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P19440

- GGT1_HUMAN

UniProt

P19440 - GGT1_HUMAN

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Protein

Gamma-glutamyltranspeptidase 1

Gene
GGT1, GGT
Organism
Homo sapiens (Human)
Status
Reviewed - 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.7 Publications

Catalytic activityi

A (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid.8 Publications
Glutathione + H2O = L-cysteinylglycine + L-glutamate.8 Publications
Leukotriene C4 + H2O = leukotriene D4 + L-glutamate.8 Publications

Enzyme regulationi

Activated by autocatalytic cleavage.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei107 – 1071Glutamate
Active sitei381 – 3811Nucleophile1 Publication
Binding sitei399 – 3991Glutamate
Binding sitei420 – 4201Glutamate

GO - Molecular functioni

  1. gamma-glutamyltransferase activity Source: UniProtKB
  2. glutathione hydrolase activity Source: UniProtKB
  3. protein binding Source: UniProtKB

GO - Biological processi

  1. arachidonic acid metabolic process Source: Reactome
  2. cellular amino acid metabolic process Source: ProtInc
  3. cysteine biosynthetic process Source: UniProtKB
  4. glutamate metabolic process Source: UniProtKB
  5. glutathione biosynthetic process Source: UniProtKB
  6. glutathione catabolic process Source: UniProtKB
  7. glutathione derivative biosynthetic process Source: Reactome
  8. glutathione metabolic process Source: UniProtKB
  9. leukotriene biosynthetic process Source: UniProtKB
  10. leukotriene metabolic process Source: Reactome
  11. regulation of immune system process Source: UniProtKB
  12. regulation of inflammatory response Source: UniProtKB
  13. small molecule metabolic process Source: Reactome
  14. spermatogenesis Source: UniProtKB
  15. xenobiotic metabolic process Source: Reactome
  16. 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:HS01957-MONOMER.
BRENDAi2.3.2.2. 2681.
ReactomeiREACT_150420. Synthesis of Leukotrienes (LT) and Eoxins (EX).
REACT_6960. Glutathione synthesis and recycling.
SABIO-RKP19440.
UniPathwayiUPA00204.

Protein family/group databases

MEROPSiT03.006.

Names & Taxonomyi

Protein namesi
Recommended name:
Gamma-glutamyltranspeptidase 1 (EC:2.3.2.2)
Short name:
GGT 1
Alternative name(s):
Gamma-glutamyltransferase 1
Glutathione hydrolase 1 (EC:3.4.19.13)
Leukotriene-C4 hydrolase (EC:3.4.19.14)
CD_antigen: CD224
Cleaved into the following 2 chains:
Gene namesi
Name:GGT1
Synonyms:GGT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:4250. GGT1.

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 44Cytoplasmic Reviewed prediction
Transmembranei5 – 2622Helical; Signal-anchor for type II membrane protein; InferredAdd
BLAST
Topological domaini27 – 569543Extracellular Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. anchored component of external side of plasma membrane Source: UniProtKB
  2. extracellular space Source: UniProt
  3. extracellular vesicular exosome Source: UniProt
  4. integral component of membrane Source: UniProtKB-KW
  5. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

Glutathionuria (GLUTH) [MIM:231950]: Autosomal recessive disease.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi100 – 1001K → N: No effect on activity. 1 Publication
Mutagenesisi102 – 1021E → Q: No effect on activity. 1 Publication
Mutagenesisi107 – 1071R → K: Reduces enzyme activity by 99%. 1 Publication
Mutagenesisi107 – 1071R → Q or H: Abolishes enzyme activity. 1 Publication
Mutagenesisi108 – 1081E → Q: Reduces enzyme activity by 98%. 1 Publication
Mutagenesisi112 – 1121R → Q: No effect on activity. 1 Publication
Mutagenesisi139 – 1391R → Q: No effect on activity. 1 Publication
Mutagenesisi147 – 1471R → Q: No effect on activity. 1 Publication
Mutagenesisi150 – 1501R → Q: No effect on activity. 1 Publication
Mutagenesisi192 – 1921C → W: Loss of autocatalytic cleavage, cell membrane localization and decrease in catalytic activity; when associated with Y-193. 1 Publication
Mutagenesisi193 – 1931E → Y: Loss of autocatalytic cleavage, cell membrane localization and decrease in catalytic activity; when associated with W-192. 1 Publication
Mutagenesisi383 – 3831H → A: Reduces enzyme activity by 66%. 1 Publication
Mutagenesisi385 – 3851S → A: No effect on activity. 1 Publication
Mutagenesisi413 – 4131S → A: No effect on activity. 1 Publication
Mutagenesisi422 – 4221D → A: Reduces enzyme activity by 90%. 1 Publication
Mutagenesisi423 – 4231D → A: Abolishes enzyme activity. Increases KM by over 1000-fold. 1 Publication
Mutagenesisi425 – 4251S → A: No effect on activity. 1 Publication
Mutagenesisi451 – 4511S → A: Reduces enzyme activity by 99%. Abolishes activity; when associated with A-452. 1 Publication
Mutagenesisi452 – 4521S → A: Reduces enzyme activity by 99%. Abolishes activity; when associated with A-451. 1 Publication
Mutagenesisi454 – 4541C → A: No effect on activity. 1 Publication
Mutagenesisi505 – 5051H → A: Reduces enzyme activity by 90%. 1 Publication
Mutagenesisi545 – 5451Q → K: Reduces enzyme activity by 97%. 1 Publication

Organism-specific databases

MIMi231950. phenotype.
Orphaneti33573. Gamma-glutamyl transpeptidase deficiency.
PharmGKBiPA28662.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 380380Gamma-glutamyltranspeptidase 1 heavy chainPRO_0000011058Add
BLAST
Chaini381 – 569189Gamma-glutamyltranspeptidase 1 light chainPRO_0000011059Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi50 ↔ 741 Publication
Glycosylationi95 – 951N-linked (GlcNAc...)2 Publications
Glycosylationi120 – 1201N-linked (GlcNAc...)5 Publications
Disulfide bondi192 ↔ 1961 Publication
Glycosylationi230 – 2301N-linked (GlcNAc...)3 Publications
Glycosylationi266 – 2661N-linked (GlcNAc...)3 Publications
Glycosylationi297 – 2971N-linked (GlcNAc...)1 Publication
Glycosylationi344 – 3441N-linked (GlcNAc...)3 Publications
Glycosylationi511 – 5111N-linked (GlcNAc...)5 Publications

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.6 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

MaxQBiP19440.
PaxDbiP19440.
PRIDEiP19440.

PTM databases

PhosphoSiteiP19440.

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

BgeeiP19440.
CleanExiHS_GGT1.
GenevestigatoriP19440.

Organism-specific databases

HPAiHPA045635.

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. 5 interactions.
IntActiP19440. 2 interactions.
MINTiMINT-2801579.
STRINGi9606.ENSP00000248923.

Structurei

Secondary structure

1
569
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi36 – 405
Beta strandi42 – 443
Helixi48 – 5912
Helixi64 – 7815
Turni79 – 824
Beta strandi87 – 959
Turni96 – 994
Beta strandi100 – 1067
Helixi122 – 1265
Helixi129 – 1313
Helixi137 – 14812
Helixi153 – 16614
Helixi172 – 1809
Helixi182 – 1876
Helixi189 – 1957
Beta strandi206 – 2083
Helixi211 – 22313
Helixi226 – 2294
Helixi234 – 24310
Helixi250 – 2556
Beta strandi259 – 2635
Beta strandi265 – 2695
Beta strandi272 – 2765
Helixi283 – 29412
Helixi300 – 3034
Helixi306 – 32722
Turni333 – 3353
Helixi339 – 3457
Helixi348 – 3558
Helixi366 – 3694
Beta strandi382 – 3876
Beta strandi393 – 3997
Turni403 – 4064
Turni411 – 4133
Helixi420 – 4234
Helixi439 – 4413
Beta strandi456 – 4605
Beta strandi465 – 47612
Helixi477 – 48913
Helixi495 – 5006
Beta strandi508 – 5114
Beta strandi513 – 5153
Helixi521 – 5299
Beta strandi534 – 5363
Beta strandi543 – 5508
Beta strandi553 – 5575
Turni560 – 5623

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GDXX-ray1.67A2-374[»]
B375-569[»]
4GG2X-ray2.21A28-380[»]
B381-569[»]
ProteinModelPortaliP19440.
SMRiP19440. Positions 33-375, 381-569.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni451 – 4522Glutamate binding

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0405.
HOGENOMiHOG000175620.
HOVERGENiHBG005835.
InParanoidiP19440.
KOiK00681.
OMAiTINAREM.
OrthoDBiEOG7V7665.
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. Align

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

MKKKLVVLGL LAVVLVLVIV GLCLWLPSAS KEPDNHVYTR AAVAADAKQC    50
SKIGRDALRD GGSAVDAAIA ALLCVGLMNA HSMGIGGGLF LTIYNSTTRK 100
AEVINAREVA PRLAFATMFN SSEQSQKGGL SVAVPGEIRG YELAHQRHGR 150
LPWARLFQPS IQLARQGFPV GKGLAAALEN KRTVIEQQPV LCEVFCRDRK 200
VLREGERLTL PQLADTYETL AIEGAQAFYN GSLTAQIVKD IQAAGGIVTA 250
EDLNNYRAEL IEHPLNISLG DVVLYMPSAP LSGPVLALIL NILKGYNFSR 300
ESVESPEQKG LTYHRIVEAF RFAYAKRTLL GDPKFVDVTE VVRNMTSEFF 350
AAQLRAQISD DTTHPISYYK PEFYTPDDGG TAHLSVVAED GSAVSATSTI 400
NLYFGSKVRS PVSGILFNNE MDDFSSPSIT NEFGVPPSPA NFIQPGKQPL 450
SSMCPTIMVG QDGQVRMVVG AAGGTQITTA TALAIIYNLW FGYDVKRAVE 500
EPRLHNQLLP NVTTVERNID QAVTAALETR HHHTQIASTF IAVVQAIVRT 550
AGGWAAASDS RKGGEPAGY 569

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 AAA35899.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti51 – 511S → L.
Corresponds to variant rs2330837 [ dbSNP | Ensembl ].
VAR_025545
Natural varianti52 – 521K → E.
Corresponds to variant rs2330838 [ dbSNP | Ensembl ].
VAR_018373
Natural varianti177 – 1771A → V.
Corresponds to variant rs3895576 [ dbSNP | Ensembl ].
VAR_018374
Natural varianti272 – 2721V → A.6 Publications
Corresponds to variant rs4049829 [ dbSNP | Ensembl ].
VAR_018372
Natural varianti419 – 4191N → D.
Corresponds to variant rs17004876 [ dbSNP | Ensembl ].
VAR_025546
Natural varianti435 – 4351V → A.
Corresponds to variant rs16986465 [ dbSNP | Ensembl ].
VAR_049181

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 344344Missing in isoform 3. VSP_008132Add
BLAST
Alternative sequencei341 – 36626VVRNM…TTHPI → ASSGVSAGGPQHDLRVLRCP APGPDL in isoform 2. VSP_001746Add
BLAST
Alternative sequencei367 – 569203Missing in isoform 2. VSP_001747Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 312SK → KS AA sequence 1 Publication
Sequence conflicti47 – 471A → K AA sequence 1 Publication
Sequence conflicti139 – 1391R → E in AAA35889. 1 Publication
Sequence conflicti356 – 3561A → S in AAI28240. 1 Publication
Sequence conflicti361 – 3611D → H in AAI28240. 1 Publication
Sequence conflicti372 – 3721E → D in AAA02886. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]
ENST00000400383; ENSP00000383233; ENSG00000100031. [P19440-1]
ENST00000401885; ENSP00000384381; ENSG00000100031. [P19440-3]
ENST00000403838; ENSP00000384820; ENSG00000100031. [P19440-3]
ENST00000404532; ENSP00000385445; ENSG00000100031. [P19440-3]
ENST00000406383; ENSP00000385975; ENSG00000100031. [P19440-1]
ENST00000425895; ENSP00000387499; ENSG00000100031. [P19440-2]
GeneIDi2678.
KEGGihsa:2678.
UCSCiuc003aan.1. human. [P19440-1]
uc003aay.1. human. [P19440-3]

Polymorphism databases

DMDMi93140064.

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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS42992.1. [P19440-1 ]
PIRi A31253. EKHUEX.
A48987.
A60439.
JS0067.
PS0312.
RefSeqi NP_001275762.1. NM_001288833.1. [P19440-1 ]
NP_038265.2. NM_013421.2. [P19440-1 ]
NP_038347.2. NM_013430.2. [P19440-1 ]
UniGenei Hs.595809.
Hs.645535.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4GDX X-ray 1.67 A 2-374 [» ]
B 375-569 [» ]
4GG2 X-ray 2.21 A 28-380 [» ]
B 381-569 [» ]
ProteinModelPortali P19440.
SMRi P19440. Positions 33-375, 381-569.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108946. 5 interactions.
IntActi P19440. 2 interactions.
MINTi MINT-2801579.
STRINGi 9606.ENSP00000248923.

Chemistry

BindingDBi P19440.
ChEMBLi CHEMBL5696.
DrugBanki DB00143. Glutathione.

Protein family/group databases

MEROPSi T03.006.

PTM databases

PhosphoSitei P19440.

Polymorphism databases

DMDMi 93140064.

Proteomic databases

MaxQBi P19440.
PaxDbi P19440.
PRIDEi P19440.

Protocols and materials databases

DNASUi 2678.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000248923 ; ENSP00000248923 ; ENSG00000100031 . [P19440-1 ]
ENST00000400380 ; ENSP00000383231 ; ENSG00000100031 . [P19440-1 ]
ENST00000400382 ; ENSP00000383232 ; ENSG00000100031 . [P19440-1 ]
ENST00000400383 ; ENSP00000383233 ; ENSG00000100031 . [P19440-1 ]
ENST00000401885 ; ENSP00000384381 ; ENSG00000100031 . [P19440-3 ]
ENST00000403838 ; ENSP00000384820 ; ENSG00000100031 . [P19440-3 ]
ENST00000404532 ; ENSP00000385445 ; ENSG00000100031 . [P19440-3 ]
ENST00000406383 ; ENSP00000385975 ; ENSG00000100031 . [P19440-1 ]
ENST00000425895 ; ENSP00000387499 ; ENSG00000100031 . [P19440-2 ]
GeneIDi 2678.
KEGGi hsa:2678.
UCSCi uc003aan.1. human. [P19440-1 ]
uc003aay.1. human. [P19440-3 ]

Organism-specific databases

CTDi 2678.
GeneCardsi GC22P024980.
H-InvDB HIX0016314.
HGNCi HGNC:4250. GGT1.
HPAi HPA045635.
MIMi 231950. phenotype.
612346. gene.
neXtProti NX_P19440.
Orphaneti 33573. Gamma-glutamyl transpeptidase deficiency.
PharmGKBi PA28662.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0405.
HOGENOMi HOG000175620.
HOVERGENi HBG005835.
InParanoidi P19440.
KOi K00681.
OMAi TINAREM.
OrthoDBi EOG7V7665.
PhylomeDBi P19440.
TreeFami TF313608.

Enzyme and pathway databases

UniPathwayi UPA00204 .
BioCyci MetaCyc:HS01957-MONOMER.
BRENDAi 2.3.2.2. 2681.
Reactomei REACT_150420. Synthesis of Leukotrienes (LT) and Eoxins (EX).
REACT_6960. Glutathione synthesis and recycling.
SABIO-RK P19440.

Miscellaneous databases

ChiTaRSi GGT1. human.
GeneWikii GGT1.
GenomeRNAii 2678.
NextBioi 10574.
PROi P19440.
SOURCEi Search...

Gene expression databases

Bgeei P19440.
CleanExi HS_GGT1.
Genevestigatori P19440.

Family and domain databases

InterProi IPR000101. GGT_peptidase.
IPR029055. Ntn_hydrolases_N.
[Graphical view ]
PANTHERi PTHR11686. PTHR11686. 1 hit.
Pfami PF01019. G_glu_transpept. 1 hit.
[Graphical view ]
PRINTSi PR01210. GGTRANSPTASE.
SUPFAMi SSF56235. SSF56235. 1 hit.
TIGRFAMsi TIGR00066. g_glut_trans. 1 hit.
PROSITEi PS00462. G_GLU_TRANSPEPTIDASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and nucleotide sequence of human gamma-glutamyl transpeptidase."
    Rajpert-De Meyts E., Heisterkamp N., Groffen J.
    Proc. Natl. Acad. Sci. U.S.A. 85:8840-8844(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-272.
    Tissue: Placenta.
  2. "The primary structure of human gamma-glutamyl transpeptidase."
    Sakamuro D., Yamazoe M., Matsuda Y., Kangawa K., Taniguchi N., Matsuo H., Yoshikawa H., Ogasawara N.
    Gene 73:1-9(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 30-58 AND 381-408, VARIANT ALA-272.
    Tissue: Kidney and Liver.
  3. "Regulation of the expression of some genes for enzymes of glutathione metabolism in hepatotoxicity and hepatocarcinogenesis."
    Pitot H.C., Goodspeed D.C., Dunn T.J., Hendrich S., Maronpot R.R., Moran S.
    Toxicol. Appl. Pharmacol. 97:23-34(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-272.
  4. "Human gamma-glutamyl transpeptidase cDNA: comparison of hepatoma and kidney mRNA in the human and rat."
    Goodspeed D.C., Dunn T.J., Miller C.D., Pitot H.C.
    Gene 76:1-9(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-272.
    Tissue: Hepatoblastoma.
  5. "An alternatively processed mRNA specific for gamma-glutamyl transpeptidase in human tissues."
    Pawlak A., Cohen E.H., Octave J.-N., Schweickhardt R., Wu S.-J., Bulle F., Chikhi N., Baik J.-H., Siegrist S., Guellaen G.
    J. Biol. Chem. 265:3256-3262(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT ALA-272.
    Tissue: Liver.
  6. "Gamma-glutamyltransferase: nucleotide sequence of the human pancreatic cDNA. Evidence for a ubiquitous gamma-glutamyltransferase polypeptide in human tissues."
    Courtay C., Oster T., Michelet F., Visvikis A., Diederich M., Wellman M., Siest G.
    Biochem. Pharmacol. 43:2527-2533(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-272.
    Tissue: Pancreas.
  7. "Human lung expresses unique gamma-glutamyl transpeptidase transcripts."
    Wetmore L.A., Gerard C., Drazen J.M.
    Proc. Natl. Acad. Sci. U.S.A. 90:7461-7465(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), LACK OF FUNCTION OF ISOFORM 3.
    Tissue: Lung.
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  9. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
    Tissue: Lung.
  11. "Renal gamma-glutamyl transpeptidases: structural and immunological studies."
    Tate S.S., Khadse V., Wellner D.
    Arch. Biochem. Biophys. 262:397-408(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 30-48 AND 381-403.
    Tissue: Kidney.
  12. "Gamma-glutamyl transpeptidase gene organization and expression: a comparative analysis in rat, mouse, pig and human species."
    Chikhi N., Holic N., Guellaen G., Laperche Y.
    Comp. Biochem. Physiol. 122B:367-380(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING, ALTERNATIVE PROMOTER USAGE.
  13. "Human kidney gamma-glutamyl transpeptidase. Catalytic properties, subunit structure, and localization of the gamma-glutamyl binding site on the light subunit."
    Tate S.S., Ross M.E.
    J. Biol. Chem. 252:6042-6045(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION, SIALIC ACID CONTENT.
    Tissue: Kidney.
  14. "In vitro translation and processing of human hepatoma cell (Hep G2) gamma-glutamyl transpeptidase."
    Tate S.S., Galbraith R.A.
    Biochem. Biophys. Res. Commun. 154:1167-1173(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION.
  15. "Significance of Arg-107 and Glu-108 in the catalytic mechanism of human gamma-glutamyl transpeptidase. Identification by site-directed mutagenesis."
    Ikeda Y., Fujii J., Taniguchi N.
    J. Biol. Chem. 268:3980-3985(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, AUTOCATALYTIC CLEAVAGE, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-100; GLU-102; ARG-107; GLU-108; ARG-112; ARG-139; ARG-147 AND ARG-150.
  16. "Human gamma-glutamyl transpeptidase mutants involving conserved aspartate residues and the unique cysteine residue of the light subunit."
    Ikeda Y., Fujii J., Taniguchi N., Meister A.
    J. Biol. Chem. 270:12471-12475(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-422; ASP-423 AND CYS-454.
  17. "Involvement of Ser-451 and Ser-452 in the catalysis of human gamma-glutamyl transpeptidase."
    Ikeda Y., Fujii J., Anderson M.E., Taniguchi N., Meister A.
    J. Biol. Chem. 270:22223-22228(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF SER-385; SER-413; SER-425; SER-451 AND SER-452.
  18. "Effects of substitutions of the conserved histidine residues in human gamma-glutamyl transpeptidase."
    Ikeda Y., Fujii J., Taniguchi N.
    J. Biochem. 119:1166-1170(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-383 AND HIS-505.
  19. Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-511.
    Tissue: Bile.
  20. "Kinetic characterization and identification of the acylation and glycosylation sites of recombinant human gamma-glutamyltranspeptidase."
    Castonguay R., Halim D., Morin M., Furtos A., Lherbet C., Bonneil E., Thibault P., Keillor J.W.
    Biochemistry 46:12253-12262(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, ACTIVE SITE, GLYCOSYLATION AT ASN-120; ASN-266; ASN-344 AND ASN-511, IDENTIFICATION BY MASS SPECTROMETRY.
  21. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-120; ASN-230 AND ASN-511.
    Tissue: Liver.
  22. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-120.
    Tissue: Leukemic T-cell.
  23. "Analysis of site-specific glycosylation of renal and hepatic gamma-glutamyl transpeptidase from normal human tissue."
    West M.B., Segu Z.M., Feasley C.L., Kang P., Klouckova I., Li C., Novotny M.V., West C.M., Mechref Y., Hanigan M.H.
    J. Biol. Chem. 285:29511-29524(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION AT ASN-95; ASN-120; ASN-230; ASN-266; ASN-297; ASN-344 AND ASN-511.
  24. "Human GGT2 does not autocleave into a functional enzyme: a cautionary tale for interpretation of microarray data on redox signaling."
    West M.B., Wickham S., Parks E.E., Sherry D.M., Hanigan M.H.
    Antioxid. Redox Signal. 19:1877-1888(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, AUTOCATALYTIC CLEAVAGE, ENZYME REGULATION, SUBCELLULAR LOCATION, GLYCOSYLATION, MUTAGENESIS OF CYS-192 AND GLU-193.
  25. "Novel insights into eukaryotic gamma-glutamyl transpeptidase 1 from the crystal structure of the glutamate-bound human enzyme."
    West M.B., Chen Y., Wickham S., Heroux A., Cahill K., Hanigan M.H., Mooers B.H.
    J. Biol. Chem. 288:31902-31913(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) IN COMPLEX WITH GLUTAMATE AND CHLORIDE IONS, FUNCTION, CATALYTIC ACTIVITY, AUTOCATALYTIC CLEAVAGE, SUBUNIT, MUTAGENESIS OF GLN-545, DISULFIDE BONDS, GLYCOSYLATION AT ASN-95; ASN-120; ASN-230; ASN-266; ASN-344 AND ASN-511.

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: September 3, 2014
This is version 166 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

External Data

Dasty 3

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