Q8LQ36 · ATX3_ORYSJ

Function

function

Interacts with key regulators of transcription and represses transcription. Acts as a histone-binding protein that regulates transcription. Acts as a deubiquitinating enzyme (By similarity).

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).
    EC:3.4.19.12 (UniProtKB | ENZYME | Rhea)

Features

Showing features for active site.

133650100150200250300
TypeIDPosition(s)Description
Active site23Nucleophile
Active site132Proton acceptor
Active site147

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentnucleus
Molecular Functioncysteine-type deubiquitinase activity
Biological Processprotein deubiquitination
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

Gene names

    • ORF names
      P0529H11.31
    • Ordered locus names
      Os01g0851400, LOC_Os01g63250

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Nipponbare
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza > Oryza sativa

Accessions

  • Primary accession
    Q8LQ36
  • Secondary accessions
    • Q0JHP3

Proteomes

Genome annotation databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue (large scale data).

TypeIDPosition(s)SourceDescription
ChainPRO_00000538371-336UniProtPutative ataxin-3 homolog
Modified residue (large scale data)275PTMeXchangePhosphoserine
Modified residue (large scale data)284PTMeXchangePhosphothreonine
Modified residue (large scale data)285PTMeXchangePhosphoserine

Proteomic databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain10-193Josephin
Domain244-263UIM
Region281-336Disordered
Compositional bias298-327Polar residues

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    336
  • Mass (Da)
    36,205
  • Last updated
    2002-10-01 v1
  • Checksum
    84020FBEA78E8715
MEEAAAASNGGLLYHEVQEGKLCAVHCVNTTLQGPFFSEFDLSALAVDLDQRERQVMSEGAAGAATTAAGDFLAEGEGSHNVSLGGDFSIQVLQKALEVWDLQVIPLDSPDVGSCLFDPELETAFICHLQDHWFCIRKVNGEWYNFNSLYPAPEHLSKFYLSAFIDTLKGSGWSIFAVRGNFPKECPMATEGSNGFGQWLTPDDARRITSSCNQVQTPTQQAGVSLVADQSEEMSEMDMIAAQQEEADLNAAIAASLMDTGGPFANYAAHEESRSQDAFAIESTSGEMSKDGNLEEQGANKSETSEPNSDNIESASGSNPKQNTTSLEGKESIKED

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias298-327Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP004072
EMBL· GenBank· DDBJ
BAB92851.1
EMBL· GenBank· DDBJ
Genomic DNA
AP008207
EMBL· GenBank· DDBJ
BAF06735.2
EMBL· GenBank· DDBJ
Genomic DNA
AP014957
EMBL· GenBank· DDBJ
BAS75251.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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