Q04760 (LGUL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lactoylglutathione lyase
EC=4.4.1.5

Alternative name(s):
Aldoketomutase
Glyoxalase I
Short name=Glx I
Ketone-aldehyde mutase
Methylglyoxalase
S-D-lactoylglutathione methylglyoxal lyase

Gene names

Name:

GLO1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	184 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.12
Catalytic activity	(R)-S-lactoylglutathione = glutathione + methylglyoxal.
Cofactor	Binds 1 zinc ion per subunit.
Enzyme regulation	Regulated by oxidation of Cys-139 in response to the redox state of the cell. Results in the alternative formation of cystine or glutathione-bound cysteine, the latter modification leading to reduced enzyme activity. Ref.10
Pathway	Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 1/2.
Subunit structure	Homodimer.
Post-translational modification	Glutathionylation at Cys-139 inhibits enzyme activity. Phosphorylated at Thr-107 in the presence of CaMK2. However, this is a consensus site for phosphorylation by CK2 so phosphorylation may be mediated by CK2 rather than CaMK2. Phosphorylation is induced by TNF and suppresses the TNF-induced transcriptional activity of NF-kappa-B. Ref.11 Ref.12 Exists in a nitric oxide (NO)-modified form. The exact nature of the modification is unknown, but it suppresses the TNF-induced transcriptional activity of NF-kappa-B.
Polymorphism	Exists in three separable isoforms which originate from two alleles in the genome. These correspond to two homodimers and one heterodimer composed of two subunits showing different electrophoretic properties.
Sequence similarities	Belongs to the glyoxalase I family.
Biophysicochemical properties	Kinetic parameters: Reduction of GLO1 was carried out by incubation with 20 mM betamercaptoethanol prior to kinetic analysis. KM=1.3 mM for methylglyoxal/glutathione (native form) Ref.10 KM=0.7 mM for methylglyoxal/glutathione (reduced form) Vmax=0.335 µmol/min/mg enzyme with methylglyoxal/glutathione as substrate (native form) Vmax=0.7 µmol/min/mg enzyme with methylglyoxal/glutathione as substrate (reduced form)
Mass spectrometry	Isoform 1: Molecular mass is 20687.4 Da from positions 2 - 184. Determined by ESI. Variant Glu-111. Ref.10 Isoform 1: Molecular mass is 20629.7 Da from positions 2 - 184. Determined by ESI. Variant Ala-111. Ref.10
Sequence caution	The sequence BAD93038.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	Metal-binding Zinc
Molecular function	Lyase
PTM	Acetylation Disulfide bond Glutathionylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Non-traceable author statement Ref.1. Source: ProtInc glutathione metabolic process Inferred from electronic annotation. Source: Compara methylglyoxal metabolic process Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from direct assay PubMed 11489834. Source: UniProtKB regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Traceable author statement PubMed 16130169. Source: UniProtKB
Molecular_function	lactoylglutathione lyase activity Inferred from direct assay PubMed 11489834. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q04760-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q04760-2)

The sequence of this isoform differs from the canonical sequence as follows:
     105-119: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.10

Chain

2 – 184

183

Lactoylglutathione lyase

PRO_0000168076

Sites

Metal binding

34

1

Zinc

Metal binding

100

1

Zinc

Metal binding

127

1

Zinc

Metal binding

173

1

Zinc

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.10

Modified residue

107

1

Phosphothreonine Ref.12

Modified residue

139

1

S-glutathionyl cysteine

Modified residue

148

1

N6-acetyllysine Ref.13

Disulfide bond

19 ↔ 20

Ref.10

Disulfide bond

61 ↔ 139

Alternate Ref.10

Natural variations

Alternative sequence

105 – 119

15

Missing in isoform 2.

VSP_041632

Natural variant

19

1

C → Y. Ref.6 Ref.9
Corresponds to variant rs17855424 [ dbSNP | Ensembl ].

VAR_031078

Natural variant

111

1

E → A. Ref.1 Ref.2 Ref.4 Ref.6 Ref.9
Corresponds to variant rs4746 [ dbSNP | Ensembl ].

VAR_013481

Experimental info

Mutagenesis

19

1

C → A: No effect on NO-mediated modification. Impaired NO-mediated modification; when associated with A-20. Loss of NO-mediated modification; when associated with A-139. Ref.11 Ref.12

Mutagenesis

20

1

C → A: No effect on NO-mediated modification. Impaired NO-mediated modification; when associated with A-19. Loss of NO-mediated modification; when associated with A-139. Ref.11 Ref.12

Mutagenesis

45

1

S → A: No effect on phosphorylation. Ref.12

Mutagenesis

61

1

C → A: No effect on NO-mediated modification. Ref.11

Mutagenesis

69

1

S → A: No effect on phosphorylation. Ref.12

Mutagenesis

94

1

S → A: No effect on phosphorylation. Ref.12

Mutagenesis

98

1

T → A: No effect on phosphorylation. Ref.12

Mutagenesis

102

1

T → A: No effect on phosphorylation. Ref.12

Mutagenesis

107

1

T → A: Loss of phosphorylation. Ref.12

Mutagenesis

139

1

C → A: Impaired NO-mediated modification. Loss of NO-mediated modification; when associated with A-19 or A-20. Ref.11 Ref.12

Secondary structure

1

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184

Helix Strand Turn

Details...

Helix

13 – 18

6

Helix

25 – 27

3

Beta strand

31 – 38

8

Helix

42 – 51

10

Beta strand

56 – 63

8

Turn

64 – 67

4

Beta strand

68 – 75

8

Helix

78 – 80

3

Helix

85 – 92

8

Beta strand

96 – 104

9

Helix

107 – 109

3

Beta strand

118 – 122

5

Beta strand

124 – 131

8

Helix

135 – 144

10

Beta strand

149 – 151

3

Beta strand

155 – 158

4

Beta strand

162 – 165

4

Beta strand

171 – 175

5

Helix

177 – 179

3

Helix

181 – 183

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 6, 2007. Version 4. Checksum: 46291B7878070028	FASTA	184	20,778
	10 20 30 40 50 60 MAEPQPPSGG LTDEAALSCC SDADPSTKDF LLQQTMLRVK DPKKSLDFYT RVLGMTLIQK 70 80 90 100 110 120 CDFPIMKFSL YFLAYEDKND IPKEKDEKIA WALSRKATLE LTHNWGTEDD ETQSYHNGNS 130 140 150 160 170 180 DPRGFGHIGI AVPDVYSACK RFEELGVKFV KKPDDGKMKG LAFIQDPDGY WIEILNPNKM ATLM
	Isoform 2 [UniParc]. Checksum: 24175E1D1C817515	FASTA	169	19,043
	10 20 30 40 50 60 MAEPQPPSGG LTDEAALSCC SDADPSTKDF LLQQTMLRVK DPKKSLDFYT RVLGMTLIQK 70 80 90 100 110 120 CDFPIMKFSL YFLAYEDKND IPKEKDEKIA WALSRKATLE LTHNSDPRGF GHIGIAVPDV 130 140 150 160 YSACKRFEEL GVKFVKKPDD GKMKGLAFIQ DPDGYWIEIL NPNKMATLM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human glyoxalase I. cDNA cloning, expression, and sequence similarity to glyoxalase I from Pseudomonas putida." Kim N.-S., Umezawa Y., Ohmura S., Kato S. J. Biol. Chem. 268:11217-11221(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-111.
[2]	"Cloning and characterization of human colon glyoxalase-I." Ranganathan S., Walsh E.S., Godwin A.K., Tew K.D. J. Biol. Chem. 268:5661-5667(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-111. Tissue: Colon.
[3]	"Optimized heterologous expression of the human zinc enzyme glyoxalase I." Ridderstroem M., Mannervik B. Biochem. J. 314:463-467(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]	"Genomic sequence of human glyoxalase-I: analysis of promoter activity and its regulation." Ranganathan S., Ciaccio P.J., Walsh E.S., Tew K.D. Gene 240:149-155(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-111.
[5]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Brain.
[6]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANTS TYR-19 AND ALA-111.
[7]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[8]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS TYR-19 AND ALA-111. Tissue: Brain, Eye and Uterus.
[10]	"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) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 13-18 AND 128-135, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, GLUTATHIONYLATION AT CYS-139, DISULFIDE BONDS. Tissue: Erythrocyte.
[11]	"Tumour necrosis factor induces phosphorylation primarily of the nitric-oxide-responsive form of glyoxalase I." de Hemptinne V., Rondas D., Vandekerckhove J., Vancompernolle K. Biochem. J. 407:121-128(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION OF NITRIC OXIDE-MODIFIED FORM, PHOSPHORYLATION, MUTAGENESIS OF CYS-19; CYS-20; CYS-61 AND CYS-139.
[12]	"Phosphorylation on Thr-106 and NO-modification of glyoxalase I suppress the TNF-induced transcriptional activity of NF-kappaB." de Hemptinne V., Rondas D., Toepoel M., Vancompernolle K. Mol. Cell. Biochem. 325:169-178(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION AT THR-107, MUTAGENESIS OF CYS-19; CYS-20; SER-45; SER-69; SER-94; THR-98; THR-102; THR-107 AND CYS-139.
[13]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-148, MASS SPECTROMETRY.
[14]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]	"Crystal structure of human glyoxalase I -- evidence for gene duplication and 3D domain swapping." Cameron A.D., Olin B., Ridderstroem M., Mannervik B., Jones T.A. EMBO J. 16:3386-3395(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[16]	"Involvement of an active-site Zn2+ ligand in the catalytic mechanism of human glyoxalase I." Ridderstroem M., Cameron A.D., Jones T.A., Mannervik B. J. Biol. Chem. 273:21623-21628(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[17]	"Reaction mechanism of glyoxalase I explored by an X-ray crystallographic analysis of the human enzyme in complex with a transition state analogue." Cameron A.D., Ridderstroem M., Olin B., Kavarana M.J., Creighton D.J., Mannervik B. Biochemistry 38:13480-13490(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D13315 mRNA. Translation: BAA02572.1.
L07837 mRNA. Translation: AAA52565.1.
S83285 mRNA. Translation: AAB49495.1.
AF146651 Genomic DNA. Translation: AAD38008.1.
AB209801 mRNA. Translation: BAD93038.1. Different initiation.
AK293345 mRNA. Translation: BAG56861.1.
AK312662 mRNA. Translation: BAG35544.1.
BT019987 mRNA. Translation: AAV38790.1.
BT019988 mRNA. Translation: AAV38791.1.
AL391415 Genomic DNA. Translation: CAI21586.1.
BC001741 mRNA. Translation: AAH01741.1.
BC011365 mRNA. Translation: AAH11365.1.
BC015934 mRNA. Translation: AAH15934.1.

IPI

IPI00220766.
IPI01021703.

PIR

A46714.
S63603.

RefSeq

NP_006699.2. NM_006708.2.

UniGene

Hs.268849.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BH5	X-ray	2.20	A/B/C/D	2-184	[»]
1FRO	X-ray	2.20	A/B/C/D	2-184	[»]
1QIN	X-ray	2.00	A/B	2-184	[»]
1QIP	X-ray	1.72	A/B/C/D	2-184	[»]
3VW9	X-ray	1.47	A/B	1-184	[»]

ProteinModelPortal

Q04760.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q04760. 3 interactions.

STRING

9606.ENSP00000362463.

PTM databases

PhosphoSite

Q04760.

Polymorphism databases

DMDM

134039205.

2D gel databases

OGP

Q04760.

REPRODUCTION-2DPAGE

IPI00220766.
Q04760.

Proteomic databases

PaxDb

Q04760.

PRIDE

Q04760.

Protocols and materials databases

DNASU

2739.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000373365; ENSP00000362463; ENSG00000124767.

GeneID

2739.

KEGG

hsa:2739.

UCSC

uc003ooc.3. human.

Organism-specific databases

CTD

2739.

GeneCards

GC06M038690.

HGNC

HGNC:4323. GLO1.

HPA

CAB040541.
CAB040542.

MIM

138750. gene.

neXtProt

NX_Q04760.

PharmGKB

PA28724.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0346.

HOVERGEN

HBG025852.

InParanoid

Q04760.

KO

K01759.

OMA

WALSRKA.

OrthoDB

EOG4TQMB3.

PhylomeDB

Q04760.

Enzyme and pathway databases

BRENDA

4.4.1.5. 2681.

SABIO-RK

Q04760.

UniPathway

UPA00619; UER00675.

Gene expression databases

Bgee

Q04760.

CleanEx

HS_GLO1.

Genevestigator

Q04760.

GermOnline

ENSG00000124767. Homo sapiens.

Family and domain databases

InterPro

IPR004360. Glyas_Fos-R_dOase_dom.
IPR004361. Glyoxalase_1.
IPR018146. Glyoxalase_1_CS.
[Graphical view]

Pfam

PF00903. Glyoxalase. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00068. glyox_I. 1 hit.

PROSITE

PS00934. GLYOXALASE_I_1. 1 hit.
PS00935. GLYOXALASE_I_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q04760.

ChEMBL

CHEMBL2424.

DrugBank

DB00143. Glutathione.

EvolutionaryTrace

Q04760.

GenomeRNAi

2739.

NextBio

10796.

SOURCE

Search...

Entry information

Entry name

LGUL_HUMAN

Accession

Primary (citable) accession number: Q04760
Secondary accession number(s): B2R6P7 , B4DDV0, P78375, Q59EL0, Q5TZW3, Q96FC0, Q96J41

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	March 6, 2007
Last modified:	May 1, 2013
This is version 144 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.