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Q9CVD2

- ATX3_MOUSE

UniProt

Q9CVD2 - ATX3_MOUSE

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Protein

Ataxin-3

Gene

Atxn3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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.1 Publication

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).

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. RNA polymerase II regulatory region DNA binding Source: Ensembl
  3. ubiquitin protein ligase binding Source: UniProtKB
  4. ubiquitin-specific protease activity Source: UniProtKB
  5. ubiquitin thiolesterase activity Source: UniProtKB

GO - Biological processi

  1. cellular response to heat Source: MGI
  2. cellular response to misfolded protein Source: UniProtKB
  3. exploration behavior Source: MGI
  4. histone H3 deacetylation Source: Ensembl
  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: MGI
  9. regulation of transcription, DNA-templated Source: UniProtKB-KW
  10. transcription, DNA-templated Source: UniProtKB-KW
  11. ubiquitin-dependent protein catabolic process Source: MGI
Complete GO annotation...

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 12

Organism-specific databases

MGIiMGI:1099442. Atxn3.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. mitochondrial matrix Source: MGI
  3. mitochondrial membrane Source: MGI
  4. nuclear inclusion body Source: MGI
  5. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi14 – 141C → A: Abolishes deubiquitinating activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 355355Ataxin-3PRO_0000053832Add
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 residuei219 – 2191Phosphoserine1 Publication
Modified residuei268 – 2681Phosphoserine1 Publication
Modified residuei273 – 2731Phosphoserine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9CVD2.
PaxDbiQ9CVD2.
PRIDEiQ9CVD2.

PTM databases

PhosphoSiteiQ9CVD2.

Expressioni

Gene expression databases

BgeeiQ9CVD2.
CleanExiMM_ATXN3.
ExpressionAtlasiQ9CVD2. baseline.
GenevestigatoriQ9CVD2.

Interactioni

Subunit structurei

Interacts with DNA repair proteins RAD23A and RAD23B (By similarity). Interacts with STUB1/CHIP (when monoubiquitinated).By similarity1 Publication

Protein-protein interaction databases

BioGridi225755. 18 interactions.
IntActiQ9CVD2. 2 interactions.
MINTiMINT-2837817.

Structurei

3D structure databases

ProteinModelPortaliQ9CVD2.
SMRiQ9CVD2. Positions 1-171, 220-264.
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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi282 – 2854Poly-Arg
Compositional biasi292 – 2976Poly-Gln

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 (PubMed:21855799).1 Publication

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.
InParanoidiQ9CVD2.
KOiK11863.
OMAiLQAAMNM.
OrthoDBiEOG779NZ3.
PhylomeDBiQ9CVD2.
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.

Q9CVD2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MESIFHEKQE GSLCAQHCLN NLLQGEYFSP VELSSIAHQL DEEERLRMAE
60 70 80 90 100
GGVTSEDYRT FLQQPSGNMD DSGFFSIQVI SNALKVWGLE LILFNSPEYQ
110 120 130 140 150
RLRIDPINER SFICNYKEHW FTVRKLGKQW FNLNSLLTGP ELISDTYLAL
160 170 180 190 200
FLAQLQQEGY SIFVVKGDLP DCEADQLLQM IKVQQMHRPK LIGEELAHLK
210 220 230 240 250
EQSALKADLE RVLEAADGSG IFDEDEDDLQ RALAISRQEI DMEDEEADLR
260 270 280 290 300
RAIQLSMQGS SRSMCENSPQ TSSPDLSSEE LRRRREAYFE KQQQQQQEVD
310 320 330 340 350
RPGPLSYPRE RPTTSSGGRR SDQGGDAVSE EDMLRAAVTM SLETAKDNLK

AERKK
Length:355
Mass (Da):40,533
Last modified:February 28, 2003 - v2
Checksum:iD148DD10EA481D5B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK008675 mRNA. Translation: BAB25825.3.
AK030842 mRNA. Translation: BAC27155.1.
CCDSiCCDS26115.1.
RefSeqiNP_083981.2. NM_029705.3.
UniGeneiMm.271914.

Genome annotation databases

EnsembliENSMUST00000021606; ENSMUSP00000021606; ENSMUSG00000021189.
GeneIDi110616.
KEGGimmu:110616.
UCSCiuc007otv.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK008675 mRNA. Translation: BAB25825.3 .
AK030842 mRNA. Translation: BAC27155.1 .
CCDSi CCDS26115.1.
RefSeqi NP_083981.2. NM_029705.3.
UniGenei Mm.271914.

3D structure databases

ProteinModelPortali Q9CVD2.
SMRi Q9CVD2. Positions 1-171, 220-264.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 225755. 18 interactions.
IntActi Q9CVD2. 2 interactions.
MINTi MINT-2837817.

Protein family/group databases

MEROPSi C86.001.

PTM databases

PhosphoSitei Q9CVD2.

Proteomic databases

MaxQBi Q9CVD2.
PaxDbi Q9CVD2.
PRIDEi Q9CVD2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000021606 ; ENSMUSP00000021606 ; ENSMUSG00000021189 .
GeneIDi 110616.
KEGGi mmu:110616.
UCSCi uc007otv.2. mouse.

Organism-specific databases

CTDi 4287.
MGIi MGI:1099442. Atxn3.

Phylogenomic databases

eggNOGi NOG327234.
GeneTreei ENSGT00390000001830.
HOGENOMi HOG000006034.
HOVERGENi HBG025648.
InParanoidi Q9CVD2.
KOi K11863.
OMAi LQAAMNM.
OrthoDBi EOG779NZ3.
PhylomeDBi Q9CVD2.
TreeFami TF314228.

Miscellaneous databases

ChiTaRSi ATXN3. mouse.
NextBioi 364339.
PROi Q9CVD2.
SOURCEi Search...

Gene expression databases

Bgeei Q9CVD2.
CleanExi MM_ATXN3.
ExpressionAtlasi Q9CVD2. baseline.
Genevestigatori Q9CVD2.

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

« Hide 'large scale' publications
  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.
    , 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  3. 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. Cited for: FUNCTION, INTERACTION WITH STUB1, UBIQUITINATION, MUTAGENESIS OF CYS-14.

Entry informationi

Entry nameiATX3_MOUSE
AccessioniPrimary (citable) accession number: Q9CVD2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: February 28, 2003
Last modified: October 29, 2014
This is version 107 of the entry and version 2 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3