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Glutaredoxin-2, mitochondrial

 GLRX2_HUMAN             Reviewed;         164 AA.
Q9NS18; Q3LR69; Q7L1N7; Q96JC0; Q9Y3D4;
30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
08-MAY-2019, entry version 163.
RecName: Full=Glutaredoxin-2, mitochondrial;
Flags: Precursor;
Name=GLRX2; Synonyms=GRX2; ORFNames=CGI-133;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Colon, and Testis;
PubMed=11297543; DOI=10.1074/jbc.M011605200;
Lundberg M., Johansson C., Chandra J., Enoksson M., Jacobsson G.,
Ljung J., Johansson M., Holmgren A.;
"Cloning and expression of a novel human glutaredoxin (Grx2) with
mitochondrial and nuclear isoforms.";
J. Biol. Chem. 276:26269-26275(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=11397793; DOI=10.1074/jbc.M100020200;
Gladyshev V.N., Liu A., Novoselov S.V., Krysan K., Sun Q.-A.,
Kryukov V.M., Kryukov G.V., Lou M.F.;
"Identification and characterization of a new mammalian glutaredoxin
(thioltransferase), Grx2.";
J. Biol. Chem. 276:30374-30380(2001).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLU-95.
NIEHS SNPs program;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-164 (ISOFORM 1).
PubMed=10810093; DOI=10.1101/gr.10.5.703;
Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
"Identification of novel human genes evolutionarily conserved in
Caenorhabditis elegans by comparative proteomics.";
Genome Res. 10:703-713(2000).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-164 (ISOFORM 1).
TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
TISSUE SPECIFICITY.
PubMed=15184054; DOI=10.1016/j.bbrc.2004.04.199;
Lundberg M., Fernandes A.P., Kumar S., Holmgren A.;
"Cellular and plasma levels of human glutaredoxin 1 and 2 detected by
sensitive ELISA systems.";
Biochem. Biophys. Res. Commun. 319:801-809(2004).
[8]
TISSUE SPECIFICITY.
PubMed=15297967; DOI=10.1016/j.humpath.2004.04.009;
Peltoniemi M., Kaarteenaho-Wiik R., Saily M., Sormunen R., Paakko P.,
Holmgren A., Soini Y., Kinnula V.L.;
"Expression of glutaredoxin is highly cell specific in human lung and
is decreased by transforming growth factor-beta in vitro and in
interstitial lung diseases in vivo.";
Hum. Pathol. 35:1000-1007(2004).
[9]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF SER-78 AND
CYS-80.
PubMed=14676218; DOI=10.1074/jbc.M312719200;
Johansson C., Lillig C.H., Holmgren A.;
"Human mitochondrial glutaredoxin reduces S-glutathionylated proteins
with high affinity accepting electrons from either glutathione or
thioredoxin reductase.";
J. Biol. Chem. 279:7537-7543(2004).
[10]
FUNCTION.
PubMed=15328416; DOI=10.1073/pnas.0401896101;
Lillig C.H., Loenn M.E., Enoksson M., Fernandes A.P., Holmgren A.;
"Short interfering RNA-mediated silencing of glutaredoxin 2 increases
the sensitivity of HeLa cells toward doxorubicin and phenylarsine
oxide.";
Proc. Natl. Acad. Sci. U.S.A. 101:13227-13232(2004).
[11]
FUNCTION.
PubMed=15649413; DOI=10.1016/j.bbrc.2004.12.067;
Enoksson M., Fernandes A.P., Prast S., Lillig C.H., Holmgren A.,
Orrenius S.;
"Overexpression of glutaredoxin 2 attenuates apoptosis by preventing
cytochrome c release.";
Biochem. Biophys. Res. Commun. 327:774-779(2005).
[12]
SUBUNIT, ACTIVITY REGULATION, METAL-BINDING, AND MUTAGENESIS OF CYS-68
AND CYS-153.
PubMed=15917333; DOI=10.1073/pnas.0500735102;
Lillig C.H., Berndt C., Vergnolle O., Loenn M.E., Hudemann C.,
Bill E., Holmgren A.;
"Characterization of human glutaredoxin 2 as iron-sulfur protein: a
possible role as redox sensor.";
Proc. Natl. Acad. Sci. U.S.A. 102:8168-8173(2005).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[14]
STRUCTURE BY NMR OF 48-164.
RIKEN structural genomics initiative (RSGI);
"Solution structure of RSGI RUH-044, an N-terminal 2 domain of
glutaredoxin 2 from human cDNA.";
Submitted (NOV-2005) to the PDB data bank.
[15]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 50-164 IN COMPLEX WITH
GLUTATHIONE, GLUTATHIONYLATION AT CYS-77, AND DISULFIDE BOND.
PubMed=17121859; DOI=10.1074/jbc.M608179200;
Johansson C., Kavanagh K.L., Gileadi O., Oppermann U.;
"Reversible sequestration of active site cysteines in a 2Fe-2S-bridged
dimer provides a mechanism for glutaredoxin 2 regulation in human
mitochondria.";
J. Biol. Chem. 282:3077-3082(2007).
-!- FUNCTION: Glutathione-dependent oxidoreductase that facilitates
the maintenance of mitochondrial redox homeostasis upon induction
of apoptosis by oxidative stress. Involved in response to hydrogen
peroxide and regulation of apoptosis caused by oxidative stress.
Acts as a very efficient catalyst of monothiol reactions because
of its high affinity for protein glutathione-mixed disulfides. Can
receive electrons not only from glutathione (GSH), but also from
thioredoxin reductase supporting both monothiol and dithiol
reactions. Efficiently catalyzes both glutathionylation and
deglutathionylation of mitochondrial complex I, which in turn
regulates the superoxide production by the complex. Overexpression
decreases the susceptibility to apoptosis and prevents loss of
cardiolipin and cytochrome c release.
{ECO:0000269|PubMed:11297543, ECO:0000269|PubMed:14676218,
ECO:0000269|PubMed:15328416, ECO:0000269|PubMed:15649413}.
-!- ACTIVITY REGULATION: The 2Fe-2S present in the homodimer leads to
inactivation of the enzyme. The 2Fe-2S may serve as a redox
sensor: the presence of one-electron oxidants or reductants
leading to the loss of the 2Fe-2S cluster, subsequent
monomerization and activation of the enzyme. Unlike other
glutaredoxins, it is not inhibited by oxidation of structural Cys
residues. {ECO:0000269|PubMed:15917333}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=5.9 mM for GSH {ECO:0000269|PubMed:14676218};
KM=0.77 mM for glutathionylated ribonuclease A
{ECO:0000269|PubMed:14676218};
KM=4.3 mM for glutathionylated BSA
{ECO:0000269|PubMed:14676218};
KM=0.11 mM for glutathionylated beta-mercaptoethanol
{ECO:0000269|PubMed:14676218};
-!- SUBUNIT: Monomer; active form. Homodimer; inactive form. The
homodimer is probably linked by 1 2Fe-2S cluster.
{ECO:0000269|PubMed:15917333, ECO:0000269|PubMed:17121859}.
-!- SUBCELLULAR LOCATION: Isoform 1: Mitochondrion.
-!- SUBCELLULAR LOCATION: Isoform 2: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Grx2a;
IsoId=Q9NS18-1; Sequence=Displayed;
Name=2; Synonyms=Grx2b;
IsoId=Q9NS18-2; Sequence=VSP_015221;
Note=Variant in position: 40:R->W.;
-!- TISSUE SPECIFICITY: Widely expressed. Expressed in brain, heart,
skeletal muscle, colon, thymus, spleen, kidney, liver, small
intestine, placenta and lung. Not expressed in peripheral blood
leukocytes. {ECO:0000269|PubMed:11297543,
ECO:0000269|PubMed:15184054, ECO:0000269|PubMed:15297967}.
-!- MISCELLANEOUS: The absence of GLRX2 dramatically sensitizes cells
to cell death induced by doxorubicin/adriamycin and phenylarsine
oxide.
-!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD34128.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
Sequence=AAH28113.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/glrx2/";
-----------------------------------------------------------------------
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EMBL; AF132495; AAF37320.2; -; mRNA.
EMBL; AF290514; AAK83089.1; -; mRNA.
EMBL; AY038988; AAK72499.1; -; mRNA.
EMBL; DQ194815; ABA03170.1; -; Genomic_DNA.
EMBL; AL136370; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF151891; AAD34128.1; ALT_FRAME; mRNA.
EMBL; BC028113; AAH28113.1; ALT_INIT; mRNA.
CCDS; CCDS1380.1; -. [Q9NS18-2]
CCDS; CCDS1381.1; -. [Q9NS18-1]
RefSeq; NP_001230328.1; NM_001243399.1.
RefSeq; NP_001306220.1; NM_001319291.1.
RefSeq; NP_057150.2; NM_016066.4. [Q9NS18-2]
RefSeq; NP_932066.1; NM_197962.2. [Q9NS18-1]
RefSeq; XP_016856886.1; XM_017001397.1.
PDB; 2CQ9; NMR; -; A=48-164.
PDB; 2FLS; X-ray; 2.05 A; A=56-164.
PDB; 2HT9; X-ray; 1.90 A; A/B=41-164.
PDBsum; 2CQ9; -.
PDBsum; 2FLS; -.
PDBsum; 2HT9; -.
SMR; Q9NS18; -.
BioGrid; 119228; 7.
IntAct; Q9NS18; 4.
STRING; 9606.ENSP00000356410; -.
DrugBank; DB00143; Glutathione.
iPTMnet; Q9NS18; -.
PhosphoSitePlus; Q9NS18; -.
BioMuta; GLRX2; -.
DMDM; 73919686; -.
EPD; Q9NS18; -.
jPOST; Q9NS18; -.
MaxQB; Q9NS18; -.
PeptideAtlas; Q9NS18; -.
PRIDE; Q9NS18; -.
ProteomicsDB; 82463; -.
ProteomicsDB; 82464; -. [Q9NS18-2]
Ensembl; ENST00000367439; ENSP00000356409; ENSG00000023572. [Q9NS18-1]
Ensembl; ENST00000367440; ENSP00000356410; ENSG00000023572. [Q9NS18-2]
Ensembl; ENST00000608166; ENSP00000494652; ENSG00000023572. [Q9NS18-1]
GeneID; 51022; -.
KEGG; hsa:51022; -.
UCSC; uc001gsz.3; human. [Q9NS18-1]
CTD; 51022; -.
DisGeNET; 51022; -.
GeneCards; GLRX2; -.
HGNC; HGNC:16065; GLRX2.
HPA; HPA023087; -.
HPA; HPA057224; -.
MIM; 606820; gene.
neXtProt; NX_Q9NS18; -.
OpenTargets; ENSG00000023572; -.
PharmGKB; PA28732; -.
GeneTree; ENSGT00940000162420; -.
HOGENOM; HOG000095204; -.
InParanoid; Q9NS18; -.
KO; K03676; -.
OMA; PRCFING; -.
OrthoDB; 1535999at2759; -.
PhylomeDB; Q9NS18; -.
TreeFam; TF319627; -.
SABIO-RK; Q9NS18; -.
ChiTaRS; GLRX2; human.
EvolutionaryTrace; Q9NS18; -.
GeneWiki; GLRX2; -.
GenomeRNAi; 51022; -.
PRO; PR:Q9NS18; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000023572; Expressed in 229 organ(s), highest expression level in sperm.
Genevisible; Q9NS18; HS.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0008794; F:arsenate reductase (glutaredoxin) activity; TAS:UniProtKB.
GO; GO:0009055; F:electron transfer activity; NAS:UniProtKB.
GO; GO:0015038; F:glutathione disulfide oxidoreductase activity; TAS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003756; F:protein disulfide isomerase activity; TAS:UniProtKB.
GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0006915; P:apoptotic process; NAS:UniProtKB.
GO; GO:0030154; P:cell differentiation; NAS:UniProtKB.
GO; GO:0045454; P:cell redox homeostasis; TAS:UniProtKB.
GO; GO:0071451; P:cellular response to superoxide; IEA:Ensembl.
GO; GO:0042262; P:DNA protection; NAS:UniProtKB.
GO; GO:0006749; P:glutathione metabolic process; TAS:UniProtKB.
GO; GO:0009966; P:regulation of signal transduction; NAS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
GO; GO:0042542; P:response to hydrogen peroxide; IDA:UniProtKB.
GO; GO:0010033; P:response to organic substance; IDA:UniProtKB.
GO; GO:0051775; P:response to redox state; TAS:UniProtKB.
GO; GO:0009266; P:response to temperature stimulus; NAS:UniProtKB.
InterPro; IPR002109; Glutaredoxin.
InterPro; IPR011899; Glutaredoxin_euk/vir.
InterPro; IPR014025; Glutaredoxin_subgr.
InterPro; IPR036249; Thioredoxin-like_sf.
Pfam; PF00462; Glutaredoxin; 1.
PRINTS; PR00160; GLUTAREDOXIN.
SUPFAM; SSF52833; SSF52833; 1.
TIGRFAMs; TIGR02180; GRX_euk; 1.
PROSITE; PS51354; GLUTAREDOXIN_2; 1.
1: Evidence at protein level;
2Fe-2S; 3D-structure; Alternative splicing; Complete proteome;
Disulfide bond; Electron transport; Glutathionylation; Iron;
Iron-sulfur; Metal-binding; Mitochondrion; Nucleus; Phosphoprotein;
Polymorphism; Redox-active center; Reference proteome;
Transit peptide; Transport.
TRANSIT 1 19 Mitochondrion. {ECO:0000255}.
CHAIN 20 164 Glutaredoxin-2, mitochondrial.
/FTId=PRO_0000011628.
DOMAIN 57 157 Glutaredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00686}.
METAL 68 68 Iron-sulfur (2Fe-2S); shared with dimeric
partner; in inactive form. {ECO:0000305}.
METAL 153 153 Iron-sulfur (2Fe-2S); shared with dimeric
partner; in inactive form. {ECO:0000305}.
BINDING 74 74 Glutathione.
{ECO:0000269|PubMed:17121859}.
BINDING 109 109 Glutathione.
{ECO:0000269|PubMed:17121859}.
BINDING 121 121 Glutathione; via amide nitrogen and
carbonyl oxygen.
{ECO:0000269|PubMed:17121859}.
MOD_RES 20 20 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 77 77 S-glutathionyl cysteine; alternate.
{ECO:0000269|PubMed:17121859}.
DISULFID 77 80 Redox-active; alternate. {ECO:0000250}.
VAR_SEQ 1 40 MIWRRAALAGTRLVWSRSGSAGWLDRAAGAAGAAAAAASG
-> MNPRDKQVSRFSPLKDVYTWVALAGIQRSGSPGRTRSA
ARR (in isoform 2).
{ECO:0000303|PubMed:11297543}.
/FTId=VSP_015221.
VARIANT 95 95 K -> E (in dbSNP:rs34237236).
{ECO:0000269|Ref.3}.
/FTId=VAR_025234.
MUTAGEN 68 68 C->S: Abolishes absorption at 320 nm and
420 nm suggesting the loss of 2Fe-2S-
binding. {ECO:0000269|PubMed:15917333}.
MUTAGEN 78 78 S->P: Specifically increases the specific
activity but decreases affinity for
glutathionylated substrates.
{ECO:0000269|PubMed:14676218}.
MUTAGEN 80 80 C->S: Strongly impairs enzymatic
activity. {ECO:0000269|PubMed:14676218}.
MUTAGEN 153 153 C->S: Abolishes absorption at 320 nm and
420 nm suggesting the loss of 2Fe-2S-
binding. {ECO:0000269|PubMed:15917333}.
HELIX 57 66 {ECO:0000244|PDB:2HT9}.
STRAND 68 73 {ECO:0000244|PDB:2HT9}.
HELIX 78 90 {ECO:0000244|PDB:2HT9}.
STRAND 95 98 {ECO:0000244|PDB:2HT9}.
HELIX 99 101 {ECO:0000244|PDB:2HT9}.
HELIX 105 116 {ECO:0000244|PDB:2HT9}.
STRAND 123 126 {ECO:0000244|PDB:2HT9}.
STRAND 129 133 {ECO:0000244|PDB:2HT9}.
HELIX 134 142 {ECO:0000244|PDB:2HT9}.
HELIX 146 152 {ECO:0000244|PDB:2HT9}.
STRAND 154 156 {ECO:0000244|PDB:2CQ9}.
HELIX 160 162 {ECO:0000244|PDB:2HT9}.
SEQUENCE 164 AA; 18052 MW; D9798A01BB532A5D CRC64;
MIWRRAALAG TRLVWSRSGS AGWLDRAAGA AGAAAAAASG MESNTSSSLE NLATAPVNQI
QETISDNCVV IFSKTSCSYC TMAKKLFHDM NVNYKVVELD LLEYGNQFQD ALYKMTGERT
VPRIFVNGTF IGGATDTHRL HKEGKLLPLV HQCYLKKSKR KEFQ


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29-926 SLC25A24 is a calcium-dependent mitochondrial solute carrier. Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane. It may act as a AT 0.1 mg

Kits Elisa; taq POLYMERASE

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Gentaur; yes we can

Pathways :
WP100: Glutathione metabolism
WP1039: Glutathione metabolism
WP104: Alanine and aspartate metabolism
WP106: Alanine and aspartate metabolism
WP1107: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1126: Tryptophan metabolism
WP1226: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1263: Mitochondrial Gene Expression
WP1301: Mitochondrial Gene Expression
WP1313: Insulin Signaling
WP1321: Myometrial Relaxation and Contraction Pathways
WP1323: EGFR1 Signaling Pathway
WP1329: Alpha6-Beta4 Integrin Signaling Pathway
WP1333: Hypothetical Network for Drug Addiction
WP1344: Wnt Signaling Pathway and Pluripotency
WP1345: T Cell Receptor Signaling Pathway
WP1348: Androgen Receptor Signaling Pathway
WP1354: B Cell Receptor Signaling Pathway
WP1355: One Carbon Metabolism
WP1362: Homologous recombination
WP1363: p38 MAPK Signaling Pathway
WP1365: Calcium Regulation in the Cardiac Cell
WP1368: Mitochondrial Gene Expression
WP1370: TGF Beta Signaling Pathway
WP1371: G Protein Signaling Pathways

Related Genes :
[GLRX2 GRX2 CGI-133] Glutaredoxin-2, mitochondrial
[Glrx2 Grx2] Glutaredoxin-2, mitochondrial
[GRX2 TTR TTR1 YDR513W D9719.17] Glutaredoxin-2, mitochondrial (Glutathione-dependent oxidoreductase 2) (Thioltransferase)
[GLRX5 C14orf87] Glutaredoxin-related protein 5, mitochondrial (Monothiol glutaredoxin-5)
[Glrx2 Grx2] Glutaredoxin-2, mitochondrial
[GRX5 YPL059W LPE13W] Monothiol glutaredoxin-5, mitochondrial
[glrx5 grx5 shiraz si:ch211-121d13.1] Glutaredoxin-related protein 5, mitochondrial (Monothiol glutaredoxin-5)
[Glrx5] Glutaredoxin-related protein 5, mitochondrial (Monothiol glutaredoxin-5)
[Glrx3 Picot Txnl2] Glutaredoxin-3 (PKC-interacting cousin of thioredoxin) (PICOT) (PKC-theta-interacting protein) (PKCq-interacting protein) (Thioredoxin-like protein 2)
[GLRX3 PICOT TXNL2 HUSSY-22] Glutaredoxin-3 (PKC-interacting cousin of thioredoxin) (PICOT) (PKC-theta-interacting protein) (PKCq-interacting protein) (Thioredoxin-like protein 2)
[GRXS16 CXIP2 At2g38270 F16M14.20] Bifunctional monothiol glutaredoxin-S16, chloroplastic (AtGrxS16) (Atypical GIY-YIG endonuclease) (EC 3.1.-.-) (CAX-interacting protein 2) (CAXIP1-like protein)
[grx5 SPAPB2B4.02] Monothiol glutaredoxin-5
[PRXIIF At3g06050 F24F17.3] Peroxiredoxin-2F, mitochondrial (EC 1.11.1.15) (Peroxiredoxin IIF) (Thioredoxin peroxidase 2F)
[Glrx Glrx1 Grx Grx1] Glutaredoxin-1 (Thioltransferase-1) (TTase-1)
[Glrx3 Picot Txnl2] Glutaredoxin-3 (PKC-interacting cousin of thioredoxin) (PICOT) (PKC-theta-interacting protein) (PKCq-interacting protein) (Thioredoxin-like protein 2)
[GLRX GRX] Glutaredoxin-1 (Thioltransferase-1) (TTase-1)
[Glrx Glrx1 Grx] Glutaredoxin-1 (Thioltransferase-1) (TTase-1)
[GRX3 YDR098C YD8557.05C] Monothiol glutaredoxin-3
[GRX4 YER174C SYGP-ORF64] Monothiol glutaredoxin-4
[GRXS15 At3g15660 MSJ11.6] Monothiol glutaredoxin-S15, mitochondrial (AtGrxS15)
[PRX1 YBL064C YBL0503 YBL0524] Peroxiredoxin PRX1, mitochondrial (Prx) (EC 1.11.1.15) (1-Cys PRX) (Mitochondrial thiol peroxidase) (mTPx) (Thioredoxin peroxidase)
[Alas2] 5-aminolevulinate synthase, erythroid-specific, mitochondrial (ALAS-E) (EC 2.3.1.37) (5-aminolevulinic acid synthase 2) (Delta-ALA synthase 2) (Delta-aminolevulinate synthase 2)
[Eci2 Peci] Enoyl-CoA delta isomerase 2, mitochondrial (EC 5.3.3.8) (Delta(3),delta(2)-enoyl-CoA isomerase) (D3,D2-enoyl-CoA isomerase) (Dodecenoyl-CoA isomerase) (Peroxisomal 3,2-trans-enoyl-CoA isomerase) (pECI)
[Immp2l] Mitochondrial inner membrane protease subunit 2 (EC 3.4.21.-) (IMP2-like protein)
[phb-2 T24H7.1] Mitochondrial prohibitin complex protein 2 (Prohibitin-2)
[atp-2 C34E10.6] ATP synthase subunit beta, mitochondrial (EC 7.1.2.2)
[dbt-1 ZK669.4] Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial (EC 2.3.1.168) (Branched-chain alpha-keto acid dehydrogenase complex component E2) (Dihydrolipoamide branched-chain transacylase E2)
[Atp5f1b Atp5b] ATP synthase subunit beta, mitochondrial (EC 7.1.2.2) (ATP synthase F1 subunit beta)
[NDC1 At5g08740 T2K12.12 T2K12_90] Alternative NAD(P)H-ubiquinone oxidoreductase C1, chloroplastic/mitochondrial (EC 1.6.5.9) (Alternative NADH dehydrogenase NDC1) (Demethylphylloquinone reductase NDC1) (EC 1.6.5.12) (NADH:ubiquinone reductase (non-electrogenic) NDC1)
[l(2)tid CG5504] Protein tumorous imaginal discs, mitochondrial (Protein lethal(2)tumorous imaginal discs) (TID50) (TID56)

Bibliography :
[30736356] RNA-Seq Transcriptome Profiling of the Queen Scallop (Aequipecten opercularis) Digestive Gland after Exposure to Domoic Acid-Producing Pseudo-nitzschia.
[30661098] GLRX inhibition enhances the effects of geftinib in EGFR-TKI-resistant NSCLC cells through FoxM1 signaling pathway.
[30537466] Protein S-glutathionylation: The linchpin for the transmission of regulatory information on redox buffering capacity in mitochondria.
[30514787] The Monothiol Glutaredoxin Grx4 Regulates Iron Homeostasis and Virulence in Cryptococcus neoformans.
[30467749] Polychlorinated biphenyl 126 exposure in rats alters skeletal muscle mitochondrial function.
[30209332] The lineage-specific, intrinsically disordered N-terminal extension of monothiol glutaredoxin 1 from trypanosomes contains a regulatory region.
[30137089] Cluster exchange reactivity of [2Fe-2S] cluster-bridged complexes of BOLA3 with monothiol glutaredoxins.
[30021840] Iron-dependent cleavage of ribosomal RNA during oxidative stress in the yeast .
[29857311] Fatiguing contractions increase protein S-glutathionylation occupancy in mouse skeletal muscle.
[29794018] The Extra-Pathway Interactome of the TCA Cycle: Expected and Unexpected Metabolic Interactions.