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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.
18-SEP-2019, entry version 165.
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; 8.
IntAct; Q9NS18; 4.
STRING; 9606.ENSP00000356410; -.
DrugBank; DB00143; Glutathione.
iPTMnet; Q9NS18; -.
PhosphoSitePlus; Q9NS18; -.
BioMuta; GLRX2; -.
DMDM; 73919686; -.
EPD; Q9NS18; -.
jPOST; Q9NS18; -.
MassIVE; Q9NS18; -.
MaxQB; Q9NS18; -.
PeptideAtlas; Q9NS18; -.
PRIDE; Q9NS18; -.
ProteomicsDB; 82463; -. [Q9NS18-1]
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; -.
Pharos; Q9NS18; -.
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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orb90117 Human Glutaredoxin 1 protein Glutaredoxin Human Recombinant produced in E.coli is a single, non-glycosylated, Polypeptide chain containing 106 amino acids having a molecular mass of 11.7 kDa. For rese 10
29-939 The SLC25 family is mitochondrial carriers that transport a variety of metabolites across the inner mitochondrial membrane. SLC25A22, also known as GC1, is 1 of the 2 mitochondrial glutamate_H+ sympor 0.1 mg
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
Pathways :
WP246: TNF-alpha NF-kB Signaling Pathway
WP391: Mitochondrial Gene Expression
WP100: Glutathione metabolism
WP1107: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP240: Alanine and aspartate metabolism
WP1301: Mitochondrial Gene Expression
WP1370: TGF Beta Signaling Pathway
WP1344: Wnt Signaling Pathway and Pluripotency
WP406: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP469: Glutathione metabolism
WP572: EGFR1 Signaling Pathway
WP465: Tryptophan metabolism
WP1345: T Cell Receptor Signaling Pathway
WP1905: RNA Polymerase I, RNA Polymerase III, and Mitochondrial Transcription
WP1411: Cell Division: First embryonic mitosis
WP1385: Nuclear Receptors
WP1333: Hypothetical Network for Drug Addiction
WP2226: Cell engulfment
WP62: Mitochondrial tRNA Synthetases
WP1313: Insulin Signaling
WP2349: vitamin B3 (niacin), NAD and NADP biosynthesis pathway
WP2353: vitamin B9 (folate) biosynthesis pathway
WP1126: Tryptophan metabolism
WP216: Striated Muscle Contraction
WP871: Mitochondrial LC-Fatty Acid Beta-Oxidation

Related Genes :
[matK] Maturase K (Fragment)
[Bathy09g02690] Uncharacterized protein
[petA] Cytochrome f
[psbX] Photosystem II reaction center X protein
[atpA] ATP synthase subunit alpha, chloroplastic (EC 7.1.2.2) (ATP synthase F1 sector subunit alpha) (F-ATPase subunit alpha)
[DR13] Homogentisate 1,2-dioxygenase
[KK1_019005] (+)-neomenthol dehydrogenase
[Bathy01g04610] ANK_REP_REGION domain-containing protein
[rbcL] Ribulose bisphosphate carboxylase large chain (EC 4.1.1.39) (Fragment)
[rps3] 30S ribosomal protein S3, chloroplastic
[KK1_002165] Putative serine/threonine-protein kinase receptor
[KK1_033810] Heme-binding protein 2
[KK1_033704] Uncharacterized protein
[] PPM-type phosphatase domain-containing protein
[Bathy06g03360] Heat Shock Protein 70, cytosolic
[rpoC2] DNA-directed RNA polymerase subunit beta'' (EC 2.7.7.6) (PEP) (Plastid-encoded RNA polymerase subunit beta'') (RNA polymerase subunit beta'')
[102598549] Exostosin domain-containing protein
[] Cinnamoyl CoA reductase (EC 1.2.1.44)
[ndhA] NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase subunit 1) (NDH subunit 1) (NADH-plastoquinone oxidoreductase subunit 1)
[KK1_010998] Uncharacterized protein
[KK1_029487] Telomerase reverse transcriptase (EC 2.7.7.49) (Telomerase catalytic subunit)
[rbcL] Ribulose bisphosphate carboxylase large chain (RuBisCO large subunit) (EC 4.1.1.39)
[KK1_045969] 40S ribosomal protein SA
[KK1_027837] Uncharacterized protein
[Bathy07g01830] Uncharacterized protein
[KK1_041115] Protein IN2-1 isogeny B (Fragment)
[] Uncharacterized protein
[KK1_000036] V-type proton ATPase catalytic subunit A
[rbcL] Ribulose bisphosphate carboxylase large chain (EC 4.1.1.39) (Fragment)
[rps2] Ribosomal protein S2 (Fragment)

Bibliography :
[31493153] The conserved CDC motif in the yeast iron regulator Aft2 mediates iron-sulfur cluster exchange and protein-protein interactions with Grx3 and Bol2.
[31382130] Glutaredoxin 2 (GRX2) deficiency exacerbates high fat diet (HFD)-induced insulin resistance, inflammation and mitochondrial dysfunction in brain injury: A mechanism involving GSK-3β.
[31357416] Sex-dependent Differences in the Bioenergetics of Liver and Muscle Mitochondria from Mice Containing a Deletion for .
[31317766] Deletion of the Glutaredoxin-2 Gene Protects Mice from Diet-Induced Weight Gain, Which Correlates with Increased Mitochondrial Respiration and Proton Leaks in Skeletal Muscle.
[31168542] Dimers of glutaredoxin 2 as mitochondrial redox sensors in selenite-induced oxidative stress.
[31062084] Cloning, expression, purification, and kinetic characterization of mitochondrial thioredoxin (TsTrx2), cytosolic thioredoxin (TsTrx1), and glutaredoxin (TsGrx1) from Taenia solium.
[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.