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NAS6 Nas6p [ Saccharomyces cerevisiae S288C ]

Gene ID: 853147, updated on 7-Jun-2026
Official Symbol
NAS6
Official Full Name
Nas6p
Primary source
SGD:S000003464
Locus tag
YGR232W
See related
AllianceGenome:SGD:S000003464; FungiDB:YGR232W; VEuPathDB:YGR232W
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Saccharomyces cerevisiae S288C (strain: S288C)
Lineage
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary
Enables proteasome regulatory particle binding activity and protein folding chaperone. Involved in proteasome regulatory particle assembly. Located in cytosol and nucleus. Orthologous to human PSMD10 (proteasome 26S subunit, non-ATPase 10). [provided by Alliance of Genome Resources, Jul 2025]
Orthologs
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See NAS6 in Genome Data Viewer
Location:
chromosome: VII
Exon count:
1
Sequence:
Chromosome: VII; NC_001139.9 (953960..954646)

Chromosome VII - NC_001139.9Genomic Context describing neighboring genes Neighboring gene Bns1p Neighboring gene prohibitin subunit PHB2 Neighboring gene Pho81p Neighboring gene flavohemoglobin

Genomic Sequence:
NC_001139.9

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Crystal structure of the homolog of the oncoprotein gankyrin, an interactor of Rb and CDK4/6. Padmanabhan B, et al. J Biol Chem, 2004 Jan 9. PMID 14583612
  2. An Allosteric Interaction Network Promotes Conformation State-Dependent Eviction of the Nas6 Assembly Chaperone from Nascent 26S Proteasomes. Nemec AA, et al. Cell Rep, 2019 Jan 8. PMID 30625330, Free PMC Article
  3. Purification, crystallization and preliminary X-ray diffraction analysis of yeast regulatory particle non-ATPase subunit 6 (Nas6p). Adachi N, et al. Acta Crystallogr D Biol Crystallogr, 2002 May. PMID 11976503
  4. Structural basis for the recognition between the regulatory particles Nas6 and Rpt3 of the yeast 26S proteasome. Nakamura Y, et al. Biochem Biophys Res Commun, 2007 Aug 3. PMID 17555716
  5. Purification, crystallization and preliminary X-ray diffraction analysis of the non-ATPase subunit Nas6 in complex with the ATPase subunit Rpt3 of the 26S proteasome from Saccharomyces cerevisiae. Nakamura Y, et al. Acta Crystallogr Sect F Struct Biol Cryst Commun, 2007 Mar 1. PMID 17329811, Free PMC Article

See all (70) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Assembly chaperone Nas6 selectively destabilizes 26S proteasomes with defective regulatory particle-core particle interfaces.
    Title: Assembly chaperone Nas6 selectively destabilizes 26S proteasomes with defective regulatory particle-core particle interfaces.
  2. Nas6 is evicted from nascent proteasomes during completion of assembly via a conformation-specific allosteric interaction of the Rpn5 subunit with the proteasomal ATPase ring.
    Title: An Allosteric Interaction Network Promotes Conformation State-Dependent Eviction of the Nas6 Assembly Chaperone from Nascent 26S Proteasomes.
  3. Data suggest that Nas6 provides a finely regulated mechanism to order the events of proteasome assembly in time.
    Title: Nucleotide-dependent switch in proteasome assembly mediated by the Nas6 chaperone.
  4. Data show that both ATPases Rpt6 and Rpt3 tails are required for the eviction of Nas6 chaperone upon proteasome assembly.
    Title: Proteasome Activation is Mediated via a Functional Switch of the Rpt6 C-terminal Tail Following Chaperone-dependent Assembly.
  5. provide a structural basis for the association between Nas6 and the heterohexameric ATPase ring of the proteasome through Rpt3
    Title: Structural basis for the recognition between the regulatory particles Nas6 and Rpt3 of the yeast 26S proteasome.
Submit: New GeneRIF Correction
Products Interactant Other Gene Complex Source Pubs Description

Homology

Gene Ontology Provided by SGD

Function Evidence Code Pubs
enables proteasome regulatory particle binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables protein folding chaperone IDA
Inferred from Direct Assay
more info
 PubMed 
Process Evidence Code Pubs
involved_in proteasome regulatory particle assembly IGI
Inferred from Genetic Interaction
more info
 PubMed 
involved_in proteasome regulatory particle assembly IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in protein folding IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
located_in cytosol IDA
Inferred from Direct Assay
more info
 PubMed 
located_in nucleus IDA
Inferred from Direct Assay
more info
 PubMed 
Preferred Names
Nas6p
NP_011748.3
  • Evolutionarily conserved 19S regulatory particle assembly-chaperone; proteasome-interacting protein involved in the assembly of the base subcomplex of the 19S proteasomal regulatory particle (RP); ortholog of human oncoprotein gankyrin, also known as p28, which interacts with the Rb tumor suppressor and CDK4/6

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_001139.9 Reference assembly

    Range
    953960..954646
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001181361.3 → NP_011748.3  Nas6p

    See identical proteins and their annotated locations for NP_011748.3

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    D6VV12, P50086
    UniProtKB/TrEMBL
    C7GNJ7, G2WEV8, N1P2L0
    Conserved Domains (2) summary
    COG0666
    Location:1 → 226
    ANKYR; Ankyrin repeat [Signal transduction mechanisms]
    sd00045
    Location:107 → 137
    ANK; ANK repeat [structural motif]
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P50086.1

Gene LinkOut

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