Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Lactoylglutathione lyase  

UniProtKB / Swiss-Prot ID :  LGUL_HUMAN

Gene Name (Synonyms) : 
GLO1  

Species :  Homo sapiens (Human). 

Subcellular Localization :   

Protein Function :  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. 

Protein Sequence MAEPQPPSGGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDFYTRVLGMTLIQKCDFPIMKFSL...
Predicted Secondary Structure CCCCCCCCCCCCCHHEEEEEECCCHHHHHHHEEEEEEEECCHHHHHHHHHHHCCCEEEECCCCCCCCEEE...
Protein Variant
LocationDescription
19C -> Y (in dbSNP:rs17855424). VAR_031078
111E -> A (in dbSNP:rs4746). VAR_013481
- top -

Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
- top -

Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAEPQP
---CCCCCC
36.86UniProtKB
Link-
35PhosphothreonineLLQQTMLRV
HEEEEEEEE
12.76Phosphositeplus
Link
61S-nitrosocysteineLIQKCDFPI
EEECCCCCC
3.60dbSNO
Link
88Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EKDEKIAWA
CCCCCHHHC
48.10Phosphositeplus
Link
107PhosphothreonineHNWGTEDDE
ECCCCCCCC
28.05Phosphositeplus
Link
107Phosphothreonine.HNWGTEDDE
ECCCCCCCC
28.05UniProtKB
Link
139S-glutathionyl cysteine; alternate.VYSACKRFE
HHHHHHHHH
2.39UniProtKB
Link
140Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YSACKRFEE
HHHHHHHHH
60.89Phosphositeplus
Link
148Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ELGVKFVKK
HCCCEEEEC
42.51Phosphositeplus
Link
148N6-acetyllysineELGVKFVKK
HCCCEEEEC
42.51HPRD
Link
148N6-acetyllysineELGVKFVKK
HCCCEEEEC
42.51Phosphositeplus
Link
148N6-acetyllysine.ELGVKFVKK
HCCCEEEEC
42.51UniProtKB
Link
- top -

Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
LGUL_HUMANin vitroHPRD:00730HPRD11513094
- top -

Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
- top -
Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Posttranslational modification of human glyoxalase 1 indicates redox-dependent regulation.";
Birkenmeier G., Stegemann C., Hoffmann R., Gunther R., Huse K.,Birkemeyer C.;
PLoS ONE 5:E10399-E10399(2010).
Cited for: PROTEIN SEQUENCE OF 13-18 AND 128-135, ENZYME REGULATION,BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY, REMOVAL OF INITIATORMETHIONINE, ACETYLATION AT ALA-2, GLUTATHIONYLATION AT CYS-139, ANDDISULFIDE BONDS.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-148, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Phosphorylation on Thr-106 and NO-modification of glyoxalase Isuppress the TNF-induced transcriptional activity of NF-kappaB.";
de Hemptinne V., Rondas D., Toepoel M., Vancompernolle K.;
Mol. Cell. Biochem. 325:169-178(2009).
Cited for: FUNCTION, PHOSPHORYLATION AT THR-107, AND MUTAGENESIS OF CYS-19;CYS-20; SER-45; SER-69; SER-94; THR-98; THR-102; THR-107 AND CYS-139.
- top -
Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures