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Q9CVD2 (ATX3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·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 homolog
Gene names
Name:Atxn3
Synonyms:Mjd
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length355 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.5

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).

Subunit structure

Interacts with DNA repair proteins RAD23A and RAD23B By similarity. Interacts with STUB1/CHIP (when monoubiquitinated). Ref.5

Subcellular location

Nucleus By similarity.

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 (Ref.5).

Post-translational modification

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

Sequence similarities

Contains 1 Josephin domain.

Contains 3 UIM (ubiquitin-interacting motif) repeats.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
Ubl conjugation pathway
   Cellular componentNucleus
   DomainRepeat
   Molecular functionHydrolase
Protease
Thiol protease
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to heat

Inferred from mutant phenotype PubMed 19843543. Source: MGI

cellular response to misfolded protein

Inferred from mutant phenotype Ref.5. Source: UniProtKB

exploration behavior

Inferred from mutant phenotype PubMed 17764659. Source: MGI

histone H3 deacetylation

Inferred from electronic annotation. Source: Ensembl

misfolded or incompletely synthesized protein catabolic process

Inferred from mutant phenotype Ref.5. Source: UniProtKB

monoubiquitinated protein deubiquitination

Inferred from direct assay Ref.5. Source: UniProtKB

proteasome-mediated ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype Ref.5. Source: UniProtKB

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

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype PubMed 17764659. Source: MGI

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 17626202PubMed 18353661PubMed 19843543PubMed 20347968. Source: MGI

mitochondrial matrix

Inferred from direct assay PubMed 18353661. Source: MGI

mitochondrial membrane

Inferred from direct assay PubMed 18353661. Source: MGI

nuclear inclusion body

Inferred from direct assay PubMed 17626202. Source: MGI

nucleus

Inferred from direct assay PubMed 18353661PubMed 19843543PubMed 20347968. Source: MGI

   Molecular_functionRNA polymerase II regulatory region DNA binding

Inferred from electronic annotation. Source: Ensembl

omega peptidase activity

Inferred from electronic annotation. Source: InterPro

ubiquitin protein ligase binding

Inferred from physical interaction Ref.5. Source: UniProtKB

ubiquitin thiolesterase activity

Inferred from direct assay Ref.5. Source: UniProtKB

ubiquitin-specific protease activity

Inferred from direct assay Ref.5. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 355355Ataxin-3
PRO_0000053832

Regions

Domain1 – 180180Josephin
Repeat224 – 24320UIM 1
Repeat244 – 26320UIM 2
Repeat329 – 34820UIM 3
Compositional bias282 – 2854Poly-Arg
Compositional bias292 – 2976Poly-Gln

Sites

Active site141Nucleophile
Active site1191Proton acceptor By similarity
Active site1341 By similarity

Amino acid modifications

Modified residue2191Phosphoserine Ref.2
Modified residue2681Phosphoserine Ref.3
Modified residue2731Phosphoserine Ref.3
Cross-link1Peptide (Met-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link200Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Experimental info

Mutagenesis141C → A: Abolishes deubiquitinating activity. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9CVD2 [UniParc].

Last modified February 28, 2003. Version 2.
Checksum: D148DD10EA481D5B

FASTA35540,533
        10         20         30         40         50         60 
MESIFHEKQE GSLCAQHCLN NLLQGEYFSP VELSSIAHQL DEEERLRMAE 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 
IKVQQMHRPK LIGEELAHLK EQSALKADLE RVLEAADGSG IFDEDEDDLQ RALAISRQEI 

       250        260        270        280        290        300 
DMEDEEADLR RAIQLSMQGS SRSMCENSPQ TSSPDLSSEE LRRRREAYFE KQQQQQQEVD 

       310        320        330        340        350 
RPGPLSYPRE RPTTSSGGRR SDQGGDAVSE EDMLRAAVTM SLETAKDNLK AERKK 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: NOD.
Tissue: Stomach and Thymus.
[2]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic brain.
[3]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268 AND SER-273, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[4]"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.
[5]"Ube2w and ataxin-3 coordinately regulate the ubiquitin ligase CHIP."
Scaglione K.M., Zavodszky E., Todi S.V., Patury S., Xu P., Rodriguez-Lebron E., Fischer S., Konen J., Djarmati A., Peng J., Gestwicki J.E., Paulson H.L.
Mol. Cell 43:599-612(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH STUB1, UBIQUITINATION, MUTAGENESIS OF CYS-14.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK008675 mRNA. Translation: BAB25825.3.
AK030842 mRNA. Translation: BAC27155.1.
RefSeqNP_083981.2. NM_029705.3.
UniGeneMm.271914.

3D structure databases

ProteinModelPortalQ9CVD2.
SMRQ9CVD2. Positions 1-171, 220-264.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid225755. 18 interactions.
IntActQ9CVD2. 2 interactions.
MINTMINT-2837817.

Protein family/group databases

MEROPSC86.001.

PTM databases

PhosphoSiteQ9CVD2.

Proteomic databases

PaxDbQ9CVD2.
PRIDEQ9CVD2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021606; ENSMUSP00000021606; ENSMUSG00000021189.
GeneID110616.
KEGGmmu:110616.
UCSCuc007otv.2. mouse.

Organism-specific databases

CTD4287.
MGIMGI:1099442. Atxn3.

Phylogenomic databases

eggNOGNOG327234.
GeneTreeENSGT00390000001830.
HOGENOMHOG000006034.
HOVERGENHBG025648.
InParanoidQ9CVD2.
KOK11863.
OMALQAAMNM.
OrthoDBEOG779NZ3.
PhylomeDBQ9CVD2.
TreeFamTF314228.

Gene expression databases

ArrayExpressQ9CVD2.
BgeeQ9CVD2.
CleanExMM_ATXN3.
GenevestigatorQ9CVD2.

Family and domain databases

InterProIPR006155. Josephin.
IPR003903. Ubiquitin-int_motif.
[Graphical view]
PfamPF02099. Josephin. 1 hit.
PF02809. UIM. 3 hits.
[Graphical view]
PRINTSPR01233. JOSEPHIN.
SMARTSM00726. UIM. 3 hits.
[Graphical view]
PROSITEPS50957. JOSEPHIN. 1 hit.
PS50330. UIM. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSATXN3. mouse.
NextBio364339.
PROQ9CVD2.
SOURCESearch...

Entry information

Entry nameATX3_MOUSE
AccessionPrimary (citable) accession number: Q9CVD2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: February 28, 2003
Last modified: April 16, 2014
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot