Gamma-glutamyltransferase 7

Protein-coding gene in the species Homo sapiens
GGT7
Identifiers
AliasesGGT7, D20S101, GGT4, GGTL3, GGTL5, dJ18C9.2, gamma-glutamyltransferase 7
External IDsOMIM: 612342; MGI: 1913385; HomoloGene: 70866; GeneCards: GGT7; OMA:GGT7 - orthologs
EC number3.4.19.13
Gene location (Human)
Chromosome 20 (human)
Chr.Chromosome 20 (human)[1]
Chromosome 20 (human)
Genomic location for GGT7
Genomic location for GGT7
Band20q11.22Start34,844,720 bp[1]
End34,872,856 bp[1]
Gene location (Mouse)
Chromosome 2 (mouse)
Chr.Chromosome 2 (mouse)[2]
Chromosome 2 (mouse)
Genomic location for GGT7
Genomic location for GGT7
Band2|2 H1Start155,490,379 bp[2]
End155,518,237 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • right hemisphere of cerebellum

  • anterior pituitary

  • apex of heart

  • right frontal lobe

  • right lobe of thyroid gland

  • Brodmann area 9

  • left lobe of thyroid gland

  • gastrocnemius muscle

  • olfactory zone of nasal mucosa

  • gastric mucosa
Top expressed in
  • nasal epithelium

  • olfactory epithelium

  • superior frontal gyrus

  • primary visual cortex

  • cerebellar cortex

  • lateral geniculate nucleus

  • medial dorsal nucleus

  • medial geniculate nucleus

  • pontine nuclei

  • dentate gyrus of hippocampal formation granule cell
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • transferase activity
  • glutathione hydrolase activity
  • acyltransferase activity
  • protein binding
  • hydrolase activity
  • hypoglycin A gamma-glutamyl transpeptidase activity
  • leukotriene C4 gamma-glutamyl transferase activity
  • peptidyltransferase activity
Cellular component
  • integral component of membrane
  • membrane
  • plasma membrane
Biological process
  • glutathione biosynthetic process
  • proteolysis
  • glutathione catabolic process
  • glutathione metabolic process
  • leukotriene D4 biosynthetic process
  • negative regulation of response to oxidative stress
  • protein biosynthesis
  • cellular amino acid metabolic process
  • glutamate metabolic process
  • cysteine biosynthetic process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

2686

207182

Ensembl

ENSG00000131067

ENSMUSG00000027603

UniProt

Q9UJ14

Q99JP7

RefSeq (mRNA)

NM_178026
NM_001351702
NM_178025

NM_144786
NM_001362898
NM_001362900

RefSeq (protein)

NP_821158
NP_001338631
NP_821158.2

NP_659035
NP_001349827
NP_001349829

Location (UCSC)Chr 20: 34.84 – 34.87 MbChr 2: 155.49 – 155.52 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Gamma-glutamyltransferase 7 is an enzyme that in humans is encoded by the GGT7 gene.[5][6][7]

Function

Gamma-glutamyltransferase is a membrane-associated protein involved in both the metabolism of glutathione and in the transpeptidation of amino acids. Changes in the activity of gamma-glutamyltransferase may signal preneoplastic or toxic conditions in the liver or kidney. The protein encoded by this gene is similar in sequence to gamma-glutamyltransferase, but its function is unknown.[7]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000131067 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000027603 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Figlewicz DA, Delattre O, Guellaen G, Krizus A, Thomas G, Zucman J, Rouleau GA (August 1993). "Mapping of human gamma-glutamyl transpeptidase genes on chromosome 22 and other human autosomes". Genomics. 17 (2): 299–305. doi:10.1006/geno.1993.1325. PMID 8104871.
  6. ^ Heisterkamp N, Groffen J, Warburton D, Sneddon TP (May 2008). "The human gamma-glutamyltransferase gene family". Human Genetics. 123 (4): 321–32. doi:10.1007/s00439-008-0487-7. PMID 18357469. S2CID 15916758.
  7. ^ a b "Entrez Gene: GGTL3 gamma-glutamyltransferase-like 3".

Further reading

  • Jikuya H, Takano J, Kikuno R, Hirosawa M, Nagase T, Nomura N, Ohara O (February 2003). "Characterization of long cDNA clones from human adult spleen. II. The complete sequences of 81 cDNA clones". DNA Research. 10 (1): 49–57. doi:10.1093/dnares/10.1.49. PMID 12693554.
  • Llamazares M, Cal S, Quesada V, López-Otín C (April 2003). "Identification and characterization of ADAMTS-20 defines a novel subfamily of metalloproteinases-disintegrins with multiple thrombospondin-1 repeats and a unique GON domain". The Journal of Biological Chemistry. 278 (15): 13382–9. doi:10.1074/jbc.M211900200. PMC 6066313. PMID 12562771.
  • He X, Di Y, Li J, Xie Y, Tang Y, Zhang F, Wei L, Zhang Y, Qin W, Huo K, Li Y, Wan D, Gu J (September 2002). "Molecular cloning and characterization of CT120, a novel membrane-associated gene involved in amino acid transport and glutathione metabolism". Biochemical and Biophysical Research Communications. 297 (3): 528–36. doi:10.1016/S0006-291X(02)02227-1. PMID 12270127.
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