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Protein

Inactive gamma-glutamyltranspeptidase 2

Gene

GGT2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei107 – 1071GlutamateBy similarity
Active sitei381 – 3811NucleophileBy similarity
Binding sitei399 – 3991GlutamateBy similarity
Binding sitei420 – 4201GlutamateBy similarity

GO - Molecular functioni

  1. gamma-glutamyltransferase activity Source: UniProtKB

GO - Biological processi

  1. glutathione biosynthetic process Source: Reactome
  2. glutathione derivative biosynthetic process Source: Reactome
  3. glutathione metabolic process Source: UniProtKB
  4. leukotriene biosynthetic process Source: UniProtKB
  5. small molecule metabolic process Source: Reactome
  6. xenobiotic metabolic process Source: Reactome
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_228214. Aflatoxin activation and detoxification.
REACT_6960. Glutathione synthesis and recycling.

Protein family/group databases

MEROPSiT03.015.

Names & Taxonomyi

Protein namesi
Recommended name:
Inactive gamma-glutamyltranspeptidase 2
Short name:
GGT 2
Alternative name(s):
Gamma-glutamyltransferase 2
Glutathione hydrolase 2
Gene namesi
Name:GGT2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:4251. GGT2.

Subcellular locationi

Cytoplasmperinuclear region 1 Publication. Endoplasmic reticulum 1 Publication
Note: Co-localizes with calnexin in the endoplasmic reticulum.

GO - Cellular componenti

  1. anchored component of external side of plasma membrane Source: UniProtKB
  2. endoplasmic reticulum Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProtKB
  4. perinuclear region of cytoplasm Source: UniProtKB
  5. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi192 – 1921W → C: No effect on the absence of autocatalytic cleavage and catalytic activity; when associated with E-193. 1 Publication
Mutagenesisi193 – 1931Y → E: No effect on the absence of autocatalytic cleavage and catalytic activity; when associated with C-192. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030Sequence AnalysisAdd
BLAST
Chaini31 – 569539Inactive gamma-glutamyltranspeptidase 2PRO_0000425541Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi230 – 2301N-linked (GlcNAc...)Sequence Analysis
Glycosylationi511 – 5111N-linked (GlcNAc...)1 Publication

Post-translational modificationi

Not cleaved by autocatalysis into a large and a small subunit resulting in loss of cell membrane localization and catalytic activity.1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiP36268.
PRIDEiP36268.

PTM databases

PhosphoSiteiP36268.

Expressioni

Tissue specificityi

Highly expressed in fetal and adult kidney and liver.

Gene expression databases

BgeeiP36268.
CleanExiHS_GGT2.
ExpressionAtlasiP36268. baseline.
GenevestigatoriP36268.

Organism-specific databases

HPAiHPA045635.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000385721.

Structurei

3D structure databases

ProteinModelPortaliP36268.
SMRiP36268. Positions 33-375, 381-569.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the gamma-glutamyltransferase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0405.
HOGENOMiHOG000175620.
HOVERGENiHBG005835.
InParanoidiP36268.
PhylomeDBiP36268.
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.
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 splicing. Align

Isoform 1 (identifier: P36268-1) [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

        10         20         30         40         50
MKKKLVVLGL LAVVLVLVIV GLCLWLPSAS KEPDNHVYTR AAMAADAKQC
60 70 80 90 100
LEIGRDTLRD GGSAVDAAIA ALLCVGLMNA HSMGIGVGLF LTIYNSTTGK
110 120 130 140 150
AEVINAREVA PRLAFASMFN SSEQSQKGGL SVAVPGEIRG YELAHQRHGR
160 170 180 190 200
LPWARLFQPS IQLARQGFPV GKGLAAVLEN KRTVIEQQPV LWYVFCRDRK
210 220 230 240 250
VLREGERLTL PRLADTYEML AIEGAQAFYN GSLMAQIVKD IQAAGGIVTA
260 270 280 290 300
EDLNNYRAEL IEHPLNISLG DAVLYMPSAR LSGPVLALIL NILKGYNFSR
310 320 330 340 350
ESVETPEQKG LTYHRIVEAF RFAYAKRTLL GDPKFVDVTE VVRNMTSEFF
360 370 380 390 400
AAQLRSQISD HTTHPISYYK PEFYTPDDGG TAHLSVVAED GSAVSATSTI
410 420 430 440 450
NLYFGSKVCS PVSGILFNNE WTTSALPAFT NEFGAPPSPA NFIQPGKQPL
460 470 480 490 500
LSMCLTIMVG QDGQVRMVVG AAGGTQITTD TALAIIYNLW FGYDVKRAVE
510 520 530 540 550
EPRLHNKLLP NVTTVERNID QAVTAALETR HHHTQIASTF IAVVQAIVRT
560
AGGWAAALDS RKGGEPAGY
Length:569
Mass (Da):61,771
Last modified:May 20, 2008 - v3
Checksum:i96458403C83B9FFF
GO
Isoform 2 (identifier: P36268-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:559
Mass (Da):60,779
Checksum:iBDDD7E3BC6876EA6
GO
Isoform 3 (identifier: P36268-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:574
Mass (Da):62,121
Checksum:iF2FCCF4EA709AEF9
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei192 – 1932WY → CPLCPGE in isoform 3. CuratedVSP_053716
Alternative sequencei404 – 41310Missing in isoform 2. 1 PublicationVSP_033757

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA36742.
UniGeneiHs.568255.

Genome annotation databases

EnsembliENST00000401924; ENSP00000385721; ENSG00000133475.
ENST00000424627; ENSP00000402035; ENSG00000133475.

Polymorphism databases

DMDMi189047137.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA36742.
UniGeneiHs.568255.

3D structure databases

ProteinModelPortaliP36268.
SMRiP36268. Positions 33-375, 381-569.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000385721.

Protein family/group databases

MEROPSiT03.015.

PTM databases

PhosphoSiteiP36268.

Polymorphism databases

DMDMi189047137.

Proteomic databases

PaxDbiP36268.
PRIDEiP36268.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000401924; ENSP00000385721; ENSG00000133475.
ENST00000424627; ENSP00000402035; ENSG00000133475.

Organism-specific databases

GeneCardsiGC22M021562.
H-InvDBHIX0037636.
HIX0041197.
HGNCiHGNC:4251. GGT2.
HPAiHPA045635.
MIMi137181. gene.
neXtProtiNX_P36268.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0405.
HOGENOMiHOG000175620.
HOVERGENiHBG005835.
InParanoidiP36268.
PhylomeDBiP36268.
TreeFamiTF313608.

Enzyme and pathway databases

ReactomeiREACT_228214. Aflatoxin activation and detoxification.
REACT_6960. Glutathione synthesis and recycling.

Miscellaneous databases

PROiP36268.
SOURCEiSearch...

Gene expression databases

BgeeiP36268.
CleanExiHS_GGT2.
ExpressionAtlasiP36268. baseline.
GenevestigatoriP36268.

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.
PROSITEiPS00462. G_GLU_TRANSPEPTIDASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [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.

Entry informationi

Entry nameiGGT2_HUMAN
AccessioniPrimary (citable) accession number: P36268
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: May 20, 2008
Last modified: January 7, 2015
This is version 123 of the entry and version 3 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.