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P36269

- GGT5_HUMAN

UniProt

P36269 - GGT5_HUMAN

Protein

Gamma-glutamyltransferase 5

Gene

GGT5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    Cleaves the gamma-glutamyl peptide bond of glutathione conjugates, but maybe not glutathione itself. Converts leukotriene C4 (LTC4) to leukotriene D4 (LTD4).

    Catalytic activityi

    A (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid.
    Glutathione + H2O = L-cysteinylglycine + L-glutamate.
    Leukotriene C4 + H2O = leukotriene D4 + L-glutamate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei110 – 1101GlutamateBy similarity
    Active sitei388 – 3881NucleophileBy similarity
    Binding sitei406 – 4061GlutamateBy similarity
    Binding sitei427 – 4271GlutamateBy similarity

    GO - Molecular functioni

    1. gamma-glutamyltransferase activity Source: UniProtKB
    2. glutathione hydrolase activity Source: UniProtKB-EC

    GO - Biological processi

    1. arachidonic acid metabolic process Source: Reactome
    2. cellular amino acid metabolic process Source: ProtInc
    3. glutathione biosynthetic process Source: UniProtKB-KW
    4. glutathione metabolic process Source: UniProtKB
    5. inflammatory response Source: Ensembl
    6. leukotriene biosynthetic process Source: UniProtKB
    7. leukotriene metabolic process Source: Reactome
    8. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Acyltransferase, Hydrolase, Protease, Transferase

    Keywords - Biological processi

    Glutathione biosynthesis, Leukotriene biosynthesis

    Enzyme and pathway databases

    BioCyciMetaCyc:HS01949-MONOMER.
    ReactomeiREACT_150420. Synthesis of Leukotrienes (LT) and Eoxins (EX).
    REACT_6960. Glutathione synthesis and recycling.
    UniPathwayiUPA00204.
    UPA00880.

    Protein family/group databases

    MEROPSiT03.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Gamma-glutamyltransferase 5 (EC:2.3.2.2)
    Short name:
    GGT 5
    Alternative name(s):
    Gamma-glutamyl transpeptidase-related enzyme
    Short name:
    GGT-rel
    Gamma-glutamyltransferase-like activity 1
    Gamma-glutamyltranspeptidase 5
    Glutathione hydrolase 5 (EC:3.4.19.13)
    Leukotriene-C4 hydrolase (EC:3.4.19.14)
    Cleaved into the following 2 chains:
    Gene namesi
    Name:GGT5
    Synonyms:GGTLA1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:4260. GGT5.

    Subcellular locationi

    Membrane By similarity; Single-pass type II membrane protein By similarity

    GO - Cellular componenti

    1. anchored component of external side of plasma membrane Source: UniProtKB
    2. integral component of membrane Source: ProtInc
    3. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162389442.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 387387Gamma-glutamyltransferase 5 heavy chainBy similarityPRO_0000011072Add
    BLAST
    Chaini388 – 586199Gamma-glutamyltransferase 5 light chainBy similarityPRO_0000011073Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi98 – 981N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi204 – 2041N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi303 – 3031N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi347 – 3471N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi535 – 5351N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi550 – 5501N-linked (GlcNAc...)1 Publication

    Post-translational modificationi

    Cleaved by autocatalysis into a large and a small subunit.By similarity

    Keywords - PTMi

    Glycoprotein, Zymogen

    Proteomic databases

    MaxQBiP36269.
    PaxDbiP36269.
    PRIDEiP36269.

    PTM databases

    PhosphoSiteiP36269.

    Expressioni

    Gene expression databases

    ArrayExpressiP36269.
    BgeeiP36269.
    CleanExiHS_GGT5.
    GenevestigatoriP36269.

    Organism-specific databases

    HPAiCAB032489.
    HPA008121.

    Interactioni

    Subunit structurei

    Heterodimer composed of the light and heavy chains. The active site is located in the light chain By similarity.By similarity

    Protein-protein interaction databases

    STRINGi9606.ENSP00000381340.

    Structurei

    3D structure databases

    ProteinModelPortaliP36269.
    SMRiP36269. Positions 38-586.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 88CytoplasmicSequence Analysis
    Topological domaini30 – 586557ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei9 – 2921Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni469 – 4702Glutamate bindingBy similarity

    Sequence similaritiesi

    Belongs to the gamma-glutamyltransferase family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0405.
    HOGENOMiHOG000175620.
    HOVERGENiHBG005835.
    KOiK00681.
    OMAiCICAVSD.
    OrthoDBiEOG7V7665.
    PhylomeDBiP36269.
    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: P36269-1) [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

    MARGYGATVS LVLLGLGLAL AVIVLAVVLS RHQAPCGPQA FAHAAVAADS    50
    KVCSDIGRAI LQQQGSPVDA TIAALVCTSV VNPQSMGLGG GVIFTIYNVT 100
    TGKVEVINAR ETVPASHAPS LLDQCAQALP LGTGAQWIGV PGELRGYAEA 150
    HRRHGRLPWA QLFQPTIALL RGGHVVAPVL SRFLHNSILR PSLQASTLRQ 200
    LFFNGTEPLR PQDPLPWPAL ATTLETVATE GVEVFYTGRL GQMLVEDIAK 250
    EGSQLTLQDL AKFQPEVVDA LEVPLGDYTL YSPPPPAGGA ILSFILNVLR 300
    GFNFSTESMA RPEGRVNVYH HLVETLKFAK GQRWRLGDPR SHPKLQNASR 350
    DLLGETLAQL IRQQIDGRGD HQLSHYSLAE AWGHGTGTSH VSVLGEDGSA 400
    VAATSTINTP FGAMVYSPRT GIILNNELLD LCERCPRGSG TTPSPVSGDR 450
    VGGAPGRCWP PVPGERSPSS MVPSILINKA QGSKLVIGGA GGELIISAVA 500
    QAIMSKLWLG FDLRAAIAAP ILHVNSKGCV EYEPNFSQEV QRGLQDRGQN 550
    QTQRPFFLNV VQAVSQEGAC VYAVSDLRKS GEAAGY 586
    Length:586
    Mass (Da):62,261
    Last modified:October 17, 2006 - v2
    Checksum:iEE37B3CE516F5788
    GO
    Isoform 2 (identifier: P36269-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         101-132: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:554
    Mass (Da):58,992
    Checksum:i86001882BE5A0D10
    GO
    Isoform 3 (identifier: P36269-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         445-445: P → PA

    Note: No experimental confirmation available.

    Show »
    Length:587
    Mass (Da):62,332
    Checksum:iC7F2285F9FFF1A22
    GO

    Sequence cautioni

    The sequence CAB55910.1 differs from that shown. Reason: Frameshift at position 446.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti408 – 4081N → Y in CAB55910. (PubMed:17974005)Curated
    Sequence conflicti437 – 4371R → W in AAA58503. (PubMed:1676842)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti11 – 111L → I.
    Corresponds to variant rs5760274 [ dbSNP | Ensembl ].
    VAR_028006
    Natural varianti330 – 3301K → R.2 Publications
    Corresponds to variant rs2275984 [ dbSNP | Ensembl ].
    VAR_028007
    Natural varianti332 – 3321Q → H.
    Corresponds to variant rs6004105 [ dbSNP | Ensembl ].
    VAR_028008
    Natural varianti475 – 4751I → V.
    Corresponds to variant rs7288201 [ dbSNP | Ensembl ].
    VAR_024455

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei101 – 13232Missing in isoform 2. 1 PublicationVSP_008146Add
    BLAST
    Alternative sequencei445 – 4451P → PA in isoform 3. 1 PublicationVSP_043470

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64099 mRNA. Translation: AAA58503.1.
    AL117414 mRNA. Translation: CAB55910.1. Frameshift.
    BT009808 mRNA. Translation: AAP88810.1.
    CT841518 mRNA. Translation: CAJ86448.1.
    AK292006 mRNA. Translation: BAF84695.1.
    AP000353 Genomic DNA. No translation available.
    AP000354 Genomic DNA. No translation available.
    CH471095 Genomic DNA. Translation: EAW59643.1.
    BC011362 mRNA. Translation: AAH11362.1.
    BC073999 mRNA. Translation: AAH73999.1.
    CCDSiCCDS13825.1. [P36269-1]
    CCDS42989.1. [P36269-2]
    CCDS42990.1. [P36269-3]
    PIRiA41125.
    T17220.
    RefSeqiNP_001093251.1. NM_001099781.1. [P36269-3]
    NP_001093252.1. NM_001099782.1. [P36269-2]
    NP_004112.2. NM_004121.2. [P36269-1]
    UniGeneiHs.437156.

    Genome annotation databases

    EnsembliENST00000263112; ENSP00000263112; ENSG00000099998. [P36269-2]
    ENST00000327365; ENSP00000330080; ENSG00000099998. [P36269-1]
    ENST00000398292; ENSP00000381340; ENSG00000099998. [P36269-3]
    GeneIDi2687.
    KEGGihsa:2687.
    UCSCiuc002zzo.4. human. [P36269-1]
    uc002zzp.4. human. [P36269-3]
    uc002zzq.4. human. [P36269-2]

    Polymorphism databases

    DMDMi116242493.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64099 mRNA. Translation: AAA58503.1 .
    AL117414 mRNA. Translation: CAB55910.1 . Frameshift.
    BT009808 mRNA. Translation: AAP88810.1 .
    CT841518 mRNA. Translation: CAJ86448.1 .
    AK292006 mRNA. Translation: BAF84695.1 .
    AP000353 Genomic DNA. No translation available.
    AP000354 Genomic DNA. No translation available.
    CH471095 Genomic DNA. Translation: EAW59643.1 .
    BC011362 mRNA. Translation: AAH11362.1 .
    BC073999 mRNA. Translation: AAH73999.1 .
    CCDSi CCDS13825.1. [P36269-1 ]
    CCDS42989.1. [P36269-2 ]
    CCDS42990.1. [P36269-3 ]
    PIRi A41125.
    T17220.
    RefSeqi NP_001093251.1. NM_001099781.1. [P36269-3 ]
    NP_001093252.1. NM_001099782.1. [P36269-2 ]
    NP_004112.2. NM_004121.2. [P36269-1 ]
    UniGenei Hs.437156.

    3D structure databases

    ProteinModelPortali P36269.
    SMRi P36269. Positions 38-586.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000381340.

    Protein family/group databases

    MEROPSi T03.002.

    PTM databases

    PhosphoSitei P36269.

    Polymorphism databases

    DMDMi 116242493.

    Proteomic databases

    MaxQBi P36269.
    PaxDbi P36269.
    PRIDEi P36269.

    Protocols and materials databases

    DNASUi 2687.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263112 ; ENSP00000263112 ; ENSG00000099998 . [P36269-2 ]
    ENST00000327365 ; ENSP00000330080 ; ENSG00000099998 . [P36269-1 ]
    ENST00000398292 ; ENSP00000381340 ; ENSG00000099998 . [P36269-3 ]
    GeneIDi 2687.
    KEGGi hsa:2687.
    UCSCi uc002zzo.4. human. [P36269-1 ]
    uc002zzp.4. human. [P36269-3 ]
    uc002zzq.4. human. [P36269-2 ]

    Organism-specific databases

    CTDi 2687.
    GeneCardsi GC22M024615.
    H-InvDB HIX0138942.
    HGNCi HGNC:4260. GGT5.
    HPAi CAB032489.
    HPA008121.
    MIMi 137168. gene.
    neXtProti NX_P36269.
    PharmGKBi PA162389442.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0405.
    HOGENOMi HOG000175620.
    HOVERGENi HBG005835.
    KOi K00681.
    OMAi CICAVSD.
    OrthoDBi EOG7V7665.
    PhylomeDBi P36269.
    TreeFami TF313608.

    Enzyme and pathway databases

    UniPathwayi UPA00204 .
    UPA00880 .
    BioCyci MetaCyc:HS01949-MONOMER.
    Reactomei REACT_150420. Synthesis of Leukotrienes (LT) and Eoxins (EX).
    REACT_6960. Glutathione synthesis and recycling.

    Miscellaneous databases

    GeneWikii GGTLA1.
    GenomeRNAii 2687.
    NextBioi 10606.
    PROi P36269.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P36269.
    Bgeei P36269.
    CleanExi HS_GGT5.
    Genevestigatori P36269.

    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. "Identification of a human gamma-glutamyl cleaving enzyme related to, but distinct from, gamma-glutamyl transpeptidase."
      Heisterkamp N., Rajpert-De Meyts E., Uribe L., Forman H.J., Groffen J.
      Proc. Natl. Acad. Sci. U.S.A. 88:6303-6307(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-330.
      Tissue: Placenta.
    2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Small intestine.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Fetal kidney.
    6. "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], VARIANT ARG-330.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
      Tissue: Brain and PNS.
    9. "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-550.
      Tissue: Liver.

    Entry informationi

    Entry nameiGGT5_HUMAN
    AccessioniPrimary (citable) accession number: P36269
    Secondary accession number(s): Q53XM9
    , Q6GMP0, Q96FC1, Q9UFM5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 143 of the entry and version 2 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. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3