Q7L3T8 · SYPM_HUMAN

  • Protein
    Probable proline--tRNA ligase, mitochondrial
  • Gene
    PARS2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

function

Mitochondrial aminoacyl-tRNA synthetase that catalyzes the specific attachment of the proline amino acid (aa) to the homologous transfer RNA (tRNA), further participating in protein synthesis. The reaction occurs in a two steps: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro).

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 Componentmitochondrial matrix
Cellular Componentmitochondrion
Molecular FunctionATP binding
Molecular Functionidentical protein binding
Molecular Functionproline-tRNA ligase activity
Biological Processprolyl-tRNA aminoacylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Probable proline--tRNA ligase, mitochondrial
  • EC number
  • Alternative names
    • Prolyl-tRNA synthetase (ProRS
      )
    • Prolyl-tRNA synthetase 2, mitochondrial

Gene names

    • Name
      PARS2

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q7L3T8
  • Secondary accessions
    • A8K0W4
    • Q9H6S5
    • Q9UFT1

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Disease & Variants

Involvement in disease

Developmental and epileptic encephalopathy 75 (DEE75)

  • Note
    • The disease may be caused by variants affecting the gene represented in this entry
  • Description
    A form of epileptic encephalopathy, a heterogeneous group of severe early-onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. DEE75 is an autosomal recessive form characterized by onset of severe refractory seizures in the first months of life.
  • See also
    MIM:618437
Natural variants in DEE75
Variant IDPosition(s)ChangeDescription
VAR_08261780I>Tin DEE75; uncertain significance; dbSNP:rs1246773873
VAR_08214995V>Iin DEE75; uncertain significance; dbSNP:rs147227819
VAR_082618202R>Gin DEE75; uncertain significance; dbSNP:rs141760650
VAR_082619203E>Kin DEE75; uncertain significance; dbSNP:rs1557762729
VAR_082620279S>Lin DEE75; uncertain significance; dbSNP:rs730882153
VAR_082621364P>Rin DEE75; uncertain significance; dbSNP:rs35201073

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_05264428in dbSNP:rs11577368
Natural variantVAR_08261780in DEE75; uncertain significance; dbSNP:rs1246773873
Natural variantVAR_08214995in DEE75; uncertain significance; dbSNP:rs147227819
Natural variantVAR_088479103found in a patient with an aminoacyl-tRNA synthetase abnormality; uncertain significance
Natural variantVAR_082618202in DEE75; uncertain significance; dbSNP:rs141760650
Natural variantVAR_082619203in DEE75; uncertain significance; dbSNP:rs1557762729
Natural variantVAR_034527235in dbSNP:rs2270004
Natural variantVAR_082620279in DEE75; uncertain significance; dbSNP:rs730882153
Natural variantVAR_082621364in DEE75; uncertain significance; dbSNP:rs35201073

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 557 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Keywords

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

Showing features for transit peptide, chain.

TypeIDPosition(s)Description
Transit peptide1-29Mitochondrion
ChainPRO_000003581830-475Probable proline--tRNA ligase, mitochondrial

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    475
  • Mass (Da)
    53,263
  • Last updated
    2004-07-05 v1
  • Checksum
    E3B1B07CB6225BA2
MEGLLTRCRALPALATCSRQLSGYVPCRFHHCAPRRGRRLLLSRVFQPQNLREDRVLSLQDKSDDLTCKSQRLMLQVGLIYPASPGCYHLLPYTVRAMEKLVRVIDQEMQAIGGQKVNMPSLSPAELWQATNRWDLMGKELLRLRDRHGKEYCLGPTHEEAITALIASQKKLSYKQLPFLLYQVTRKFRDEPRPRFGLLRGREFYMKDMYTFDSSPEAAQQTYSLVCDAYCSLFNKLGLPFVKVQADVGTIGGTVSHEFQLPVDIGEDRLAICPRCSFSANMETLDLSQMNCPACQGPLTKTKGIEVGHTFYLGTKYSSIFNAQFTNVCGKPTLAEMGCYGLGVTRILAAAIEVLSTEDCVRWPSLLAPYQACLIPPKKGSKEQAASELIGQLYDHITEAVPQLHGEVLLDDRTHLTIGNRLKDANKFGYPFVIIAGKRALEDPAHFEVWCQNTGEVAFLTKDGVMDLLTPVQTV

Sequence caution

The sequence BAB15178.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AK025585
EMBL· GenBank· DDBJ
BAB15178.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AK289679
EMBL· GenBank· DDBJ
BAF82368.1
EMBL· GenBank· DDBJ
mRNA
AL139244
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CH471059
EMBL· GenBank· DDBJ
EAX06669.1
EMBL· GenBank· DDBJ
Genomic DNA
BC007956
EMBL· GenBank· DDBJ
AAH07956.2
EMBL· GenBank· DDBJ
mRNA
BC011758
EMBL· GenBank· DDBJ
AAH11758.2
EMBL· GenBank· DDBJ
mRNA
AL117473
EMBL· GenBank· DDBJ
CAB55948.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any 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. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp