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Protein

Glutathione hydrolase 1 proenzyme

Gene

GGT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. Isoform 3 seems to be inactive.6 Publications

Miscellaneous

Cys-454 was thought to bind the gamma-glutamyl moiety, but mutagenesis of this residue had no effect on activity.
Chloride ions bound in the active site cavity may contribute to stabilize the protein fold.

Catalytic activityi

A (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid.5 Publications
Glutathione + H2O = L-cysteinylglycine + L-glutamate.1 Publication
Leukotriene C4 + H2O = leukotriene D4 + L-glutamate.By similarity

Activity regulationi

Activated by autocatalytic cleavage.1 Publication

Pathwayi: glutathione metabolism

This protein is involved in the pathway glutathione metabolism, which is part of Sulfur metabolism.
View all proteins of this organism that are known to be involved in the pathway glutathione metabolism and in Sulfur metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei107Glutamate1 Publication1
Active sitei381Nucleophile1 Publication1
Binding sitei399Glutamate1 Publication1
Binding sitei420Glutamate1 Publication1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAcyltransferase, Hydrolase, Protease, Transferase
Biological processGlutathione biosynthesis
LigandSialic acid

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER66-34394
ReactomeiR-HSA-174403 Glutathione synthesis and recycling
R-HSA-2142691 Synthesis of Leukotrienes (LT) and Eoxins (EX)
R-HSA-5423646 Aflatoxin activation and detoxification
R-HSA-5579022 Defective GGT1 causes Glutathionuria (GLUTH)
R-HSA-9035968 Defective GGT1 causes Glutathionuria (GLUTH)
SABIO-RKiP19440
UniPathwayi
UPA00204

Protein family/group databases

MEROPSiT03.006

Chemistry databases

SwissLipidsiSLP:000001454

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione hydrolase 1 proenzyme (EC:3.4.19.131 Publication)
Alternative name(s):
Gamma-glutamyltransferase 1
Gamma-glutamyltranspeptidase 11 Publication (EC:2.3.2.25 Publications)
Short name:
GGT 1
Leukotriene-C4 hydrolase (EC:3.4.19.14By similarity)
CD_antigen: CD224
Cleaved into the following 2 chains:
Gene namesi
Name:GGT1
Synonyms:GGT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

EuPathDBiHostDB:ENSG00000100031.18
HGNCiHGNC:4250 GGT1
MIMi612346 gene
neXtProtiNX_P19440

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; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 4CytoplasmicSequence analysis4
Transmembranei5 – 26Helical; Signal-anchor for type II membrane proteinCuratedAdd BLAST22
Topological domaini27 – 569ExtracellularSequence analysisAdd BLAST543

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

Glutathionuria (GLUTH)1 Publication
The disease is caused by mutations affecting the gene represented in this entry. A large homozygous deletion that removes several exons of all isoforms of GGT1 has been found in one family affected by glutathionuria.1 Publication
Disease descriptionA very rare, autosomal recessive metabolic disorder characterized by the presence of glutathione in the urine, due to generalized gamma-glutamyl transpeptidase deficiency. Most patients manifest mild to moderate mental retardation, and behavioral disturbance. Seizures, tremor, marfanoid features and strabismus are observed in some patients.
See also OMIM:231950

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi100K → N: No effect on activity. 1 Publication1
Mutagenesisi102E → Q: No effect on activity. 1 Publication1
Mutagenesisi107R → K: Reduces enzyme activity by 99%. 1 Publication1
Mutagenesisi107R → Q or H: Abolishes enzyme activity. 1 Publication1
Mutagenesisi108E → Q: Reduces enzyme activity by 98%. 1 Publication1
Mutagenesisi112R → Q: No effect on activity. 1 Publication1
Mutagenesisi139R → Q: No effect on activity. 1 Publication1
Mutagenesisi147R → Q: No effect on activity. 1 Publication1
Mutagenesisi150R → Q: No effect on activity. 1 Publication1
Mutagenesisi192C → W: Loss of autocatalytic cleavage, cell membrane localization and decrease in catalytic activity; when associated with Y-193. 1 Publication1
Mutagenesisi193E → Y: Loss of autocatalytic cleavage, cell membrane localization and decrease in catalytic activity; when associated with W-192. 1 Publication1
Mutagenesisi383H → A: Reduces enzyme activity by 66%. 1 Publication1
Mutagenesisi385S → A: No effect on activity. 1 Publication1
Mutagenesisi413S → A: No effect on activity. 1 Publication1
Mutagenesisi422D → A: Reduces enzyme activity by 90%. 1 Publication1
Mutagenesisi423D → A: Abolishes enzyme activity. Increases KM by over 1000-fold. 1 Publication1
Mutagenesisi425S → A: No effect on activity. 1 Publication1
Mutagenesisi451S → A: Reduces enzyme activity by 99%. Abolishes activity; when associated with A-452. 1 Publication1
Mutagenesisi452S → A: Reduces enzyme activity by 99%. Abolishes activity; when associated with A-451. 1 Publication1
Mutagenesisi454C → A: No effect on activity. 1 Publication1
Mutagenesisi505H → A: Reduces enzyme activity by 90%. 1 Publication1
Mutagenesisi545Q → K: Reduces enzyme activity by 97%. 1 Publication1

Keywords - Diseasei

Mental retardation

Organism-specific databases

DisGeNETi2678
MalaCardsiGGT1
MIMi231950 phenotype
OpenTargetsiENSG00000100031
Orphaneti33573 Gamma-glutamyl transpeptidase deficiency
PharmGKBiPA28662

Chemistry databases

ChEMBLiCHEMBL5696
DrugBankiDB00143 Glutathione

Polymorphism and mutation databases

BioMutaiGGT1
DMDMi93140064

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000110581 – 380Glutathione hydrolase 1 heavy chainAdd BLAST380
ChainiPRO_0000011059381 – 569Glutathione hydrolase 1 light chainAdd BLAST189

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi50 ↔ 741 Publication
Glycosylationi95N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi120N-linked (GlcNAc...) asparagine5 Publications1
Disulfide bondi192 ↔ 1961 Publication
Glycosylationi230N-linked (GlcNAc...) asparagine3 Publications1
Glycosylationi266N-linked (GlcNAc...) asparagine3 Publications1
Glycosylationi297N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi344N-linked (GlcNAc...) asparagine3 Publications1
Glycosylationi511N-linked (GlcNAc...) asparagine5 Publications1

Post-translational modificationi

N-glycosylated on both chains. Contains hexoses, hexosamines and sialic acid residues. Glycosylation profiles tested in kidney and liver tissues reveal the presence of tissue-specific and site-specific glycan composition, despite the overlap in composition among the N-glycans. A total of 36 glycan compositions, with 40 unique structures are observed. Up to 15 different glycans are observed at a single site, with site-specific variation in glycan composition. The difference in glycosylation profiles in the 2 tissues do not affect the enzyme activity.9 Publications
Cleaved by autocatalysis into a large and a small subunit and the autocatalytic cleavage is essential to the functional activation of the enzyme.

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

EPDiP19440
MaxQBiP19440
PaxDbiP19440
PeptideAtlasiP19440
PRIDEiP19440
ProteomicsDBi53662
53663 [P19440-2]
53664 [P19440-3]

PTM databases

GlyConnecti1261
iPTMnetiP19440
PhosphoSitePlusiP19440

Expressioni

Tissue specificityi

Detected in fetal and adult kidney and liver, adult pancreas, stomach, intestine, placenta and lung. Isoform 3 is lung-specific. There are several other tissue-specific forms that arise from alternative promoter usage but that produce the same protein.

Gene expression databases

BgeeiENSG00000100031 Expressed in 89 organ(s), highest expression level in adult mammalian kidney
CleanExiHS_GGT1
ExpressionAtlasiP19440 baseline and differential
GenevisibleiP19440 HS

Organism-specific databases

HPAiHPA045635
HPA047534
HPA065444

Interactioni

Subunit structurei

Heterodimer composed of the light and heavy chains. The active site is located in the light chain.2 Publications

Protein-protein interaction databases

BioGridi108946, 8 interactors
IntActiP19440, 2 interactors
MINTiP19440
STRINGi9606.ENSP00000248923

Chemistry databases

BindingDBiP19440

Structurei

Secondary structure

1569
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP19440
SMRiP19440
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni451 – 452Glutamate binding2

Sequence similaritiesi

Belongs to the gamma-glutamyltransferase family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2410 Eukaryota
COG0405 LUCA
GeneTreeiENSGT00550000074591
HOGENOMiHOG000175620
HOVERGENiHBG005835
InParanoidiP19440
KOiK18592
OMAiTKNMFLD
OrthoDBiEOG091G03Y3
PhylomeDBiP19440
TreeFamiTF313608

Family and domain databases

InterProiView protein in InterPro
IPR000101 GGT_peptidase
IPR029055 Ntn_hydrolases_N
PANTHERiPTHR11686 PTHR11686, 1 hit
SUPFAMiSSF56235 SSF56235, 1 hit
TIGRFAMsiTIGR00066 g_glut_trans, 1 hit
PROSITEiView protein in PROSITE
PS00462 G_GLU_TRANSPEPTIDASE, 1 hit

Sequences (3+)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative promoter usage and alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 15 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P19440-1) [UniParc]FASTAAdd to basket

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.

« Hide
        10         20         30         40         50
MKKKLVVLGL LAVVLVLVIV GLCLWLPSAS KEPDNHVYTR AAVAADAKQC
60 70 80 90 100
SKIGRDALRD GGSAVDAAIA ALLCVGLMNA HSMGIGGGLF LTIYNSTTRK
110 120 130 140 150
AEVINAREVA PRLAFATMFN SSEQSQKGGL SVAVPGEIRG YELAHQRHGR
160 170 180 190 200
LPWARLFQPS IQLARQGFPV GKGLAAALEN KRTVIEQQPV LCEVFCRDRK
210 220 230 240 250
VLREGERLTL PQLADTYETL AIEGAQAFYN GSLTAQIVKD IQAAGGIVTA
260 270 280 290 300
EDLNNYRAEL IEHPLNISLG DVVLYMPSAP LSGPVLALIL NILKGYNFSR
310 320 330 340 350
ESVESPEQKG LTYHRIVEAF RFAYAKRTLL GDPKFVDVTE VVRNMTSEFF
360 370 380 390 400
AAQLRAQISD DTTHPISYYK PEFYTPDDGG TAHLSVVAED GSAVSATSTI
410 420 430 440 450
NLYFGSKVRS PVSGILFNNE MDDFSSPSIT NEFGVPPSPA NFIQPGKQPL
460 470 480 490 500
SSMCPTIMVG QDGQVRMVVG AAGGTQITTA TALAIIYNLW FGYDVKRAVE
510 520 530 540 550
EPRLHNQLLP NVTTVERNID QAVTAALETR HHHTQIASTF IAVVQAIVRT
560
AGGWAAASDS RKGGEPAGY
Note: Produced by alternative promoter usage.
Length:569
Mass (Da):61,410
Last modified:March 7, 2006 - v2
Checksum:i71AE12485239A69F
GO
Isoform 2 (identifier: P19440-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     341-366: VVRNMTSEFFAAQLRAQISDDTTHPI → ASSGVSAGGPQHDLRVLRCPAPGPDL
     367-569: Missing.

Note: Produced by alternative splicing of isoform 1.
Show »
Length:366
Mass (Da):39,420
Checksum:i726B492DEFA85BE2
GO
Isoform 3 (identifier: P19440-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-344: Missing.

Note: Produced by alternative promoter usage.
Show »
Length:225
Mass (Da):24,080
Checksum:i46765CED537C40C3
GO

Computationally mapped potential isoform sequencesi

There are 15 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E7ETN1E7ETN1_HUMAN
Glutathione hydrolase 1 proenzyme
GGT1
97Annotation score:
C9JGF3C9JGF3_HUMAN
Glutathione hydrolase 1 proenzyme
GGT1
30Annotation score:
B5MC36B5MC36_HUMAN
Glutathione hydrolase 1 proenzyme
GGT1
218Annotation score:
B5MC34B5MC34_HUMAN
Glutathione hydrolase 1 proenzyme
GGT1
252Annotation score:
E7ET76E7ET76_HUMAN
Glutathione hydrolase 1 proenzyme
GGT1
463Annotation score:
E7ETJ6E7ETJ6_HUMAN
Glutathione hydrolase 1 proenzyme
GGT1
127Annotation score:
E7ETR7E7ETR7_HUMAN
Glutathione hydrolase 1 proenzyme
GGT1
174Annotation score:
E7ERN9E7ERN9_HUMAN
Glutathione hydrolase 1 proenzyme
GGT1
80Annotation score:
E7ENJ5E7ENJ5_HUMAN
Glutathione hydrolase 1 proenzyme
GGT1
120Annotation score:
E7EVF8E7EVF8_HUMAN
Glutathione hydrolase 1 proenzyme
GGT1
116Annotation score:
There are more potential isoformsShow all

Sequence cautioni

The sequence AAA35899 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti30 – 31SK → KS AA sequence (PubMed:2896486).Curated2
Sequence conflicti47A → K AA sequence (PubMed:2896486).Curated1
Sequence conflicti139R → E in AAA35889 (PubMed:1968061).Curated1
Sequence conflicti356A → S in AAI28240 (PubMed:15489334).Curated1
Sequence conflicti361D → H in AAI28240 (PubMed:15489334).Curated1
Sequence conflicti372E → D in AAA02886 (PubMed:7689219).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02554551S → L. Corresponds to variant dbSNP:rs2330837Ensembl.1
Natural variantiVAR_01837352K → E. Corresponds to variant dbSNP:rs2330838Ensembl.1
Natural variantiVAR_018374177A → V. Corresponds to variant dbSNP:rs3895576Ensembl.1
Natural variantiVAR_018372272V → A6 PublicationsCorresponds to variant dbSNP:rs4049829Ensembl.1
Natural variantiVAR_025546419N → D. Corresponds to variant dbSNP:rs17004876Ensembl.1
Natural variantiVAR_049181435V → A. Corresponds to variant dbSNP:rs1062459Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0081321 – 344Missing in isoform 3. 2 PublicationsAdd BLAST344
Alternative sequenceiVSP_001746341 – 366VVRNM…TTHPI → ASSGVSAGGPQHDLRVLRCP APGPDL in isoform 2. 1 PublicationAdd BLAST26
Alternative sequenceiVSP_001747367 – 569Missing in isoform 2. 1 PublicationAdd BLAST203

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04131 mRNA Translation: AAA52547.1
M24087 mRNA Translation: AAA35899.1 Different initiation.
M24903 mRNA Translation: AAA52546.1
J05235 mRNA Translation: AAA35889.1
X60069 mRNA Translation: CAA42674.1
L20490 mRNA Translation: AAA02884.1
L20493 mRNA Translation: AAA02886.1
CR456494 mRNA Translation: CAG30380.1
AP000356 Genomic DNA No translation available.
BC025927 mRNA Translation: AAH25927.1
BC069473 mRNA Translation: AAH69473.1
BC069504 mRNA Translation: AAH69504.1
BC128238 mRNA Translation: AAI28239.1
BC128239 mRNA Translation: AAI28240.1
CCDSiCCDS42992.1 [P19440-1]
PIRiA31253 EKHUEX
A48987
A60439
JS0067
PS0312
RefSeqiNP_001275762.1, NM_001288833.1 [P19440-1]
NP_038265.2, NM_013421.2 [P19440-1]
NP_038347.2, NM_013430.2 [P19440-1]
UniGeneiHs.595809
Hs.645535

Genome annotation databases

EnsembliENST00000248923; ENSP00000248923; ENSG00000100031 [P19440-1]
ENST00000400380; ENSP00000383231; ENSG00000100031 [P19440-1]
ENST00000400382; ENSP00000383232; ENSG00000100031 [P19440-1]
ENST00000401885; ENSP00000384381; ENSG00000100031 [P19440-3]
ENST00000403838; ENSP00000384820; ENSG00000100031 [P19440-3]
ENST00000404532; ENSP00000385445; ENSG00000100031 [P19440-3]
ENST00000425895; ENSP00000387499; ENSG00000100031 [P19440-2]
GeneIDi2678
KEGGihsa:2678
UCSCiuc003aan.2 human [P19440-1]

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing, Polymorphism

Similar proteinsi

Cross-referencesi

Web resourcesi

Wikipedia

Gamma-glutamyl transpeptidase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04131 mRNA Translation: AAA52547.1
M24087 mRNA Translation: AAA35899.1 Different initiation.
M24903 mRNA Translation: AAA52546.1
J05235 mRNA Translation: AAA35889.1
X60069 mRNA Translation: CAA42674.1
L20490 mRNA Translation: AAA02884.1
L20493 mRNA Translation: AAA02886.1
CR456494 mRNA Translation: CAG30380.1
AP000356 Genomic DNA No translation available.
BC025927 mRNA Translation: AAH25927.1
BC069473 mRNA Translation: AAH69473.1
BC069504 mRNA Translation: AAH69504.1
BC128238 mRNA Translation: AAI28239.1
BC128239 mRNA Translation: AAI28240.1
CCDSiCCDS42992.1 [P19440-1]
PIRiA31253 EKHUEX
A48987
A60439
JS0067
PS0312
RefSeqiNP_001275762.1, NM_001288833.1 [P19440-1]
NP_038265.2, NM_013421.2 [P19440-1]
NP_038347.2, NM_013430.2 [P19440-1]
UniGeneiHs.595809
Hs.645535

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4GDXX-ray1.67A2-374[»]
B375-569[»]
4GG2X-ray2.21A28-380[»]
B381-569[»]
4Z9OX-ray2.30A28-380[»]
B381-569[»]
4ZBKX-ray2.18A28-380[»]
B381-569[»]
4ZC6X-ray2.10A28-380[»]
B381-569[»]
4ZCGX-ray2.22A28-380[»]
B381-569[»]
5V4QX-ray2.20A28-380[»]
B381-569[»]
ProteinModelPortaliP19440
SMRiP19440
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108946, 8 interactors
IntActiP19440, 2 interactors
MINTiP19440
STRINGi9606.ENSP00000248923

Chemistry databases

BindingDBiP19440
ChEMBLiCHEMBL5696
DrugBankiDB00143 Glutathione
SwissLipidsiSLP:000001454

Protein family/group databases

MEROPSiT03.006

PTM databases

GlyConnecti1261
iPTMnetiP19440
PhosphoSitePlusiP19440

Polymorphism and mutation databases

BioMutaiGGT1
DMDMi93140064

Proteomic databases

EPDiP19440
MaxQBiP19440
PaxDbiP19440
PeptideAtlasiP19440
PRIDEiP19440
ProteomicsDBi53662
53663 [P19440-2]
53664 [P19440-3]

Protocols and materials databases

DNASUi2678
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000248923; ENSP00000248923; ENSG00000100031 [P19440-1]
ENST00000400380; ENSP00000383231; ENSG00000100031 [P19440-1]
ENST00000400382; ENSP00000383232; ENSG00000100031 [P19440-1]
ENST00000401885; ENSP00000384381; ENSG00000100031 [P19440-3]
ENST00000403838; ENSP00000384820; ENSG00000100031 [P19440-3]
ENST00000404532; ENSP00000385445; ENSG00000100031 [P19440-3]
ENST00000425895; ENSP00000387499; ENSG00000100031 [P19440-2]
GeneIDi2678
KEGGihsa:2678
UCSCiuc003aan.2 human [P19440-1]

Organism-specific databases

CTDi2678
DisGeNETi2678
EuPathDBiHostDB:ENSG00000100031.18
GeneCardsiGGT1
H-InvDBiHIX0016314
HGNCiHGNC:4250 GGT1
HPAiHPA045635
HPA047534
HPA065444
MalaCardsiGGT1
MIMi231950 phenotype
612346 gene
neXtProtiNX_P19440
OpenTargetsiENSG00000100031
Orphaneti33573 Gamma-glutamyl transpeptidase deficiency
PharmGKBiPA28662
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2410 Eukaryota
COG0405 LUCA
GeneTreeiENSGT00550000074591
HOGENOMiHOG000175620
HOVERGENiHBG005835
InParanoidiP19440
KOiK18592
OMAiTKNMFLD
OrthoDBiEOG091G03Y3
PhylomeDBiP19440
TreeFamiTF313608

Enzyme and pathway databases

UniPathwayi
UPA00204

BioCyciMetaCyc:MONOMER66-34394
ReactomeiR-HSA-174403 Glutathione synthesis and recycling
R-HSA-2142691 Synthesis of Leukotrienes (LT) and Eoxins (EX)
R-HSA-5423646 Aflatoxin activation and detoxification
R-HSA-5579022 Defective GGT1 causes Glutathionuria (GLUTH)
R-HSA-9035968 Defective GGT1 causes Glutathionuria (GLUTH)
SABIO-RKiP19440

Miscellaneous databases

ChiTaRSiGGT1 human
GeneWikiiGGT1
GenomeRNAii2678
PROiPR:P19440
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000100031 Expressed in 89 organ(s), highest expression level in adult mammalian kidney
CleanExiHS_GGT1
ExpressionAtlasiP19440 baseline and differential
GenevisibleiP19440 HS

Family and domain databases

InterProiView protein in InterPro
IPR000101 GGT_peptidase
IPR029055 Ntn_hydrolases_N
PANTHERiPTHR11686 PTHR11686, 1 hit
SUPFAMiSSF56235 SSF56235, 1 hit
TIGRFAMsiTIGR00066 g_glut_trans, 1 hit
PROSITEiView protein in PROSITE
PS00462 G_GLU_TRANSPEPTIDASE, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiGGT1_HUMAN
AccessioniPrimary (citable) accession number: P19440
Secondary accession number(s): Q08247
, Q14404, Q8TBS1, Q9UMK1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: March 7, 2006
Last modified: November 7, 2018
This is version 204 of the entry and version 2 of the sequence. See complete history.
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.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  7. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  8. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
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