CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007708
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cys-Gly metallodipeptidase DUG1 
Protein Synonyms/Alias
 Deficient in utilization of glutathione protein 1; GSH degradosomal complex subunit DUG1 
Gene Name
 DUG1 
Gene Synonyms/Alias
 YFR044C 
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
16FQKIDSLKPQFFSRLacetylation[1]
16FQKIDSLKPQFFSRLubiquitination[2]
127KLVIDEAKGIMKGRGacetylation[1]
277MVAPLTEKEKALYKDacetylation[1]
340AKTVIPAKVFGKFSIubiquitination[2]
378KSLNSPNKCRTELIHubiquitination[2]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] 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, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301] 
Functional Description
 Catalytic component of the GSH degradosomal complex involved in the degradation of glutathione (GSH) and other peptides containing a gamma-glu-X bond. Functions also in a DUG2- DUG3-independent manner as a dipeptidase with high specificity for Cys-Gly and no activity toward tri- or tetrapeptides. 
Sequence Annotation
 ACT_SITE 104 104 By similarity.
 ACT_SITE 171 171 Proton acceptor (By similarity).
 METAL 102 102 Zinc 2 (By similarity).
 METAL 137 137 Zinc 1 (By similarity).
 METAL 137 137 Zinc 2 (By similarity).
 METAL 172 172 Zinc 1 (By similarity).
 METAL 200 200 Zinc 2 (By similarity).
 METAL 450 450 Zinc 1 (By similarity).
 MOD_RES 451 451 Phosphoserine.  
Keyword
 Complete proteome; Cytoplasm; Dipeptidase; Hydrolase; Manganese; Metal-binding; Metalloprotease; Phosphoprotein; Protease; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 481 AA 
Protein Sequence
MSHSLTSVFQ KIDSLKPQFF SRLTKAIQIP AVSSDESLRS KVFDKAKFIS EQLSQSGFHD 60
IKMVDLGIQP PPISTPNLSL PPVILSRFGS DPSKKTVLVY GHYDVQPAQL EDGWDTEPFK 120
LVIDEAKGIM KGRGVTDDTG PLLSWINVVD AFKASGQEFP VNLVTCFEGM EESGSLKLDE 180
LIKKEANGYF KGVDAVCISD NYWLGTKKPV LTYGLRGCNY YQTIIEGPSA DLHSGIFGGV 240
VAEPMIDLMQ VLGSLVDSKG KILIDGIDEM VAPLTEKEKA LYKDIEFSVE ELNAATGSKT 300
SLYDKKEDIL MHRWRYPSLS IHGVEGAFSA QGAKTVIPAK VFGKFSIRTV PDMDSEKLTS 360
LVQKHCDAKF KSLNSPNKCR TELIHDGAYW VSDPFNAQFT AAKKATKLVY GVDPDFTREG 420
GSIPITLTFQ DALNTSVLLL PMGRGDDGAH SINEKLDISN FVGGMKTMAA YLQYYSESPE 480
N 481 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:SGD.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0070573; F:metallodipeptidase activity; IMP:SGD.
 GO:0008242; F:omega peptidase activity; IGI:SGD.
 GO:0034701; F:tripeptidase activity; IEA:InterPro.
 GO:0006751; P:glutathione catabolic process; IMP:SGD.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 
Interpro
 IPR017153; GSH_degradosome_DUG1.
 IPR002933; Peptidase_M20.
 IPR011650; Peptidase_M20_dimer. 
Pfam
 PF07687; M20_dimer
 PF01546; Peptidase_M20 
SMART
  
PROSITE
 PS00758; ARGE_DAPE_CPG2_1
 PS00759; ARGE_DAPE_CPG2_2 
PRINTS