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Q04760 (LGUL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length184 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Required for normal osteoclastogenesis. Ref.13 Ref.17 Ref.19

Catalytic activity

(R)-S-lactoylglutathione = glutathione + methylglyoxal. Ref.17 Ref.19

Cofactor

Binds 1 zinc ion per subunit. In the homodimer, two zinc ions are bound between subunits. Ref.17 Ref.19

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. Ref.17 Ref.19

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.13

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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 184183Lactoylglutathione lyase
PRO_0000168076

Regions

Region157 – 1582Substrate binding

Sites

Active site1731Proton donor/acceptor Ref.17 Ref.18
Metal binding341Zinc; shared with dimeric partner
Metal binding1001Zinc; shared with dimeric partner
Metal binding1271Zinc; via tele nitrogen
Metal binding1731Zinc
Binding site341Substrate; shared with dimeric partner
Binding site381Substrate; shared with dimeric partner
Binding site1041Substrate; shared with dimeric partner
Binding site1231Substrate
Binding site1271Substrate

Amino acid modifications

Modified residue21N-acetylalanine Ref.10 Ref.12
Modified residue881N6-succinyllysine By similarity
Modified residue1071Phosphothreonine Ref.13
Modified residue1391S-glutathionyl cysteine; alternate
Modified residue1481N6-acetyllysine; alternate Ref.14
Modified residue1481N6-succinyllysine; alternate By similarity
Disulfide bond19 ↔ 20 Ref.10
Disulfide bond61 ↔ 139Alternate Ref.10

Natural variations

Alternative sequence105 – 11915Missing in isoform 2.
VSP_041632
Natural variant191C → Y. Ref.6 Ref.9
Corresponds to variant rs17855424 [ dbSNP | Ensembl ].
VAR_031078
Natural variant1111E → A. Ref.1 Ref.2 Ref.4 Ref.6 Ref.9
Corresponds to variant rs4746 [ dbSNP | Ensembl ].
VAR_013481

Experimental info

Mutagenesis191C → 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.13
Mutagenesis201C → 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.13
Mutagenesis341Q → E: Reduces enzyme activity by 99%. Ref.17
Mutagenesis451S → A: No effect on phosphorylation. Ref.13
Mutagenesis611C → A: No effect on NO-mediated modification. Ref.11
Mutagenesis691S → A: No effect on phosphorylation. Ref.13
Mutagenesis941S → A: No effect on phosphorylation. Ref.13
Mutagenesis981T → A: No effect on phosphorylation. Ref.13
Mutagenesis1001E → Q: Reduces enzyme activity by over 99%. Ref.17
Mutagenesis1021T → A: No effect on phosphorylation. Ref.13
Mutagenesis1071T → A: Loss of phosphorylation. Ref.13
Mutagenesis1391C → A: Impaired NO-mediated modification. Loss of NO-mediated modification; when associated with A-19 or A-20. Ref.11 Ref.13
Mutagenesis1731E → Q: Abolishes enzyme activity. Ref.17

Secondary structure

....................................... 184
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 6, 2007. Version 4.
Checksum: 46291B7878070028

FASTA18420,778
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 24175E1D1C817515
Show »

FASTA16919,043

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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.
[14]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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].
[16]"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) IN COMPLEX WITH S-BENZYL-GLUTATHIONE AND ZINC.
[17]"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) IN COMPLEX WITH ZINC AND S-HEXYLGLUTATHIONE, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, ACTIVE SITE, SUBUNIT, MUTAGENESIS OF GLN-34; GLU-100 AND GLU-173.
[18]"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 (1.72 ANGSTROMS) IN COMPLEXES WITH S-(N-HYDROXY-N-IODOPHENYLCARBAMOYL)GLUTATHIONE; S-P-NITROBENZYLOXYCARBONYLGLUTATHIONE AND ZINC, ACTIVE SITE.
[19]"Design and evaluation of azaindole-substituted N-hydroxypyridones as glyoxalase I inhibitors."
Chiba T., Ohwada J., Sakamoto H., Kobayashi T., Fukami T.A., Irie M., Miura T., Ohara K., Koyano H.
Bioorg. Med. Chem. Lett. 22:7486-7489(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS) IN COMPLEX WITH SYNTHETIC INHIBITOR AND ZINC, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR.
+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.
CCDSCCDS4837.1. [Q04760-1]
PIRA46714.
S63603.
RefSeqNP_006699.2. NM_006708.2. [Q04760-1]
UniGeneHs.268849.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BH5X-ray2.20A/B/C/D2-184[»]
1FROX-ray2.20A/B/C/D2-184[»]
1QINX-ray2.00A/B2-184[»]
1QIPX-ray1.72A/B/C/D2-184[»]
3VW9X-ray1.47A/B1-184[»]
3W0TX-ray1.35A/B/C/D1-184[»]
3W0UX-ray1.70A/B1-184[»]
ProteinModelPortalQ04760.
SMRQ04760. Positions 3-184.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109001. 9 interactions.
IntActQ04760. 3 interactions.
STRING9606.ENSP00000362463.

Chemistry

BindingDBQ04760.
ChEMBLCHEMBL2424.
DrugBankDB00143. Glutathione.

PTM databases

PhosphoSiteQ04760.

Polymorphism databases

DMDM134039205.

2D gel databases

OGPQ04760.
REPRODUCTION-2DPAGEIPI00220766.
Q04760.

Proteomic databases

MaxQBQ04760.
PaxDbQ04760.
PRIDEQ04760.

Protocols and materials databases

DNASU2739.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373365; ENSP00000362463; ENSG00000124767. [Q04760-1]
GeneID2739.
KEGGhsa:2739.
UCSCuc003ooc.3. human. [Q04760-1]

Organism-specific databases

CTD2739.
GeneCardsGC06M038643.
HGNCHGNC:4323. GLO1.
HPACAB040541.
CAB040542.
MIM138750. gene.
neXtProtNX_Q04760.
PharmGKBPA28724.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0346.
HOVERGENHBG025852.
InParanoidQ04760.
KOK01759.
OMAWALSRKA.
OrthoDBEOG7XPZ6W.
PhylomeDBQ04760.
TreeFamTF105011.

Enzyme and pathway databases

BRENDA4.4.1.5. 2681.
SABIO-RKQ04760.
UniPathwayUPA00619; UER00675.

Gene expression databases

BgeeQ04760.
CleanExHS_GLO1.
GenevestigatorQ04760.

Family and domain databases

Gene3D3.10.180.10. 1 hit.
InterProIPR029068. Glyas_Bleomycin-R_OHBP_Dase.
IPR004360. Glyas_Fos-R_dOase_dom.
IPR004361. Glyoxalase_1.
IPR018146. Glyoxalase_1_CS.
[Graphical view]
PfamPF00903. Glyoxalase. 1 hit.
[Graphical view]
SUPFAMSSF54593. SSF54593. 1 hit.
TIGRFAMsTIGR00068. glyox_I. 1 hit.
PROSITEPS00934. GLYOXALASE_I_1. 1 hit.
PS00935. GLYOXALASE_I_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ04760.
GeneWikiGLO1.
Lactoylglutathione_lyase.
GenomeRNAi2739.
NextBio10796.
PROQ04760.
SOURCESearch...

Entry information

Entry nameLGUL_HUMAN
AccessionPrimary (citable) accession number: Q04760
Secondary accession number(s): B2R6P7 expand/collapse secondary AC list , B4DDV0, P78375, Q59EL0, Q5TZW3, Q96FC0, Q96J41
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: March 6, 2007
Last modified: July 9, 2014
This is version 154 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM