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P40072 (SLX8_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length274 AA.
Sequence statusComplete.
Protein existenceEvidence 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.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.13 Ref.15

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Heterodimer. Interacts with SLX5/HEX3. Ref.3 Ref.6 Ref.7 Ref.8 Ref.9 Ref.15

Subcellular location

Nucleusnucleolus. Note: Localizes at the replication centers. Ref.11 Ref.15

Sequence similarities

Contains 1 RING-type zinc finger.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SLX5P328282EBI-22661,EBI-8276

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 274274E3 ubiquitin-protein ligase complex SLX5-SLX8 subunit SLX8
PRO_0000056336

Regions

Zinc finger206 – 25045RING-type

Amino acid modifications

Modified residue501Phosphoserine Ref.10 Ref.14 Ref.16
Modified residue661Phosphothreonine Ref.10 Ref.16
Modified residue671Phosphoserine Ref.10 Ref.16

Sequences

Sequence LengthMass (Da)Tools
P40072 [UniParc].

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

FASTA27430,764
        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' 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. expand/collapse author list , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.
Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"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.
[4]"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.
[5]"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.
[6]"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.
[7]"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.
[8]"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.
[9]"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.
[10]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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.
[16]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; THR-66 AND SER-67, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U18916 Genomic DNA. Translation: AAC03214.1.
BK006939 Genomic DNA. Translation: DAA07776.1.
PIRS50619.
RefSeqNP_011041.3. NM_001179006.3.

3D structure databases

ProteinModelPortalP40072.
SMRP40072. Positions 176-261.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36861. 320 interactions.
DIPDIP-1365N.
IntActP40072. 4 interactions.
MINTMINT-396089.
STRING4932.YER116C.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYER116C; YER116C; YER116C.
GeneID856852.
KEGGsce:YER116C.

Organism-specific databases

CYGDYER116c.
SGDS000000918. SLX8.

Phylogenomic databases

eggNOGCOG5574.
OrthoDBEOG7H1K05.

Enzyme and pathway databases

BioCycYEAST:G3O-30280-MONOMER.
UniPathwayUPA00143.

Gene expression databases

GenevestigatorP40072.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamPF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTSM00184. RING. 1 hit.
[Graphical view]
PROSITEPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio983189.
PROP40072.

Entry information

Entry nameSLX8_YEAST
AccessionPrimary (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: April 16, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome V

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways