Reviewed, UniProtKB/Swiss-Prot P32828 (SLX5_YEAST)

Names and origin

Protein names

Recommended name:
    E3 ubiquitin-protein ligase complex SLX5-SLX8 subunit SLX5
    EC=6.3.2.-
Alternative name(s):
    Synthetic lethal of unknown function protein 5
    Hexose metabolism-related protein HEX3

Gene names

Name:	SLX5
Synonyms:	HEX3
Ordered Locus Names:	YDL013W
ORF Names:	D2875

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	619 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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. Along with SIR2, promotes silencing of genes at telomeric or ribosomal DNA (rDNA) loci. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Heterodimer. Interacts with SLX8 and SIR2. Ref.3 Ref.6 Ref.7 Ref.8 Ref.11 Ref.13
Subcellular location	Nucleus › nucleolus.

Ontologies

Keywords
Biological process	DNA damage DNA repair Transcription Transcription regulation Ubl conjugation pathway
Cellular component	Nucleus
Molecular function	Ligase Repressor
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW protein sumoylation Ref.5 Inferred from genetic interaction. Source: SGD protein ubiquitination Ref.6 Ref.8 Inferred from direct assay. Source: SGD regulation of transcription Inferred from electronic annotation. Source: UniProtKB-KW telomere maintenance Inferred from mutant phenotype. Source: SGD transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell ubiquitin ligase complex Ref.8 Inferred from direct assay. Source: SGD
Molecular function	SUMO binding Ref.8 Inferred from direct assay. Source: SGD ligase activity Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
JSN1	P47135	1	EBI-8276,EBI-9422
SLX8	P40072	1	EBI-8276,EBI-22661
SMT3	Q12306	2	EBI-8276,EBI-17490
SSK1	Q07084	1	EBI-8276,EBI-18184

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 619	619	E3 ubiquitin-protein ligase complex SLX5-SLX8 subunit SLX5		PRO_0000083954
Amino acid modifications
	Modified residue	29	1	Phosphoserine Ref.12

Sequences

	Sequence		Length	Mass (Da)
	P32828-1 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: 75846FEA93A65AE9	FASTA	619	71,071
	10 20 30 40 50 60 MHSDTNGRTK SNNSPSDNNP NETVILIDSD KEEDASIREA NLPVRLYPDR RVGRRRDALN 70 80 90 100 110 120 RFVRSDSRSR NSQRTHITAS SERPDFQANN DDITIIREVG RFFGDDGPID PSAHYVDLDQ 130 140 150 160 170 180 EPGSETLETP RTIQVDNTNG YLNDNGNNNE SDDGLTIVEE RTTRPRVTLN LPGGERLEVT 190 200 210 220 230 240 ATTTDIPIRR SFEFQEDLGA SRRQLLRRSA TRARNLFVDR SDENDEDWTD DTHNLPEAIQ 250 260 270 280 290 300 RARRESRMRM SRRIAERQRR VQQQRVSSDE NISTSIRLQS IRERIQSYTP DIRSAFHRAE 310 320 330 340 350 360 SLHEFRSILQ NVAPITLQEC EEELMALFTE FRNQLLQNWA IDRVRNTQEE ALRLHREALE 370 380 390 400 410 420 RQERTAGRVF HRGTLRESIT NYLNFNGEDG FLSRLWSGPA LSDADEERHT QNIIDMIQER 430 440 450 460 470 480 EERERDVVMK NLMNKTRAQQ EEFEARAASL PEGYSASFDT TPKMKLDITK NGKEETIIVT 490 500 510 520 530 540 DDDLAKTLED IPVCCLCGAE LGVGIPDDFT GISQKDRGVS FEGLVSKYKF HCPYQTLARP 550 560 570 580 590 600 SMLDRDLSKR TFIASCGHAF CGRCFARIDN AKKKSKMPKK KLAQLKGSAH PDNYGPKLCP 610 ADSCKKLIRS RGRLKEVYF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Costanzo G., Sternglanz R. Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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: 11139495] [Abstract] Cited for: FUNCTION IN DEGRADATION OF SUMOYLATED PROTEINS, INTERACTION WITH SLX8.
[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: 16325482] [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: 16387868] [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: 18032921] [Abstract] Cited for: UBIQUITIN-PROTEIN LIGASE ACTIVITY, FUNCTION IN STIMULATION OF UBIQUITIN CONJUGASTING ENZYMES, INTERACTION WITH SLX8.
[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: 17669696] [Abstract] Cited for: FUNCTION IN DEGRADATION OF SUMOYLATED PROTEINS, INTERACTION WITH SLX5/HEX3.
[8]	"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: 17848550] [Abstract] Cited for: FUNCTION IN DEGRADATION OF SUMOYLATED PROTEINS, INTERACTION WITH SLX8.
[9]	"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: 17591698] [Abstract] Cited for: FUNCTION IN NEGATIVE REGULATION OF RECOMBINATION.
[10]	"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: 18499666] [Abstract] Cited for: FUNCTION IN DEGRADATION OF SUMOYLATED PROTEINS.
[11]	"Slx5 promotes transcriptional silencing and is required for robust growth in the absence of Sir2." Darst R.P., Garcia S.N., Koch M.R., Pillus L. Mol. Cell. Biol. 28:1361-1372(2008) [PubMed: 18086879] [Abstract] Cited for: FUNCTION IN TRANSCRIPTIONAL SILENCING, INTERACTION WITH SIR2, SUBCELLULAR LOCATION.
[12]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, MASS SPECTROMETRY.
[13]	"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: 18948542] [Abstract] Cited for: FUNCTION IN DEGRADATION OF SUMOYLATED PROTEINS, INTERACTION WITH SLX8, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L07745 Genomic DNA. Translation: AAA34671.1. Z48432 Genomic DNA. Translation: CAA88346.1. Z74061 Genomic DNA. Translation: CAA98570.1.
PIR	S30780.
RefSeq	NP_010271.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:727N.
IntAct	P32828. 16 interactions.
STRING	P32828.
Proteomic databases
PeptideAtlas	P32828.
PRIDE	P32828.
Genome annotation databases
Ensembl	YDL013W; YDL013W; YDL013W; Saccharomyces cerevisiae. [Genome view]
GeneID	851549.
KEGG	sce:YDL013W.
NMPDR	fig|4932.3.peg.1013.
Organism-specific databases
CYGD	YDL013w.
SGD	S000002171. SLX5.
Phylogenomic databases
HOGENOM	P32828.
OMA	GRCFARI
OrthoDB	EOG9CZCZ6
Gene expression databases
ArrayExpress	P32828.
Genevestigator	P32828.
GermOnline	YDL013W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001841. Znf_RING. [Graphical view]
SMART	SM00184. RING. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	968967.

Entry information

Entry name

SLX5_YEAST

Accession

Primary (citable) accession number: P32828

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	November 24, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)