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Protein

Glutaredoxin-1

Gene

Glrx

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

Functioni

Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Enzyme and pathway databases

ReactomeiR-MMU-499943. Synthesis and interconversion of nucleotide di- and triphosphates.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutaredoxin-1
Alternative name(s):
Thioltransferase-1
Short name:
TTase-1
Gene namesi
Name:Glrx
Synonyms:Glrx1, Grx, Grx1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:2135625. Glrx.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI
  • mitochondrion Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi23 – 231C → S: Loss of activity. 1 Publication
Mutagenesisi26 – 261C → S: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 107106Glutaredoxin-1PRO_0000141601Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei9 – 91N6-succinyllysineCombined sources
Disulfide bondi23 ↔ 26Redox-active
Disulfide bondi79 ↔ 83By similarity

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

EPDiQ9QUH0.
MaxQBiQ9QUH0.
PaxDbiQ9QUH0.
PRIDEiQ9QUH0.

PTM databases

iPTMnetiQ9QUH0.
PhosphoSiteiQ9QUH0.
SwissPalmiQ9QUH0.

Expressioni

Gene expression databases

BgeeiQ9QUH0.
CleanExiMM_GLRX.
ExpressionAtlasiQ9QUH0. baseline and differential.
GenevisibleiQ9QUH0. MM.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000022082.

Structurei

3D structure databases

ProteinModelPortaliQ9QUH0.
SMRiQ9QUH0. Positions 2-106.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 106104GlutaredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glutaredoxin family.Curated
Contains 1 glutaredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiKOG1752. Eukaryota.
COG0695. LUCA.
GeneTreeiENSGT00390000003677.
HOGENOMiHOG000095204.
HOVERGENiHBG000283.
InParanoidiQ9QUH0.
KOiK03676.
OMAiVFIGEEC.
OrthoDBiEOG7QRQWZ.
PhylomeDBiQ9QUH0.
TreeFamiTF326994.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR011767. GLR_AS.
IPR002109. Glutaredoxin.
IPR011899. Glutaredoxin_euk/vir.
IPR014025. Glutaredoxin_subgr.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00462. Glutaredoxin. 1 hit.
[Graphical view]
PRINTSiPR00160. GLUTAREDOXIN.
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR02180. GRX_euk. 1 hit.
PROSITEiPS00195. GLUTAREDOXIN_1. 1 hit.
PS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9QUH0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQEFVNCKI QSGKVVVFIK PTCPYCRKTQ EILSQLPFKQ GLLEFVDITA
60 70 80 90 100
TNNTSAIQDY LQQLTGARTV PRVFIGKDCI GGCSDLISMQ QTGELMTRLK

QIGALQL
Length:107
Mass (Da):11,871
Last modified:January 23, 2007 - v3
Checksum:iDC0C7718DCD8805F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB013137 mRNA. Translation: BAA86926.1.
AF109314 mRNA. Translation: AAF04780.1.
AF276917 mRNA. Translation: AAF86464.1.
BC012642 mRNA. Translation: AAH12642.1.
CCDSiCCDS26651.1.
RefSeqiNP_444338.2. NM_053108.4.
XP_006517540.1. XM_006517477.1.
UniGeneiMm.25844.

Genome annotation databases

EnsembliENSMUST00000022082; ENSMUSP00000022082; ENSMUSG00000021591.
GeneIDi93692.
KEGGimmu:93692.
UCSCiuc007rfx.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB013137 mRNA. Translation: BAA86926.1.
AF109314 mRNA. Translation: AAF04780.1.
AF276917 mRNA. Translation: AAF86464.1.
BC012642 mRNA. Translation: AAH12642.1.
CCDSiCCDS26651.1.
RefSeqiNP_444338.2. NM_053108.4.
XP_006517540.1. XM_006517477.1.
UniGeneiMm.25844.

3D structure databases

ProteinModelPortaliQ9QUH0.
SMRiQ9QUH0. Positions 2-106.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000022082.

PTM databases

iPTMnetiQ9QUH0.
PhosphoSiteiQ9QUH0.
SwissPalmiQ9QUH0.

Proteomic databases

EPDiQ9QUH0.
MaxQBiQ9QUH0.
PaxDbiQ9QUH0.
PRIDEiQ9QUH0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022082; ENSMUSP00000022082; ENSMUSG00000021591.
GeneIDi93692.
KEGGimmu:93692.
UCSCiuc007rfx.2. mouse.

Organism-specific databases

CTDi2745.
MGIiMGI:2135625. Glrx.

Phylogenomic databases

eggNOGiKOG1752. Eukaryota.
COG0695. LUCA.
GeneTreeiENSGT00390000003677.
HOGENOMiHOG000095204.
HOVERGENiHBG000283.
InParanoidiQ9QUH0.
KOiK03676.
OMAiVFIGEEC.
OrthoDBiEOG7QRQWZ.
PhylomeDBiQ9QUH0.
TreeFamiTF326994.

Enzyme and pathway databases

ReactomeiR-MMU-499943. Synthesis and interconversion of nucleotide di- and triphosphates.

Miscellaneous databases

PROiQ9QUH0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QUH0.
CleanExiMM_GLRX.
ExpressionAtlasiQ9QUH0. baseline and differential.
GenevisibleiQ9QUH0. MM.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR011767. GLR_AS.
IPR002109. Glutaredoxin.
IPR011899. Glutaredoxin_euk/vir.
IPR014025. Glutaredoxin_subgr.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00462. Glutaredoxin. 1 hit.
[Graphical view]
PRINTSiPR00160. GLUTAREDOXIN.
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR02180. GRX_euk. 1 hit.
PROSITEiPS00195. GLUTAREDOXIN_1. 1 hit.
PS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse glutaredoxin -- cDNA cloning, high level expression in E. coli and its possible implication in redox regulation of the DNA binding activity in transcription factor PEBP2."
    Nakamura T., Ohno T., Hirota K., Nishiyama A., Nakamura H., Wada H., Yodoi J.
    Free Radic. Res. 31:357-365(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS.
    Tissue: Spleen.
  2. "Cloning and sequencing of mouse glutaredoxin (grx) cDNA."
    Miranda-Vizuete A., Pedrajas J.R., Damdimopoulos A.E., Spyrou G.
    DNA Seq. 10:179-182(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  3. Reddy P.G., Bhuyan D.K., Bhuyan K.C.
    Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: CFW.
    Tissue: Lens.
  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].
    Strain: FVB/N.
    Tissue: Colon.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  6. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-9, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiGLRX1_MOUSE
AccessioniPrimary (citable) accession number: Q9QUH0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 129 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.