CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020476
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Lactoylglutathione lyase 
Protein Synonyms/Alias
 Aldoketomutase; Glyoxalase I; Glx I; Ketone-aldehyde mutase; Methylglyoxalase; S-D-lactoylglutathione methylglyoxal lyase 
Gene Name
 Glo1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
44LRIKDPKKSLDFYTRacetylation[1]
60LGLTLLQKLDFPAMKacetylation[1]
60LGLTLLQKLDFPAMKubiquitination[2]
88IPKDKSEKTAWTFSRacetylation[1, 3]
88IPKDKSEKTAWTFSRsuccinylation[3]
88IPKDKSEKTAWTFSRubiquitination[2]
96TAWTFSRKATLELTHubiquitination[2]
140PDVYSACKRFEELGVacetylation[1, 4]
140PDVYSACKRFEELGVubiquitination[2]
148RFEELGVKFVKKPDDacetylation[1, 3, 4, 5]
148RFEELGVKFVKKPDDsuccinylation[3]
148RFEELGVKFVKKPDDubiquitination[2]
151ELGVKFVKKPDDGKMacetylation[1, 4]
152LGVKFVKKPDDGKMKacetylation[1]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [4] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [5] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758
Functional Description
 Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. Involved in the regulation of TNF-induced transcriptional activity of NF- kappa-B (By similarity). 
Sequence Annotation
 METAL 34 34 Zinc (By similarity).
 METAL 100 100 Zinc (By similarity).
 METAL 127 127 Zinc (By similarity).
 METAL 173 173 Zinc (By similarity).
 MOD_RES 2 2 N-acetylalanine (By similarity).
 MOD_RES 107 107 Phosphothreonine (By similarity).
 MOD_RES 139 139 S-glutathionyl cysteine (By similarity).
 MOD_RES 148 148 N6-acetyllysine (By similarity).
 DISULFID 19 20 By similarity.  
Keyword
 3D-structure; Acetylation; Complete proteome; Disulfide bond; Glutathionylation; Lyase; Metal-binding; Phosphoprotein; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 184 AA 
Protein Sequence
MAEPQPASSG LTDETAFSCC SDPDPSTKDF LLQQTMLRIK DPKKSLDFYT RVLGLTLLQK 60
LDFPAMKFSL YFLAYEDKND IPKDKSEKTA WTFSRKATLE LTHNWGTEDD ETQSYHNGNS 120
DPRGFGHIGI AVPDVYSACK RFEELGVKFV KKPDDGKMKG LAFIQDPDGY WIEILNPNKI 180
ATII 184 
Gene Ontology
 GO:0004462; F:lactoylglutathione lyase activity; ISS:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0005975; P:carbohydrate metabolic process; IEA:Compara.
 GO:0006749; P:glutathione metabolic process; IEA:Compara.
 GO:0009438; P:methylglyoxal metabolic process; IEA:Compara.
 GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
 GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:MGI. 
Interpro
 IPR004360; Glyas_Fos-R_dOase_dom.
 IPR004361; Glyoxalase_1.
 IPR018146; Glyoxalase_1_CS. 
Pfam
 PF00903; Glyoxalase 
SMART
  
PROSITE
 PS00934; GLYOXALASE_I_1
 PS00935; GLYOXALASE_I_2 
PRINTS