Reviewed, UniProtKB/Swiss-Prot P19440 (GGT1_HUMAN)

Names and origin

Protein names

Recommended name:
    Gamma-glutamyltranspeptidase 1
    EC=2.3.2.2
Alternative name(s):
    Gamma-glutamyltransferase 1
      Short name=GGT 1
    CD_antigen=CD224
Cleaved into the following 2 chains:
    1- Recommended name:
            Gamma-glutamyltranspeptidase 1 heavy chain
    2- Recommended name:
            Gamma-glutamyltranspeptidase 1 light chain

Gene names

Name:	GGT1
Synonyms:	GGT

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	569 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracelular GSH level. It is part of the cell antioxidant defense mechanism. Catalyzes the transfer of the glutamyl moiety of glutathione to amino acids and dipeptide acceptors. Alternatively, glutathione can be hydrolyzed to give Cys-Gly and gamma glutamate. Isoform 3 seems to be inactive. Ref.7
Catalytic activity	(5-L-glutamyl)-peptide + an amino acid = peptide + 5-L-glutamyl amino acid.
Pathway	Sulfur metabolism; glutathione metabolism.
Subunit structure	Heterodimer composed of the light and heavy chains. The active site is located in the light chain.
Subcellular location	Membrane; Single-pass type II membrane protein.
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. It is not known if the sialic acid residues are present on N-linked or on O-linked glycans. Ref.13 Ref.14 Ref.19 Ref.20 Ref.21
Involvement in disease	Defects in GGT1 are a cause of glutathionuria [MIM:231950]; also known as gamma-glutamyltranspeptidase deficiency. It is an autosomal recessive disease.
Miscellaneous	Cys-454 was thought to bind the gamma-glutamyl moiety, but mutagenesis of this residue had no effect on activity.
Sequence similarities	Belongs to the gamma-glutamyltransferase family.

Ontologies

Keywords
Biological process	Glutathione biosynthesis
Cellular component	Membrane
Coding sequence diversity	Alternative promoter usage Alternative splicing Polymorphism
Domain	Signal-anchor Transmembrane
Ligand	Sialic acid
Molecular function	Acyltransferase Transferase
PTM	Glycoprotein Zymogen
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cellular amino acid metabolic process Ref.1 Traceable author statement. Source: ProtInc glutathione biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acyltransferase activity Inferred from electronic annotation. Source: UniProtKB-KW gamma-glutamyltransferase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 380	380	Gamma-glutamyltranspeptidase 1 heavy chain		PRO_0000011058
	Chain	381 – 569	189	Gamma-glutamyltranspeptidase 1 light chain		PRO_0000011059
Regions
	Topological domain	1 – 4	4	Cytoplasmic Potential
	Transmembrane	5 – 26	22	Signal-anchor for type II membrane protein Probable
	Topological domain	27 – 569	543	Extracellular Potential
Amino acid modifications
	Glycosylation	95	1	N-linked (GlcNAc...) Potential
	Glycosylation	120	1	N-linked (GlcNAc...) Ref.20 Ref.21
	Glycosylation	230	1	N-linked (GlcNAc...) Ref.20
	Glycosylation	266	1	N-linked (GlcNAc...) Potential
	Glycosylation	297	1	N-linked (GlcNAc...) Potential
	Glycosylation	344	1	N-linked (GlcNAc...) Potential
	Glycosylation	511	1	N-linked (GlcNAc...) Ref.19 Ref.20
Natural variations
	Alternative sequence	1 – 344	344	Missing in isoform 3.		VSP_008132
	Alternative sequence	341 – 366	26	VVRNM…TTHPI → ASSGVSAGGPQHDLRVLRCP APGPDL in isoform 2.		VSP_001746
	Alternative sequence	367 – 569	203	Missing in isoform 2.		VSP_001747
	Natural variant	51	1	S → L: dbSNP rs2330837.		VAR_025545
	Natural variant	52	1	K → E: dbSNP rs2330838.		VAR_018373
	Natural variant	177	1	A → V: dbSNP rs3895576.		VAR_018374
	Natural variant	272	1	V → A: dbSNP rs4049829. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6		VAR_018372
	Natural variant	419	1	N → D: dbSNP rs17004876.		VAR_025546
	Natural variant	435	1	V → A: dbSNP rs16986465.		VAR_049181
Experimental info
	Mutagenesis	100	1	K → N: No effect on activity. Ref.15
	Mutagenesis	102	1	E → Q: No effect on activity. Ref.15
	Mutagenesis	107	1	R → K: Reduces enzyme activity by 99%. Ref.15
	Mutagenesis	107	1	R → Q or H: Abolishes enzyme activity. Ref.15
	Mutagenesis	108	1	E → Q: Reduces enzyme activity by 98%. Ref.15
	Mutagenesis	112	1	R → Q: No effect on activity. Ref.15
	Mutagenesis	139	1	R → Q: No effect on activity. Ref.15
	Mutagenesis	147	1	R → Q: No effect on activity. Ref.15
	Mutagenesis	150	1	R → Q: No effect on activity. Ref.15
	Mutagenesis	383	1	H → A: Reduces enzyme activity by 66%. Ref.18
	Mutagenesis	385	1	S → A: No effect on activity. Ref.17
	Mutagenesis	413	1	S → A: No effect on activity. Ref.17
	Mutagenesis	422	1	D → A: Reduces enzyme activity by 90%. Ref.16
	Mutagenesis	423	1	D → A: Abolishes enzyme activity. Increases KM by over 1000-fold. Ref.16
	Mutagenesis	425	1	S → A: No effect on activity. Ref.17
	Mutagenesis	451	1	S → A: Reduces enzyme activity by 99%. Abolishes activity; when associated with A-452. Ref.17
	Mutagenesis	452	1	S → A: Reduces enzyme activity by 99%. Abolishes activity; when associated with A-451. Ref.17
	Mutagenesis	454	1	C → A: No effect on activity. Ref.16
	Mutagenesis	505	1	H → A: Reduces enzyme activity by 90%. Ref.18
	Sequence conflict	30 – 31	2	SK → KS AA sequence Ref.11
	Sequence conflict	47	1	A → K AA sequence Ref.11
	Sequence conflict	139	1	R → E in AAA35889. Ref.5
	Sequence conflict	372	1	E → D in AAA02886. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 7, 2006. Version 2. Checksum: 71AE12485239A69F	FASTA	569	61,410
	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
	Isoform 2. Checksum: 726B492DEFA85BE2	FASTA	366	39,420
	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 ASSGVSAGGP QHDLRVLRCP APGPDL
	Isoform 3. Checksum: 46765CED537C40C3	FASTA	225	24,080
	10 20 30 40 50 60 MTSEFFAAQL RAQISDDTTH PISYYKPEFY TPDDGGTAHL SVVAEDGSAV SATSTINLYF 70 80 90 100 110 120 GSKVRSPVSG ILFNNEMDDF SSPSITNEFG VPPSPANFIQ PGKQPLSSMC PTIMVGQDGQ 130 140 150 160 170 180 VRMVVGAAGG TQITTATALA IIYNLWFGYD VKRAVEEPRL HNQLLPNVTT VERNIDQAVT 190 200 210 220 AALETRHHHT QIASTFIAVV QAIVRTAGGW AAASDSRKGG EPAGY

References

	« Hide 'large scale' referencesShow '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: 2904146] [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: 2907498] [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: 2563599] [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: 2568315] [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: 1968061] [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: 1378736] [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: 7689219] [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:RESEARCH84.1-RESEARCH84.11(2004) [PubMed: 15461802] [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. , 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: 10591208] [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: 15489334] [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: 2896486] [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: 10392451] [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: 19463] [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: 2900635] [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: 8095045] [Abstract] Cited for: 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: 7759490] [Abstract] Cited for: 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: 7673200] [Abstract] Cited for: 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: 8827453] [Abstract] Cited for: 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: 15084671] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-511, MASS SPECTROMETRY. Tissue: Bile.
[20]	"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: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-120; ASN-230 AND ASN-511, MASS SPECTROMETRY. Tissue: Liver.
[21]	"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: 19349973] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-120, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

Wikipedia

Gamma-glutamyl transpeptidase entry

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
IPI	IPI00018901. IPI00217717. IPI00339263.
PIR	EKHUEX. A31253. A48987. A60439. JS0067. PS0312.
RefSeq	NP_001027536.1. NP_001027537.1. NP_005256.2. NP_038347.2.
UniGene	Hs.595809 Hs.645535
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	P19440.
Protein family/group databases
MEROPS	T03.006.
Proteomic databases
PRIDE	P19440.
Genome annotation databases
Ensembl	ENST00000248923; ENSP00000248923; ENSG00000100031; Homo sapiens. [Genome view] ENST00000400380; ENSP00000383231; ENSG00000100031; Homo sapiens. [Genome view] ENST00000400382; ENSP00000383232; ENSG00000100031; Homo sapiens. [Genome view] ENST00000400383; ENSP00000383233; ENSG00000100031; Homo sapiens. [Genome view] ENST00000401885; ENSP00000384381; ENSG00000100031; Homo sapiens. [Genome view] ENST00000403838; ENSP00000384820; ENSG00000100031; Homo sapiens. [Genome view] ENST00000404223; ENSP00000385016; ENSG00000100031; Homo sapiens. [Genome view] ENST00000404532; ENSP00000385445; ENSG00000100031; Homo sapiens. [Genome view] ENST00000404920; ENSP00000385001; ENSG00000100031; Homo sapiens. [Genome view] ENST00000406383; ENSP00000385975; ENSG00000100031; Homo sapiens. [Genome view] ENST00000411974; ENSP00000389935; ENSG00000100031; Homo sapiens. [Genome view] ENST00000412658; ENSP00000393537; ENSG00000100031; Homo sapiens. [Genome view] ENST00000412898; ENSP00000408151; ENSG00000100031; Homo sapiens. [Genome view] ENST00000417817; ENSP00000391495; ENSG00000100031; Homo sapiens. [Genome view] ENST00000419133; ENSP00000395271; ENSG00000100031; Homo sapiens. [Genome view] ENST00000421833; ENSP00000407166; ENSG00000100031; Homo sapiens. [Genome view] ENST00000425895; ENSP00000387499; ENSG00000100031; Homo sapiens. [Genome view] ENST00000428338; ENSP00000405534; ENSG00000100031; Homo sapiens. [Genome view] ENST00000428855; ENSP00000415068; ENSG00000100031; Homo sapiens. [Genome view] ENST00000430030; ENSP00000413768; ENSG00000100031; Homo sapiens. [Genome view] ENST00000430289; ENSP00000417044; ENSG00000100031; Homo sapiens. [Genome view] ENST00000432761; ENSP00000402405; ENSG00000100031; Homo sapiens. [Genome view] ENST00000432867; ENSP00000398589; ENSG00000100031; Homo sapiens. [Genome view] ENST00000438643; ENSP00000403826; ENSG00000100031; Homo sapiens. [Genome view] ENST00000441130; ENSP00000398842; ENSG00000100031; Homo sapiens. [Genome view] ENST00000445029; ENSP00000393135; ENSG00000100031; Homo sapiens. [Genome view] ENST00000446402; ENSP00000389538; ENSG00000100031; Homo sapiens. [Genome view] ENST00000447416; ENSP00000400621; ENSG00000100031; Homo sapiens. [Genome view] ENST00000450398; ENSP00000405935; ENSG00000100031; Homo sapiens. [Genome view] ENST00000451366; ENSP00000387796; ENSG00000100031; Homo sapiens. [Genome view] ENST00000452551; ENSP00000415553; ENSG00000100031; Homo sapiens. [Genome view] ENST00000455483; ENSP00000415024; ENSG00000100031; Homo sapiens. [Genome view] ENST00000456869; ENSP00000415129; ENSG00000100031; Homo sapiens. [Genome view] ENST00000458485; ENSP00000390022; ENSG00000100031; Homo sapiens. [Genome view]
GeneID	2678.
KEGG	hsa:2678.
UCSC	uc003aan.1. human. uc003aay.1. human.
Organism-specific databases
CTD	2678.
GeneCards	GC22P023304.
H-InvDB	HIX0016314. HIX0041180.
HGNC	HGNC:4250. GGT1.
MIM	231950. phenotype. 612346. gene.
Orphanet	33573. Gamma-glutamyl transpeptidase deficiency.
PharmGKB	PA28662.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P19440.
HOVERGEN	P19440.
OMA	PLATHAG.
Enzyme and pathway databases
BioCyc	MetaCyc:MON-10101. MetaCyc:MON-10102.
BRENDA	2.3.2.2. 247.
Gene expression databases
Bgee	P19440.
CleanEx	HS_GGT1.
Genevestigator	P19440.
GermOnline	ENSG00000100031. Homo sapiens.
Family and domain databases
InterPro	IPR000101. GGT_peptidase. [Graphical view]
PANTHER	PTHR11686. GGT_peptidase. 1 hit.
Pfam	PF01019. G_glu_transpept. 1 hit. [Graphical view]
PRINTS	PR01210. GGTRANSPTASE.
TIGRFAMs	TIGR00066. g_glut_trans. 1 hit.
PROSITE	PS00462. G_GLU_TRANSPEPTIDASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
DrugBank	DB00143. Glutathione.
NextBio	10574.
SOURCE	Search...

Entry information

Entry name

GGT1_HUMAN

Accession

Primary (citable) accession number: P19440
Secondary accession number(s): Q08247 , Q14404, Q8TBS1, Q9UMK1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	March 7, 2006
Last modified:	November 3, 2009
This is version 115 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.