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O35815

- ATX3_RAT

UniProt

O35815 - ATX3_RAT

Protein

Ataxin-3

Gene

Atxn3

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      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 By similarity.By similarity

    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 acceptorPROSITE-ProRule annotation
    Active sitei134 – 1341PROSITE-ProRule annotation

    GO - Molecular functioni

    1. omega peptidase activity Source: InterPro
    2. protein binding Source: RGD
    3. RNA polymerase II regulatory region DNA binding Source: RGD
    4. ubiquitin protein ligase binding Source: UniProtKB
    5. ubiquitin-specific protease activity Source: UniProtKB
    6. ubiquitin thiolesterase activity Source: UniProtKB

    GO - Biological processi

    1. cellular response to heat Source: Ensembl
    2. cellular response to misfolded protein Source: UniProtKB
    3. exploration behavior Source: Ensembl
    4. histone H3 deacetylation Source: RGD
    5. misfolded or incompletely synthesized protein catabolic process Source: UniProtKB
    6. monoubiquitinated protein deubiquitination Source: UniProtKB
    7. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
    8. regulation of cell-substrate adhesion Source: Ensembl
    9. regulation of transcription, DNA-templated Source: UniProtKB-KW
    10. 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 homolog
    Gene namesi
    Name:Atxn3
    Synonyms:Mjd, Sca3
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 6

    Organism-specific databases

    RGDi621567. Atxn3.

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

    1. mitochondrial matrix Source: Ensembl
    2. mitochondrial membrane Source: Ensembl
    3. nuclear inclusion body Source: Ensembl
    4. nucleus Source: RGD

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi14 – 141C → A or S: Loss of enzyme activity. 1 Publication
    Mutagenesisi119 – 1191H → A: Loss of enzyme activity. 1 Publication
    Mutagenesisi134 – 1341N → A: Loss of enzyme activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 355355Ataxin-3PRO_0000053833Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki1 – 1Peptide (Met-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki200 – 200Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei268 – 2681PhosphoserineBy similarity
    Modified residuei273 – 2731PhosphoserineBy similarity

    Post-translational modificationi

    Monoubiquitinated by UBE2W, possibly leading to activate the deubiquitinating enzyme activity.By similarity

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiO35815.
    PRIDEiO35815.

    PTM databases

    PhosphoSiteiO35815.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.

    Gene expression databases

    GenevestigatoriO35815.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi248780. 2 interactions.
    STRINGi10116.ENSRNOP00000007505.

    Structurei

    3D structure databases

    ProteinModelPortaliO35815.
    SMRiO35815. Positions 1-185.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 180180JosephinPROSITE-ProRule annotationAdd
    BLAST
    Repeati224 – 24320UIM 1Add
    BLAST
    Repeati244 – 26320UIM 2Add
    BLAST
    Repeati329 – 34820UIM 3Add
    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.
    GeneTreeiENSGT00390000001830.
    HOGENOMiHOG000006034.
    HOVERGENiHBG025648.
    InParanoidiO35815.
    KOiK11863.
    OMAiLQAAMNM.
    OrthoDBiEOG779NZ3.
    PhylomeDBiO35815.
    TreeFamiTF314228.

    Family and domain databases

    InterProiIPR006155. Josephin.
    IPR003903. Ubiquitin-int_motif.
    [Graphical view]
    PfamiPF02099. Josephin. 1 hit.
    PF02809. UIM. 3 hits.
    [Graphical view]
    PRINTSiPR01233. JOSEPHIN.
    SMARTiSM00726. UIM. 3 hits.
    [Graphical view]
    PROSITEiPS50957. JOSEPHIN. 1 hit.
    PS50330. UIM. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O35815-1 [UniParc]FASTAAdd to Basket

    « Hide

    MESIFHEKQE GSLCAQHCLN NLLQGEYFSP VELSSIAHQL DEEERLRMAE    50
    GGVTSEDYRT FLQQPSGNMD DSGFFSIQVI SNALKVWGLE LILFNSPEYQ 100
    RLRIDPINER SFICNYKEHW FTVRKLGKQW FNLNSLLTGP ELISDTYLAL 150
    FLAQLQQEGY SIFVVKGDLP DCEADQLLQM IKVQQMHRPK LIGEELAHLK 200
    EQSALKADLE RVLEAADGPG MFDDDEDDLQ RALAMSRQEI DMEDEEADLR 250
    RAIQLSMQGS SRGMCEDSPQ TSSTDLSSEE LRKRREAYFE KQQHQQQEAD 300
    RPGYLSYPCE RPTTSSGGLR SNQAGNAMSE EDVLRATVTV SLETAKDSLK 350
    AERKK 355
    Length:355
    Mass (Da):40,446
    Last modified:January 1, 1998 - v1
    Checksum:i87B6A6EE54FF29F5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y12319 mRNA. Translation: CAA72986.1.
    RefSeqiNP_067734.1. NM_021702.1.
    UniGeneiRn.42932.

    Genome annotation databases

    EnsembliENSRNOT00000007505; ENSRNOP00000007505; ENSRNOG00000005470.
    GeneIDi60331.
    KEGGirno:60331.
    UCSCiRGD:621567. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y12319 mRNA. Translation: CAA72986.1 .
    RefSeqi NP_067734.1. NM_021702.1.
    UniGenei Rn.42932.

    3D structure databases

    ProteinModelPortali O35815.
    SMRi O35815. Positions 1-185.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 248780. 2 interactions.
    STRINGi 10116.ENSRNOP00000007505.

    Protein family/group databases

    MEROPSi C86.001.

    PTM databases

    PhosphoSitei O35815.

    Proteomic databases

    PaxDbi O35815.
    PRIDEi O35815.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000007505 ; ENSRNOP00000007505 ; ENSRNOG00000005470 .
    GeneIDi 60331.
    KEGGi rno:60331.
    UCSCi RGD:621567. rat.

    Organism-specific databases

    CTDi 4287.
    RGDi 621567. Atxn3.

    Phylogenomic databases

    eggNOGi NOG327234.
    GeneTreei ENSGT00390000001830.
    HOGENOMi HOG000006034.
    HOVERGENi HBG025648.
    InParanoidi O35815.
    KOi K11863.
    OMAi LQAAMNM.
    OrthoDBi EOG779NZ3.
    PhylomeDBi O35815.
    TreeFami TF314228.

    Miscellaneous databases

    NextBioi 611965.
    PROi O35815.

    Gene expression databases

    Genevestigatori O35815.

    Family and domain databases

    InterProi IPR006155. Josephin.
    IPR003903. Ubiquitin-int_motif.
    [Graphical view ]
    Pfami PF02099. Josephin. 1 hit.
    PF02809. UIM. 3 hits.
    [Graphical view ]
    PRINTSi PR01233. JOSEPHIN.
    SMARTi SM00726. UIM. 3 hits.
    [Graphical view ]
    PROSITEi PS50957. JOSEPHIN. 1 hit.
    PS50330. UIM. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of the rat spinocerebellar ataxia type 3 gene."
      Schmitt I., Brattig T., Gossen M., Riess O.
      Neurogenetics 1:103-112(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain and Testis.
    2. "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, MUTAGENESIS OF CYS-14; HIS-119 AND ASN-134, FUNCTION.
    3. "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.

    Entry informationi

    Entry nameiATX3_RAT
    AccessioniPrimary (citable) accession number: O35815
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 28, 2003
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 101 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3