P25787 · PSA2_HUMAN

  • Protein
    Proteasome subunit alpha type-2
  • Gene
    PSMA2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex).

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 Componentcytosol
Cellular Componentextracellular exosome
Cellular Componentextracellular region
Cellular Componentficolin-1-rich granule lumen
Cellular Componentnucleoplasm
Cellular Componentnucleus
Cellular ComponentP-body
Cellular Componentproteasome complex
Cellular Componentproteasome core complex
Cellular Componentproteasome core complex, alpha-subunit complex
Cellular Componentsecretory granule lumen
Biological Processproteasome-mediated ubiquitin-dependent protein catabolic process
Biological Processresponse to virus

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Proteasome subunit alpha type-2
  • Alternative names
    • Macropain subunit C3
    • Multicatalytic endopeptidase complex subunit C3
    • Proteasome component C3
    • Proteasome subunit alpha-2
      (alpha-2
      )

Gene names

    • Name
      PSMA2
    • Synonyms
      HC3, PSC3

Organism names

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

Accessions

  • Primary accession
    P25787
  • Secondary accessions
    • Q6ICS6
    • Q9BU45

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm
Nucleus
Note: Translocated from the cytoplasm into the nucleus following interaction with AKIRIN2, which bridges the proteasome with the nuclear import receptor IPO9 (PubMed:34711951).
Colocalizes with TRIM5 in cytoplasmic bodies (By similarity).

Keywords

Disease & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_036278110in a colorectal cancer sample; somatic mutation

Variants

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The viewer provides 127 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain, modified residue (large scale data).

TypeIDPosition(s)SourceDescription
Initiator methionine1UniProtRemoved
Modified residue2UniProtN-acetylalanine
ChainPRO_00001240772-234UniProtProteasome subunit alpha type-2
Modified residue6UniProtPhosphotyrosine
Modified residue7UniProtPhosphoserine
Modified residue (large scale data)7PRIDEPhosphoserine
Modified residue14UniProtPhosphoserine
Modified residue (large scale data)14PRIDEPhosphoserine
Modified residue16UniProtPhosphoserine
Modified residue24UniProtPhosphotyrosine
Modified residue (large scale data)57PRIDEPhosphotyrosine
Modified residue70UniProtN6-acetyllysine
Modified residue76UniProtPhosphotyrosine
Modified residue (large scale data)76PRIDEPhosphotyrosine
Modified residue (large scale data)77PRIDEPhosphoserine
Modified residue (large scale data)97PRIDEPhosphotyrosine
Modified residue (large scale data)101PRIDEPhosphotyrosine
Modified residue121UniProtPhosphotyrosine
Modified residue171UniProtN6-acetyllysine
Modified residue (large scale data)222PRIDEPhosphothreonine

Post-translational modification

Phosphorylated on tyrosine residues; which may be important for nuclear import.

Keywords

Proteomic databases

2D gel databases

PTM databases

Expression

Induction

Down-regulated by antioxidants BO-653 and probucol. Down-regulated in response to enterovirus 71 (EV71) infection (at protein level).

Gene expression databases

Organism-specific databases

Interaction

Subunit

The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is a barrel-shaped complex made of 28 subunits that are arranged in four stacked rings. The two outer rings are each formed by seven alpha subunits, and the two inner rings are formed by seven beta subunits. The proteolytic activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7.

Binary interactions

Protein-protein interaction databases

Chemistry

Miscellaneous

Family & Domains

Sequence similarities

Belongs to the peptidase T1A family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    234
  • Mass (Da)
    25,899
  • Last updated
    2007-01-23 v2
  • Checksum
    63CB56A233583836
MAERGYSFSLTTFSPSGKLVQIEYALAAVAGGAPSVGIKAANGVVLATEKKQKSILYDERSVHKVEPITKHIGLVYSGMGPDYRVLVHRARKLAQQYYLVYQEPIPTAQLVQRVASVMQEYTQSGGVRPFGVSLLICGWNEGRPYLFQSDPSGAYFAWKATAMGKNYVNGKTFLEKRYNEDLELEDAIHTAILTLKESFEGQMTEDNIEVGICNEAGFRRLTPTEVKDYLAAIA

Computationally mapped potential isoform sequences

There are 6 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
H3BT36H3BT36_HUMANPSMA248
C9JCK5C9JCK5_HUMANPSMA2164
A0A024RA52A0A024RA52_HUMANPSMA2234
H7C3A7H7C3A7_HUMANPSMA218
A0A7I2YQP7A0A7I2YQP7_HUMAN156
A0A7I2V2H3A0A7I2V2H3_HUMAN182

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
D00760
EMBL· GenBank· DDBJ
BAA00657.1
EMBL· GenBank· DDBJ
mRNA
AK290654
EMBL· GenBank· DDBJ
BAF83343.1
EMBL· GenBank· DDBJ
mRNA
CR450317
EMBL· GenBank· DDBJ
CAG29313.1
EMBL· GenBank· DDBJ
mRNA
CH236951
EMBL· GenBank· DDBJ
EAL24005.1
EMBL· GenBank· DDBJ
Genomic DNA
CH471073
EMBL· GenBank· DDBJ
EAW94152.1
EMBL· GenBank· DDBJ
Genomic DNA
BC002900
EMBL· GenBank· DDBJ
AAH02900.2
EMBL· GenBank· DDBJ
mRNA
BC047697
EMBL· GenBank· DDBJ
AAH47697.1
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.
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