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PFD1 prefolding complex chaperone subunit [ Saccharomyces cerevisiae S288C ]

Gene ID: 853260, updated on 3-Nov-2024

Summary

Official Symbol
PFD1
Official Full Name
prefolding complex chaperone subunit
Primary source
SGD:S000003715
Locus tag
YJL179W
See related
AllianceGenome:SGD:S000003715; FungiDB:YJL179W; VEuPathDB:YJL179W
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Saccharomyces cerevisiae S288C (strain: S288C)
Lineage
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Also known as
GIM6
Summary
Enables unfolded protein binding activity. Involved in cytoskeleton organization; positive regulation of transcription elongation by RNA polymerase II; and protein folding. Part of prefoldin complex. Orthologous to human PFDN1 (prefoldin subunit 1). [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

See PFD1 in Genome Data Viewer
Location:
chromosome: X
Exon count:
1
Sequence:
Chromosome: X; NC_001142.9 (88787..89116)

Chromosome X - NC_001142.9Genomic Context describing neighboring genes Neighboring gene Rbh1p Neighboring gene ATP synthase complex assembly protein ATP12 Neighboring gene Atg27p Neighboring gene ribosomal 60S subunit protein L17B

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General gene information

Gene Ontology Provided by SGD

Function Evidence Code Pubs
enables protein folding chaperone IBA
Inferred from Biological aspect of Ancestor
more info
 
enables unfolded protein binding IBA
Inferred from Biological aspect of Ancestor
more info
 
enables unfolded protein binding IEA
Inferred from Electronic Annotation
more info
 
enables unfolded protein binding IMP
Inferred from Mutant Phenotype
more info
PubMed 
Process Evidence Code Pubs
involved_in cytoskeleton organization IMP
Inferred from Mutant Phenotype
more info
PubMed 
involved_in positive regulation of transcription elongation by RNA polymerase II IGI
Inferred from Genetic Interaction
more info
PubMed 
involved_in positive regulation of transcription elongation by RNA polymerase II IMP
Inferred from Mutant Phenotype
more info
PubMed 
involved_in protein folding IBA
Inferred from Biological aspect of Ancestor
more info
 
involved_in protein folding IEA
Inferred from Electronic Annotation
more info
 
involved_in protein folding IMP
Inferred from Mutant Phenotype
more info
PubMed 
Component Evidence Code Pubs
is_active_in cytoplasm IBA
Inferred from Biological aspect of Ancestor
more info
 
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
 
part_of prefoldin complex IEA
Inferred from Electronic Annotation
more info
 
part_of prefoldin complex IMP
Inferred from Mutant Phenotype
more info
PubMed 

General protein information

Preferred Names
prefolding complex chaperone subunit
NP_012356.2
  • Subunit of heterohexameric prefoldin; prefoldin binds cytosolic chaperonin and transfers target proteins to it; involved in the biogenesis of actin and of alpha- and gamma-tubulin; prefoldin complex also localizes to chromatin of actively transcribed genes in the nucleus and facilitates transcriptional elongation

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_001142.9 Reference assembly

    Range
    88787..89116
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001181612.2NP_012356.2  TPA: prefolding complex chaperone subunit [Saccharomyces cerevisiae S288C]

    See identical proteins and their annotated locations for NP_012356.2

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    D6VW10, E9P8V7, P46988
    UniProtKB/TrEMBL
    A6ZQF5, B3LPU6, C7GS05, C8ZB40, G2WGJ6, N1P8Z6
    Conserved Domains (1) summary
    cl09111
    Location:12109
    Prefoldin; Prefoldin is a hexameric molecular chaperone complex, found in both eukaryotes and archaea, that binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits ...