Q9V0N9 · PSB2_PYRAB

Function

function

Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.

Catalytic activity

  • Cleavage of peptide bonds with very broad specificity.
    EC:3.4.25.1 (UniProtKB | ENZYME | Rhea)

Activity regulation

The formation of the proteasomal ATPase PAN-20S proteasome complex, via the docking of the C-termini of PAN into the intersubunit pockets in the alpha-rings, triggers opening of the gate for substrate entry. Interconversion between the open-gate and close-gate conformations leads to a dynamic regulation of the 20S proteasome proteolysis activity.

Features

Showing features for active site.

120720406080100120140160180200
TypeIDPosition(s)Description
Active site11Nucleophile

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
Cellular Componentproteasome core complex, beta-subunit complex
Molecular Functionthreonine-type endopeptidase activity
Biological Processproteasomal protein catabolic process

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Proteasome subunit beta 2
  • EC number
  • Alternative names
    • 20S proteasome beta subunit 2
    • Proteasome core protein PsmB 2

Gene names

    • Name
      psmB2
    • ORF names
      PAB1867
    • Ordered locus names
      PYRAB07500

Organism names

Accessions

  • Primary accession
    Q9V0N9
  • Secondary accessions
    • G8ZGV1

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for propeptide, chain.

TypeIDPosition(s)Description
PropeptidePRO_00000266671-10Removed in mature form; by autocatalysis
ChainPRO_000002666811-207Proteasome subunit beta 2

Keywords

Interaction

Subunit

The 20S proteasome core is composed of 14 alpha and 14 beta subunits that assemble into four stacked heptameric rings, resulting in a barrel-shaped structure. The two inner rings, each composed of seven catalytic beta subunits, are sandwiched by two outer rings, each composed of seven alpha subunits. The catalytic chamber with the active sites is on the inside of the barrel. Has a gated structure, the ends of the cylinder being occluded by the N-termini of the alpha-subunits. Is capped at one or both ends by the proteasome regulatory ATPase, PAN.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the peptidase T1B family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    207
  • Mass (Da)
    22,671
  • Last updated
    2000-05-01 v1
  • Checksum
    9FBD9B0519434939
MLQLTEKFKGTTTVGIVCSDGVVLAADRRASLGNIVYAKNVTKIHKIDEHLAIAGAGDVGDILNLVRLLRAEAKLYYAQSGKRMSVKALATLLANMLNGARMLPYLAWFLVGGFDEKPRLYSVDMMGGITEDKYVAAGSGMEFAYSVLDSEYREDLKVREGIKIAVEAINSAIKRDVFSGDGIMVVTITEEGYRELSNSRLKAILRQ

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJ248285
EMBL· GenBank· DDBJ
CAB49664.1
EMBL· GenBank· DDBJ
Genomic DNA
HE613800
EMBL· GenBank· DDBJ
CCE70146.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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