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Q9CPU0

- LGUL_MOUSE

UniProt

Q9CPU0 - LGUL_MOUSE

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Protein

Lactoylglutathione lyase

Gene

Glo1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
Complete GO annotation...

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

BgeeiQ9CPU0.
CleanExiMM_GLO1.
ExpressionAtlasiQ9CPU0. baseline and differential.
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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAEPQPASSG LTDETAFSCC SDPDPSTKDF LLQQTMLRIK DPKKSLDFYT
60 70 80 90 100
RVLGLTLLQK LDFPAMKFSL YFLAYEDKND IPKDKSEKTA WTFSRKATLE
110 120 130 140 150
LTHNWGTEDD ETQSYHNGNS DPRGFGHIGI AVPDVYSACK RFEELGVKFV
160 170 180
KKPDDGKMKG LAFIQDPDGY WIEILNPNKI ATII
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

Bgeei Q9CPU0.
CleanExi MM_GLO1.
ExpressionAtlasi Q9CPU0. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 121 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