Q3THG9 · AASD1_MOUSE

  • Protein
    Alanyl-tRNA editing protein Aarsd1
  • Gene
    Aarsd1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

function

Functions in trans to edit the amino acid moiety from incorrectly charged Ser-tRNA(Ala).

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site.

141250100150200250300350400
TypeIDPosition(s)Description
Binding site109Zn2+ (UniProtKB | ChEBI)
Binding site113Zn2+ (UniProtKB | ChEBI)
Binding site209Zn2+ (UniProtKB | ChEBI)
Binding site213Zn2+ (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Molecular Functionalanine-tRNA ligase activity
Molecular Functionaminoacyl-tRNA editing activity
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular Functionnucleic acid binding
Molecular FunctionSer-tRNA(Ala) hydrolase activity
Biological Processalanyl-tRNA aminoacylation
Biological Processregulation of translational fidelity

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Alanyl-tRNA editing protein Aarsd1
  • Alternative names
    • Alanyl-tRNA deacylase alaX (AlaX; AlaXp-II)
    • Alanyl-tRNA synthetase domain-containing protein 1

Gene names

    • Name
      Aarsd1
    • Synonyms
      Alax

Organism names

  • Taxonomic identifier
  • Strains
    • BALB/cJ
    • C57BL/6J
    • FVB/N
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q3THG9
  • Secondary accessions
    • Q3UWH8
    • Q8BVJ6
    • Q99JS9

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00002774661-412Alanyl-tRNA editing protein Aarsd1
Modified residue174Phosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q3THG9Irak1 Q62406-14EBI-646572, EBI-488313

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    412
  • Mass (Da)
    44,971
  • Last updated
    2007-02-06 v2
  • Checksum
    3FFD32304A379B44
MAFLCQRDSYAREFTTTVVSCSPAELQTDASGGKKEVLSGFHVVLEDTLLFPEGGGQPDDRGTINDISVLRVTRRGAQADHFTESPLSPGSQVQVRVDWERRFDHMQQHSGQHLITAVADLLFGLKTTSWELGRLRSVIELDSPSVTAEQVAAIEQSVNQKIRDRLPVSVRELSLDDPEVEQVRGRGLPDDHAGPIRVVTIEGVDSNMCCGTHVSNLSDLQVIKILGTEKGKKNKSNLIFLAGNRVLKWMERSHGSEKALTSLLKCGVEDHVEAVKKLQNATKLLQKNNLNLLRDLAVHTAHSLRSSPAWGGVVTLHRKEGDSEFMNIIANEIGSEETLLFLTVGDEKGAGLFLLAGPAEAVETLGPRVAEVLEGKGAGKKGRFQGKATKMSRRAEAQALLQDYVSTQSAEE

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict80in Ref. 1; BAE22937
Sequence conflict175in Ref. 1; BAE40227
Sequence conflict292in Ref. 1; BAE22937

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AK078016
EMBL· GenBank· DDBJ
BAC37098.1
EMBL· GenBank· DDBJ
mRNA
AK136332
EMBL· GenBank· DDBJ
BAE22937.1
EMBL· GenBank· DDBJ
mRNA
AK168281
EMBL· GenBank· DDBJ
BAE40227.1
EMBL· GenBank· DDBJ
mRNA
BC005711
EMBL· GenBank· DDBJ
AAH05711.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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