P36268 (GGT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Gamma-glutamyltranspeptidase 2
Short name=GGT 2
EC=2.3.2.2

Alternative name(s):
Gamma-glutamyltransferase 2

Cleaved into the following 2 chains:

1. Gamma-glutamyltranspeptidase 2 heavy chain
2. Gamma-glutamyltranspeptidase 2 light chain

Gene names

Name:

GGT2

Organism

Homo sapiens (Human)

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; catalyzes the transfer of the glutamyl moiety of glutathione to amino acids and dipeptide acceptors By similarity.
Catalytic activity	(5-L-glutamyl)-peptide + an amino acid = peptide + 5-L-glutamyl amino acid. Glutathione + H2O = L-cysteinylglycine + L-glutamate.
Pathway	Sulfur metabolism; glutathione metabolism.
Subcellular location	Membrane; Single-pass type II membrane protein By similarity.
Tissue specificity	Highly expressed in fetal and adult kidney and liver.
Miscellaneous	Corresponds to the light chain of other gamma-glutamyltransferase family members.
Sequence similarities	Belongs to the gamma-glutamyltransferase family.

Ontologies

Keywords
Biological process	Glutathione biosynthesis
Cellular component	Membrane
Coding sequence diversity	Alternative splicing
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Acyltransferase Transferase
PTM	Glycoprotein Zymogen
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	glutathione biosynthetic process Non-traceable author statement. Source: UniProtKB leukotriene biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB xenobiotic metabolic process Traceable author statement. Source: Reactome
Cellular component	anchored to external side of plasma membrane Traceable author statement. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	gamma-glutamyltransferase activity Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P36268-1)

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.

Isoform 2 (identifier: P36268-2)

The sequence of this isoform differs from the canonical sequence as follows:
     404-413: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 380	380	Gamma-glutamyltranspeptidase 2 heavy chain By similarity		PRO_0000205981
	Chain	381 – 569	189	Gamma-glutamyltranspeptidase 2 light chain By similarity		PRO_0000334692
Regions
	Topological domain	1 – 4	4	Cytoplasmic Potential
	Transmembrane	5 – 26	22	Helical; Signal-anchor for type II membrane protein; By similarity
	Topological domain	27 – 569	543	Extracellular Potential
Amino acid modifications
	Glycosylation	230	1	N-linked (GlcNAc...) Potential
	Glycosylation	511	1	N-linked (GlcNAc...) Ref.3
Natural variations
	Alternative sequence	404 – 413	10	Missing in isoform 2.		VSP_033757

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 20, 2008. Version 3. Checksum: 96458403C83B9FFF	FASTA	569	61,771
	10 20 30 40 50 60 MKKKLVVLGL LAVVLVLVIV GLCLWLPSAS KEPDNHVYTR AAMAADAKQC LEIGRDTLRD 70 80 90 100 110 120 GGSAVDAAIA ALLCVGLMNA HSMGIGVGLF LTIYNSTTGK AEVINAREVA PRLAFASMFN 130 140 150 160 170 180 SSEQSQKGGL SVAVPGEIRG YELAHQRHGR LPWARLFQPS IQLARQGFPV GKGLAAVLEN 190 200 210 220 230 240 KRTVIEQQPV LWYVFCRDRK VLREGERLTL PRLADTYEML AIEGAQAFYN GSLMAQIVKD 250 260 270 280 290 300 IQAAGGIVTA EDLNNYRAEL IEHPLNISLG DAVLYMPSAR LSGPVLALIL NILKGYNFSR 310 320 330 340 350 360 ESVETPEQKG LTYHRIVEAF RFAYAKRTLL GDPKFVDVTE VVRNMTSEFF AAQLRSQISD 370 380 390 400 410 420 HTTHPISYYK PEFYTPDDGG TAHLSVVAED GSAVSATSTI NLYFGSKVCS PVSGILFNNE 430 440 450 460 470 480 WTTSALPAFT NEFGAPPSPA NFIQPGKQPL LSMCLTIMVG QDGQVRMVVG AAGGTQITTD 490 500 510 520 530 540 TALAIIYNLW FGYDVKRAVE EPRLHNKLLP NVTTVERNID QAVTAALETR HHHTQIASTF 550 560 IAVVQAIVRT AGGWAAALDS RKGGEPAGY
	Isoform 2 [UniParc]. Checksum: BDDD7E3BC6876EA6	FASTA	559	60,779
	10 20 30 40 50 60 MKKKLVVLGL LAVVLVLVIV GLCLWLPSAS KEPDNHVYTR AAMAADAKQC LEIGRDTLRD 70 80 90 100 110 120 GGSAVDAAIA ALLCVGLMNA HSMGIGVGLF LTIYNSTTGK AEVINAREVA PRLAFASMFN 130 140 150 160 170 180 SSEQSQKGGL SVAVPGEIRG YELAHQRHGR LPWARLFQPS IQLARQGFPV GKGLAAVLEN 190 200 210 220 230 240 KRTVIEQQPV LWYVFCRDRK VLREGERLTL PRLADTYEML AIEGAQAFYN GSLMAQIVKD 250 260 270 280 290 300 IQAAGGIVTA EDLNNYRAEL IEHPLNISLG DAVLYMPSAR LSGPVLALIL NILKGYNFSR 310 320 330 340 350 360 ESVETPEQKG LTYHRIVEAF RFAYAKRTLL GDPKFVDVTE VVRNMTSEFF AAQLRSQISD 370 380 390 400 410 420 HTTHPISYYK PEFYTPDDGG TAHLSVVAED GSAVSATSTI NLYGILFNNE WTTSALPAFT 430 440 450 460 470 480 NEFGAPPSPA NFIQPGKQPL LSMCLTIMVG QDGQVRMVVG AAGGTQITTD TALAIIYNLW 490 500 510 520 530 540 FGYDVKRAVE EPRLHNKLLP NVTTVERNID QAVTAALETR HHHTQIASTF IAVVQAIVRT 550 AGGWAAALDS RKGGEPAGY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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].
[2]	"Different gamma-glutamyl transpeptidase mRNAs are expressed in human liver and kidney." Pawlak A., Wu S.-J., Bulle F., Suzuki A., Chikhi N., Ferry N., Baik J.-H., Siegrist S., Guellaen G. Biochem. Biophys. Res. Commun. 164:912-918(1989) [PubMed: 2573352] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 362-569 (ISOFORM 2).
[3]	"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-511, MASS SPECTROMETRY. Tissue: Liver.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP000550 Genomic DNA. No translation available. BG743316 mRNA. No translation available. AA632626 mRNA. No translation available. M30479 , M30475, M30476, M30477, M30478 Genomic DNA. Translation: AAA52765.1. M30474 mRNA. Translation: AAA52548.1.
IPI	IPI00878291. IPI00894564.
PIR	A36742.
UniGene	Hs.568255. Hs.645533.
3D structure databases
ProteinModelPortal	P36268.
SMR	P36268. Positions 34-569.
ModBase	Search...
Protein-protein interaction databases
STRING	P36268.
Protein family/group databases
MEROPS	T03.015.
PTM databases
PhosphoSite	P36268.
Polymorphism databases
DMDM	189047137.
Proteomic databases
PRIDE	P36268.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000401924; ENSP00000385721; ENSG00000133475. ENST00000402582; ENSP00000384349; ENSG00000133475. ENST00000424627; ENSP00000402035; ENSG00000133475.
Organism-specific databases
GeneCards	GC22M021562.
H-InvDB	HIX0037636.
HGNC	HGNC:4251. GGT2.
MIM	137181. gene.
neXtProt	NX_P36268.
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00550000074591.
HOGENOM	HBG738311.
HOVERGEN	HBG005835.
InParanoid	P36268.
OrthoDB	EOG4VDPZ6.
PhylomeDB	P36268.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism.
Gene expression databases
Bgee	P36268.
CleanEx	HS_GGT2.
Genevestigator	P36268.
GermOnline	ENSG00000133475. 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.
PROSITE	PS00462. G_GLU_TRANSPEPTIDASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

GGT2_HUMAN

Accession

Primary (citable) accession number: P36268

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	May 20, 2008
Last modified:	December 14, 2011
This is version 95 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.