Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P19440 (GGT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Gamma-glutamyltranspeptidase 1

Short name=GGT 1
EC=2.3.2.2
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
Gene names
Name:GGT1
Synonyms:GGT
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length569 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7 Ref.15 Ref.16 Ref.17 Ref.18 Ref.23 Ref.25

Catalytic activity

A (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid. Ref.15 Ref.16 Ref.17 Ref.18 Ref.20 Ref.23 Ref.24 Ref.25

Glutathione + H2O = L-cysteinylglycine + L-glutamate. Ref.15 Ref.16 Ref.17 Ref.18 Ref.20 Ref.23 Ref.24 Ref.25

Leukotriene C4 + H2O = leukotriene D4 + L-glutamate. Ref.15 Ref.16 Ref.17 Ref.18 Ref.20 Ref.23 Ref.24 Ref.25

Enzyme regulation

Activated by autocatalytic cleavage. Ref.24

Pathway

Sulfur metabolism; glutathione metabolism.

Subunit structure

Heterodimer composed of the light and heavy chains. The active site is located in the light chain. Ref.15 Ref.25

Subcellular location

Cell membrane; Single-pass type II membrane protein Ref.15 Ref.24.

Tissue specificity

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.

Post-translational modification

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. Ref.13 Ref.14 Ref.20 Ref.23 Ref.24 Ref.25

Cleaved by autocatalysis into a large and a small subunit and the autocatalytic cleavage is essential to the functional activation of the enzyme.

Involvement in disease

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

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.

Sequence similarities

Belongs to the gamma-glutamyltransferase family.

Sequence caution

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

Ontologies

Keywords
   Biological processGlutathione biosynthesis
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative promoter usage
Alternative splicing
Polymorphism
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   LigandSialic acid
   Molecular functionAcyltransferase
Hydrolase
Protease
Transferase
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processarachidonic acid metabolic process

Traceable author statement. Source: Reactome

cellular amino acid metabolic process

Traceable author statement Ref.1. Source: ProtInc

cysteine biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

glutamate metabolic process

Inferred from direct assay Ref.25. Source: UniProtKB

glutathione biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

glutathione catabolic process

Inferred from direct assay Ref.20. Source: UniProtKB

glutathione derivative biosynthetic process

Traceable author statement. Source: Reactome

glutathione metabolic process

Traceable author statement PubMed 18357469. Source: UniProtKB

leukotriene biosynthetic process

Inferred from mutant phenotype PubMed 14754911. Source: UniProtKB

leukotriene metabolic process

Traceable author statement. Source: Reactome

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of immune system process

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of inflammatory response

Inferred from sequence or structural similarity. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

spermatogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

xenobiotic metabolic process

Traceable author statement. Source: Reactome

zymogen activation

Inferred from direct assay Ref.24. Source: UniProtKB

   Cellular_componentanchored component of external side of plasma membrane

Traceable author statement PubMed 18357469. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from direct assay Ref.24. Source: UniProtKB

   Molecular_functiongamma-glutamyltransferase activity

Inferred from direct assay Ref.23Ref.24Ref.25. Source: UniProtKB

glutathione hydrolase activity

Inferred from direct assay Ref.24. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]
Isoform 1 (identifier: P19440-1)

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.
Note: Produced by alternative promoter usage.
Isoform 2 (identifier: P19440-2)

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.
Isoform 3 (identifier: P19440-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-344: Missing.
Note: Produced by alternative promoter usage.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 380380Gamma-glutamyltranspeptidase 1 heavy chain
PRO_0000011058
Chain381 – 569189Gamma-glutamyltranspeptidase 1 light chain
PRO_0000011059

Regions

Topological domain1 – 44Cytoplasmic Potential
Transmembrane5 – 2622Helical; Signal-anchor for type II membrane protein; Probable
Topological domain27 – 569543Extracellular Potential
Region451 – 4522Glutamate binding

Sites

Active site3811Nucleophile Ref.20
Binding site1071Glutamate
Binding site3991Glutamate
Binding site4201Glutamate

Amino acid modifications

Glycosylation951N-linked (GlcNAc...) Ref.23 Ref.25
Glycosylation1201N-linked (GlcNAc...) Ref.20 Ref.21 Ref.22 Ref.23 Ref.25
Glycosylation2301N-linked (GlcNAc...) Ref.21 Ref.23 Ref.25
Glycosylation2661N-linked (GlcNAc...) Ref.20 Ref.23 Ref.25
Glycosylation2971N-linked (GlcNAc...) Ref.23
Glycosylation3441N-linked (GlcNAc...) Ref.20 Ref.23 Ref.25
Glycosylation5111N-linked (GlcNAc...) Ref.19 Ref.20 Ref.21 Ref.23 Ref.25
Disulfide bond50 ↔ 74 Ref.25
Disulfide bond192 ↔ 196 Ref.25

Natural variations

Alternative sequence1 – 344344Missing in isoform 3.
VSP_008132
Alternative sequence341 – 36626VVRNM…TTHPI → ASSGVSAGGPQHDLRVLRCP APGPDL in isoform 2.
VSP_001746
Alternative sequence367 – 569203Missing in isoform 2.
VSP_001747
Natural variant511S → L.
Corresponds to variant rs2330837 [ dbSNP | Ensembl ].
VAR_025545
Natural variant521K → E.
Corresponds to variant rs2330838 [ dbSNP | Ensembl ].
VAR_018373
Natural variant1771A → V.
Corresponds to variant rs3895576 [ dbSNP | Ensembl ].
VAR_018374
Natural variant2721V → A. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6
Corresponds to variant rs4049829 [ dbSNP | Ensembl ].
VAR_018372
Natural variant4191N → D.
Corresponds to variant rs17004876 [ dbSNP | Ensembl ].
VAR_025546
Natural variant4351V → A.
Corresponds to variant rs16986465 [ dbSNP | Ensembl ].
VAR_049181

Experimental info

Mutagenesis1001K → N: No effect on activity. Ref.15
Mutagenesis1021E → Q: No effect on activity. Ref.15
Mutagenesis1071R → K: Reduces enzyme activity by 99%. Ref.15
Mutagenesis1071R → Q or H: Abolishes enzyme activity. Ref.15
Mutagenesis1081E → Q: Reduces enzyme activity by 98%. Ref.15
Mutagenesis1121R → Q: No effect on activity. Ref.15
Mutagenesis1391R → Q: No effect on activity. Ref.15
Mutagenesis1471R → Q: No effect on activity. Ref.15
Mutagenesis1501R → Q: No effect on activity. Ref.15
Mutagenesis1921C → W: Loss of autocatalytic cleavage, cell membrane localization and decrease in catalytic activity; when associated with Y-193. Ref.24
Mutagenesis1931E → Y: Loss of autocatalytic cleavage, cell membrane localization and decrease in catalytic activity; when associated with W-192. Ref.24
Mutagenesis3831H → A: Reduces enzyme activity by 66%. Ref.18
Mutagenesis3851S → A: No effect on activity. Ref.17
Mutagenesis4131S → A: No effect on activity. Ref.17
Mutagenesis4221D → A: Reduces enzyme activity by 90%. Ref.16
Mutagenesis4231D → A: Abolishes enzyme activity. Increases KM by over 1000-fold. Ref.16
Mutagenesis4251S → A: No effect on activity. Ref.17
Mutagenesis4511S → A: Reduces enzyme activity by 99%. Abolishes activity; when associated with A-452. Ref.17
Mutagenesis4521S → A: Reduces enzyme activity by 99%. Abolishes activity; when associated with A-451. Ref.17
Mutagenesis4541C → A: No effect on activity. Ref.16
Mutagenesis5051H → A: Reduces enzyme activity by 90%. Ref.18
Mutagenesis5451Q → K: Reduces enzyme activity by 97%. Ref.25
Sequence conflict30 – 312SK → KS AA sequence Ref.11
Sequence conflict471A → K AA sequence Ref.11
Sequence conflict1391R → E in AAA35889. Ref.5
Sequence conflict3561A → S in AAI28240. Ref.10
Sequence conflict3611D → H in AAI28240. Ref.10
Sequence conflict3721E → D in AAA02886. Ref.7

Secondary structure

........................................................................................... 569
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 7, 2006. Version 2.
Checksum: 71AE12485239A69F

FASTA56961,410
        10         20         30         40         50         60 
MKKKLVVLGL LAVVLVLVIV GLCLWLPSAS KEPDNHVYTR AAVAADAKQC SKIGRDALRD 

        70         80         90        100        110        120 
GGSAVDAAIA ALLCVGLMNA HSMGIGGGLF LTIYNSTTRK AEVINAREVA PRLAFATMFN 

       130        140        150        160        170        180 
SSEQSQKGGL SVAVPGEIRG YELAHQRHGR LPWARLFQPS IQLARQGFPV GKGLAAALEN 

       190        200        210        220        230        240 
KRTVIEQQPV LCEVFCRDRK VLREGERLTL PQLADTYETL AIEGAQAFYN GSLTAQIVKD 

       250        260        270        280        290        300 
IQAAGGIVTA EDLNNYRAEL IEHPLNISLG DVVLYMPSAP LSGPVLALIL NILKGYNFSR 

       310        320        330        340        350        360 
ESVESPEQKG LTYHRIVEAF RFAYAKRTLL GDPKFVDVTE VVRNMTSEFF AAQLRAQISD 

       370        380        390        400        410        420 
DTTHPISYYK PEFYTPDDGG TAHLSVVAED GSAVSATSTI NLYFGSKVRS PVSGILFNNE 

       430        440        450        460        470        480 
MDDFSSPSIT NEFGVPPSPA NFIQPGKQPL SSMCPTIMVG QDGQVRMVVG AAGGTQITTA 

       490        500        510        520        530        540 
TALAIIYNLW FGYDVKRAVE EPRLHNQLLP NVTTVERNID QAVTAALETR HHHTQIASTF 

       550        560 
IAVVQAIVRT AGGWAAASDS RKGGEPAGY 

« Hide

Isoform 2 [UniParc].

Checksum: 726B492DEFA85BE2
Show »

FASTA36639,420
Isoform 3 [UniParc].

Checksum: 46765CED537C40C3
Show »

FASTA22524,080

References

« Hide 'large scale' references
[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]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"A proteomic analysis of human bile."
Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.
Mol. Cell. Proteomics 3:715-728(2004) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Wikipedia

Gamma-glutamyl transpeptidase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIREKHUEX. A31253.
A48987.
A60439.
JS0067.
PS0312.
RefSeqNP_001275762.1. NM_001288833.1.
NP_038265.2. NM_013421.2.
NP_038347.2. NM_013430.2.
UniGeneHs.595809.
Hs.645535.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4GDXX-ray1.67A2-374[»]
B375-569[»]
4GG2X-ray2.21A28-380[»]
B381-569[»]
ProteinModelPortalP19440.
SMRP19440. Positions 33-375, 381-569.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108946. 5 interactions.
IntActP19440. 2 interactions.
MINTMINT-2801579.
STRING9606.ENSP00000248923.

Chemistry

BindingDBP19440.
ChEMBLCHEMBL5696.
DrugBankDB00143. Glutathione.

Protein family/group databases

MEROPST03.006.

PTM databases

PhosphoSiteP19440.

Polymorphism databases

DMDM93140064.

Proteomic databases

PaxDbP19440.
PRIDEP19440.

Protocols and materials databases

DNASU2678.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000248923; 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]
GeneID2678.
KEGGhsa:2678.
UCSCuc003aan.1. human. [P19440-1]
uc003aay.1. human. [P19440-3]

Organism-specific databases

CTD2678.
GeneCardsGC22P024980.
H-InvDBHIX0016314.
HGNCHGNC:4250. GGT1.
HPAHPA045635.
MIM231950. phenotype.
612346. gene.
neXtProtNX_P19440.
Orphanet33573. Gamma-glutamyl transpeptidase deficiency.
PharmGKBPA28662.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0405.
HOGENOMHOG000175620.
HOVERGENHBG005835.
InParanoidP19440.
KOK00681.
OMAFMLVHLA.
OrthoDBEOG7V7665.
PhylomeDBP19440.
TreeFamTF313608.

Enzyme and pathway databases

BioCycMetaCyc:HS01957-MONOMER.
BRENDA2.3.2.2. 2681.
ReactomeREACT_111217. Metabolism.
SABIO-RKP19440.
UniPathwayUPA00204.

Gene expression databases

BgeeP19440.
CleanExHS_GGT1.
GenevestigatorP19440.

Family and domain databases

InterProIPR000101. GGT_peptidase.
[Graphical view]
PANTHERPTHR11686. PTHR11686. 1 hit.
PfamPF01019. G_glu_transpept. 1 hit.
[Graphical view]
PRINTSPR01210. GGTRANSPTASE.
TIGRFAMsTIGR00066. g_glut_trans. 1 hit.
PROSITEPS00462. G_GLU_TRANSPEPTIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGGT1. human.
GeneWikiGGT1.
GenomeRNAi2678.
NextBio10574.
PROP19440.
SOURCESearch...

Entry information

Entry nameGGT1_HUMAN
AccessionPrimary (citable) accession number: P19440
Secondary accession number(s): Q08247 expand/collapse secondary AC list , Q14404, Q8TBS1, Q9UMK1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: March 7, 2006
Last modified: April 16, 2014
This is version 162 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries