P55035 · PSMD4_DROME

Function

function

Binds and presumably selects ubiquitin-conjugates for destruction.

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 Componentnucleoplasm
Cellular Componentnucleus
Cellular Componentproteasome complex
Cellular Componentproteasome regulatory particle
Cellular Componentproteasome regulatory particle, base subcomplex
Molecular Functionpolyubiquitin modification-dependent protein binding
Molecular Functionubiquitin conjugating enzyme binding
Molecular Functionzinc ion binding
Biological Processmitotic sister chromatid segregation
Biological Processproteasome-mediated ubiquitin-dependent protein catabolic process

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    26S proteasome non-ATPase regulatory subunit 4
  • Alternative names
    • 26S proteasome regulatory subunit RPN10
    • 26S proteasome regulatory subunit S5A
    • 54 kDa subunit of mu particle
    • Multiubiquitin chain-binding protein
    • p54

Gene names

    • Name
      Rpn10
    • Synonyms
      PROS-54, Pros54
    • ORF names
      CG7619

Organism names

  • Taxonomic identifier
  • Strain
    • Berkeley
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora

Accessions

  • Primary accession
    P55035
  • Secondary accessions
    • Q86R87
    • Q9V473

Proteomes

Organism-specific databases

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001738301-39626S proteasome non-ATPase regulatory subunit 4

Proteomic databases

Expression

Gene expression databases

Interaction

Subunit

The 26S proteasome is composed of a core protease, known as the 20S proteasome, capped at one or both ends by the 19S regulatory complex (RC). The RC is composed of at least 18 different subunits in two subcomplexes, the base and the lid, which form the portions proximal and distal to the 20S proteolytic core, respectively (By similarity).
Interacts with Ubc4

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P55035Ubc4 P524862EBI-146479, EBI-224571
BINARY P55035Ubqn Q9VWD94EBI-146479, EBI-100499

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain1-188VWFA
Domain212-231UIM 1
Region225-278Disordered
Domain276-295UIM 2
Domain303-322UIM 3
Region311-341Disordered
Compositional bias325-339Basic and acidic residues
Region360-396Disordered
Compositional bias377-396Basic and acidic residues

Sequence similarities

Belongs to the proteasome subunit S5A family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    396
  • Mass (Da)
    42,618
  • Last updated
    2001-11-02 v2
  • Checksum
    061418F6F7FE819F
MVLESTMICFDNSDFQRNGDYFPTRLIVQRDGINLVCLTKLRSNPENNVGLMTLSNTVEVLATLTSDAGRIFSKMHLVQPKGEINLLTGIRIAHLVLKHRQGKNHKMRIVVFVGSPINHEEGDLVKQAKRLKKEKVNVDIVSFGDHGNNNEILTAFINALNGKDGTGSHLVSVPRGSVLSDALLSSPIIQGEDGMGGAGLGGNVFEFGVDPNEDPELALALRVSMEEQRQRQESEQRRANPDGAPPTGGDAGGGGGVSGSGPGNEESAGAENEANTEEAMLQRALALSTETPEDNLPDFANMTEEEQIAFAMQMSMQDAPDDSVTQQAKRPKTDEANAPMDVDEDYSEVIGDPAFLQSVLENLPGVDPQSEAVRDAVGSLNKDKDKKSDGKDSQKK

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
M9PIG8M9PIG8_DROMERpn10396

Sequence caution

The sequence AAL90071.2 differs from that shown. Reason: Erroneous initiation Extended N-terminus.

Features

Showing features for sequence conflict, compositional bias.

TypeIDPosition(s)Description
Sequence conflict9in Ref. 1; AAB35145
Compositional bias325-339Basic and acidic residues
Compositional bias377-396Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
S79502
EMBL· GenBank· DDBJ
AAB35145.1
EMBL· GenBank· DDBJ
Genomic DNA
AE014296
EMBL· GenBank· DDBJ
AAF51741.1
EMBL· GenBank· DDBJ
Genomic DNA
AY089333
EMBL· GenBank· DDBJ
AAL90071.2
EMBL· GenBank· DDBJ
mRNA Different initiation

Genome annotation databases

Similar Proteins

Disclaimer

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