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    SEM1 proteasome regulatory particle lid subunit SEM1 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 851967, updated on 18-Sep-2024

    Summary

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    Official Symbol
    SEM1
    Official Full Name
    proteasome regulatory particle lid subunit SEM1
    Primary source
    SGD:S000007235
    Locus tag
    YDR363W-A
    See related
    AllianceGenome:SGD:S000007235; FungiDB:YDR363W-A; VEuPathDB:YDR363W-A
    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
    DSS1; HOD1
    Summary
    Involved in several processes, including SAGA complex localization to transcription regulatory region; maintenance of DNA trinucleotide repeats; and proteolysis. Located in cytosol and proteasome storage granule. Part of proteasome regulatory particle, lid subcomplex and transcription export complex 2. [provided by Alliance of Genome Resources, Apr 2022]
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    Genomic context

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    See SEM1 in Genome Data Viewer
    Location:
    chromosome: IV
    Exon count:
    1
    Sequence:
    Chromosome: IV; NC_001136.10 (1202128..1202397)

    Chromosome IV - NC_001136.10Genomic Context describing neighboring genes Neighboring gene Esc2p Neighboring gene tRNA-Lys Neighboring gene Cdc40p Neighboring gene pre-rRNA-processing protein ESF1

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001136.10

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Functional inactivation of the conserved Sem1p in yeast by intrabodies. Reinman M, et al. Yeast, 2003 Sep. PMID 12961755
    2. Designed proteins to modulate cellular networks. Cortajarena AL, et al. ACS Chem Biol, 2010 Jun 18. PMID 20020775, Free PMC Article
    3. Structural assembly of the nucleic-acid-binding Thp3-Csn12-Sem1 complex functioning in mRNA splicing. Kuang Z, et al. Nucleic Acids Res, 2022 Aug 26. PMID 35904806, Free PMC Article
    4. Sem1p and Ubp6p orchestrate telomeric silencing by modulating histone H2B ubiquitination and H3 acetylation. Qin S, et al. Nucleic Acids Res, 2009 Apr. PMID 19188254, Free PMC Article
    5. Kluyveromyces lactis SSO1 and SEB1 genes are functional in Saccharomyces cerevisiae and enhance production of secreted proteins when overexpressed. Toikkanen JH, et al. Yeast, 2004 Sep. PMID 15449305

    See all (117) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Sem1 has a distinct, chaperone-like function specific to early stages of proteasome assembly.
      Title: The intrinsically disordered Sem1 protein functions as a molecular tether during proteasome lid biogenesis.
    2. Results demonstrate that Sem1p and Ubp6p maintain telomeric heterochromatin structure through modulation of histone covalent modifications and association of silencing factors independently of the proteolytic function of the proteasome.
      Title: Sem1p and Ubp6p orchestrate telomeric silencing by modulating histone H2B ubiquitination and H3 acetylation.
    3. These data enabled the discovery of links between components of the mRNA export and splicing machineries and Sem1/Dss1, a component of the 19S proteasome.
      Title: A genetic interaction map of RNA-processing factors reveals links between Sem1/Dss1-containing complexes and mRNA export and splicing.
    Submit: New GeneRIF Correction

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Gene Ontology Provided by SGD

    Function Evidence Code Pubs
    enables molecular_function ND
    No biological Data available
    more info
    		  
    Process Evidence Code Pubs
    involved_in SAGA complex localization to transcription regulatory region IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in double-strand break repair via homologous recombination IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in filamentous growth IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in mRNA export from nucleus HGI PubMed 
    involved_in mRNA export from nucleus IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in mRNA export from nucleus IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in mRNA export from nucleus IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    involved_in maintenance of DNA trinucleotide repeats IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in proteasome assembly IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in proteasome assembly IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in proteasome-mediated ubiquitin-dependent protein catabolic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in proteasome-mediated ubiquitin-dependent protein catabolic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in protein folding IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in regulation of cell cycle IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in ubiquitin-dependent protein catabolic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    part_of proteasome complex IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    part_of proteasome complex IEA
    Inferred from Electronic Annotation
    more info
    		  
    part_of proteasome regulatory particle, lid subcomplex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    part_of proteasome regulatory particle, lid subcomplex IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in proteasome storage granule IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    part_of transcription export complex 2 IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    proteasome regulatory particle lid subunit SEM1
    NP_010651.3
    • 19S proteasome regulatory particle lid subcomplex component; role in Ub-dependent proteolysis and proteasome stability; involved in TREX-2 mediated mRNA export, and in the prevention of transcription-associated genome instability; ubiquitinated by Nedd4-like E3-ligase, Rsp5p; human ortholog DSS1, a BRCA1 binding protein implicated in cancer, complements the yeast null; drives trinucleotide repeat expansion; protein abundance increases in response to DNA replication stress

    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_001136.10 Reference assembly

      Range
      1202128..1202397
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001184328.3 → NP_010651.3  TPA: proteasome regulatory particle lid subunit SEM1 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_010651.3

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VSZ2, O94742
      UniProtKB/TrEMBL
      A6ZYW2, B3LFT9, C7GMH3, G2WBA0, N1P799
      Conserved Domains (1) summary
      cd13768
      Location:28 → 84
      DSS1_Sem1; proteasome complex subunit DSS1/Sem1
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    O94742.1

    Gene LinkOut

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