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    RPN14 Rpn14p [ Saccharomyces cerevisiae S288C ]

    Gene ID: 852880, updated on 9-Dec-2024

    Summary

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    Official Symbol
    RPN14
    Official Full Name
    Rpn14p
    Primary source
    SGD:S000002972
    Locus tag
    YGL004C
    See related
    AllianceGenome:SGD:S000002972; FungiDB:YGL004C; VEuPathDB:YGL004C
    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 protein folding chaperone. Involved in proteasome regulatory particle assembly and ubiquitin-dependent protein catabolic process. Located in cytosol and nucleus. Orthologous to human PAAF1 (proteasomal ATPase associated factor 1). [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    See RPN14 in Genome Data Viewer
    Location:
    chromosome: VII
    Exon count:
    1
    Sequence:
    Chromosome: VII; NC_001139.9 (490703..491956, complement)

    Chromosome VII - NC_001139.9Genomic Context describing neighboring genes Neighboring gene calcium-transporting ATPase PMC1 Neighboring gene Golgi transport complex subunit COG7 Neighboring gene Cdh1p Neighboring gene Erp6p

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001139.9

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Inhibition of 26S proteasome activity by α-synuclein is mediated by the proteasomal chaperone Rpn14/PAAF1. Galka D, et al. Aging Cell, 2024 May. PMID 38415292, Free PMC Article
    2. New crystal structure of the proteasome-dedicated chaperone Rpn14 at 1.6 Å resolution. Kim S, et al. Acta Crystallogr Sect F Struct Biol Cryst Commun, 2012 May 1. PMID 22691779, Free PMC Article
    3. Crystal structure of yeast rpn14, a chaperone of the 19 S regulatory particle of the proteasome. Kim S, et al. J Biol Chem, 2010 May 14. PMID 20236927, Free PMC Article
    4. Conformational dynamics of the Rpt6 ATPase in proteasome assembly and Rpn14 binding. Ehlinger A, et al. Structure, 2013 May 7. PMID 23562395, Free PMC Article
    5. An inducible chaperone adapts proteasome assembly to stress. Hanssum A, et al. Mol Cell, 2014 Aug 21. PMID 25042801, Free PMC Article

    See all (51) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Rpn14 binds selectively to Rpt6's four-helix bundle, with surprisingly high affinity
      Title: Conformational dynamics of the Rpt6 ATPase in proteasome assembly and Rpn14 binding.
    2. crystal structure of Rpn14 with an E384A mutation is presented in space group P2(1) at 1.6 A resolution
      Title: New crystal structure of the proteasome-dedicated chaperone Rpn14 at 1.6 Å resolution.
    3. By inspection of structural data along with genetic and biochemical data, we determined the specific residues of Rpn14 and Rpt6 for complementary charge interactions that are required for 19 S RP assembly
      Title: Crystal structure of yeast rpn14, a chaperone of the 19 S regulatory particle of the proteasome.
    4. RPN14 protein involved in the efficient recognition of 26S proteasome for the proteolysis of ubiquitinated Gcn4p.
      Title: Rpn13p and Rpn14p are involved in the recognition of ubiquitinated Gcn4p by the 26S proteasome.
    Submit: New GeneRIF Correction

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Homology

    Gene Ontology Provided by SGD

    Function Evidence Code Pubs
    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
    		  
    involved_in ubiquitin-dependent protein catabolic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytoplasm HDA PubMed 
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in nucleus IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in nucleus IEA
    Inferred from Electronic Annotation
    more info
    		  
    part_of proteasome complex IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    Rpn14p
    NP_011511.3
    • Evolutionarily conserved 19S regulatory particle assembly-chaperone; proteasome-interacting protein involved in the assembly of the base subcomplex of the 19S proteasome regulatory particle (RP); null mutants accumulate ubiquitinated Gcn4p and display decreased 26S proteasome stability; interacts with Rpt5p

    NCBI Reference Sequences (RefSeq)

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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
      490703..491956 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001180869.3 → NP_011511.3  TPA: Rpn14p [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_011511.3

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VUD4, P53196
      UniProtKB/TrEMBL
      G2WE90, N1P210
      Conserved Domains (2) summary
      sd00039
      Location:96 → 133
      7WD40; WD40 repeat [structural motif]
      cl29593
      Location:133 → 357
      WD40; WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from ...
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P53196.1

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