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PRE2 proteasome core particle subunit beta 5 [ Saccharomyces cerevisiae S288C ]

Gene ID: 856218, updated on 13-Apr-2024

Summary

Gene symbol
PRE2
Gene description
proteasome core particle subunit beta 5
Primary source
SGD:S000006307
Locus tag
YPR103W
See related
AllianceGenome:SGD:S000006307
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
DOA3; PRG1; SRR2
Summary
Enables endopeptidase activity. Involved in proteasomal ubiquitin-independent protein catabolic process; proteasome core complex assembly; and proteasome-mediated ubiquitin-dependent protein catabolic process. Located in cytosol and nucleus. Part of proteasome core complex, beta-subunit complex. Human ortholog(s) of this gene implicated in JMP syndrome. Orthologous to several human genes including PSMB5 (proteasome 20S subunit beta 5) and PSMB8 (proteasome 20S subunit beta 8). [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

Location:
chromosome: XVI
Exon count:
1
Sequence:
Chromosome: XVI; NC_001148.4 (732349..733212)

Chromosome XVI - NC_001148.4Genomic Context describing neighboring genes Neighboring gene Snt309p Neighboring gene ribosomal 60S subunit protein L11A Neighboring gene Fhl1p Neighboring gene Golgi transport complex subunit COG4

Bibliography

Pathways from PubChem

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General gene information

Gene Ontology Provided by SGD

Function Evidence Code Pubs
enables endopeptidase activity IBA
Inferred from Biological aspect of Ancestor
more info
 
enables endopeptidase activity IMP
Inferred from Mutant Phenotype
more info
PubMed 
enables threonine-type endopeptidase activity IEA
Inferred from Electronic Annotation
more info
 
Component Evidence Code Pubs
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
 
located_in cytosol HDA PubMed 
is_active_in cytosol IBA
Inferred from Biological aspect of Ancestor
more info
 
located_in nucleus HDA PubMed 
is_active_in nucleus IBA
Inferred from Biological aspect of Ancestor
more info
 
located_in nucleus IEA
Inferred from Electronic Annotation
more info
 
located_in peroxisome IDA
Inferred from Direct Assay
more info
PubMed 
part_of proteasome complex IEA
Inferred from Electronic Annotation
more info
 
part_of proteasome core complex IEA
Inferred from Electronic Annotation
more info
 
part_of proteasome core complex, beta-subunit complex IBA
Inferred from Biological aspect of Ancestor
more info
 
part_of proteasome core complex, beta-subunit complex IDA
Inferred from Direct Assay
more info
PubMed 
part_of proteasome core complex, beta-subunit complex IEA
Inferred from Electronic Annotation
more info
 

General protein information

Preferred Names
proteasome core particle subunit beta 5
NP_015428.1
  • Beta 5 subunit of the 20S proteasome; responsible for the chymotryptic activity of the proteasome; localizes to peroxisomes in oleate-growing cells

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_001148.4 Reference assembly

    Range
    732349..733212
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001184200.1NP_015428.1  TPA: proteasome core particle subunit beta 5 [Saccharomyces cerevisiae S288C]

    See identical proteins and their annotated locations for NP_015428.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    D6W4A1, P30656
    UniProtKB/TrEMBL
    A0A6A5Q5W3, A6ZWY3, B3LK67, B5VTP4, C7GXR4, C8ZJC5, G2WPR9, N1NVK9
    Conserved Domains (1) summary
    cd03761
    Location:76264
    proteasome_beta_type_5; proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that ...