SLX5 SUMO-targeted ubiquitin ligase complex subunit SLX5 [Saccharomyces cerevisiae S288C] - Gene

Summary

Go to the top of the page Help

Gene symbol: SLX5
Gene description: SUMO-targeted ubiquitin ligase complex subunit SLX5
Primary source: FungiDB:YDL013W
Locus tag: YDL013W
See related: SGD:S000002171; AllianceGenome:SGD:S000002171; VEuPathDB:YDL013W
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: HEX3; ULS2
Summary: Enables SUMO binding activity. Contributes to ubiquitin-protein transferase activity. Involved in several processes, including protein modification by small protein conjugation; telomere maintenance; and ubiquitin-dependent protein catabolic process. Located in chromosome, centromeric region and nucleus. Part of SUMO-targeted ubiquitin ligase complex. [provided by Alliance of Genome Resources, Apr 2022]
NEW: Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help

See SLX5 in Genome Data Viewer

Location:: chromosome: IV

Exon count:: 1

Sequence:: Chromosome: IV; NC_001136.10 (429067..430926)

Chromosome IV - NC_001136.10 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to reference sequence details

Genomic Sequence:: NC_001136.10

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the page Help

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

SLX5 deletion confers tolerance to oxidative stress in Saccharomyces cerevisiae.
Title: SLX5 deletion confers tolerance to oxidative stress in Saccharomyces cerevisiae.
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.
MATalpha2 (alpha2) mutants with impaired DNA binding become inaccessible to the Slx5/Slx8 pathway but are still rapidly degraded through efficient shunting to the Doa10 pathway.
Title: DNA binding by the MATα2 transcription factor controls its access to alternative ubiquitin-modification pathways.
SLX5 suppressor mutations of tdp1 wss1 synthetic lethality created new lysine residues in a 398 amino acid domain that is completely free of lysine. They result in the auto-ubiquitination and partial proteolysis of Slx5.
Title: A Lysine Desert Protects a Novel Domain in the Slx5-Slx8 SUMO Targeted Ub Ligase To Maintain Sumoylation Levels in Saccharomyces cerevisiae.
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.
Siz1 can be ubiquitylated in vivo and is degraded in an Slx5-dependent manner.
Title: A SUMO-targeted ubiquitin ligase is involved in the degradation of the nuclear pool of the SUMO E3 ligase Siz1.
distinct SUMO ligases work in concert with Esc2 and Slx5-Slx8 to control substrate specificity and sumoylation homeostasis to prevent GCRs.
Title: Distinct SUMO ligases cooperate with Esc2 and Slx5 to suppress duplication-mediated genome rearrangements.
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.
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.
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.

Submit: New GeneRIF Correction See all GeneRIFs (16)

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

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables SUMO binding	IDA Inferred from Direct Assay more info	PubMed
enables SUMO binding	IPI Inferred from Physical Interaction more info	PubMed
enables transferase activity	IEA Inferred from Electronic Annotation more info
contributes_to ubiquitin-protein transferase activity	IBA Inferred from Biological aspect of Ancestor more info
contributes_to ubiquitin-protein transferase activity	IDA Inferred from Direct Assay 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 apoptotic process	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein ubiquitination	IEA Inferred from Electronic Annotation more info
involved_in telomere maintenance	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
part_of SUMO-targeted ubiquitin ligase complex	IBA Inferred from Biological aspect of Ancestor more info
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	IDA Inferred from Direct Assay more info	PubMed
located_in chromosome, centromeric region	IEA Inferred from Electronic Annotation more info
located_in kinetochore	IEA Inferred from Electronic Annotation more info
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 SLX5

NP_010271.3

EC 2.3.2.27

Subunit of the Slx5-Slx8 SUMO-targeted Ub ligase (STUbL) complex; role in Ub-mediated degradation of histone variant Cse4p preventing mislocalization to euchromatin; role in proteolysis of spindle positioning protein Kar9p, and DNA repair proteins Rad52p and Rad57p; forms SUMO-dependent nuclear foci, including DNA repair centers; contains a RING domain and two SIM motifs; associates with the centromere; 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

NC_001136.10 Reference assembly

Range

429067..430926

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001180072.3 → NP_010271.3 TPA: SUMO-targeted ubiquitin ligase complex subunit SLX5 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_010271.3

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VRX6, P32828

UniProtKB/TrEMBL

A0A6A5PY40, A6ZXV5, B3LGS0, C7GW65, C8Z4Q6, G2WCE2, N1P4D7

Conserved Domains (1) summary

pfam06030
Location:106 → 184

DUF916; Bacterial protein of unknown function (DUF916)