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P36268 (GGT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inactive gamma-glutamyltranspeptidase 2

Short name=GGT 2
Alternative name(s):
Gamma-glutamyltransferase 2
Glutathione hydrolase 2
Gene names
Name:GGT2
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

Isoform 1, isoform 2 and isoform 3 lack catalytic activity due to its inability to undergo the autocatalytic cleavage needed to produce a mature, enzymatically active heterodimer (Ref.4).

Subcellular location

Cytoplasmperinuclear region. Endoplasmic reticulum. Note: Co-localizes with calnexin in the endoplasmic reticulum. Ref.4

Tissue specificity

Highly expressed in fetal and adult kidney and liver.

Post-translational modification

Not cleaved by autocatalysis into a large and a small subunit resulting in loss of cell membrane localization and catalytic activity (Ref.4). Ref.4

Sequence similarities

Belongs to the gamma-glutamyltransferase family.

Alternative products

This entry describes 3 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.
Isoform 3 (identifier: P36268-3)

The sequence of this isoform differs from the canonical sequence as follows:
     192-193: WY → CPLCPGE

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Potential
Chain31 – 569539Inactive gamma-glutamyltranspeptidase 2
PRO_0000425541

Regions

Region451 – 4522Glutamate binding By similarity

Sites

Active site3811Nucleophile By similarity
Binding site1071Glutamate By similarity
Binding site3991Glutamate By similarity
Binding site4201Glutamate By similarity

Amino acid modifications

Glycosylation2301N-linked (GlcNAc...) Potential
Glycosylation5111N-linked (GlcNAc...) Ref.3

Natural variations

Alternative sequence192 – 1932WY → CPLCPGE in isoform 3.
VSP_053716
Alternative sequence404 – 41310Missing in isoform 2.
VSP_033757

Experimental info

Mutagenesis1921W → C: No effect on the absence of autocatalytic cleavage and catalytic activity; when associated with E-193. Ref.4
Mutagenesis1931Y → E: No effect on the absence of autocatalytic cleavage and catalytic activity; when associated with C-192. Ref.4

Sequences

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

Last modified May 20, 2008. Version 3.
Checksum: 96458403C83B9FFF

FASTA56961,771
        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 

« Hide

Isoform 2 [UniParc].

Checksum: BDDD7E3BC6876EA6
Show »

FASTA55960,779
Isoform 3 [UniParc].

Checksum: F2FCCF4EA709AEF9
Show »

FASTA57462,121

References

« Hide '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. 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].
[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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-511.
Tissue: Liver.
[4]"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: ALTERNATIVE SPLICING (ISOFORMS 1; 2 AND 3), ABSENCE OF CATALYTIC ACTIVITY AND AUTOCATALYTIC CLEAVAGE, SUBCELLULAR LOCATION, GLYCOSYLATION, MUTAGENESIS OF TRP-192 AND TYR-193.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP000550 Genomic DNA. No translation available.
BG743316 mRNA. No translation available.
AA632626 mRNA. No translation available.
M30479 expand/collapse EMBL AC list , M30475, M30476, M30477, M30478 Genomic DNA. Translation: AAA52765.1.
M30474 mRNA. Translation: AAA52548.1.
PIRA36742.
UniGeneHs.568255.

3D structure databases

ProteinModelPortalP36268.
SMRP36268. Positions 33-375, 381-569.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000385721.

Protein family/group databases

MEROPST03.015.

PTM databases

PhosphoSiteP36268.

Polymorphism databases

DMDM189047137.

Proteomic databases

PaxDbP36268.
PRIDEP36268.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000401924; ENSP00000385721; ENSG00000133475.
ENST00000424627; ENSP00000402035; ENSG00000133475.

Organism-specific databases

GeneCardsGC22M021562.
H-InvDBHIX0037636.
HIX0041197.
HGNCHGNC:4251. GGT2.
HPAHPA045635.
MIM137181. gene.
neXtProtNX_P36268.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0405.
HOGENOMHOG000175620.
HOVERGENHBG005835.
InParanoidP36268.
PhylomeDBP36268.
TreeFamTF313608.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

BgeeP36268.
CleanExHS_GGT2.
GenevestigatorP36268.

Family and domain databases

InterProIPR000101. GGT_peptidase.
IPR029055. Ntn_hydrolases_N.
[Graphical view]
PANTHERPTHR11686. PTHR11686. 1 hit.
PfamPF01019. G_glu_transpept. 1 hit.
[Graphical view]
PRINTSPR01210. GGTRANSPTASE.
SUPFAMSSF56235. SSF56235. 1 hit.
PROSITEPS00462. G_GLU_TRANSPEPTIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP36268.
SOURCESearch...

Entry information

Entry nameGGT2_HUMAN
AccessionPrimary (citable) accession number: P36268
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: May 20, 2008
Last modified: June 11, 2014
This is version 118 of the entry and version 3 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

MIM cross-references

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

Human chromosome 22

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