UniProt Accession

 LGUL_HUMAN; Q04760; B2R6P7; B4DDV0; P78375; Q59EL0; Q5TZW3; Q96FC0; Q96J41 

Genbank Protein ID

 D13315; L07837; S83285; AF146651; AB209801; AK293345; AK312662; BT019987; BT019988; AL391415; BC001741; BC011365; BC015934 

Genbank Nucleotide ID

 BAA02572.1; AAA52565.1; AAB49495.1; AAD38008.1; BAD93038.1; BAG56861.1; BAG35544.1; AAV38790.1; AAV38791.1; CAI21586.1; AAH01741.1; AAH11365.1; AAH15934.1 

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

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
44	LRVKDPKKSLDFYTR	ubiquitination	[1]
88	IPKEKDEKIAWALSR	ubiquitination	[2, 3]
140	PDVYSACKRFEELGV	ubiquitination	[2, 3, 4, 5]
148	RFEELGVKFVKKPDD	acetylation	[6, 7, 8, 9]
148	RFEELGVKFVKKPDD	ubiquitination	[1, 2, 3, 5, 9]

Reference

 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [6] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [7] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [8] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [9] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 

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. 

Sequence Annotation

 METAL 34 34 Zinc.
 METAL 100 100 Zinc.
 METAL 127 127 Zinc.
 METAL 173 173 Zinc.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 107 107 Phosphothreonine.
 MOD_RES 139 139 S-glutathionyl cysteine; alternate.
 MOD_RES 148 148 N6-acetyllysine.
 DISULFID 19 20
 DISULFID 61 139 Alternate; alternate.  

Keyword

 3D-structure; Acetylation; Alternative splicing; Complete proteome; Direct protein sequencing; Disulfide bond; Glutathionylation; Lyase; Metal-binding; Phosphoprotein; Polymorphism; Reference proteome; Zinc. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 184 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; TAS:UniProtKB.
 GO:0004462; F:lactoylglutathione lyase activity; IDA:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0005975; P:carbohydrate metabolic process; NAS:ProtInc.
 GO:0006749; P:glutathione metabolic process; IEA:Compara.
 GO:0009438; P:methylglyoxal metabolic process; IEA:Compara.
 GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
 GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IEA:Compara. 

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