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Protein

Gamma-glutamyltranspeptidase 1

Gene

GGT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

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

Enzyme 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

  • gamma-glutamyltransferase activity Source: UniProtKB
  • glutathione hydrolase activity Source: UniProtKB

GO - Biological processi

  • cellular amino acid metabolic process Source: ProtInc
  • cysteine biosynthetic process Source: UniProtKB
  • glutamate metabolic process Source: UniProtKB
  • glutathione biosynthetic process Source: UniProtKB
  • glutathione catabolic process Source: UniProtKB
  • glutathione metabolic process Source: UniProtKB
  • leukotriene biosynthetic process Source: UniProtKB
  • leukotriene metabolic process Source: Reactome
  • regulation of immune system process Source: UniProtKB
  • regulation of inflammatory response Source: UniProtKB
  • spermatogenesis Source: UniProtKB
  • xenobiotic metabolic process Source: Reactome
  • zymogen activation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Hydrolase, Protease, Transferase

Keywords - Biological processi

Glutathione biosynthesis

Keywords - Ligandi

Sialic 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.
SABIO-RKP19440.
UniPathwayiUPA00204.

Protein family/group databases

MEROPSiT03.006.

Chemistry databases

SwissLipidsiSLP:000001454.

Names & Taxonomyi

Protein namesi
Recommended name:
Gamma-glutamyltranspeptidase 11 Publication (EC:2.3.2.25 Publications)
Short name:
GGT 1
Alternative name(s):
Gamma-glutamyltransferase 1
Glutathione hydrolase 1 (EC:3.4.19.131 Publication)
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

HGNCiHGNC:4250. GGT1.

Subcellular locationi

  • Cell membrane 2 Publications; Single-pass type II membrane protein 2 Publications

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

GO - Cellular componenti

  • anchored component of external side of plasma membrane Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

Glutathionuria (GLUTH)
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAutosomal recessive disease.
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

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 – 380Gamma-glutamyltranspeptidase 1 heavy chainAdd BLAST380
ChainiPRO_0000011059381 – 569Gamma-glutamyltranspeptidase 1 light chainAdd BLAST189

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi50 ↔ 741 Publication
Glycosylationi95N-linked (GlcNAc...)2 Publications1
Glycosylationi120N-linked (GlcNAc...)5 Publications1
Disulfide bondi192 ↔ 1961 Publication
Glycosylationi230N-linked (GlcNAc...)3 Publications1
Glycosylationi266N-linked (GlcNAc...)3 Publications1
Glycosylationi297N-linked (GlcNAc...)1 Publication1
Glycosylationi344N-linked (GlcNAc...)3 Publications1
Glycosylationi511N-linked (GlcNAc...)5 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.

PTM databases

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.
CleanExiHS_GGT1.
ExpressionAtlasiP19440. baseline and differential.
GenevisibleiP19440. HS.

Organism-specific databases

HPAiHPA045635.
HPA047534.

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. 7 interactors.
IntActiP19440. 2 interactors.
MINTiMINT-2801579.
STRINGi9606.ENSP00000248923.

Chemistry databases

BindingDBiP19440.

Structurei

Secondary structure

1569
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi36 – 40Combined sources5
Beta strandi42 – 44Combined sources3
Helixi48 – 59Combined sources12
Helixi64 – 78Combined sources15
Turni79 – 82Combined sources4
Beta strandi87 – 95Combined sources9
Turni96 – 99Combined sources4
Beta strandi100 – 106Combined sources7
Helixi122 – 126Combined sources5
Helixi129 – 131Combined sources3
Helixi137 – 148Combined sources12
Helixi153 – 166Combined sources14
Helixi172 – 180Combined sources9
Helixi182 – 187Combined sources6
Helixi189 – 195Combined sources7
Beta strandi206 – 208Combined sources3
Helixi211 – 223Combined sources13
Helixi226 – 229Combined sources4
Helixi234 – 243Combined sources10
Helixi250 – 255Combined sources6
Beta strandi259 – 263Combined sources5
Beta strandi265 – 269Combined sources5
Beta strandi272 – 276Combined sources5
Helixi283 – 294Combined sources12
Helixi300 – 303Combined sources4
Helixi306 – 327Combined sources22
Turni333 – 335Combined sources3
Helixi339 – 345Combined sources7
Helixi348 – 355Combined sources8
Helixi366 – 369Combined sources4
Beta strandi382 – 387Combined sources6
Beta strandi393 – 399Combined sources7
Turni403 – 406Combined sources4
Beta strandi407 – 409Combined sources3
Turni411 – 413Combined sources3
Helixi420 – 423Combined sources4
Beta strandi427 – 429Combined sources3
Beta strandi432 – 434Combined sources3
Helixi439 – 441Combined sources3
Beta strandi456 – 460Combined sources5
Beta strandi465 – 476Combined sources12
Helixi477 – 489Combined sources13
Helixi495 – 500Combined sources6
Beta strandi508 – 511Combined sources4
Beta strandi513 – 515Combined sources3
Helixi521 – 529Combined sources9
Beta strandi534 – 536Combined sources3
Beta strandi543 – 550Combined sources8
Beta strandi553 – 557Combined sources5
Turni560 – 562Combined sources3

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[»]
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.
OMAiKPFMVIG.
OrthoDBiEOG091G03Y3.
PhylomeDBiP19440.
TreeFamiTF313608.

Family and domain databases

InterProiIPR000101. GGT_peptidase.
IPR029055. Ntn_hydrolases_N.
[Graphical view]
PANTHERiPTHR11686. PTHR11686. 1 hit.
PfamiPF01019. G_glu_transpept. 1 hit.
[Graphical view]
PRINTSiPR01210. GGTRANSPTASE.
SUPFAMiSSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR00066. g_glut_trans. 1 hit.
PROSITEiPS00462. G_GLU_TRANSPEPTIDASE. 1 hit.
[Graphical view]

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

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

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 rs2330837dbSNPEnsembl.1
Natural variantiVAR_01837352K → E.Corresponds to variant rs2330838dbSNPEnsembl.1
Natural variantiVAR_018374177A → V.Corresponds to variant rs3895576dbSNPEnsembl.1
Natural variantiVAR_018372272V → A.6 PublicationsCorresponds to variant rs4049829dbSNPEnsembl.1
Natural variantiVAR_025546419N → D.Corresponds to variant rs17004876dbSNPEnsembl.1
Natural variantiVAR_049181435V → A.Corresponds to variant rs16986465dbSNPEnsembl.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

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[»]
ProteinModelPortaliP19440.
SMRiP19440.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108946. 7 interactors.
IntActiP19440. 2 interactors.
MINTiMINT-2801579.
STRINGi9606.ENSP00000248923.

Chemistry databases

BindingDBiP19440.
ChEMBLiCHEMBL5696.
DrugBankiDB00143. Glutathione.
SwissLipidsiSLP:000001454.

Protein family/group databases

MEROPSiT03.006.

PTM databases

iPTMnetiP19440.
PhosphoSitePlusiP19440.

Polymorphism and mutation databases

BioMutaiGGT1.
DMDMi93140064.

Proteomic databases

EPDiP19440.
MaxQBiP19440.
PaxDbiP19440.
PeptideAtlasiP19440.
PRIDEiP19440.

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.
GeneCardsiGGT1.
H-InvDBHIX0016314.
HGNCiHGNC:4250. GGT1.
HPAiHPA045635.
HPA047534.
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.
OMAiKPFMVIG.
OrthoDBiEOG091G03Y3.
PhylomeDBiP19440.
TreeFamiTF313608.

Enzyme and pathway databases

UniPathwayiUPA00204.
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.
SABIO-RKP19440.

Miscellaneous databases

ChiTaRSiGGT1. human.
GeneWikiiGGT1.
GenomeRNAii2678.
PROiP19440.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000100031.
CleanExiHS_GGT1.
ExpressionAtlasiP19440. baseline and differential.
GenevisibleiP19440. HS.

Family and domain databases

InterProiIPR000101. GGT_peptidase.
IPR029055. Ntn_hydrolases_N.
[Graphical view]
PANTHERiPTHR11686. PTHR11686. 1 hit.
PfamiPF01019. G_glu_transpept. 1 hit.
[Graphical view]
PRINTSiPR01210. GGTRANSPTASE.
SUPFAMiSSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR00066. g_glut_trans. 1 hit.
PROSITEiPS00462. G_GLU_TRANSPEPTIDASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGGT1_HUMAN
AccessioniPrimary (citable) accession number: P19440
Secondary accession number(s): Q08247
, Q14404, Q8TBS1, Q9UMK1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: March 7, 2006
Last modified: November 30, 2016
This is version 188 of the entry and version 2 of the sequence. [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

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.

Keywords - Technical termi

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

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.