Q8R040 · RPP21_MOUSE

  • Protein
    Ribonuclease P protein subunit p21
  • Gene
    Rpp21
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    3/5

Function

function

Component of ribonuclease P, a ribonucleoprotein complex that generates mature tRNA molecules by cleaving their 5'-ends.

Features

Showing features for binding site.

115020406080100120140
TypeIDPosition(s)Description
Binding site62Zn2+ (UniProtKB | ChEBI)
Binding site65Zn2+ (UniProtKB | ChEBI)
Binding site92Zn2+ (UniProtKB | ChEBI)
Binding site95Zn2+ (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 Componentnucleolar ribonuclease P complex
Molecular Functionmetal ion binding
Molecular Functionribonuclease P activity
Molecular Functionribonuclease P RNA binding
Biological Processresponse to xenobiotic stimulus
Biological ProcesstRNA 5'-leader removal
Biological ProcesstRNA processing

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ribonuclease P protein subunit p21
  • Short names
    RNaseP protein p21
  • Alternative names
    • Ribonucleoprotein V

Gene names

    • Name
      Rpp21
    • Synonyms
      Cat60

Organism names

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

Accessions

  • Primary accession
    Q8R040
  • Secondary accessions
    • Q80XY3
    • Q811B7
    • Q9CPX1

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylalanine
ChainPRO_00001538462-150Ribonuclease P protein subunit p21

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

RNase P consists of a catalytic RNA moiety and about 10 protein subunits; POP1, POP4, POP5, POP7, RPP14, RPP21, RPP25, RPP30, RPP38 and RPP40. Within the RNase P complex, POP1, POP7 and RPP25 form the 'finger' subcomplex, POP5, RPP14, RPP40 and homodimeric RPP30 form the 'palm' subcomplex, and RPP21, POP4 and RPP38 form the 'wrist' subcomplex. All subunits of the RNase P complex interact with the catalytic RNA.

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region121-150Disordered

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    150
  • Mass (Da)
    17,243
  • Last updated
    2004-07-05 v2
  • Checksum
    EDB5C52A6F2FF519
MAGPVKDREAFQRLSFLYQAAHCVLSQNPENQALARFYCHTEKTIAKRLVLRQDPSVKRTLCRSCSSLLIPGLTCTQRQRRRKGQRWTVQTCLTCQRSQRFLNDPKHLLWGDRPEAQLENQADINPSEPLPNIADLPKENIQTQALNTSE

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
Q80XY2Q80XY2_MOUSERpp2171
G3UWS0G3UWS0_MOUSERpp2151

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict18in Ref. 1; AAP03887
Sequence conflict47-53in Ref. 2; CAD44293
Sequence conflict141in Ref. 4; AAH28491

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY251016
EMBL· GenBank· DDBJ
AAP03887.1
EMBL· GenBank· DDBJ
mRNA
AJ504717
EMBL· GenBank· DDBJ
CAD44293.1
EMBL· GenBank· DDBJ
mRNA
AK002780
EMBL· GenBank· DDBJ
BAB22353.1
EMBL· GenBank· DDBJ
mRNA
AK003455
EMBL· GenBank· DDBJ
BAB22800.1
EMBL· GenBank· DDBJ
mRNA
BC028491
EMBL· GenBank· DDBJ
AAH28491.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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