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Q04760

- LGUL_HUMAN

UniProt

Q04760 - LGUL_HUMAN

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Protein
Lactoylglutathione lyase
Gene
GLO1
Organism
Homo sapiens (Human)
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.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)

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

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

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 – 1231Substrate
Metal bindingi127 – 1271Zinc; via tele nitrogen
Binding sitei127 – 1271Substrate
Active sitei173 – 1731Proton donor/acceptor2 Publications
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: 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
Complete GO annotation...

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
Complete GO annotation...

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 – 11Removed1 Publication
Chaini2 – 184183Lactoylglutathione lyase
PRO_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-succinyllysine By similarity
Modified residuei107 – 1071Phosphothreonine1 Publication
Modified residuei139 – 1391S-glutathionyl cysteine; alternate
Modified residuei148 – 1481N6-acetyllysine; alternate1 Publication
Modified residuei148 – 1481N6-succinyllysine; alternate By similarity

Post-translational modificationi

Glutathionylation at Cys-139 inhibits enzyme activity.
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.2 Publications

Protein-protein interaction databases

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

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiQ04760.

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the glyoxalase I family.

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.
VSP_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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 154 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

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