → A: No effect on ubiquitination. 1 Publication

    Keywords - Diseasei

    Neurodegeneration, Spinocerebellar ataxia

    Organism-specific databases

    MIMi109150. phenotype.
    Orphaneti276238. Machado-Joseph disease type 1.
    276241. Machado-Joseph disease type 2.
    276244. Machado-Joseph disease type 3.
    PharmGKBiPA134971833.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 364364Ataxin-3PRO_0000053831Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki1 – 1Peptide (Met-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki200 – 200Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei219 – 2191PhosphoserineBy similarity

    Post-translational modificationi

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

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP54252.
    PaxDbiP54252.
    PRIDEiP54252.

    PTM databases

    PhosphoSiteiP54252.

    Miscellaneous databases

    PMAP-CutDBA7LFZ5.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiP54252.
    BgeeiP54252.
    GenevestigatoriP54252.

    Organism-specific databases

    HPAiCAB021976.
    HPA024123.

    Interactioni

    Subunit structurei

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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself5EBI-946046,EBI-946046
    C16orf70Q9BSU12EBI-946046,EBI-946080
    RAD23BP547272EBI-946046,EBI-954531
    UBCP0CG482EBI-946046,EBI-3390054
    VCPP5507210EBI-946068,EBI-355164

    Protein-protein interaction databases

    BioGridi110433. 72 interactions.
    IntActiP54252. 22 interactions.
    MINTiMINT-272839.

    Structurei

    Secondary structure

    364
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi1 – 33
    Helixi14 – 229
    Beta strandi23 – 253
    Helixi30 – 4920
    Turni53 – 553
    Helixi56 – 627
    Beta strandi70 – 734
    Helixi78 – 858
    Turni86 – 883
    Beta strandi90 – 967
    Turni97 – 1004
    Helixi106 – 1083
    Beta strandi109 – 1168
    Beta strandi119 – 1268
    Beta strandi129 – 1346
    Beta strandi141 – 1433
    Helixi145 – 15814
    Beta strandi161 – 1677
    Helixi173 – 1764
    Helixi178 – 1803
    Helixi222 – 24019
    Beta strandi243 – 2453
    Helixi246 – 25712

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1YZBNMR-A1-182[»]
    2AGANMR-A1-185[»]
    2DOSNMR-A1-171[»]
    2JRINMR-A1-182[»]
    2KLZNMR-A222-263[»]
    DisProtiDP00576.
    ProteinModelPortaliP54252.
    SMRiP54252. Positions 1-185, 220-264.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP54252.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 180180JosephinPROSITE-ProRule annotationAdd
    BLAST
    Repeati224 – 24320UIM 1Add
    BLAST
    Repeati244 – 26320UIM 2Add
    BLAST
    Repeati331 – 34818UIM 3Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi292 – 30514Poly-GlnAdd
    BLAST

    Domaini

    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.By similarity

    Sequence similaritiesi

    Contains 1 Josephin domain.PROSITE-ProRule annotation
    Contains 3 UIM (ubiquitin-interacting motif) repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG327234.
    HOVERGENiHBG025648.
    KOiK11863.
    OrthoDBiEOG779NZ3.
    PhylomeDBiP54252.
    TreeFamiTF314228.

    Family and domain databases

    InterProiIPR006155. Josephin.
    IPR003903. Ubiquitin-int_motif.
    [Graphical view]
    PfamiPF02099. Josephin. 1 hit.
    PF02809. UIM. 2 hits.
    [Graphical view]
    PRINTSiPR01233. JOSEPHIN.
    SMARTiSM00726. UIM. 2 hits.
    [Graphical view]
    PROSITEiPS50957. JOSEPHIN. 1 hit.
    PS50330. UIM. 2 hits.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P54252-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MESIFHEKQE GSLCAQHCLN NLLQGEYFSP VELSSIAHQL DEEERMRMAE    50
    GGVTSEDYRT FLQQPSGNMD DSGFFSIQVI SNALKVWGLE LILFNSPEYQ 100
    RLRIDPINER SFICNYKEHW FTVRKLGKQW FNLNSLLTGP ELISDTYLAL 150
    FLAQLQQEGY SIFVVKGDLP DCEADQLLQM IRVQQMHRPK LIGEELAQLK 200
    EQRVHKTDLE RVLEANDGSG MLDEDEEDLQ RALALSRQEI DMEDEEADLR 250
    RAIQLSMQGS SRNISQDMTQ TSGTNLTSEE LRKRREAYFE KQQQKQQQQQ 300
    QQQQQGDLSG QSSHPCERPA TSSGALGSDL GKACSPFIMF ATFTLYLTYE 350
    LHVIFALHYS SFPL 364
    Length:364
    Mass (Da):41,781
    Last modified:March 2, 2010 - v4
    Checksum:i4B2477EB67C30EFF
    GO
    Isoform 2 (identifier: P54252-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         332-364: KACSPFIMFATFTLYLTYELHVIFALHYSSFPL → DAMSEEDMLQAAVTMSLETVRNDLKTEGKK

    Show »
    Length:361
    Mass (Da):41,250
    Checksum:i90C3EF73BB26CAFD
    GO
    Isoform 3 (identifier: P54252-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         10-64: Missing.
         332-364: KACSPFIMFATFTLYLTYELHVIFALHYSSFPL → DAMSEEDMLQAAVTMSLETVRNDLKTEGKK

    Show »
    Length:306
    Mass (Da):35,006
    Checksum:iD2103044A948A525
    GO
    Isoform 4 (identifier: P54252-4) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:346
    Mass (Da):39,638
    Checksum:iD4DE7B21BDE6C4F1
    GO
    Isoform 5 (identifier: P54252-5) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:182
    Mass (Da):20,633
    Checksum:iF6BDA4CEE7251228
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti252 – 2521A → T in AAB63352. (PubMed:9274833)Curated
    Sequence conflicti252 – 2521A → T in AAB63353. (PubMed:9274833)Curated
    Sequence conflicti252 – 2521A → T in AAB63354. (PubMed:9274833)Curated

    Polymorphismi

    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.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti212 – 2121V → M.3 Publications
    Corresponds to variant rs1048755 [ dbSNP | Ensembl ].
    VAR_013688
    Natural varianti306 – 3061G → QQQQQQQQQQQQR.3 Publications
    VAR_013689
    Natural varianti349 – 36416Missing in allele MJD1a. 1 Publication
    VAR_013690Add
    BLAST

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 179179Missing in isoform 5. CuratedVSP_047085Add
    BLAST
    Alternative sequencei10 – 6455Missing in isoform 3. CuratedVSP_002783Add
    BLAST
    Alternative sequencei63 – 7715Missing in isoform 4. CuratedVSP_047086Add
    BLAST
    Alternative sequencei332 – 36433KACSP…SSFPL → DAMSEEDMLQAAVTMSLETV RNDLKTEGKK in isoform 2, isoform 3, isoform 4 and isoform 5. 2 PublicationsVSP_002784Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS32143.1. [P54252-3]
    CCDS45154.1. [P54252-4]
    CCDS53908.1. [P54252-5]
    CCDS9900.1. [P54252-2]
    PIRiS50830.
    RefSeqiNP_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]
    UniGeneiHs.532632.

    Genome annotation databases

    EnsembliENST00000340660; ENSP00000339110; ENSG00000066427. [P54252-3]
    ENST00000393287; ENSP00000376965; ENSG00000066427. [P54252-2]
    ENST00000502250; ENSP00000425322; ENSG00000066427. [P54252-5]
    ENST00000503767; ENSP00000426697; ENSG00000066427. [P54252-4]
    ENST00000532032; ENSP00000437157; ENSG00000066427. [P54252-1]
    GeneIDi4287.
    KEGGihsa:4287.
    UCSCiuc001yac.4. human. [P54252-2]
    uc001yad.4. human. [P54252-3]
    uc021rzo.1. human. [P54252-1]

    Polymorphism databases

    DMDMi290457685.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism, Triplet repeat expansion

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS32143.1. [P54252-3 ]
    CCDS45154.1. [P54252-4 ]
    CCDS53908.1. [P54252-5 ]
    CCDS9900.1. [P54252-2 ]
    PIRi S50830.
    RefSeqi NP_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 ]
    UniGenei Hs.532632.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1YZB NMR - A 1-182 [» ]
    2AGA NMR - A 1-185 [» ]
    2DOS NMR - A 1-171 [» ]
    2JRI NMR - A 1-182 [» ]
    2KLZ NMR - A 222-263 [» ]
    DisProti DP00576.
    ProteinModelPortali P54252.
    SMRi P54252. Positions 1-185, 220-264.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110433. 72 interactions.
    IntActi P54252. 22 interactions.
    MINTi MINT-272839.

    Protein family/group databases

    MEROPSi C86.001.

    PTM databases

    PhosphoSitei P54252.

    Polymorphism databases

    DMDMi 290457685.

    Proteomic databases

    MaxQBi P54252.
    PaxDbi P54252.
    PRIDEi P54252.

    Protocols and materials databases

    DNASUi 4287.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000340660 ; ENSP00000339110 ; ENSG00000066427 . [P54252-3 ]
    ENST00000393287 ; ENSP00000376965 ; ENSG00000066427 . [P54252-2 ]
    ENST00000502250 ; ENSP00000425322 ; ENSG00000066427 . [P54252-5 ]
    ENST00000503767 ; ENSP00000426697 ; ENSG00000066427 . [P54252-4 ]
    ENST00000532032 ; ENSP00000437157 ; ENSG00000066427 . [P54252-1 ]
    GeneIDi 4287.
    KEGGi hsa:4287.
    UCSCi uc001yac.4. human. [P54252-2 ]
    uc001yad.4. human. [P54252-3 ]
    uc021rzo.1. human. [P54252-1 ]

    Organism-specific databases

    CTDi 4287.
    GeneCardsi GC14M092524.
    GeneReviewsi ATXN3.
    HGNCi HGNC:7106. ATXN3.
    HPAi CAB021976.
    HPA024123.
    MIMi 109150. phenotype.
    607047. gene.
    neXtProti NX_P54252.
    Orphaneti 276238. Machado-Joseph disease type 1.
    276241. Machado-Joseph disease type 2.
    276244. Machado-Joseph disease type 3.
    PharmGKBi PA134971833.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG327234.
    HOVERGENi HBG025648.
    KOi K11863.
    OrthoDBi EOG779NZ3.
    PhylomeDBi P54252.
    TreeFami TF314228.

    Miscellaneous databases

    EvolutionaryTracei P54252.
    GeneWikii Ataxin_3.
    GenomeRNAii 4287.
    NextBioi 16875.
    PMAP-CutDB A7LFZ5.
    PROi P54252.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P54252.
    Bgeei P54252.
    Genevestigatori P54252.

    Family and domain databases

    InterProi IPR006155. Josephin.
    IPR003903. Ubiquitin-int_motif.
    [Graphical view ]
    Pfami PF02099. Josephin. 1 hit.
    PF02809. UIM. 2 hits.
    [Graphical view ]
    PRINTSi PR01233. JOSEPHIN.
    SMARTi SM00726. UIM. 2 hits.
    [Graphical view ]
    PROSITEi PS50957. JOSEPHIN. 1 hit.
    PS50330. UIM. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. 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. 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. 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.
      , 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. 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. 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.

    Entry informationi

    Entry nameiATX3_HUMAN
    AccessioniPrimary (citable) accession number: P54252
    Secondary accession number(s): A7LFZ5
    , D6RDL9, E9PB63, O15284, O15285, O15286, Q8N189, Q96TC3, Q96TC4, Q9H3N0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: March 2, 2010
    Last modified: October 1, 2014
    This is version 152 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3