U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination
    • Showing Current items.

    SLX8 SUMO-targeted ubiquitin ligase complex subunit SLX8 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 856852, updated on 28-Oct-2024

    Summary

    Go to the top of the page Help
    Official Symbol
    SLX8
    Official Full Name
    SUMO-targeted ubiquitin ligase complex subunit SLX8
    Primary source
    SGD:S000000918
    Locus tag
    YER116C
    See related
    AllianceGenome:SGD:S000000918; FungiDB:YER116C; VEuPathDB:YER116C
    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 ubiquitin-protein transferase activity. Involved in DNA damage response; protein modification by small protein conjugation; and telomere maintenance. Located in kinetochore and nucleus. Part of SUMO-targeted ubiquitin ligase complex. [provided by Alliance of Genome Resources, Oct 2024]
    NEW
    Try the new Gene table
    Try the new Transcript table

    Genomic context

    Go to the top of the page Help
    See SLX8 in Genome Data Viewer
    Location:
    chromosome: V
    Exon count:
    1
    Sequence:
    Chromosome: V; NC_001137.3 (395348..396172, complement)

    Chromosome V - NC_001137.3Genomic Context describing neighboring genes Neighboring gene Boi2p Neighboring gene Spr6p Neighboring gene ribosomal 60S subunit protein L23B Neighboring gene osmosensor SHO1

    Genomic regions, transcripts, and products

    Go to the top of the page Help
    Genomic Sequence:
    NC_001137.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

    Go to the top of the pageHelp

    Related articles in PubMed

    1. Purification of the yeast Slx5-Slx8 protein complex and characterization of its DNA-binding activity. Yang L, et al. Nucleic Acids Res, 2006. PMID 17020915, Free PMC Article
    2. Suppression of genomic instability by SLX5 and SLX8 in Saccharomyces cerevisiae. Zhang C, et al. DNA Repair (Amst), 2006 Mar 7. PMID 16325482
    3. The SUMO-targeted ubiquitin ligase subunit Slx5 resides in nuclear foci and at sites of DNA breaks. Cook CE, et al. Cell Cycle, 2009 Apr 1. PMID 19270524, Free PMC Article
    4. SUMO expression shortens the lag phase of Saccharomyces cerevisiae yeast growth caused by complex interactive effects of major mixed fermentation inhibitors found in hot-compressed water-treated lignocellulosic hydrolysate. Jayakody LN, et al. Appl Microbiol Biotechnol, 2015 Jan. PMID 25359478
    5. SUMO-Targeted Ubiquitin Ligases (STUbLs) Reduce the Toxicity and Abnormal Transcriptional Activity Associated With a Mutant, Aggregation-Prone Fragment of Huntingtin. Ohkuni K, et al. Front Genet, 2018. PMID 30279700, Free PMC Article

    See all (119) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Co-localization of the budding yeast STUbL Slx5/Slx8 and ubiquitin at seven genomic loci termed "ubiquitin hotspots" contribute to stress tolerance.
      Title: Slx5/Slx8-dependent ubiquitin hotspots on chromatin contribute to stress tolerance.
    2. RecQ-like helicase Sgs1 subcellular localization is regulated by SUMO-targeted ubiquitin ligase Slx5-Slx8 in response to DNA damage, presumably to prevent illegitimate recombination events.
      Title: Disruption of SUMO-targeted ubiquitin ligases Slx5-Slx8/RNF4 alters RecQ-like helicase Sgs1/BLM localization in yeast and human cells.
    3. the DNA-damage targeting of Slx5/Slx8 depends on formation of the heterodimer and that this occurs at a subset of nuclear foci also containing DNA damage repair and checkpoint factors.
      Title: The SUMO-targeted ubiquitin ligase subunit Slx5 resides in nuclear foci and at sites of DNA breaks.
    4. Component or regulator of the small ubiquitin-related modifier (SUMO) protein pathway.
      Title: Genetic analysis connects SLX5 and SLX8 to the SUMO pathway in Saccharomyces cerevisiae.
    5. study shows a nuclear pore subcomplex and Slx5/Slx8, a SUMO-dependent ubiquitin ligase physically interact; findings suggest that DNA strand breaks are shunted to nuclear pores for a repair pathway controlled by a conserved SUMO-dependent E3 ligase
      Title: Functional targeting of DNA damage to a nuclear pore-associated SUMO-dependent ubiquitin ligase.
    6. Slx5-Slx8 ubiquitin ligase is stimulated by poly-SUMO conjugates and that it can ubiquitinate a poly-small ubiquitin-like modifier chain
      Title: Activation of the Slx5-Slx8 ubiquitin ligase by poly-small ubiquitin-like modifier conjugates.
    7. The Slx5-Slx8 complex functions as a two-component ubiquitin ligase and controls genome stability via ubiquination.
      Title: The yeast Slx5-Slx8 DNA integrity complex displays ubiquitin ligase activity.
    8. Slx8 and Slx5 complex is capable of interacting directly with the SUMO pathway
      Title: Stimulation of in vitro sumoylation by Slx5-Slx8: evidence for a functional interaction with the SUMO pathway.
    9. the Hex3.Slx8 complex has a robust substrate-specific E3 ubiquitin ligase activity.
      Title: The yeast Hex3.Slx8 heterodimer is a ubiquitin ligase stimulated by substrate sumoylation.
    10. Data suggest that, during replication, the Slx5-Slx8 complex helps prevent DNA lesions that are acted upon by recombination, and inhibits Rad51-independent recombination via modulating the sumoylation of DNA repair proteins.
      Title: The Slx5-Slx8 complex affects sumoylation of DNA repair proteins and negatively regulates recombination.
    Submit: New GeneRIF Correction

    Interactions

    Go to the top of the page Help
    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

    Go to the top of the page Help

    Homology

    Gene Ontology Provided by SGD

    Function Evidence Code Pubs
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables transferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ubiquitin protein ligase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    contributes_to ubiquitin-protein transferase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables ubiquitin-protein transferase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables zinc ion binding RCA
    inferred from Reviewed Computational Analysis
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in DNA damage response IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in DNA damage response IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in DNA repair IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in protein sumoylation IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in protein sumoylation IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in protein ubiquitination IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in protein ubiquitination IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in protein ubiquitination IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in protein ubiquitination IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in telomere maintenance IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    part_of SUMO-targeted ubiquitin ligase complex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in chromosome IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in chromosome, centromeric region IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in cytoplasm HDA PubMed 
    located_in kinetochore IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in kinetochore IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in nucleus HDA PubMed 
    located_in nucleus IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in nucleus IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

    Go to the top of the page Help
    Preferred Names
    SUMO-targeted ubiquitin ligase complex subunit SLX8
    NP_011041.3
    • Subunit of Slx5-Slx8 SUMO-targeted ubiquitin ligase (STUbL) complex; role in proteolysis of spindle positioning protein Kar9, DNA repair proteins Rad52p and Rad57p; stimulated by SUMO-modified substrates; contains a C-terminal RING domain; forms nuclear foci upon DNA replication stress; required for maintenance of genome integrity like human ortholog RNF4

    NCBI Reference Sequences (RefSeq)

    Go to the top of the page Help

    NEW Try the new Transcript table

    Genome Annotation

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

    Reference assembly

    Genomic

    1. NC_001137.3 Reference assembly

      Range
      395348..396172 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001179006.3 → NP_011041.3  TPA: SUMO-targeted ubiquitin ligase complex subunit SLX8 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_011041.3

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D3DM22, P40072
      UniProtKB/TrEMBL
      A6ZR71, B3LRN2, B5VHP2, C8Z7D3, G2WD08, N1P5A8
      Conserved Domains (1) summary
      COG5574
      Location:1 → 264
      PEX10; RING-finger-containing E3 ubiquitin ligase [Posttranslational modification, protein turnover, chaperones]
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P40072.1

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

    Other Literature Sources
    Molecular Biology Databases
    Research Materials
    Tools