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Q9CPU0

- LGUL_MOUSE

UniProt

Q9CPU0 - LGUL_MOUSE

Protein

Lactoylglutathione lyase

Gene

Glo1

Organism
Mus musculus (Mouse)
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 (23 Jan 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.1 Publication

    Catalytic activityi

    (R)-S-lactoylglutathione = glutathione + methylglyoxal.1 Publication

    Cofactori

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

    Enzyme regulationi

    Subject to competitive inhibition by methyl-gerfelin.1 Publication

    Pathwayi

    Sites

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

    GO - Molecular functioni

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

    GO - Biological processi

    1. carbohydrate metabolic process Source: Ensembl
    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: MGI

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:95742. Glo1.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 184183Lactoylglutathione lyasePRO_0000168078Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Disulfide bondi19 ↔ 20By similarity
    Modified residuei88 – 881N6-succinyllysine1 Publication
    Modified residuei107 – 1071PhosphothreonineBy similarity
    Modified residuei139 – 1391S-glutathionyl cysteineBy similarity
    Modified residuei148 – 1481N6-acetyllysine; alternateBy similarity
    Modified residuei148 – 1481N6-succinyllysine; alternate1 Publication

    Post-translational modificationi

    Glutathionylation at Cys-139 inhibits enzyme activity.By similarity
    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 By similarity.By similarity
    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 By similarity.By similarity

    Keywords - PTMi

    Acetylation, Disulfide bond, Glutathionylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9CPU0.
    PaxDbiQ9CPU0.
    PRIDEiQ9CPU0.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00321734.
    Q9CPU0.
    UCD-2DPAGEQ9CPU0.

    PTM databases

    PhosphoSiteiQ9CPU0.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9CPU0.
    BgeeiQ9CPU0.
    CleanExiMM_GLO1.
    GenevestigatoriQ9CPU0.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    IntActiQ9CPU0. 5 interactions.
    MINTiMINT-2513171.

    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
    Helixi64 – 663
    Beta strandi68 – 758
    Helixi78 – 803
    Helixi85 – 928
    Beta strandi95 – 10410
    Helixi107 – 1093
    Beta strandi118 – 1225
    Beta strandi125 – 1317
    Helixi135 – 14410
    Beta strandi149 – 1513
    Beta strandi155 – 1584
    Beta strandi162 – 1654
    Beta strandi171 – 1755
    Turni177 – 1793
    Helixi180 – 1823

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ZA0X-ray1.70A/B1-184[»]
    4KYHX-ray2.50A/B1-184[»]
    4KYKX-ray2.00A/B1-184[»]
    ProteinModelPortaliQ9CPU0.
    SMRiQ9CPU0. Positions 4-183.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9CPU0.

    Family & Domainsi

    Region

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

    Sequence similaritiesi

    Belongs to the glyoxalase I family.Curated

    Phylogenomic databases

    eggNOGiCOG0346.
    GeneTreeiENSGT00390000009312.
    HOGENOMiHOG000232011.
    HOVERGENiHBG025852.
    InParanoidiQ9CPU0.
    KOiK01759.
    OMAiWALSRKA.
    OrthoDBiEOG7XPZ6W.
    PhylomeDBiQ9CPU0.
    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]

    Sequencei

    Sequence statusi: Complete.

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

    Q9CPU0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAEPQPASSG LTDETAFSCC SDPDPSTKDF LLQQTMLRIK DPKKSLDFYT    50
    RVLGLTLLQK LDFPAMKFSL YFLAYEDKND IPKDKSEKTA WTFSRKATLE 100
    LTHNWGTEDD ETQSYHNGNS DPRGFGHIGI AVPDVYSACK RFEELGVKFV 150
    KKPDDGKMKG LAFIQDPDGY WIEILNPNKI ATII 184
    Length:184
    Mass (Da):20,810
    Last modified:January 23, 2007 - v3
    Checksum:iF6B5667A65454D18
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti92 – 921T → M in AAH24663. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK002386 mRNA. Translation: BAB22060.1.
    AK003567 mRNA. Translation: BAB22863.1.
    AK005055 mRNA. Translation: BAB23781.1.
    AK031832 mRNA. Translation: BAC27570.1.
    AK049703 mRNA. Translation: BAC33882.1.
    BC024663 mRNA. Translation: AAH24663.1.
    BC081432 mRNA. Translation: AAH81432.1.
    CCDSiCCDS28600.1.
    RefSeqiNP_001107032.1. NM_001113560.1.
    NP_079650.3. NM_025374.3.
    UniGeneiMm.261984.

    Genome annotation databases

    EnsembliENSMUST00000024823; ENSMUSP00000024823; ENSMUSG00000024026.
    ENSMUST00000167624; ENSMUSP00000126586; ENSMUSG00000024026.
    GeneIDi109801.
    KEGGimmu:109801.
    UCSCiuc012aos.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK002386 mRNA. Translation: BAB22060.1 .
    AK003567 mRNA. Translation: BAB22863.1 .
    AK005055 mRNA. Translation: BAB23781.1 .
    AK031832 mRNA. Translation: BAC27570.1 .
    AK049703 mRNA. Translation: BAC33882.1 .
    BC024663 mRNA. Translation: AAH24663.1 .
    BC081432 mRNA. Translation: AAH81432.1 .
    CCDSi CCDS28600.1.
    RefSeqi NP_001107032.1. NM_001113560.1.
    NP_079650.3. NM_025374.3.
    UniGenei Mm.261984.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2ZA0 X-ray 1.70 A/B 1-184 [» ]
    4KYH X-ray 2.50 A/B 1-184 [» ]
    4KYK X-ray 2.00 A/B 1-184 [» ]
    ProteinModelPortali Q9CPU0.
    SMRi Q9CPU0. Positions 4-183.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9CPU0. 5 interactions.
    MINTi MINT-2513171.

    Chemistry

    ChEMBLi CHEMBL2175.

    PTM databases

    PhosphoSitei Q9CPU0.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00321734.
    Q9CPU0.
    UCD-2DPAGE Q9CPU0.

    Proteomic databases

    MaxQBi Q9CPU0.
    PaxDbi Q9CPU0.
    PRIDEi Q9CPU0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000024823 ; ENSMUSP00000024823 ; ENSMUSG00000024026 .
    ENSMUST00000167624 ; ENSMUSP00000126586 ; ENSMUSG00000024026 .
    GeneIDi 109801.
    KEGGi mmu:109801.
    UCSCi uc012aos.1. mouse.

    Organism-specific databases

    CTDi 2739.
    MGIi MGI:95742. Glo1.

    Phylogenomic databases

    eggNOGi COG0346.
    GeneTreei ENSGT00390000009312.
    HOGENOMi HOG000232011.
    HOVERGENi HBG025852.
    InParanoidi Q9CPU0.
    KOi K01759.
    OMAi WALSRKA.
    OrthoDBi EOG7XPZ6W.
    PhylomeDBi Q9CPU0.
    TreeFami TF105011.

    Enzyme and pathway databases

    UniPathwayi UPA00619 ; UER00675 .

    Miscellaneous databases

    ChiTaRSi GLO1. mouse.
    EvolutionaryTracei Q9CPU0.
    NextBioi 362781.
    PROi Q9CPU0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9CPU0.
    Bgeei Q9CPU0.
    CleanExi MM_GLO1.
    Genevestigatori Q9CPU0.

    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. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Embryo, Kidney, Liver, Medulla oblongata and Spinal cord.
    2. "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].
      Strain: C57BL/6 and Czech II.
      Tissue: Brain and Mammary gland.
    3. "Identification of glyoxalase-I as a protein marker in a mouse model of extremes in trait anxiety."
      Kroemer S.A., Kessler M.S., Milfay D., Birg I.N., Bunck M., Czibere L., Panhuysen M., Puetz B., Deussing J.M., Holsboer F., Landgraf R., Turck C.W.
      J. Neurosci. 25:4375-4384(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, EXPRESSION IN CD-1 STRAIN.
    4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-88 AND LYS-148, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    5. "The identification of an osteoclastogenesis inhibitor through the inhibition of glyoxalase I."
      Kawatani M., Okumura H., Honda K., Kanoh N., Muroi M., Dohmae N., Takami M., Kitagawa M., Futamura Y., Imoto M., Osada H.
      Proc. Natl. Acad. Sci. U.S.A. 105:11691-11696(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH METHYL-GERFELIN, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, SUBUNIT.

    Entry informationi

    Entry nameiLGUL_MOUSE
    AccessioniPrimary (citable) accession number: Q9CPU0
    Secondary accession number(s): Q543L3, Q8R3T1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 6, 2002
    Last sequence update: January 23, 2007
    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

    Miscellaneousi

    Miscellaneous

    Expressed at higher levels in CD-1 mice which have been bred for low-anxiety-related behavior than in those which have been bred for high-anxiety-related behavior.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3