CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006228
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase complex SLX5-SLX8 subunit SLX5 
Protein Synonyms/Alias
 Hexose metabolism-related protein HEX3; Synthetic lethal of unknown function protein 5 
Gene Name
 SLX5 
Gene Synonyms/Alias
 HEX3; YDL013W; D2875 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
430RERDVVMKNLMNKTRubiquitination[1]
Reference
 [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301
Functional Description
 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. 
Sequence Annotation
 MOD_RES 14 14 Phosphoserine.
 MOD_RES 29 29 Phosphoserine.  
Keyword
 Complete proteome; DNA damage; DNA repair; Ligase; Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription; Transcription regulation; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 619 AA 
Protein Sequence
MHSDTNGRTK SNNSPSDNNP NETVILIDSD KEEDASIREA NLPVRLYPDR RVGRRRDALN 60
RFVRSDSRSR NSQRTHITAS SERPDFQANN DDITIIREVG RFFGDDGPID PSAHYVDLDQ 120
EPGSETLETP RTIQVDNTNG YLNDNGNNNE SDDGLTIVEE RTTRPRVTLN LPGGERLEVT 180
ATTTDIPIRR SFEFQEDLGA SRRQLLRRSA TRARNLFVDR SDENDEDWTD DTHNLPEAIQ 240
RARRESRMRM SRRIAERQRR VQQQRVSSDE NISTSIRLQS IRERIQSYTP DIRSAFHRAE 300
SLHEFRSILQ NVAPITLQEC EEELMALFTE FRNQLLQNWA IDRVRNTQEE ALRLHREALE 360
RQERTAGRVF HRGTLRESIT NYLNFNGEDG FLSRLWSGPA LSDADEERHT QNIIDMIQER 420
EERERDVVMK NLMNKTRAQQ EEFEARAASL PEGYSASFDT TPKMKLDITK NGKEETIIVT 480
DDDLAKTLED IPVCCLCGAE LGVGIPDDFT GISQKDRGVS FEGLVSKYKF HCPYQTLARP 540
SMLDRDLSKR TFIASCGHAF CGRCFARIDN AKKKSKMPKK KLAQLKGSAH PDNYGPKLCP 600
ADSCKKLIRS RGRLKEVYF 619 
Gene Ontology
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:SGD.
 GO:0000151; C:ubiquitin ligase complex; IDA:SGD.
 GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
 GO:0032183; F:SUMO binding; IDA:SGD.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
 GO:0016925; P:protein sumoylation; IMP:SGD.
 GO:0016567; P:protein ubiquitination; IDA:SGD.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006974; P:response to DNA damage stimulus; IMP:SGD.
 GO:0000723; P:telomere maintenance; IMP:SGD.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR001841; Znf_RING. 
Pfam
  
SMART
 SM00184; RING 
PROSITE
  
PRINTS