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Q9NS18

- GLRX2_HUMAN

UniProt

Q9NS18 - GLRX2_HUMAN

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Protein

Glutaredoxin-2, mitochondrial

Gene

GLRX2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.4 Publications

Enzyme regulationi

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.1 Publication

Kineticsi

  1. KM=5.9 mM for GSH1 Publication
  2. KM=0.77 mM for glutathionylated ribonuclease A1 Publication
  3. KM=4.3 mM for glutathionylated BSA1 Publication
  4. KM=0.11 mM for glutathionylated beta-mercaptoethanol1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi68 – 681Iron-sulfur (2Fe-2S); shared with dimeric partner; in inactive formCurated
Binding sitei74 – 741Glutathione1 Publication
Binding sitei109 – 1091Glutathione1 Publication
Binding sitei121 – 1211Glutathione; via amide nitrogen and carbonyl oxygen1 Publication
Metal bindingi153 – 1531Iron-sulfur (2Fe-2S); shared with dimeric partner; in inactive formCurated

GO - Molecular functioni

  1. 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
  2. arsenate reductase (glutaredoxin) activity Source: UniProtKB
  3. electron carrier activity Source: UniProtKB
  4. glutathione disulfide oxidoreductase activity Source: UniProtKB
  5. metal ion binding Source: UniProtKB-KW
  6. protein disulfide isomerase activity Source: UniProtKB
  7. protein disulfide oxidoreductase activity Source: InterPro

GO - Biological processi

  1. apoptotic process Source: UniProtKB
  2. cell differentiation Source: UniProtKB
  3. cell redox homeostasis Source: UniProtKB
  4. DNA protection Source: UniProtKB
  5. glutathione metabolic process Source: UniProtKB
  6. protein folding Source: GOC
  7. regulation of signal transduction Source: UniProtKB
  8. regulation of transcription, DNA-templated Source: UniProtKB
  9. response to hydrogen peroxide Source: UniProtKB
  10. response to organic substance Source: UniProtKB
  11. response to redox state Source: UniProtKB
  12. response to temperature stimulus Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

2Fe-2S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

SABIO-RKQ9NS18.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutaredoxin-2, mitochondrial
Gene namesi
Name:GLRX2
Synonyms:GRX2
ORF Names:CGI-133
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:16065. GLRX2.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi68 – 681C → S: Abolishes absorption at 320 nm and 420 nm suggesting the loss of 2Fe-2S-binding. 1 Publication
Mutagenesisi78 – 781S → P: Specifically increases the specific activity but decreases affinity for glutathionylated substrates. 1 Publication
Mutagenesisi80 – 801C → S: Strongly impairs enzymatic activity. 1 Publication
Mutagenesisi153 – 1531C → S: Abolishes absorption at 320 nm and 420 nm suggesting the loss of 2Fe-2S-binding. 1 Publication

Organism-specific databases

PharmGKBiPA28732.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1919MitochondrionSequence AnalysisAdd
BLAST
Chaini20 – 164145Glutaredoxin-2, mitochondrialPRO_0000011628Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi77 ↔ 80Redox-active; alternateBy similarity
Modified residuei77 – 771S-glutathionyl cysteine; alternate1 Publication

Keywords - PTMi

Disulfide bond, Glutathionylation

Proteomic databases

MaxQBiQ9NS18.
PaxDbiQ9NS18.
PRIDEiQ9NS18.

PTM databases

PhosphoSiteiQ9NS18.

Expressioni

Tissue specificityi

Widely expressed. Expressed in brain, heart, skeletal muscle, colon, thymus, spleen, kidney, liver, small intestine, placenta and lung. Not expressed in peripheral blood leukocytes.3 Publications

Gene expression databases

BgeeiQ9NS18.
CleanExiHS_GLRX2.
GenevestigatoriQ9NS18.

Organism-specific databases

HPAiHPA023087.

Interactioni

Subunit structurei

Monomer; active form. Homodimer; inactive form. The homodimer is probably linked by 1 2Fe-2S cluster.2 Publications

Protein-protein interaction databases

BioGridi119228. 2 interactions.
STRINGi9606.ENSP00000356410.

Structurei

Secondary structure

1
164
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi57 – 6610
Beta strandi68 – 736
Helixi78 – 9013
Beta strandi95 – 984
Helixi99 – 1013
Helixi105 – 11612
Beta strandi123 – 1264
Beta strandi129 – 1335
Helixi134 – 1429
Helixi146 – 1527
Beta strandi154 – 1563

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CQ9NMR-A48-164[»]
2FLSX-ray2.05A56-164[»]
2HT9X-ray1.90A/B41-164[»]
ProteinModelPortaliQ9NS18.
SMRiQ9NS18. Positions 54-164.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NS18.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini57 – 157101GlutaredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

eggNOGiCOG0695.
GeneTreeiENSGT00390000003677.
HOGENOMiHOG000095204.
HOVERGENiHBG096801.
InParanoidiQ9NS18.
KOiK03676.
OMAiGMESNTS.
OrthoDBiEOG7QRQWZ.
PhylomeDBiQ9NS18.
TreeFamiTF319627.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR002109. 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.
PROSITEiPS51354. GLUTAREDOXIN_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: Q9NS18) [UniParc]FASTAAdd to Basket

Also known as: Grx2a

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

        10         20         30         40         50
MIWRRAALAG TRLVWSRSGS AGWLDRAAGA AGAAAAAASG MESNTSSSLE
60 70 80 90 100
NLATAPVNQI QETISDNCVV IFSKTSCSYC TMAKKLFHDM NVNYKVVELD
110 120 130 140 150
LLEYGNQFQD ALYKMTGERT VPRIFVNGTF IGGATDTHRL HKEGKLLPLV
160
HQCYLKKSKR KEFQ
Length:164
Mass (Da):18,052
Last modified:October 1, 2000 - v1
Checksum:iD9798A01BB532A5D
GO
Isoform 2 (identifier: Q9NS18-2) [UniParc]FASTAAdd to Basket

Also known as: Grx2b

The sequence of this isoform differs from the canonical sequence as follows:
     1-40: MIWRRAALAG...AGAAAAAASG → MNPRDKQVSR...PGRTRSAARR

Show »
Length:165
Mass (Da):18,726
Checksum:iD4A1F78015B516D4
GO

Sequence cautioni

The sequence AAD34128.1 differs from that shown. Reason: Frameshift at several positions.
The sequence AAH28113.1 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti95 – 951K → E.1 Publication
Corresponds to variant rs34237236 [ dbSNP | Ensembl ].
VAR_025234
Isoform 2 (identifier: Q9NS18-2)
Natural varianti40 – 401R → W.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4040MIWRR…AAASG → MNPRDKQVSRFSPLKDVYTW VALAGIQRSGSPGRTRSAAR R in isoform 2. 1 PublicationVSP_015221Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF132495 mRNA. Translation: AAF37320.2.
AF290514 mRNA. Translation: AAK83089.1.
AY038988 mRNA. Translation: AAK72499.1.
DQ194815 Genomic DNA. Translation: ABA03170.1.
AL136370 Genomic DNA. Translation: CAI10820.1.
AL136370 Genomic DNA. Translation: CAI10821.1.
AF151891 mRNA. Translation: AAD34128.1. Frameshift.
BC028113 mRNA. Translation: AAH28113.1. Different initiation.
CCDSiCCDS1380.1. [Q9NS18-2]
CCDS1381.1. [Q9NS18-1]
RefSeqiNP_001230328.1. NM_001243399.1.
NP_057150.2. NM_016066.4. [Q9NS18-2]
NP_932066.1. NM_197962.2. [Q9NS18-1]
XP_005245288.1. XM_005245231.2.
UniGeneiHs.458283.

Genome annotation databases

EnsembliENST00000367439; ENSP00000356409; ENSG00000023572. [Q9NS18-1]
ENST00000367440; ENSP00000356410; ENSG00000023572. [Q9NS18-2]
GeneIDi51022.
KEGGihsa:51022.
UCSCiuc001gsz.2. human. [Q9NS18-1]
uc001gta.2. human. [Q9NS18-2]

Polymorphism databases

DMDMi73919686.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF132495 mRNA. Translation: AAF37320.2 .
AF290514 mRNA. Translation: AAK83089.1 .
AY038988 mRNA. Translation: AAK72499.1 .
DQ194815 Genomic DNA. Translation: ABA03170.1 .
AL136370 Genomic DNA. Translation: CAI10820.1 .
AL136370 Genomic DNA. Translation: CAI10821.1 .
AF151891 mRNA. Translation: AAD34128.1 . Frameshift.
BC028113 mRNA. Translation: AAH28113.1 . Different initiation.
CCDSi CCDS1380.1. [Q9NS18-2 ]
CCDS1381.1. [Q9NS18-1 ]
RefSeqi NP_001230328.1. NM_001243399.1.
NP_057150.2. NM_016066.4. [Q9NS18-2 ]
NP_932066.1. NM_197962.2. [Q9NS18-1 ]
XP_005245288.1. XM_005245231.2.
UniGenei Hs.458283.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2CQ9 NMR - A 48-164 [» ]
2FLS X-ray 2.05 A 56-164 [» ]
2HT9 X-ray 1.90 A/B 41-164 [» ]
ProteinModelPortali Q9NS18.
SMRi Q9NS18. Positions 54-164.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119228. 2 interactions.
STRINGi 9606.ENSP00000356410.

Chemistry

DrugBanki DB00143. Glutathione.

PTM databases

PhosphoSitei Q9NS18.

Polymorphism databases

DMDMi 73919686.

Proteomic databases

MaxQBi Q9NS18.
PaxDbi Q9NS18.
PRIDEi Q9NS18.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000367439 ; ENSP00000356409 ; ENSG00000023572 . [Q9NS18-1 ]
ENST00000367440 ; ENSP00000356410 ; ENSG00000023572 . [Q9NS18-2 ]
GeneIDi 51022.
KEGGi hsa:51022.
UCSCi uc001gsz.2. human. [Q9NS18-1 ]
uc001gta.2. human. [Q9NS18-2 ]

Organism-specific databases

CTDi 51022.
GeneCardsi GC01M193065.
HGNCi HGNC:16065. GLRX2.
HPAi HPA023087.
MIMi 606820. gene.
neXtProti NX_Q9NS18.
PharmGKBi PA28732.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0695.
GeneTreei ENSGT00390000003677.
HOGENOMi HOG000095204.
HOVERGENi HBG096801.
InParanoidi Q9NS18.
KOi K03676.
OMAi GMESNTS.
OrthoDBi EOG7QRQWZ.
PhylomeDBi Q9NS18.
TreeFami TF319627.

Enzyme and pathway databases

SABIO-RK Q9NS18.

Miscellaneous databases

EvolutionaryTracei Q9NS18.
GeneWikii GLRX2.
GenomeRNAii 51022.
NextBioi 53548.
PROi Q9NS18.
SOURCEi Search...

Gene expression databases

Bgeei Q9NS18.
CleanExi HS_GLRX2.
Genevestigatori Q9NS18.

Family and domain databases

Gene3Di 3.40.30.10. 1 hit.
InterProi IPR002109. Glutaredoxin.
IPR011899. Glutaredoxin_euk/vir.
IPR014025. Glutaredoxin_subgr.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF00462. Glutaredoxin. 1 hit.
[Graphical view ]
PRINTSi PR00160. GLUTAREDOXIN.
SUPFAMi SSF52833. SSF52833. 1 hit.
TIGRFAMsi TIGR02180. GRX_euk. 1 hit.
PROSITEi PS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of a novel human glutaredoxin (Grx2) with mitochondrial and nuclear isoforms."
    Lundberg M., Johansson C., Chandra J., Enoksson M., Jacobsson G., Ljung J., Johansson M., Holmgren A.
    J. Biol. Chem. 276:26269-26275(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Colon and Testis.
  2. "Identification and characterization of a new mammalian glutaredoxin (thioltransferase), Grx2."
    Gladyshev V.N., Liu A., Novoselov S.V., Krysan K., Sun Q.-A., Kryukov V.M., Kryukov G.V., Lou M.F.
    J. Biol. Chem. 276:30374-30380(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. NIEHS SNPs program
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLU-95.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    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.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
    Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
    Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-164 (ISOFORM 1).
  6. "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] OF 4-164 (ISOFORM 1).
    Tissue: Mammary gland.
  7. "Cellular and plasma levels of human glutaredoxin 1 and 2 detected by sensitive ELISA systems."
    Lundberg M., Fernandes A.P., Kumar S., Holmgren A.
    Biochem. Biophys. Res. Commun. 319:801-809(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  8. "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."
    Peltoniemi M., Kaarteenaho-Wiik R., Saily M., Sormunen R., Paakko P., Holmgren A., Soini Y., Kinnula V.L.
    Hum. Pathol. 35:1000-1007(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  9. "Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase."
    Johansson C., Lillig C.H., Holmgren A.
    J. Biol. Chem. 279:7537-7543(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF SER-78 AND CYS-80.
  10. "Short interfering RNA-mediated silencing of glutaredoxin 2 increases the sensitivity of HeLa cells toward doxorubicin and phenylarsine oxide."
    Lillig C.H., Loenn M.E., Enoksson M., Fernandes A.P., Holmgren A.
    Proc. Natl. Acad. Sci. U.S.A. 101:13227-13232(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Overexpression of glutaredoxin 2 attenuates apoptosis by preventing cytochrome c release."
    Enoksson M., Fernandes A.P., Prast S., Lillig C.H., Holmgren A., Orrenius S.
    Biochem. Biophys. Res. Commun. 327:774-779(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Characterization of human glutaredoxin 2 as iron-sulfur protein: a possible role as redox sensor."
    Lillig C.H., Berndt C., Vergnolle O., Loenn M.E., Hudemann C., Bill E., Holmgren A.
    Proc. Natl. Acad. Sci. U.S.A. 102:8168-8173(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, ENZYME REGULATION, METAL-BINDING, MUTAGENESIS OF CYS-68 AND CYS-153.
  13. "Solution structure of RSGI RUH-044, an N-terminal 2 domain of glutaredoxin 2 from human cDNA."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 48-164.
  14. "Reversible sequestration of active site cysteines in a 2Fe-2S-bridged dimer provides a mechanism for glutaredoxin 2 regulation in human mitochondria."
    Johansson C., Kavanagh K.L., Gileadi O., Oppermann U.
    J. Biol. Chem. 282:3077-3082(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 50-164 IN COMPLEX WITH GLUTATHIONE, GLUTATHIONYLATION AT CYS-77, DISULFIDE BOND.

Entry informationi

Entry nameiGLRX2_HUMAN
AccessioniPrimary (citable) accession number: Q9NS18
Secondary accession number(s): Q3LR69
, Q7L1N7, Q96JC0, Q9Y3D4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: October 1, 2000
Last modified: October 29, 2014
This is version 123 of the entry and version 1 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

Miscellaneous

The absence of GLRX2 dramatically sensitizes cells to cell death induced by doxorubicin/adriamycin and phenylarsine oxide.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3