Q32PI8 · RT27_BOVIN

  • Protein
    Small ribosomal subunit protein mS27
  • Gene
    MRPS27
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

function

RNA-binding component of the mitochondrial small ribosomal subunit (mt-SSU) that plays a role in mitochondrial protein synthesis. Stimulates mitochondrial mRNA translation of subunit components of the mitochondrial electron transport chain. Binds to the mitochondrial 12S rRNA (12S mt-rRNA) and tRNA(Glu). Overexpressed in hepatocellular carcinoma tissues compared with adjacent non-tumoral liver tissues.

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 inner membrane
Cellular Componentmitochondrial small ribosomal subunit
Cellular Componentmitochondrion
Molecular Functionmitochondrial ribosome binding
Molecular FunctionrRNA binding
Molecular FunctiontRNA binding
Biological Processcell population proliferation
Biological Processpositive regulation of mitochondrial translation

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Small ribosomal subunit protein mS27
  • Alternative names
    • 28S ribosomal protein S27, mitochondrial
      (MRP-S27; S27mt)
    • Mitochondrial ribosomal protein S27

Gene names

    • Name
      MRPS27

Organism names

  • Taxonomic identifier
  • Strain
    • Crossbred X Angus
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos

Accessions

  • Primary accession
    Q32PI8
  • Secondary accessions
    • P82677

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for transit peptide, chain.

TypeIDPosition(s)Description
Transit peptide1-8Mitochondrion
ChainPRO_00002615859-415Small ribosomal subunit protein mS27

Proteomic databases

Interaction

Subunit

Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins (PubMed:11344316).
Interacts with NOA1 (By similarity).
Interacts with MIEF1 upstream open reading frame protein (By similarity).
Interacts with METTL17 (By similarity).

Protein-protein interaction databases

Family & Domains

Features

Showing features for repeat, region, compositional bias, coiled coil.

TypeIDPosition(s)Description
Repeat105-139PPR 1
Repeat140-175PPR 2
Region292-325Disordered
Compositional bias300-319Acidic residues
Coiled coil368-415

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
    415
  • Mass (Da)
    47,955
  • Last updated
    2005-12-06 v1
  • Checksum
    AC765A6DBE9A9296
MAAPMVRRAIFLARNVLLPQLSLAGKRYLLSAAYEDSRKWEARAKEDCHLADLASLMDKTYERKLPVSSLTISRFVDNISSREEIDHAEYYLYKFRHSPNCWYLRNWTIHTWIRQCLKYGAQDKALYTLVNKVQYGIFPDNYTFNLLMDHFIKKENYKDALSVVFEIMMQEAFEVPSTQLLSLYVLYQCLAKKTDFSWEEERNFGASLLLPGLKQKNSVGLSSQLYGYALLGKVELQQGLRAVYHNMPLLWRPGYLDRALQVMEKVASSPEDGKLCREALGVLDRALKALTAPAQESPEEQPQEGEESPASEELMEQLDVEETEQSKLPRYVERYEALHSKLQALGKVESESLLTLTTQLVKEQLPTCEAEDIATYEQKLQEWHLELVNLIEREKEMREKARLKHEARRAAKAAA

Features

Showing features for sequence conflict, compositional bias.

TypeIDPosition(s)Description
Sequence conflict201-202in Ref. 2; AA sequence
Compositional bias300-319Acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BC108100
EMBL· GenBank· DDBJ
AAI08101.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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