E3 ubiquitin-protein ligase complex SLX5-SLX8 subunit SLX8 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P40072 (SLX8_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 103. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
E3 ubiquitin-protein ligase complex SLX5-SLX8 subunit SLX8
EC=6.3.2.-

Alternative name(s):
Synthetic lethal of unknown function protein 8

Gene names

Name:	SLX8
Ordered Locus Names:	YER116C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	274 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Mediates ubiquitination and susbsequent desumoylation/degradation of sumoylated proteins and proteins containing SUMO-like domains. Promotes UBC4-dependent ubiquitination that mediates the proteolytic down-regulation of sumoylated proteins. Involved in the stimulation of ubiquitin conjugating enzymes, including UBC1, UBC4, UBC5 and UBC13-MMS2. Acts as a critical suppressor of gross chromosomal rearrangements (GCRs) during normal cell cycle progression. Has a role in localizing the DNA damage protein DCD2. Involved in stabilizing, restarting or resolving transiently stalled replication forks. Prevents accumulation of DNA damage during cell cycle progression. Inhibits RAD51-independent recombination via modulating the sumoylation of DNA repair proteins. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.15
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Heterodimer. Interacts with SLX5/HEX3. Ref.4 Ref.7 Ref.8 Ref.9 Ref.10 Ref.15
Subcellular location	Nucleus › nucleolus. Note: Localizes at the replication centers. Ref.11 Ref.15
Sequence similarities	Contains 1 RING-type zinc finger.

Ontologies

Keywords
Biological process	DNA damage DNA repair Ubl conjugation pathway
Cellular component	Nucleus
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW protein sumoylation Inferred from mutant phenotype Ref.6. Source: SGD response to DNA damage stimulus Inferred from mutant phenotype Ref.4 Ref.5. Source: SGD telomere maintenance Inferred from mutant phenotype PubMed 16428246. Source: SGD
Cellular_component	cytoplasm Inferred from direct assay PubMed 22842922. Source: SGD nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay PubMed 19270524 PubMed 22842922. Source: SGD ubiquitin ligase complex Inferred from direct assay Ref.10. Source: SGD
Molecular_function	ubiquitin-protein ligase activity Inferred from direct assay Ref.10. Source: SGD zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SLX5	P32828	2	EBI-22661,EBI-8276

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 274

274

E3 ubiquitin-protein ligase complex SLX5-SLX8 subunit SLX8

PRO_0000056336

Regions

Zinc finger

206 – 250

RING-type

Amino acid modifications

Modified residue

Phosphoserine Ref.3 Ref.14

Modified residue

Phosphothreonine Ref.3

Modified residue

Phosphoserine Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

P40072 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 358DB6D137155DC1
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FASTA

274

30,764

        10         20         30         40         50         60 
MARRPDNQNP EGENLRIKRV RLESVRQNDE EEENEVSRTQ NIVTDNRHDS PEAVVEIIGE 

        70         80         90        100        110        120 
RALENTSEED GDDDLSLFRA LEEDPGSDHN TSNNDSGNHD RETMHTEEPE ASSGNNITLT 

       130        140        150        160        170        180 
NNVEELHTMD VLSQTANTPS ASPMLDAAPP TTKPGTNSKE QTVDLTADAI DLDAEEQQVL 

       190        200        210        220        230        240 
QISDDDFQEE TKEAPKEYGA AKDYRCPICF EPPETALMTL CGHVFCCPCL FQMVNSSRTC 

       250        260        270 
RQFGHCALCR SKVYLKDVRL IILRKKQVKK KVKS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome V." Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. Davis R.W. Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; THR-66 AND SER-67, MASS SPECTROMETRY. Strain: ADR376.
[4]	"Requirement for three novel protein complexes in the absence of the Sgs1 DNA helicase in Saccharomyces cerevisiae." Mullen J.R., Kaliraman V., Ibrahim S.S., Brill S.J. Genetics 157:103-118(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN DEGRADATION OF SUMOYLATED PROTEINS, INTERACTION WITH SLX5.
[5]	"Suppression of genomic instability by SLX5 and SLX8 in Saccharomyces cerevisiae." Zhang C., Roberts T.M., Yang J., Desai R., Brown G.W. DNA Repair 5:336-346(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN STABILIZATION OF DNA DAMAGE.
[6]	"Genetic analysis connects SLX5 and SLX8 to the SUMO pathway in Saccharomyces cerevisiae." Wang Z., Jones G.M., Prelich G. Genetics 172:1499-1509(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN STABILIZATION OF DNA DAMAGE.
[7]	"The yeast Slx5-Slx8 DNA integrity complex displays ubiquitin ligase activity." Ii T., Fung J., Mullen J.R., Brill S.J. Cell Cycle 6:2800-2809(2007) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITIN-PROTEIN LIGASE ACTIVITY, FUNCTION IN STIMULATION OF UBIQUITIN CONJUGASTING ENZYMES, INTERACTION WITH SLX5/HEX3.
[8]	"Stimulation of in vitro sumoylation by Slx5-Slx8: evidence for a functional interaction with the SUMO pathway." Ii T., Mullen J.R., Slagle C.E., Brill S.J. DNA Repair 6:1679-1691(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN DEGRADATION OF SUMOYLATED PROTEINS, INTERACTION WITH SLX5/HEX3.
[9]	"Ubiquitin-dependent proteolytic control of SUMO conjugates." Uzunova K., Goettsche K., Miteva M., Weisshaar S.R., Glanemann C., Schnellhardt M., Niessen M., Scheel H., Hofmann K., Johnson E.S., Praefcke G.J.K., Dohmen R.J. J. Biol. Chem. 282:34167-34175(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN DEGRADATION OF SUMOYLATED PROTEINS, LIGASE ACTIVITY, INTERACTION WITH SLX5.
[10]	"The yeast Hex3.Slx8 heterodimer is a ubiquitin ligase stimulated by substrate sumoylation." Xie Y., Kerscher O., Kroetz M.B., McConchie H.F., Sung P., Hochstrasser M. J. Biol. Chem. 282:34176-34184(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN DEGRADATION OF SUMOYLATED PROTEINS, LIGASE ACTIVITY, INTERACTION WITH SLX5.
[11]	"The Slx5-Slx8 complex affects sumoylation of DNA repair proteins and negatively regulates recombination." Burgess R.C., Rahman S., Lisby M., Rothstein R., Zhao X. Mol. Cell. Biol. 27:6153-6162(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN NEGATIVE REGULATION OF RECOMBINATION, SUBCELLULAR LOCATION.
[12]	"A genetic screen for increased loss of heterozygosity in Saccharomyces cerevisiae." Andersen M.P., Nelson Z.W., Hetrick E.D., Gottschling D.E. Genetics 179:1179-1195(2008) [PubMed] [Europe PMC] [Abstract] Cited for: DELETION ANALYSIS.
[13]	"Activation of the Slx5-Slx8 ubiquitin ligase by poly-small ubiquitin-like modifier conjugates." Mullen J.R., Brill S.J. J. Biol. Chem. 283:19912-19921(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN DEGRADATION OF SUMOYLATED PROTEINS.
[14]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, MASS SPECTROMETRY.
[15]	"Functional targeting of DNA damage to a nuclear pore-associated SUMO-dependent ubiquitin ligase." Nagai S., Dubrana K., Tsai-Pflugfelder M., Davidson M.B., Roberts T.M., Brown G.W., Varela E., Hediger F., Gasser S.M., Krogan N.J. Science 322:597-602(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN DEGRADATION OF SUMOYLATED PROTEINS, INTERACTION WITH SLX5/HEX3, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U18916 Genomic DNA. Translation: AAC03214.1. BK006939 Genomic DNA. Translation: DAA07776.1.
PIR	S50619.
RefSeq	NP_011041.3. NM_001179006.3.
3D structure databases
ProteinModelPortal	P40072.
SMR	P40072. Positions 200-263.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1365N.
IntAct	P40072. 4 interactions.
MINT	MINT-396089.
STRING	4932.YER116C.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YER116C; YER116C; YER116C.
GeneID	856852.
KEGG	sce:YER116C. sce:YER120W.
Organism-specific databases
CYGD	YER116c.
SGD	S000000918. SLX8.
Phylogenomic databases
eggNOG	COG5574.
OrthoDB	EOG44N22N.
Enzyme and pathway databases
UniPathway	UPA00143.
Gene expression databases
Genevestigator	P40072.
GermOnline	YER116C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	3.30.40.10. 1 hit.
InterPro	IPR018957. Znf_C3HC4_RING-type. IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. IPR017907. Znf_RING_CS. [Graphical view]
Pfam	PF00097. zf-C3HC4. 1 hit. [Graphical view]
SMART	SM00184. RING. 1 hit. [Graphical view]
PROSITE	PS00518. ZF_RING_1. 1 hit. PS50089. ZF_RING_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	983189.

Entry information

Entry name

SLX8_YEAST

Accession

Primary (citable) accession number: P40072
Secondary accession number(s): D3DM22

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	May 1, 2013
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome V

Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents