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P54252

- ATX3_HUMAN

UniProt

P54252 - ATX3_HUMAN

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Protein

Ataxin-3

Gene

ATXN3

Organism
Homo sapiens (Human)
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.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. ubiquitin protein ligase binding Source: UniProtKB
  7. ubiquitin-specific protease activity Source: UniProtKB
  8. 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
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
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. nucleoplasm Source: ProtInc
  4. nucleus Source: ParkinsonsUK-UCL
Complete GO annotation...

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

BgeeiP54252.
ExpressionAtlasiP54252. baseline and differential.
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
HAP1P542576EBI-946046,EBI-712814
PARK2O602605EBI-9684323,EBI-716346
RAD23BP547272EBI-946046,EBI-954531
UBCP0CG482EBI-946046,EBI-3390054
VCPP5507210EBI-946068,EBI-355164

Protein-protein interaction databases

BioGridi110433. 76 interactions.
IntActiP54252. 24 interactions.
MINTiMINT-272839.

Structurei

Secondary structure

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

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.
GeneTreeiENSGT00390000001830.
HOVERGENiHBG025648.
InParanoidiP54252.
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

        10         20         30         40         50
MESIFHEKQE GSLCAQHCLN NLLQGEYFSP VELSSIAHQL DEEERMRMAE
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 IRVQQMHRPK LIGEELAQLK
210 220 230 240 250
EQRVHKTDLE RVLEANDGSG MLDEDEEDLQ RALALSRQEI DMEDEEADLR
260 270 280 290 300
RAIQLSMQGS SRNISQDMTQ TSGTNLTSEE LRKRREAYFE KQQQKQQQQQ
310 320 330 340 350
QQQQQGDLSG QSSHPCERPA TSSGALGSDL GKACSPFIMF ATFTLYLTYE
360
LHVIFALHYS SFPL
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. 3 Publications
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]
ENST00000502250; ENSP00000425322; ENSG00000066427. [P54252-5]
ENST00000503767; ENSP00000426697; ENSG00000066427. [P54252-4]
ENST00000532032; ENSP00000437157; ENSG00000066427. [P54252-1]
ENST00000558190; ENSP00000478320; ENSG00000066427. [P54252-2]
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. 76 interactions.
IntActi P54252. 24 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 ]
ENST00000502250 ; ENSP00000425322 ; ENSG00000066427 . [P54252-5 ]
ENST00000503767 ; ENSP00000426697 ; ENSG00000066427 . [P54252-4 ]
ENST00000532032 ; ENSP00000437157 ; ENSG00000066427 . [P54252-1 ]
ENST00000558190 ; ENSP00000478320 ; ENSG00000066427 . [P54252-2 ]
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.
GeneTreei ENSGT00390000001830.
HOVERGENi HBG025648.
InParanoidi P54252.
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

Bgeei P54252.
ExpressionAtlasi P54252. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 153 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