GLO1
entrez
2739
canonical
uniprot
Q04760
canonical
ensembl
ENSG00000124767
resolver
ensp
ENSP00000362463
resolver
genesymbol
GLO1
resolver
hgnc
HGNC:4323
resolver
uniprot
B2R6P7
resolver
uniprot
B4DDV0
resolver
uniprot
P78375
resolver
uniprot
Q59EL0
resolver
uniprot
Q5TZW3
resolver
uniprot
Q96FC0
resolver
uniprot
Q96J41
resolver
uniprot
X5DNM4
resolver
uniprot_entry
LGUL_HUMAN
resolver
uniprot_entry
X5DNM4_HUMAN
resolver
uniprot_sec
B2R6P7
resolver
uniprot_sec
B4DDV0
resolver
uniprot_sec
P78375
resolver
uniprot_sec
Q59EL0
resolver
uniprot_sec
Q5TZW3
resolver
uniprot_sec
Q96FC0
resolver
uniprot_sec
Q96J41
resolver
activity_regulation
ACTIVITY 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. {ECO:0000269|PubMed:20454679}.
uniprot
proteins
amino_acid_sequence
MAEPQPPSGGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDFYTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDEKIAWALSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNKMATLM
uniprot
proteins
ec_number
4.4.1.5
uniprot
proteins
function
FUNCTION: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione (PubMed:20454679, PubMed:23122816, PubMed:9705294). Involved in the regulation of TNF-induced transcriptional activity of NF-kappa-B (PubMed:19199007). Required for normal osteoclastogenesis (By similarity). {ECO:0000250|UniProtKB:Q9CPU0, ECO:0000269|PubMed:19199007, ECO:0000269|PubMed:20454679, ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9705294}.
uniprot
proteins
mass_dalton
20778
uniprot
proteins
mutagenesis
MUTAGEN 19; /note="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."; /evidence="ECO:0000269|PubMed:17576200, ECO:0000269|PubMed:19199007"; MUTAGEN 20; /note="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."; /evidence="ECO:0000269|PubMed:17576200, ECO:0000269|PubMed:19199007"; MUTAGEN 34; /note="Q->E: Reduces enzyme activity by 99%."; /evidence="ECO:0000269|PubMed:9705294"; MUTAGEN 45; /note="S->A: No effect on phosphorylation."; /evidence="ECO:0000269|PubMed:19199007"; MUTAGEN 61; /note="C->A: No effect on NO-mediated modification."; /evidence="ECO:0000269|PubMed:17576200"; MUTAGEN 69; /note="S->A: No effect on phosphorylation."; /evidence="ECO:0000269|PubMed:19199007"; MUTAGEN 94; /note="S->A: No effect on phosphorylation."; /evidence="ECO:0000269|PubMed:19199007"; MUTAGEN 98; /note="T->A: No effect on phosphorylation."; /evidence="ECO:0000269|PubMed:19199007"; MUTAGEN 100; /note="E->Q: Reduces enzyme activity by over 99%."; /evidence="ECO:0000269|PubMed:9705294"; MUTAGEN 102; /note="T->A: No effect on phosphorylation."; /evidence="ECO:0000269|PubMed:19199007"; MUTAGEN 107; /note="T->A: Loss of phosphorylation."; /evidence="ECO:0000269|PubMed:19199007"; MUTAGEN 139; /note="C->A: Impaired NO-mediated modification. Loss of NO-mediated modification; when associated with A-19 or A-20."; /evidence="ECO:0000269|PubMed:17576200, ECO:0000269|PubMed:19199007"; MUTAGEN 173; /note="E->Q: Abolishes enzyme activity."; /evidence="ECO:0000269|PubMed:9705294
uniprot
proteins
pathway_participation
PATHWAY: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 1/2.
uniprot
proteins
post_translational_modification
PTM: Glutathionylation at Cys-139 inhibits enzyme activity. {ECO:0000269|PubMed:20454679}.; PTM: 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. {ECO:0000269|PubMed:17576200, ECO:0000269|PubMed:19199007}.; PTM: 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. {ECO:0000269|PubMed:19199007}.
uniprot
proteins
protein_family
Glyoxalase I family
uniprot
proteins
pubmed
10521255
uniprot
proteins
pubmed
10564821
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17576200
uniprot
proteins
pubmed
19199007
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
20454679
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23122816
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
7684374
uniprot
proteins
pubmed
8449929
uniprot
proteins
pubmed
8670058
uniprot
proteins
pubmed
9218781
uniprot
proteins
pubmed
9705294
uniprot
proteins
sequence_length
184
uniprot
proteins