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Q16775

- GLO2_HUMAN

UniProt

Q16775 - GLO2_HUMAN

Protein

Hydroxyacylglutathione hydrolase, mitochondrial

Gene

HAGH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 2 (01 Sep 2009)
      Previous versions | rss
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    Functioni

    Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.

    Catalytic activityi

    S-(2-hydroxyacyl)glutathione + H2O = glutathione + a 2-hydroxy carboxylate.

    Cofactori

    Binds 2 zinc ions per subunit.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi102 – 1021Zinc 1
    Metal bindingi104 – 1041Zinc 1
    Metal bindingi106 – 1061Zinc 2
    Metal bindingi107 – 1071Zinc 2
    Metal bindingi158 – 1581Zinc 1
    Metal bindingi182 – 1821Zinc 1
    Metal bindingi182 – 1821Zinc 2
    Metal bindingi221 – 2211Zinc 2

    GO - Molecular functioni

    1. hydroxyacylglutathione hydrolase activity Source: UniProtKB
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. glutathione biosynthetic process Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi3.1.2.6. 5596.
    SABIO-RKQ16775.
    UniPathwayiUPA00619; UER00676.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hydroxyacylglutathione hydrolase, mitochondrial (EC:3.1.2.6)
    Alternative name(s):
    Glyoxalase II
    Short name:
    Glx II
    Gene namesi
    Name:HAGH
    Synonyms:GLO2, HAGH1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:4805. HAGH.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. extracellular vesicular exosome Source: UniProt
    3. mitochondrial matrix Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    MIMi138760. gene+phenotype.
    PharmGKBiPA29179.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 1313MitochondrionSequence AnalysisAdd
    BLAST
    Chaini14 – 308295Hydroxyacylglutathione hydrolase, mitochondrialPRO_0000192342Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei116 – 1161N6-acetyllysineBy similarity
    Modified residuei229 – 2291N6-acetyllysine; alternate1 Publication
    Modified residuei229 – 2291N6-succinyllysine; alternateBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ16775.
    PaxDbiQ16775.
    PRIDEiQ16775.

    PTM databases

    PhosphoSiteiQ16775.

    Expressioni

    Tissue specificityi

    Expressed in liver and kidney.1 Publication

    Gene expression databases

    ArrayExpressiQ16775.
    BgeeiQ16775.
    CleanExiHS_HAGH.
    GenevestigatoriQ16775.

    Organism-specific databases

    HPAiCAB033531.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    BioGridi109279. 6 interactions.
    IntActiQ16775. 1 interaction.
    STRINGi9606.ENSP00000380514.

    Structurei

    Secondary structure

    1
    308
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi50 – 567
    Turni57 – 593
    Beta strandi60 – 678
    Turni68 – 714
    Beta strandi72 – 776
    Helixi81 – 9111
    Beta strandi94 – 996
    Helixi105 – 1084
    Helixi111 – 1177
    Beta strandi122 – 1265
    Beta strandi134 – 1363
    Beta strandi142 – 1454
    Beta strandi148 – 1547
    Beta strandi157 – 1593
    Beta strandi163 – 1686
    Beta strandi170 – 1745
    Beta strandi177 – 1815
    Helixi197 – 2059
    Turni206 – 2105
    Beta strandi216 – 2216
    Helixi224 – 23411
    Helixi239 – 25416
    Helixi263 – 2697
    Turni271 – 2766
    Helixi278 – 2847
    Helixi289 – 30214

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1QH3X-ray1.90A/B49-308[»]
    1QH5X-ray1.45A/B49-308[»]
    2F50model-A64-225[»]
    ProteinModelPortaliQ16775.
    SMRiQ16775. Positions 49-308.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ16775.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni191 – 1933Substrate binding
    Regioni221 – 2233Substrate binding
    Regioni297 – 3004Substrate binding

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0491.
    HOGENOMiHOG000058041.
    HOVERGENiHBG001152.
    InParanoidiQ16775.
    KOiK01069.
    OMAiSTPCHTT.
    PhylomeDBiQ16775.
    TreeFamiTF105273.

    Family and domain databases

    Gene3Di3.60.15.10. 1 hit.
    HAMAPiMF_01374. Glyoxalase_2.
    InterProiIPR001279. Beta-lactamas-like.
    IPR017782. Hydroxyacylglutathione_Hdrlase.
    [Graphical view]
    PfamiPF00753. Lactamase_B. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005457. Glx. 1 hit.
    SMARTiSM00849. Lactamase_B. 1 hit.
    [Graphical view]
    SUPFAMiSSF56281. SSF56281. 1 hit.
    TIGRFAMsiTIGR03413. GSH_gloB. 1 hit.

    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 and alternative initiation. Align

    Isoform 1 (identifier: Q16775-1) [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

    MVVGRGLLGR RSLAALGAAC ARRGLGPALL GVFCHTDLRK NLTVDEGTMK    50
    VEVLPALTDN YMYLVIDDET KEAAIVDPVQ PQKVVDAARK HGVKLTTVLT 100
    THHHWDHAGG NEKLVKLESG LKVYGGDDRI GALTHKITHL STLQVGSLNV 150
    KCLATPCHTS GHICYFVSKP GGSEPPAVFT GDTLFVAGCG KFYEGTADEM 200
    CKALLEVLGR LPPDTRVYCG HEYTINNLKF ARHVEPGNAA IREKLAWAKE 250
    KYSIGEPTVP STLAEEFTYN PFMRVREKTV QQHAGETDPV TTMRAVRREK 300
    DQFKMPRD 308
    Length:308
    Mass (Da):33,806
    Last modified:September 1, 2009 - v2
    Checksum:i64E5C214B6EC61CB
    GO
    Isoform 2 (identifier: Q16775-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-48: Missing.

    Note: Produced by alternative splicing. Also produced by alternative initiation at Met-49 of isoform 1.

    Show »
    Length:260
    Mass (Da):28,860
    Checksum:i4C3DEC87FB27A1D2
    GO
    Isoform 3 (identifier: Q16775-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         146-236: GSLNVKCLAT...NLKFARHVEP → TPCLWLAAGS...WQRSLPTTPS
         237-308: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:236
    Mass (Da):25,455
    Checksum:i25A00E2EAD5E9A15
    GO

    Sequence cautioni

    The sequence AAH00840.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAA62483.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti67 – 671D → G in BAG60445. (PubMed:14702039)Curated
    Sequence conflicti121 – 1211L → P in BAG61219. (PubMed:14702039)Curated
    Sequence conflicti202 – 2021K → E in BAF82844. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4848Missing in isoform 2. 1 PublicationVSP_037929Add
    BLAST
    Alternative sequencei146 – 23691GSLNV…RHVEP → TPCLWLAAGSSMKGLRMRCV KLCWRSWAGSPRTQESTVAT STPSTTSSLHATWSPAMPPS GRSWPGPRRSTASGSPQCHP PWQRSLPTTPS in isoform 3. 1 PublicationVSP_055199Add
    BLAST
    Alternative sequencei237 – 30872Missing in isoform 3. 1 PublicationVSP_055200Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK290155 mRNA. Translation: BAF82844.1.
    AK298174 mRNA. Translation: BAG60445.1.
    AK299173 mRNA. Translation: BAG61219.1.
    AE006639 Genomic DNA. Translation: AAK61294.1.
    AC012180 Genomic DNA. No translation available.
    BC000840 mRNA. Translation: AAH00840.1. Different initiation.
    BC002627 mRNA. Translation: AAH02627.2.
    X90999 mRNA. Translation: CAA62483.1. Different initiation.
    CCDSiCCDS10447.2. [Q16775-1]
    CCDS32366.1. [Q16775-2]
    CCDS66900.1. [Q16775-3]
    RefSeqiNP_001035517.1. NM_001040427.1. [Q16775-2]
    NP_001273178.1. NM_001286249.1.
    NP_005317.2. NM_005326.4. [Q16775-1]
    UniGeneiHs.157394.

    Genome annotation databases

    EnsembliENST00000397353; ENSP00000380511; ENSG00000063854. [Q16775-2]
    ENST00000397356; ENSP00000380514; ENSG00000063854. [Q16775-1]
    ENST00000455446; ENSP00000406552; ENSG00000063854. [Q16775-3]
    GeneIDi3029.
    KEGGihsa:3029.
    UCSCiuc002cmz.3. human. [Q16775-1]

    Polymorphism databases

    DMDMi257051015.

    Keywords - Coding sequence diversityi

    Alternative initiation, Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK290155 mRNA. Translation: BAF82844.1 .
    AK298174 mRNA. Translation: BAG60445.1 .
    AK299173 mRNA. Translation: BAG61219.1 .
    AE006639 Genomic DNA. Translation: AAK61294.1 .
    AC012180 Genomic DNA. No translation available.
    BC000840 mRNA. Translation: AAH00840.1 . Different initiation.
    BC002627 mRNA. Translation: AAH02627.2 .
    X90999 mRNA. Translation: CAA62483.1 . Different initiation.
    CCDSi CCDS10447.2. [Q16775-1 ]
    CCDS32366.1. [Q16775-2 ]
    CCDS66900.1. [Q16775-3 ]
    RefSeqi NP_001035517.1. NM_001040427.1. [Q16775-2 ]
    NP_001273178.1. NM_001286249.1.
    NP_005317.2. NM_005326.4. [Q16775-1 ]
    UniGenei Hs.157394.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1QH3 X-ray 1.90 A/B 49-308 [» ]
    1QH5 X-ray 1.45 A/B 49-308 [» ]
    2F50 model - A 64-225 [» ]
    ProteinModelPortali Q16775.
    SMRi Q16775. Positions 49-308.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109279. 6 interactions.
    IntActi Q16775. 1 interaction.
    STRINGi 9606.ENSP00000380514.

    Chemistry

    BindingDBi Q16775.
    ChEMBLi CHEMBL2261.
    DrugBanki DB00143. Glutathione.

    PTM databases

    PhosphoSitei Q16775.

    Polymorphism databases

    DMDMi 257051015.

    Proteomic databases

    MaxQBi Q16775.
    PaxDbi Q16775.
    PRIDEi Q16775.

    Protocols and materials databases

    DNASUi 3029.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000397353 ; ENSP00000380511 ; ENSG00000063854 . [Q16775-2 ]
    ENST00000397356 ; ENSP00000380514 ; ENSG00000063854 . [Q16775-1 ]
    ENST00000455446 ; ENSP00000406552 ; ENSG00000063854 . [Q16775-3 ]
    GeneIDi 3029.
    KEGGi hsa:3029.
    UCSCi uc002cmz.3. human. [Q16775-1 ]

    Organism-specific databases

    CTDi 3029.
    GeneCardsi GC16M001845.
    HGNCi HGNC:4805. HAGH.
    HPAi CAB033531.
    MIMi 138760. gene+phenotype.
    neXtProti NX_Q16775.
    PharmGKBi PA29179.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0491.
    HOGENOMi HOG000058041.
    HOVERGENi HBG001152.
    InParanoidi Q16775.
    KOi K01069.
    OMAi STPCHTT.
    PhylomeDBi Q16775.
    TreeFami TF105273.

    Enzyme and pathway databases

    UniPathwayi UPA00619 ; UER00676 .
    BRENDAi 3.1.2.6. 5596.
    SABIO-RK Q16775.

    Miscellaneous databases

    EvolutionaryTracei Q16775.
    GeneWikii HAGH.
    GenomeRNAii 3029.
    NextBioi 11990.
    PROi Q16775.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q16775.
    Bgeei Q16775.
    CleanExi HS_HAGH.
    Genevestigatori Q16775.

    Family and domain databases

    Gene3Di 3.60.15.10. 1 hit.
    HAMAPi MF_01374. Glyoxalase_2.
    InterProi IPR001279. Beta-lactamas-like.
    IPR017782. Hydroxyacylglutathione_Hdrlase.
    [Graphical view ]
    Pfami PF00753. Lactamase_B. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF005457. Glx. 1 hit.
    SMARTi SM00849. Lactamase_B. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56281. SSF56281. 1 hit.
    TIGRFAMsi TIGR03413. GSH_gloB. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "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] (ISOFORMS 1; 2 AND 3).
      Tissue: Thalamus.
    2. "Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16."
      Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.
      Hum. Mol. Genet. 10:339-352(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] (ISOFORM 1).
      Tissue: Cervix and Uterus.
    5. "Molecular cloning, heterologous expression, and characterization of human glyoxalase II."
      Ridderstroem M., Saccucci F., Hellman U., Bergman T., Principato G., Mannervik B.
      J. Biol. Chem. 271:319-323(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 37-308 (ISOFORMS 1/2).
      Tissue: Liver.
    6. "The human hydroxyacylglutathione hydrolase (HAGH) gene encodes both cytosolic and mitochondrial forms of glyoxalase II."
      Cordell P.A., Futers T.S., Grant P.J., Pease R.J.
      J. Biol. Chem. 279:28653-28661(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, ALTERNATIVE INITIATION, ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
    7. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-229, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue."
      Cameron A.D., Ridderstroem M., Olin B., Mannervik B.
      Structure 7:1067-1077(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 49-308 IN COMPLEX WITH SUBSTRATE ANALOGS AND ZINC IONS.
      Tissue: Liver.

    Entry informationi

    Entry nameiGLO2_HUMAN
    AccessioniPrimary (citable) accession number: Q16775
    Secondary accession number(s): A8K290
    , B4DP33, B4DRA7, E7EN93
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: September 1, 2009
    Last modified: October 1, 2014
    This is version 134 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3