GGT6
Identifiers
Aliases	GGT6, gamma-glutamyltransferase 6
External IDs	OMIM: 612341 MGI: 1918772 HomoloGene: 51918 GeneCards: GGT6
EC number	3.4.19.13
Gene location (Human) Chr. Chromosome 17 (human)[1] Band 17p13.2 Start 4,556,927 bp[1] End 4,560,818 bp[1]
Gene location (Mouse) Chr. Chromosome 11 (mouse)[2] Band 11|11 B4 Start 72,326,352 bp[2] End 72,329,226 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in pancreatic ductal cell parotid gland skin of abdomen rectum body of pancreas kidney duodenum minor salivary gland renal medulla vulva Top expressed in lip left colon Paneth cell esophagus jejunum left lobe of liver ileum proximal tubule duodenum skin of abdomen More reference expression data BioGPS n/a
Gene ontology Molecular function transferase activity glutathione hydrolase activity acyltransferase activity hydrolase activity hypoglycin A gamma-glutamyl transpeptidase activity molecular function leukotriene C4 gamma-glutamyl transferase activity Cellular component integral component of membrane extracellular exosome membrane Biological process glutathione biosynthetic process proteolysis glutathione catabolic process glutathione metabolic process leukotriene D4 biosynthetic process biological process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 124975 71522 Ensembl ENSG00000167741 ENSMUSG00000040471 UniProt Q6P531 Q6PDE7 RefSeq (mRNA) NM_153338 NM_001122890 NM_001288702 NM_001288703 NM_001288704 NM_027819 RefSeq (protein) NP_001116362 NP_001275631 NP_001275632 NP_001275633 NP_699169 NP_082095 Location (UCSC) Chr 17: 4.56 – 4.56 Mb Chr 11: 72.33 – 72.33 Mb PubMed search [3] [4]
Wikidata
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Gamma-glutamyltransferase 6 is a protein that in humans is encoded by the GGT6 gene. ^[5]

Function

GGT6 belongs to the gamma-glutamyltransferase (GGT; EC 2.3.2.2) gene family. GGT is a membrane-bound extracellular enzyme that cleaves gamma-glutamyl peptide bonds in glutathione and other peptides and transfers the gamma-glutamyl moiety to acceptors. GGT is also key to glutathione homeostasis because it provides substrates for glutathione synthesis (Heisterkamp et al., 2008 [PubMed 18357469]).

References

Further reading

This article incorporates text from the United States National Library of Medicine, which is in the public domain.