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P36268

- GGT2_HUMAN

UniProt

P36268 - GGT2_HUMAN

Protein

Inactive gamma-glutamyltranspeptidase 2

Gene

GGT2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 3 (20 May 2008)
      Previous versions | rss
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    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

    Enzyme and pathway databases

    ReactomeiREACT_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. perinuclear region of cytoplasm Source: UniProtKB
    4. plasma membrane Source: Reactome

    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...)2 Publications

    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.
    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

    MKKKLVVLGL LAVVLVLVIV GLCLWLPSAS KEPDNHVYTR AAMAADAKQC    50
    LEIGRDTLRD GGSAVDAAIA ALLCVGLMNA HSMGIGVGLF LTIYNSTTGK 100
    AEVINAREVA PRLAFASMFN SSEQSQKGGL SVAVPGEIRG YELAHQRHGR 150
    LPWARLFQPS IQLARQGFPV GKGLAAVLEN KRTVIEQQPV LWYVFCRDRK 200
    VLREGERLTL PRLADTYEML AIEGAQAFYN GSLMAQIVKD IQAAGGIVTA 250
    EDLNNYRAEL IEHPLNISLG DAVLYMPSAR LSGPVLALIL NILKGYNFSR 300
    ESVETPEQKG LTYHRIVEAF RFAYAKRTLL GDPKFVDVTE VVRNMTSEFF 350
    AAQLRSQISD HTTHPISYYK PEFYTPDDGG TAHLSVVAED GSAVSATSTI 400
    NLYFGSKVCS PVSGILFNNE WTTSALPAFT NEFGAPPSPA NFIQPGKQPL 450
    LSMCLTIMVG QDGQVRMVVG AAGGTQITTD TALAIIYNLW FGYDVKRAVE 500
    EPRLHNKLLP NVTTVERNID QAVTAALETR HHHTQIASTF IAVVQAIVRT 550
    AGGWAAALDS RKGGEPAGY 569
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi A36742.
    UniGenei Hs.568255.

    3D structure databases

    ProteinModelPortali P36268.
    SMRi P36268. Positions 33-375, 381-569.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000385721.

    Protein family/group databases

    MEROPSi T03.015.

    PTM databases

    PhosphoSitei P36268.

    Polymorphism databases

    DMDMi 189047137.

    Proteomic databases

    PaxDbi P36268.
    PRIDEi P36268.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000401924 ; ENSP00000385721 ; ENSG00000133475 .
    ENST00000424627 ; ENSP00000402035 ; ENSG00000133475 .

    Organism-specific databases

    GeneCardsi GC22M021562.
    H-InvDB HIX0037636.
    HIX0041197.
    HGNCi HGNC:4251. GGT2.
    HPAi HPA045635.
    MIMi 137181. gene.
    neXtProti NX_P36268.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0405.
    HOGENOMi HOG000175620.
    HOVERGENi HBG005835.
    InParanoidi P36268.
    PhylomeDBi P36268.
    TreeFami TF313608.

    Enzyme and pathway databases

    Reactomei REACT_6960. Glutathione synthesis and recycling.

    Miscellaneous databases

    PROi P36268.
    SOURCEi Search...

    Gene expression databases

    Bgeei P36268.
    CleanExi HS_GGT2.
    Genevestigatori P36268.

    Family and domain databases

    InterProi IPR000101. GGT_peptidase.
    IPR029055. Ntn_hydrolases_N.
    [Graphical view ]
    PANTHERi PTHR11686. PTHR11686. 1 hit.
    Pfami PF01019. G_glu_transpept. 1 hit.
    [Graphical view ]
    PRINTSi PR01210. GGTRANSPTASE.
    SUPFAMi SSF56235. SSF56235. 1 hit.
    PROSITEi PS00462. G_GLU_TRANSPEPTIDASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 120 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