Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 201 (16 Oct 2019)
Sequence version 4 (06 Mar 2007)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Lactoylglutathione lyase

Gene

GLO1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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.3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+2 PublicationsNote: Binds 1 zinc ion per subunit. In the homodimer, two zinc ions are bound between subunits.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

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.1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Reduction of GLO1 was carried out by incubation with 20 mM betamercaptoethanol prior to kinetic analysis.
  1. KM=1.3 mM for methylglyoxal/glutathione (native form)1 Publication
  2. KM=0.7 mM for methylglyoxal/glutathione (reduced form)1 Publication
  1. Vmax=0.335 µmol/min/mg enzyme with methylglyoxal/glutathione as substrate (native form)1 Publication
  2. Vmax=0.7 µmol/min/mg enzyme with methylglyoxal/glutathione as substrate (reduced form)1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: methylglyoxal degradation

This protein is involved in step 1 of the subpathway that synthesizes (R)-lactate from methylglyoxal.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Lactoylglutathione lyase (HEL-S-74), Lactoylglutathione lyase (GLO1), Lactoylglutathione lyase (GLO1)
  2. Hydroxyacylglutathione hydrolase, mitochondrial (HAGH)
This subpathway is part of the pathway methylglyoxal degradation, which is itself part of Secondary metabolite metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (R)-lactate from methylglyoxal, the pathway methylglyoxal degradation and in Secondary metabolite metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi34Zinc; shared with dimeric partner3 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei34Substrate; shared with dimeric partner1
Binding sitei38Substrate; shared with dimeric partner1
Metal bindingi100Zinc; shared with dimeric partner3 Publications1
Binding sitei104Substrate; shared with dimeric partner1
Binding sitei123Substrate1
Metal bindingi127Zinc; via tele nitrogen3 Publications1
Binding sitei127Substrate1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei173Proton donor/acceptor2 Publications1
Metal bindingi173Zinc3 Publications1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionLyase
LigandMetal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
4.4.1.5 2681

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-70268 Pyruvate metabolism

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q04760

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00619;UER00675

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:GLO1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 6

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:4323 GLO1

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
138750 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q04760

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi19C → 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. 2 Publications1
Mutagenesisi20C → 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. 2 Publications1
Mutagenesisi34Q → E: Reduces enzyme activity by 99%. 1 Publication1
Mutagenesisi45S → A: No effect on phosphorylation. 1 Publication1
Mutagenesisi61C → A: No effect on NO-mediated modification. 1 Publication1
Mutagenesisi69S → A: No effect on phosphorylation. 1 Publication1
Mutagenesisi94S → A: No effect on phosphorylation. 1 Publication1
Mutagenesisi98T → A: No effect on phosphorylation. 1 Publication1
Mutagenesisi100E → Q: Reduces enzyme activity by over 99%. 1 Publication1
Mutagenesisi102T → A: No effect on phosphorylation. 1 Publication1
Mutagenesisi107T → A: Loss of phosphorylation. 1 Publication1
Mutagenesisi139C → A: Impaired NO-mediated modification. Loss of NO-mediated modification; when associated with A-19 or A-20. 2 Publications1
Mutagenesisi173E → Q: Abolishes enzyme activity. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
2739

Open Targets

More...
OpenTargetsi
ENSG00000124767

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA28724

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
Q04760

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2424

Drug and drug target database

More...
DrugBanki
DB00143 Glutathione
DB00328 Indometacin
DB03345 Mercaptoethanol
DB08179 methyl 4-(2,3-dihydroxy-5-methylphenoxy)-2-hydroxy-6-methylbenzoate
DB03330 S-(N-Hydroxy-N-Iodophenylcarbamoyl)Glutathione
DB03602 S-Benzyl-Glutathione
DB04132 S-Hexylglutathione
DB03130 S-P-Nitrobenzyloxycarbonylglutathione

DrugCentral

More...
DrugCentrali
Q04760

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
GLO1

Domain mapping of disease mutations (DMDM)

More...
DMDMi
134039205

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources1 Publication
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001680762 – 184Lactoylglutathione lyaseAdd BLAST183

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineCombined sources1 Publication1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi19 ↔ 201 Publication
Disulfide bondi61 ↔ 139Alternate1 Publication
Modified residuei88N6-succinyllysineBy similarity1
Modified residuei107Phosphothreonine1 Publication1
Modified residuei139S-glutathionyl cysteine; alternate1 Publication1
Modified residuei148N6-acetyllysine; alternateCombined sources1
Modified residuei148N6-succinyllysine; alternateBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Glutathionylation at Cys-139 inhibits enzyme activity.1 Publication
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.2 Publications
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.

Keywords - PTMi

Acetylation, Disulfide bond, Glutathionylation, Phosphoprotein

Proteomic databases

The CPTAC Assay portal

More...
CPTACi
CPTAC-1416
CPTAC-1417
CPTAC-1418
CPTAC-1419
CPTAC-1420

Encyclopedia of Proteome Dynamics

More...
EPDi
Q04760

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q04760

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...
MassIVEi
Q04760

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q04760

PeptideAtlas

More...
PeptideAtlasi
Q04760

PRoteomics IDEntifications database

More...
PRIDEi
Q04760

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
58281 [Q04760-1]
58282 [Q04760-2]

2D gel databases

USC-OGP 2-DE database

More...
OGPi
Q04760

REPRODUCTION-2DPAGE

More...
REPRODUCTION-2DPAGEi
IPI00220766
Q04760

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q04760

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q04760

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q04760

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000124767 Expressed in 236 organ(s), highest expression level in prostate gland

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q04760 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q04760 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB040541
CAB040542
HPA059791

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

3 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
109001, 50 interactors

Protein interaction database and analysis system

More...
IntActi
Q04760, 7 interactors

Molecular INTeraction database

More...
MINTi
Q04760

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000362463

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
Q04760

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1184
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q04760

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q04760

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini31 – 177VOCPROSITE-ProRule annotationAdd BLAST147

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni157 – 158Substrate binding2

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the glyoxalase I family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IU7X Eukaryota
ENOG4111FDV LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000009312

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q04760

KEGG Orthology (KO)

More...
KOi
K01759

Identification of Orthologs from Complete Genome Data

More...
OMAi
KTAWTFS

Database of Orthologous Groups

More...
OrthoDBi
1513831at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q04760

TreeFam database of animal gene trees

More...
TreeFami
TF105011

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.10.180.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR029068 Glyas_Bleomycin-R_OHBP_Dase
IPR004360 Glyas_Fos-R_dOase_dom
IPR004361 Glyoxalase_1
IPR018146 Glyoxalase_1_CS
IPR037523 VOC

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00903 Glyoxalase, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF54593 SSF54593, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00068 glyox_I, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00934 GLYOXALASE_I_1, 1 hit
PS00935 GLYOXALASE_I_2, 1 hit
PS51819 VOC, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: Q04760-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MAEPQPPSGG LTDEAALSCC SDADPSTKDF LLQQTMLRVK DPKKSLDFYT
60 70 80 90 100
RVLGMTLIQK CDFPIMKFSL YFLAYEDKND IPKEKDEKIA WALSRKATLE
110 120 130 140 150
LTHNWGTEDD ETQSYHNGNS DPRGFGHIGI AVPDVYSACK RFEELGVKFV
160 170 180
KKPDDGKMKG LAFIQDPDGY WIEILNPNKM ATLM
Length:184
Mass (Da):20,778
Last modified:March 6, 2007 - v4
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i46291B7878070028
GO
Isoform 2 (identifier: Q04760-2) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:169
Mass (Da):19,043
Checksum:i24175E1D1C817515
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence BAD93038 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Isoform 1 : Molecular mass is 20687.4 Da from positions 2 - 184. Determined by ESI. Variant Glu-111.1 Publication
Isoform 1 : Molecular mass is 20629.7 Da from positions 2 - 184. Determined by ESI. Variant Ala-111.1 Publication

<p>This subsection of the ‘Sequence’ section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement_in_disease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi

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.

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_03107819C → Y2 PublicationsCorresponds to variant dbSNP:rs17855424Ensembl.1
Natural variantiVAR_013481111E → A5 PublicationsCorresponds to variant dbSNP:rs4746EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_041632105 – 119Missing in isoform 2. 1 PublicationAdd BLAST15

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
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 No translation available.
BC001741 mRNA Translation: AAH01741.1
BC011365 mRNA Translation: AAH11365.1
BC015934 mRNA Translation: AAH15934.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS4837.1 [Q04760-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
A46714
S63603

NCBI Reference Sequences

More...
RefSeqi
NP_006699.2, NM_006708.2 [Q04760-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000373365; ENSP00000362463; ENSG00000124767 [Q04760-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
2739

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:2739

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 No translation available.
BC001741 mRNA Translation: AAH01741.1
BC011365 mRNA Translation: AAH11365.1
BC015934 mRNA Translation: AAH15934.1
CCDSiCCDS4837.1 [Q04760-1]
PIRiA46714
S63603
RefSeqiNP_006699.2, NM_006708.2 [Q04760-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB 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[»]
SMRiQ04760
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi109001, 50 interactors
IntActiQ04760, 7 interactors
MINTiQ04760
STRINGi9606.ENSP00000362463

Chemistry databases

BindingDBiQ04760
ChEMBLiCHEMBL2424
DrugBankiDB00143 Glutathione
DB00328 Indometacin
DB03345 Mercaptoethanol
DB08179 methyl 4-(2,3-dihydroxy-5-methylphenoxy)-2-hydroxy-6-methylbenzoate
DB03330 S-(N-Hydroxy-N-Iodophenylcarbamoyl)Glutathione
DB03602 S-Benzyl-Glutathione
DB04132 S-Hexylglutathione
DB03130 S-P-Nitrobenzyloxycarbonylglutathione
DrugCentraliQ04760

PTM databases

iPTMnetiQ04760
PhosphoSitePlusiQ04760
SwissPalmiQ04760

Polymorphism and mutation databases

BioMutaiGLO1
DMDMi134039205

2D gel databases

OGPiQ04760
REPRODUCTION-2DPAGEiIPI00220766
Q04760

Proteomic databases

CPTACiCPTAC-1416
CPTAC-1417
CPTAC-1418
CPTAC-1419
CPTAC-1420
EPDiQ04760
jPOSTiQ04760
MassIVEiQ04760
PaxDbiQ04760
PeptideAtlasiQ04760
PRIDEiQ04760
ProteomicsDBi58281 [Q04760-1]
58282 [Q04760-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
2739

Genome annotation databases

EnsembliENST00000373365; ENSP00000362463; ENSG00000124767 [Q04760-1]
GeneIDi2739
KEGGihsa:2739

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
2739
DisGeNETi2739

GeneCards: human genes, protein and diseases

More...
GeneCardsi
GLO1
HGNCiHGNC:4323 GLO1
HPAiCAB040541
CAB040542
HPA059791
MIMi138750 gene
neXtProtiNX_Q04760
OpenTargetsiENSG00000124767
PharmGKBiPA28724

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IU7X Eukaryota
ENOG4111FDV LUCA
GeneTreeiENSGT00390000009312
InParanoidiQ04760
KOiK01759
OMAiKTAWTFS
OrthoDBi1513831at2759
PhylomeDBiQ04760
TreeFamiTF105011

Enzyme and pathway databases

UniPathwayiUPA00619;UER00675
BRENDAi4.4.1.5 2681
ReactomeiR-HSA-70268 Pyruvate metabolism
SABIO-RKiQ04760

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
GLO1 human
EvolutionaryTraceiQ04760

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
GLO1
Lactoylglutathione_lyase

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
2739
PharosiQ04760

Protein Ontology

More...
PROi
PR:Q04760

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000124767 Expressed in 236 organ(s), highest expression level in prostate gland
ExpressionAtlasiQ04760 baseline and differential
GenevisibleiQ04760 HS

Family and domain databases

Gene3Di3.10.180.10, 1 hit
InterProiView protein in InterPro
IPR029068 Glyas_Bleomycin-R_OHBP_Dase
IPR004360 Glyas_Fos-R_dOase_dom
IPR004361 Glyoxalase_1
IPR018146 Glyoxalase_1_CS
IPR037523 VOC
PfamiView protein in Pfam
PF00903 Glyoxalase, 1 hit
SUPFAMiSSF54593 SSF54593, 1 hit
TIGRFAMsiTIGR00068 glyox_I, 1 hit
PROSITEiView protein in PROSITE
PS00934 GLYOXALASE_I_1, 1 hit
PS00935 GLYOXALASE_I_2, 1 hit
PS51819 VOC, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiLGUL_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q04760
Secondary accession number(s): B2R6P7
, B4DDV0, P78375, Q59EL0, Q5TZW3, Q96FC0, Q96J41
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: March 6, 2007
Last modified: October 16, 2019
This is version 201 of the entry and version 4 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  7. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again