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Q04760

- LGUL_HUMAN

UniProt

Q04760 - LGUL_HUMAN

Protein

Lactoylglutathione lyase

Gene

GLO1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 4 (06 Mar 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. Involved in the regulation of TNF-induced transcriptional activity of NF-kappa-B. Required for normal osteoclastogenesis.3 Publications

    Catalytic activityi

    (R)-S-lactoylglutathione = glutathione + methylglyoxal.2 Publications

    Cofactori

    Binds 1 zinc ion per subunit. In the homodimer, two zinc ions are bound between subunits.2 Publications

    Enzyme regulationi

    Regulated by oxidation of Cys-139 in response to the redox state of the cell. Results in the alternative formation of cystine or glutathione-bound cysteine, the latter modification leading to reduced enzyme activity.1 Publication

    Kineticsi

    Reduction of GLO1 was carried out by incubation with 20 mM betamercaptoethanol prior to kinetic analysis.

    1. KM=1.3 mM for methylglyoxal/glutathione (native form)1 Publication
    2. KM=0.7 mM for methylglyoxal/glutathione (reduced form)1 Publication

    Vmax=0.335 µmol/min/mg enzyme with methylglyoxal/glutathione as substrate (native form)1 Publication

    Vmax=0.7 µmol/min/mg enzyme with methylglyoxal/glutathione as substrate (reduced form)1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi34 – 341Zinc; shared with dimeric partner3 Publications
    Binding sitei34 – 341Substrate; shared with dimeric partner
    Binding sitei38 – 381Substrate; shared with dimeric partner
    Metal bindingi100 – 1001Zinc; shared with dimeric partner3 Publications
    Binding sitei104 – 1041Substrate; shared with dimeric partner
    Binding sitei123 – 1231Substrate
    Metal bindingi127 – 1271Zinc; via tele nitrogen3 Publications
    Binding sitei127 – 1271Substrate
    Active sitei173 – 1731Proton donor/acceptor2 Publications
    Metal bindingi173 – 1731Zinc3 Publications

    GO - Molecular functioni

    1. lactoylglutathione lyase activity Source: UniProtKB
    2. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. carbohydrate metabolic process Source: ProtInc
    2. glutathione metabolic process Source: Ensembl
    3. methylglyoxal metabolic process Source: Ensembl
    4. negative regulation of apoptotic process Source: UniProtKB
    5. osteoclast differentiation Source: UniProtKB
    6. regulation of transcription from RNA polymerase II promoter Source: Ensembl

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi4.4.1.5. 2681.
    SABIO-RKQ04760.
    UniPathwayiUPA00619; UER00675.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lactoylglutathione lyase (EC:4.4.1.5)
    Alternative name(s):
    Aldoketomutase
    Glyoxalase I
    Short name:
    Glx I
    Ketone-aldehyde mutase
    Methylglyoxalase
    S-D-lactoylglutathione methylglyoxal lyase
    Gene namesi
    Name:GLO1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:4323. GLO1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. extracellular vesicular exosome Source: UniProt

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi19 – 191C → A: No effect on NO-mediated modification. Impaired NO-mediated modification; when associated with A-20. Loss of NO-mediated modification; when associated with A-139. 2 Publications
    Mutagenesisi20 – 201C → A: No effect on NO-mediated modification. Impaired NO-mediated modification; when associated with A-19. Loss of NO-mediated modification; when associated with A-139. 2 Publications
    Mutagenesisi34 – 341Q → E: Reduces enzyme activity by 99%. 1 Publication
    Mutagenesisi45 – 451S → A: No effect on phosphorylation. 1 Publication
    Mutagenesisi61 – 611C → A: No effect on NO-mediated modification. 1 Publication
    Mutagenesisi69 – 691S → A: No effect on phosphorylation. 1 Publication
    Mutagenesisi94 – 941S → A: No effect on phosphorylation. 1 Publication
    Mutagenesisi98 – 981T → A: No effect on phosphorylation. 1 Publication
    Mutagenesisi100 – 1001E → Q: Reduces enzyme activity by over 99%. 1 Publication
    Mutagenesisi102 – 1021T → A: No effect on phosphorylation. 1 Publication
    Mutagenesisi107 – 1071T → A: Loss of phosphorylation. 1 Publication
    Mutagenesisi139 – 1391C → A: Impaired NO-mediated modification. Loss of NO-mediated modification; when associated with A-19 or A-20. 2 Publications
    Mutagenesisi173 – 1731E → Q: Abolishes enzyme activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA28724.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 184183Lactoylglutathione lyasePRO_0000168076Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Disulfide bondi19 ↔ 201 Publication
    Disulfide bondi61 ↔ 139Alternate1 Publication
    Modified residuei88 – 881N6-succinyllysineBy similarity
    Modified residuei107 – 1071Phosphothreonine2 Publications
    Modified residuei139 – 1391S-glutathionyl cysteine; alternate1 Publication
    Modified residuei148 – 1481N6-acetyllysine; alternate1 Publication
    Modified residuei148 – 1481N6-succinyllysine; alternateBy similarity

    Post-translational modificationi

    Glutathionylation at Cys-139 inhibits enzyme activity.1 Publication
    Phosphorylated at Thr-107 in the presence of CaMK2. However, this is a consensus site for phosphorylation by CK2 so phosphorylation may be mediated by CK2 rather than CaMK2. Phosphorylation is induced by TNF and suppresses the TNF-induced transcriptional activity of NF-kappa-B.2 Publications
    Exists in a nitric oxide (NO)-modified form. The exact nature of the modification is unknown, but it suppresses the TNF-induced transcriptional activity of NF-kappa-B.

    Keywords - PTMi

    Acetylation, Disulfide bond, Glutathionylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ04760.
    PaxDbiQ04760.
    PRIDEiQ04760.

    2D gel databases

    OGPiQ04760.
    REPRODUCTION-2DPAGEIPI00220766.
    Q04760.

    PTM databases

    PhosphoSiteiQ04760.

    Expressioni

    Gene expression databases

    BgeeiQ04760.
    CleanExiHS_GLO1.
    GenevestigatoriQ04760.

    Organism-specific databases

    HPAiCAB040541.
    CAB040542.

    Interactioni

    Subunit structurei

    Homodimer.3 Publications

    Protein-protein interaction databases

    BioGridi109001. 9 interactions.
    IntActiQ04760. 3 interactions.
    STRINGi9606.ENSP00000362463.

    Structurei

    Secondary structure

    1
    184
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi13 – 186
    Helixi25 – 273
    Beta strandi31 – 388
    Helixi42 – 5110
    Beta strandi56 – 638
    Turni64 – 674
    Beta strandi68 – 758
    Helixi78 – 803
    Helixi85 – 928
    Beta strandi95 – 10410
    Helixi107 – 1093
    Beta strandi118 – 1225
    Beta strandi124 – 1318
    Helixi135 – 14410
    Beta strandi149 – 1513
    Beta strandi155 – 1584
    Beta strandi162 – 1654
    Beta strandi171 – 1755
    Helixi177 – 1793
    Helixi181 – 1833

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BH5X-ray2.20A/B/C/D2-184[»]
    1FROX-ray2.20A/B/C/D2-184[»]
    1QINX-ray2.00A/B2-184[»]
    1QIPX-ray1.72A/B/C/D2-184[»]
    3VW9X-ray1.47A/B1-184[»]
    3W0TX-ray1.35A/B/C/D1-184[»]
    3W0UX-ray1.70A/B1-184[»]
    ProteinModelPortaliQ04760.
    SMRiQ04760. Positions 3-184.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ04760.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni157 – 1582Substrate binding

    Sequence similaritiesi

    Belongs to the glyoxalase I family.Curated

    Phylogenomic databases

    eggNOGiCOG0346.
    HOVERGENiHBG025852.
    InParanoidiQ04760.
    KOiK01759.
    OMAiWALSRKA.
    OrthoDBiEOG7XPZ6W.
    PhylomeDBiQ04760.
    TreeFamiTF105011.

    Family and domain databases

    Gene3Di3.10.180.10. 1 hit.
    InterProiIPR029068. Glyas_Bleomycin-R_OHBP_Dase.
    IPR004360. Glyas_Fos-R_dOase_dom.
    IPR004361. Glyoxalase_1.
    IPR018146. Glyoxalase_1_CS.
    [Graphical view]
    PfamiPF00903. Glyoxalase. 1 hit.
    [Graphical view]
    SUPFAMiSSF54593. SSF54593. 1 hit.
    TIGRFAMsiTIGR00068. glyox_I. 1 hit.
    PROSITEiPS00934. GLYOXALASE_I_1. 1 hit.
    PS00935. GLYOXALASE_I_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q04760-1) [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

    MAEPQPPSGG LTDEAALSCC SDADPSTKDF LLQQTMLRVK DPKKSLDFYT    50
    RVLGMTLIQK CDFPIMKFSL YFLAYEDKND IPKEKDEKIA WALSRKATLE 100
    LTHNWGTEDD ETQSYHNGNS DPRGFGHIGI AVPDVYSACK RFEELGVKFV 150
    KKPDDGKMKG LAFIQDPDGY WIEILNPNKM ATLM 184
    Length:184
    Mass (Da):20,778
    Last modified:March 6, 2007 - v4
    Checksum:i46291B7878070028
    GO
    Isoform 2 (identifier: Q04760-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         105-119: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:169
    Mass (Da):19,043
    Checksum:i24175E1D1C817515
    GO

    Sequence cautioni

    The sequence BAD93038.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Mass spectrometryi

    Isoform 1 : Molecular mass is 20687.4 Da from positions 2 - 184. Determined by ESI. Variant Glu-111.1 Publication
    Isoform 1 : Molecular mass is 20629.7 Da from positions 2 - 184. Determined by ESI. Variant Ala-111.1 Publication

    Polymorphismi

    Exists in three separable isoforms which originate from two alleles in the genome. These correspond to two homodimers and one heterodimer composed of two subunits showing different electrophoretic properties.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti19 – 191C → Y.2 Publications
    Corresponds to variant rs17855424 [ dbSNP | Ensembl ].
    VAR_031078
    Natural varianti111 – 1111E → A.5 Publications
    Corresponds to variant rs4746 [ dbSNP | Ensembl ].
    VAR_013481

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei105 – 11915Missing in isoform 2. 1 PublicationVSP_041632Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D13315 mRNA. Translation: BAA02572.1.
    L07837 mRNA. Translation: AAA52565.1.
    S83285 mRNA. Translation: AAB49495.1.
    AF146651 Genomic DNA. Translation: AAD38008.1.
    AB209801 mRNA. Translation: BAD93038.1. Different initiation.
    AK293345 mRNA. Translation: BAG56861.1.
    AK312662 mRNA. Translation: BAG35544.1.
    BT019987 mRNA. Translation: AAV38790.1.
    BT019988 mRNA. Translation: AAV38791.1.
    AL391415 Genomic DNA. Translation: CAI21586.1.
    BC001741 mRNA. Translation: AAH01741.1.
    BC011365 mRNA. Translation: AAH11365.1.
    BC015934 mRNA. Translation: AAH15934.1.
    CCDSiCCDS4837.1. [Q04760-1]
    PIRiA46714.
    S63603.
    RefSeqiNP_006699.2. NM_006708.2. [Q04760-1]
    UniGeneiHs.268849.

    Genome annotation databases

    EnsembliENST00000373365; ENSP00000362463; ENSG00000124767. [Q04760-1]
    GeneIDi2739.
    KEGGihsa:2739.
    UCSCiuc003ooc.3. human. [Q04760-1]

    Polymorphism databases

    DMDMi134039205.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D13315 mRNA. Translation: BAA02572.1 .
    L07837 mRNA. Translation: AAA52565.1 .
    S83285 mRNA. Translation: AAB49495.1 .
    AF146651 Genomic DNA. Translation: AAD38008.1 .
    AB209801 mRNA. Translation: BAD93038.1 . Different initiation.
    AK293345 mRNA. Translation: BAG56861.1 .
    AK312662 mRNA. Translation: BAG35544.1 .
    BT019987 mRNA. Translation: AAV38790.1 .
    BT019988 mRNA. Translation: AAV38791.1 .
    AL391415 Genomic DNA. Translation: CAI21586.1 .
    BC001741 mRNA. Translation: AAH01741.1 .
    BC011365 mRNA. Translation: AAH11365.1 .
    BC015934 mRNA. Translation: AAH15934.1 .
    CCDSi CCDS4837.1. [Q04760-1 ]
    PIRi A46714.
    S63603.
    RefSeqi NP_006699.2. NM_006708.2. [Q04760-1 ]
    UniGenei Hs.268849.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BH5 X-ray 2.20 A/B/C/D 2-184 [» ]
    1FRO X-ray 2.20 A/B/C/D 2-184 [» ]
    1QIN X-ray 2.00 A/B 2-184 [» ]
    1QIP X-ray 1.72 A/B/C/D 2-184 [» ]
    3VW9 X-ray 1.47 A/B 1-184 [» ]
    3W0T X-ray 1.35 A/B/C/D 1-184 [» ]
    3W0U X-ray 1.70 A/B 1-184 [» ]
    ProteinModelPortali Q04760.
    SMRi Q04760. Positions 3-184.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109001. 9 interactions.
    IntActi Q04760. 3 interactions.
    STRINGi 9606.ENSP00000362463.

    Chemistry

    BindingDBi Q04760.
    ChEMBLi CHEMBL2424.
    DrugBanki DB00143. Glutathione.

    PTM databases

    PhosphoSitei Q04760.

    Polymorphism databases

    DMDMi 134039205.

    2D gel databases

    OGPi Q04760.
    REPRODUCTION-2DPAGE IPI00220766.
    Q04760.

    Proteomic databases

    MaxQBi Q04760.
    PaxDbi Q04760.
    PRIDEi Q04760.

    Protocols and materials databases

    DNASUi 2739.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000373365 ; ENSP00000362463 ; ENSG00000124767 . [Q04760-1 ]
    GeneIDi 2739.
    KEGGi hsa:2739.
    UCSCi uc003ooc.3. human. [Q04760-1 ]

    Organism-specific databases

    CTDi 2739.
    GeneCardsi GC06M038643.
    HGNCi HGNC:4323. GLO1.
    HPAi CAB040541.
    CAB040542.
    MIMi 138750. gene.
    neXtProti NX_Q04760.
    PharmGKBi PA28724.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0346.
    HOVERGENi HBG025852.
    InParanoidi Q04760.
    KOi K01759.
    OMAi WALSRKA.
    OrthoDBi EOG7XPZ6W.
    PhylomeDBi Q04760.
    TreeFami TF105011.

    Enzyme and pathway databases

    UniPathwayi UPA00619 ; UER00675 .
    BRENDAi 4.4.1.5. 2681.
    SABIO-RK Q04760.

    Miscellaneous databases

    EvolutionaryTracei Q04760.
    GeneWikii GLO1.
    Lactoylglutathione_lyase.
    GenomeRNAii 2739.
    NextBioi 10796.
    PROi Q04760.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q04760.
    CleanExi HS_GLO1.
    Genevestigatori Q04760.

    Family and domain databases

    Gene3Di 3.10.180.10. 1 hit.
    InterProi IPR029068. Glyas_Bleomycin-R_OHBP_Dase.
    IPR004360. Glyas_Fos-R_dOase_dom.
    IPR004361. Glyoxalase_1.
    IPR018146. Glyoxalase_1_CS.
    [Graphical view ]
    Pfami PF00903. Glyoxalase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54593. SSF54593. 1 hit.
    TIGRFAMsi TIGR00068. glyox_I. 1 hit.
    PROSITEi PS00934. GLYOXALASE_I_1. 1 hit.
    PS00935. GLYOXALASE_I_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human glyoxalase I. cDNA cloning, expression, and sequence similarity to glyoxalase I from Pseudomonas putida."
      Kim N.-S., Umezawa Y., Ohmura S., Kato S.
      J. Biol. Chem. 268:11217-11221(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-111.
    2. "Cloning and characterization of human colon glyoxalase-I."
      Ranganathan S., Walsh E.S., Godwin A.K., Tew K.D.
      J. Biol. Chem. 268:5661-5667(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-111.
      Tissue: Colon.
    3. "Optimized heterologous expression of the human zinc enzyme glyoxalase I."
      Ridderstroem M., Mannervik B.
      Biochem. J. 314:463-467(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "Genomic sequence of human glyoxalase-I: analysis of promoter activity and its regulation."
      Ranganathan S., Ciaccio P.J., Walsh E.S., Tew K.D.
      Gene 240:149-155(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-111.
    5. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    6. "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 AND 2), VARIANTS TYR-19 AND ALA-111.
    7. "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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    8. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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), VARIANTS TYR-19 AND ALA-111.
      Tissue: Brain, Eye and Uterus.
    10. "Posttranslational modification of human glyoxalase 1 indicates redox-dependent regulation."
      Birkenmeier G., Stegemann C., Hoffmann R., Gunther R., Huse K., Birkemeyer C.
      PLoS ONE 5:E10399-E10399(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 13-18 AND 128-135, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, GLUTATHIONYLATION AT CYS-139, DISULFIDE BONDS.
      Tissue: Erythrocyte.
    11. "Tumour necrosis factor induces phosphorylation primarily of the nitric-oxide-responsive form of glyoxalase I."
      de Hemptinne V., Rondas D., Vandekerckhove J., Vancompernolle K.
      Biochem. J. 407:121-128(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF NITRIC OXIDE-MODIFIED FORM, PHOSPHORYLATION, MUTAGENESIS OF CYS-19; CYS-20; CYS-61 AND CYS-139.
    12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Phosphorylation on Thr-106 and NO-modification of glyoxalase I suppress the TNF-induced transcriptional activity of NF-kappaB."
      de Hemptinne V., Rondas D., Toepoel M., Vancompernolle K.
      Mol. Cell. Biochem. 325:169-178(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT THR-107, MUTAGENESIS OF CYS-19; CYS-20; SER-45; SER-69; SER-94; THR-98; THR-102; THR-107 AND CYS-139.
    14. "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-148, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Crystal structure of human glyoxalase I -- evidence for gene duplication and 3D domain swapping."
      Cameron A.D., Olin B., Ridderstroem M., Mannervik B., Jones T.A.
      EMBO J. 16:3386-3395(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH S-BENZYL-GLUTATHIONE AND ZINC.
    17. "Involvement of an active-site Zn2+ ligand in the catalytic mechanism of human glyoxalase I."
      Ridderstroem M., Cameron A.D., Jones T.A., Mannervik B.
      J. Biol. Chem. 273:21623-21628(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH ZINC AND S-HEXYLGLUTATHIONE, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, ACTIVE SITE, SUBUNIT, MUTAGENESIS OF GLN-34; GLU-100 AND GLU-173.
    18. "Reaction mechanism of glyoxalase I explored by an X-ray crystallographic analysis of the human enzyme in complex with a transition state analogue."
      Cameron A.D., Ridderstroem M., Olin B., Kavarana M.J., Creighton D.J., Mannervik B.
      Biochemistry 38:13480-13490(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) IN COMPLEXES WITH S-(N-HYDROXY-N-IODOPHENYLCARBAMOYL)GLUTATHIONE; S-P-NITROBENZYLOXYCARBONYLGLUTATHIONE AND ZINC, ACTIVE SITE.
    19. "Design and evaluation of azaindole-substituted N-hydroxypyridones as glyoxalase I inhibitors."
      Chiba T., Ohwada J., Sakamoto H., Kobayashi T., Fukami T.A., Irie M., Miura T., Ohara K., Koyano H.
      Bioorg. Med. Chem. Lett. 22:7486-7489(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS) IN COMPLEX WITH SYNTHETIC INHIBITOR AND ZINC, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR.

    Entry informationi

    Entry nameiLGUL_HUMAN
    AccessioniPrimary (citable) accession number: Q04760
    Secondary accession number(s): B2R6P7
    , B4DDV0, P78375, Q59EL0, Q5TZW3, Q96FC0, Q96J41
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: March 6, 2007
    Last modified: October 1, 2014
    This is version 155 of the entry and version 4 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3