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E3 ubiquitin-protein ligase complex SLX5-SLX8 subunit SLX5 (EC 2.3.2.27) (Hexose metabolism-related protein HEX3) (RING-type E3 ubiquitin transferase SLX5) (Synthetic lethal of unknown function protein 5)

 SLX5_YEAST              Reviewed;         619 AA.
P32828; D6VRX6;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1993, sequence version 1.
27-SEP-2017, entry version 142.
RecName: Full=E3 ubiquitin-protein ligase complex SLX5-SLX8 subunit SLX5;
EC=2.3.2.27;
AltName: Full=Hexose metabolism-related protein HEX3;
AltName: Full=RING-type E3 ubiquitin transferase SLX5 {ECO:0000305};
AltName: Full=Synthetic lethal of unknown function protein 5;
Name=SLX5; Synonyms=HEX3; OrderedLocusNames=YDL013W; ORFNames=D2875;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Costanzo G., Sternglanz R.;
Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
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.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
FUNCTION IN DEGRADATION OF SUMOYLATED PROTEINS, AND INTERACTION WITH
SLX8.
PubMed=11139495;
Mullen J.R., Kaliraman V., Ibrahim S.S., Brill S.J.;
"Requirement for three novel protein complexes in the absence of the
Sgs1 DNA helicase in Saccharomyces cerevisiae.";
Genetics 157:103-118(2001).
[5]
FUNCTION IN STABILIZATION OF DNA DAMAGE.
PubMed=16325482; DOI=10.1016/j.dnarep.2005.10.010;
Zhang C., Roberts T.M., Yang J., Desai R., Brown G.W.;
"Suppression of genomic instability by SLX5 and SLX8 in Saccharomyces
cerevisiae.";
DNA Repair 5:336-346(2006).
[6]
FUNCTION IN STABILIZATION OF DNA DAMAGE.
PubMed=16387868; DOI=10.1534/genetics.105.052811;
Wang Z., Jones G.M., Prelich G.;
"Genetic analysis connects SLX5 and SLX8 to the SUMO pathway in
Saccharomyces cerevisiae.";
Genetics 172:1499-1509(2006).
[7]
UBIQUITIN-PROTEIN LIGASE ACTIVITY, FUNCTION IN STIMULATION OF
UBIQUITIN CONJUGASTING ENZYMES, AND INTERACTION WITH SLX8.
PubMed=18032921; DOI=10.4161/cc.6.22.4882;
Ii T., Fung J., Mullen J.R., Brill S.J.;
"The yeast Slx5-Slx8 DNA integrity complex displays ubiquitin ligase
activity.";
Cell Cycle 6:2800-2809(2007).
[8]
FUNCTION IN DEGRADATION OF SUMOYLATED PROTEINS, AND INTERACTION WITH
SLX5/HEX3.
PubMed=17669696; DOI=10.1016/j.dnarep.2007.06.004;
Ii T., Mullen J.R., Slagle C.E., Brill S.J.;
"Stimulation of in vitro sumoylation by Slx5-Slx8: evidence for a
functional interaction with the SUMO pathway.";
DNA Repair 6:1679-1691(2007).
[9]
FUNCTION IN DEGRADATION OF SUMOYLATED PROTEINS, AND INTERACTION WITH
SLX8.
PubMed=17848550; DOI=10.1074/jbc.M706025200;
Xie Y., Kerscher O., Kroetz M.B., McConchie H.F., Sung P.,
Hochstrasser M.;
"The yeast Hex3.Slx8 heterodimer is a ubiquitin ligase stimulated by
substrate sumoylation.";
J. Biol. Chem. 282:34176-34184(2007).
[10]
FUNCTION IN NEGATIVE REGULATION OF RECOMBINATION.
PubMed=17591698; DOI=10.1128/MCB.00787-07;
Burgess R.C., Rahman S., Lisby M., Rothstein R., Zhao X.;
"The Slx5-Slx8 complex affects sumoylation of DNA repair proteins and
negatively regulates recombination.";
Mol. Cell. Biol. 27:6153-6162(2007).
[11]
FUNCTION IN DEGRADATION OF SUMOYLATED PROTEINS.
PubMed=18499666; DOI=10.1074/jbc.M802690200;
Mullen J.R., Brill S.J.;
"Activation of the Slx5-Slx8 ubiquitin ligase by poly-small ubiquitin-
like modifier conjugates.";
J. Biol. Chem. 283:19912-19921(2008).
[12]
FUNCTION IN TRANSCRIPTIONAL SILENCING, INTERACTION WITH SIR2, AND
SUBCELLULAR LOCATION.
PubMed=18086879; DOI=10.1128/MCB.01291-07;
Darst R.P., Garcia S.N., Koch M.R., Pillus L.;
"Slx5 promotes transcriptional silencing and is required for robust
growth in the absence of Sir2.";
Mol. Cell. Biol. 28:1361-1372(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[14]
FUNCTION IN DEGRADATION OF SUMOYLATED PROTEINS, INTERACTION WITH SLX8,
AND SUBCELLULAR LOCATION.
PubMed=18948542; DOI=10.1126/science.1162790;
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.;
"Functional targeting of DNA damage to a nuclear pore-associated SUMO-
dependent ubiquitin ligase.";
Science 322:597-602(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-29, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
-!- FUNCTION: Mediates ubiquitination and subsequent
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. {ECO:0000269|PubMed:11139495,
ECO:0000269|PubMed:16325482, ECO:0000269|PubMed:16387868,
ECO:0000269|PubMed:17591698, ECO:0000269|PubMed:17669696,
ECO:0000269|PubMed:17848550, ECO:0000269|PubMed:18032921,
ECO:0000269|PubMed:18086879, ECO:0000269|PubMed:18499666,
ECO:0000269|PubMed:18948542}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Heterodimer. Interacts with SLX8 and SIR2.
{ECO:0000269|PubMed:11139495, ECO:0000269|PubMed:17669696,
ECO:0000269|PubMed:17848550, ECO:0000269|PubMed:18032921,
ECO:0000269|PubMed:18086879, ECO:0000269|PubMed:18948542}.
-!- INTERACTION:
Q12250:RPN5; NbExp=3; IntAct=EBI-8276, EBI-15935;
P40072:SLX8; NbExp=3; IntAct=EBI-8276, EBI-22661;
Q07084:SSK1; NbExp=2; IntAct=EBI-8276, EBI-18184;
Q12049:THP3; NbExp=2; IntAct=EBI-8276, EBI-34263;
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000269|PubMed:18086879, ECO:0000269|PubMed:18948542}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; L07745; AAA34671.1; -; Genomic_DNA.
EMBL; Z48432; CAA88346.1; -; Genomic_DNA.
EMBL; Z74061; CAA98570.1; -; Genomic_DNA.
EMBL; BK006938; DAA11836.1; -; Genomic_DNA.
PIR; S30780; S30780.
RefSeq; NP_010271.3; NM_001180072.3.
ProteinModelPortal; P32828; -.
BioGrid; 32041; 842.
DIP; DIP-727N; -.
IntAct; P32828; 28.
MINT; MINT-390201; -.
STRING; 4932.YDL013W; -.
iPTMnet; P32828; -.
MaxQB; P32828; -.
PRIDE; P32828; -.
TopDownProteomics; P32828; -.
EnsemblFungi; YDL013W; YDL013W; YDL013W.
GeneID; 851549; -.
KEGG; sce:YDL013W; -.
EuPathDB; FungiDB:YDL013W; -.
SGD; S000002171; SLX5.
HOGENOM; HOG000001024; -.
InParanoid; P32828; -.
OMA; FHCPYQT; -.
OrthoDB; EOG092C1L6A; -.
BioCyc; YEAST:G3O-29443-MONOMER; -.
UniPathway; UPA00143; -.
PRO; PR:P32828; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0000775; C:chromosome, centromeric region; IDA:SGD.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0033768; C:SUMO-targeted ubiquitin ligase complex; IDA:SGD.
GO; GO:0032183; F:SUMO binding; IDA:SGD.
GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:SGD.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0016925; P:protein sumoylation; IMP:SGD.
GO; GO:0016567; P:protein ubiquitination; IDA:SGD.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IMP:SGD.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0000723; P:telomere maintenance; IMP:SGD.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
1: Evidence at protein level;
Complete proteome; DNA damage; DNA repair; Nucleus; Phosphoprotein;
Reference proteome; Repressor; Transcription;
Transcription regulation; Transferase; Ubl conjugation pathway.
CHAIN 1 619 E3 ubiquitin-protein ligase complex SLX5-
SLX8 subunit SLX5.
/FTId=PRO_0000083954.
MOD_RES 14 14 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 29 29 Phosphoserine.
{ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
SEQUENCE 619 AA; 71071 MW; 75846FEA93A65AE9 CRC64;
MHSDTNGRTK SNNSPSDNNP NETVILIDSD KEEDASIREA NLPVRLYPDR RVGRRRDALN
RFVRSDSRSR NSQRTHITAS SERPDFQANN DDITIIREVG RFFGDDGPID PSAHYVDLDQ
EPGSETLETP RTIQVDNTNG YLNDNGNNNE SDDGLTIVEE RTTRPRVTLN LPGGERLEVT
ATTTDIPIRR SFEFQEDLGA SRRQLLRRSA TRARNLFVDR SDENDEDWTD DTHNLPEAIQ
RARRESRMRM SRRIAERQRR VQQQRVSSDE NISTSIRLQS IRERIQSYTP DIRSAFHRAE
SLHEFRSILQ NVAPITLQEC EEELMALFTE FRNQLLQNWA IDRVRNTQEE ALRLHREALE
RQERTAGRVF HRGTLRESIT NYLNFNGEDG FLSRLWSGPA LSDADEERHT QNIIDMIQER
EERERDVVMK NLMNKTRAQQ EEFEARAASL PEGYSASFDT TPKMKLDITK NGKEETIIVT
DDDLAKTLED IPVCCLCGAE LGVGIPDDFT GISQKDRGVS FEGLVSKYKF HCPYQTLARP
SMLDRDLSKR TFIASCGHAF CGRCFARIDN AKKKSKMPKK KLAQLKGSAH PDNYGPKLCP
ADSCKKLIRS RGRLKEVYF


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