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Protein

Glutathione reductase, mitochondrial

Gene

GSR

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

Functioni

Maintains high levels of reduced glutathione in the cytosol.

Catalytic activityi

2 glutathione + NADP+ = glutathione disulfide + NADPH.

Cofactori

FADNote: Binds 1 FAD per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei511 – 5111Proton acceptor

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi94 – 1029FAD

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

BioCyciMetaCyc:HS02602-MONOMER.
BRENDAi1.8.1.7. 2681.
ReactomeiREACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.
REACT_264249. Detoxification of Reactive Oxygen Species.
REACT_355377. TP53 Regulates Metabolic Genes.
SABIO-RKP00390.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione reductase, mitochondrial (EC:1.8.1.7)
Short name:
GR
Short name:
GRase
Gene namesi
Name:GSR
Synonyms:GLUR, GRD1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:4623. GSR.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

Pathology & Biotechi

Organism-specific databases

MIMi138300. gene+phenotype.
Orphaneti90030. Hemolytic anemia due to glutathione reductase deficiency.
PharmGKBiPA29014.

Chemistry

DrugBankiDB00262. Carmustine.
DB03147. Flavin adenine dinucleotide.
DB00143. Glutathione.

Polymorphism and mutation databases

BioMutaiGSR.
DMDMi14916998.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4343MitochondrionSequence AnalysisAdd
BLAST
Chaini44 – 522479Glutathione reductase, mitochondrialPRO_0000030276Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei97 – 971N6-acetyllysineBy similarity
Disulfide bondi102 ↔ 107Redox-active1 Publication
Disulfide bondi134 – 134Interchain1 Publication

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

PaxDbiP00390.
PRIDEiP00390.

2D gel databases

REPRODUCTION-2DPAGEIPI00759575.

PTM databases

PhosphoSiteiP00390.

Expressioni

Gene expression databases

BgeeiP00390.
CleanExiHS_GSR.
ExpressionAtlasiP00390. baseline and differential.
GenevisibleiP00390. HS.

Organism-specific databases

HPAiCAB008632.
HPA001538.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.1 Publication

Protein-protein interaction databases

BioGridi109191. 26 interactions.
IntActiP00390. 4 interactions.
MINTiMINT-5000460.
STRINGi9606.ENSP00000221130.

Structurei

Secondary structure

1
522
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi62 – 643Combined sources
Beta strandi66 – 705Combined sources
Helixi74 – 8512Combined sources
Beta strandi90 – 967Combined sources
Helixi100 – 1056Combined sources
Helixi107 – 12317Combined sources
Turni124 – 1307Combined sources
Helixi140 – 16425Combined sources
Beta strandi168 – 1725Combined sources
Beta strandi174 – 1763Combined sources
Beta strandi183 – 1864Combined sources
Beta strandi189 – 1924Combined sources
Beta strandi196 – 1983Combined sources
Beta strandi202 – 2043Combined sources
Turni209 – 2113Combined sources
Helixi215 – 2173Combined sources
Helixi221 – 2244Combined sources
Beta strandi232 – 2376Combined sources
Helixi241 – 25212Combined sources
Beta strandi256 – 2605Combined sources
Beta strandi262 – 2665Combined sources
Helixi272 – 28413Combined sources
Beta strandi288 – 2903Combined sources
Beta strandi293 – 3008Combined sources
Beta strandi302 – 31110Combined sources
Beta strandi319 – 33113Combined sources
Beta strandi335 – 3384Combined sources
Turni340 – 3434Combined sources
Helixi344 – 3474Combined sources
Beta strandi370 – 3723Combined sources
Helixi374 – 3774Combined sources
Helixi383 – 39816Combined sources
Beta strandi413 – 4153Combined sources
Beta strandi417 – 4193Combined sources
Beta strandi421 – 4255Combined sources
Helixi428 – 4358Combined sources
Helixi437 – 4393Combined sources
Beta strandi440 – 4478Combined sources
Helixi450 – 4545Combined sources
Beta strandi461 – 4688Combined sources
Turni469 – 4724Combined sources
Beta strandi473 – 4819Combined sources
Helixi484 – 49613Combined sources
Helixi501 – 5055Combined sources
Beta strandi511 – 5144Combined sources
Helixi515 – 5195Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ALGNMR-A480-503[»]
1BWCX-ray2.10A45-522[»]
1DNCX-ray1.70A45-522[»]
1GRAX-ray2.00A45-522[»]
1GRBX-ray1.85A45-522[»]
1GREX-ray2.00A45-522[»]
1GRFX-ray2.00A45-522[»]
1GRGX-ray2.00A45-522[»]
1GRHX-ray3.00A45-522[»]
1GRTX-ray2.30A45-522[»]
1GSNX-ray1.70A45-522[»]
1K4QX-ray1.90A62-522[»]
1XANX-ray2.00A62-522[»]
2AAQX-ray2.60A44-522[»]
2GH5X-ray1.70A/B45-522[»]
2GRTX-ray2.70A62-522[»]
3DJGX-ray1.80X59-522[»]
3DJJX-ray1.10A45-522[»]
3DK4X-ray1.20A45-522[»]
3DK8X-ray1.10A45-522[»]
3DK9X-ray0.95A45-522[»]
3GRSX-ray1.54A45-522[»]
3GRTX-ray2.50A62-522[»]
3SQPX-ray2.21A/B45-522[»]
4GR1X-ray2.40A45-522[»]
4GRTX-ray2.80A62-522[»]
5GRTX-ray2.40A62-522[»]
ProteinModelPortaliP00390.
SMRiP00390. Positions 61-522.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00390.

Family & Domainsi

Domaini

Each subunit can be divided into 4 domains that are consecutive along the polypeptide chain. Domains 1 and 2 bind FAD and NADPH, respectively. Domain 4 forms the interface.

Sequence similaritiesi

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

eggNOGiCOG1249.
GeneTreeiENSGT00390000007578.
HOGENOMiHOG000276712.
HOVERGENiHBG004959.
InParanoidiP00390.
KOiK00383.
OMAiSFDPMII.
OrthoDBiEOG7HHWS0.
PhylomeDBiP00390.
TreeFamiTF105353.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR006322. Glutathione_Rdtase_euk/bac.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view]
PfamiPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01421. gluta_reduc_1. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

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

This entry describes 5 isoformsi produced by alternative splicing and alternative initiation. AlignAdd to basket

Isoform Mitochondrial (identifier: P00390-1) [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

        10         20         30         40         50
MALLPRALSA GAGPSWRRAA RAFRGFLLLL PEPAALTRAL SRAMACRQEP
60 70 80 90 100
QPQGPPPAAG AVASYDYLVI GGGSGGLASA RRAAELGARA AVVESHKLGG
110 120 130 140 150
TCVNVGCVPK KVMWNTAVHS EFMHDHADYG FPSCEGKFNW RVIKEKRDAY
160 170 180 190 200
VSRLNAIYQN NLTKSHIEII RGHAAFTSDP KPTIEVSGKK YTAPHILIAT
210 220 230 240 250
GGMPSTPHES QIPGASLGIT SDGFFQLEEL PGRSVIVGAG YIAVEMAGIL
260 270 280 290 300
SALGSKTSLM IRHDKVLRSF DSMISTNCTE ELENAGVEVL KFSQVKEVKK
310 320 330 340 350
TLSGLEVSMV TAVPGRLPVM TMIPDVDCLL WAIGRVPNTK DLSLNKLGIQ
360 370 380 390 400
TDDKGHIIVD EFQNTNVKGI YAVGDVCGKA LLTPVAIAAG RKLAHRLFEY
410 420 430 440 450
KEDSKLDYNN IPTVVFSHPP IGTVGLTEDE AIHKYGIENV KTYSTSFTPM
460 470 480 490 500
YHAVTKRKTK CVMKMVCANK EEKVVGIHMQ GLGCDEMLQG FAVAVKMGAT
510 520
KADFDNTVAI HPTSSEELVT LR
Length:522
Mass (Da):56,257
Last modified:July 11, 2001 - v2
Checksum:iDD8E2BA9D6E3757B
GO
Isoform Cytoplasmic (identifier: P00390-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-43: Missing.

Note: Produced by alternative initiation of isoform Mitochondrial.
Show »
Length:479
Mass (Da):51,701
Checksum:i3C0A194C96E880E7
GO
Isoform 2 (identifier: P00390-3) [UniParc]FASTAAdd to basket

Also known as: delta8

The sequence of this isoform differs from the canonical sequence as follows:
     266-294: Missing.

Show »
Length:493
Mass (Da):53,027
Checksum:iEFBA71DCDCFF1529
GO
Isoform 3 (identifier: P00390-4) [UniParc]FASTAAdd to basket

Also known as: delta9

The sequence of this isoform differs from the canonical sequence as follows:
     295-347: Missing.

Note: Expressed at very high levels in peripheral blood.
Show »
Length:469
Mass (Da):50,497
Checksum:i0AD475B02A87C63E
GO
Isoform 4 (identifier: P00390-5) [UniParc]FASTAAdd to basket

Also known as: delta8+9

The sequence of this isoform differs from the canonical sequence as follows:
     266-294: Missing.
     295-347: Missing.

Show »
Length:440
Mass (Da):47,267
Checksum:i793E0A9F8706B1B5
GO

Sequence cautioni

The sequence AAP88037.1 differs from that shown. Reason: Erroneous initiation. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti153 – 1531R → C.1 Publication
Corresponds to variant rs8190955 [ dbSNP | Ensembl ].
VAR_019079
Natural varianti232 – 2321G → R.
Corresponds to variant rs8190976 [ dbSNP | Ensembl ].
VAR_051775
Natural varianti232 – 2321G → S.1 Publication
Corresponds to variant rs8190976 [ dbSNP | Ensembl ].
VAR_019080
Natural varianti261 – 2611I → V.1 Publication
Corresponds to variant rs8190997 [ dbSNP | Ensembl ].
VAR_019081
Natural varianti297 – 2971E → D.1 Publication
Corresponds to variant rs8191004 [ dbSNP | Ensembl ].
VAR_019082
Natural varianti314 – 3141P → H.
Corresponds to variant rs2020916 [ dbSNP | Ensembl ].
VAR_014554

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4343Missing in isoform Cytoplasmic. 1 PublicationVSP_018972Add
BLAST
Alternative sequencei266 – 29429Missing in isoform 2 and isoform 4. 1 PublicationVSP_042908Add
BLAST
Alternative sequencei295 – 34753Missing in isoform 3 and isoform 4. 1 PublicationVSP_042909Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15722 mRNA. Translation: CAA33744.1.
AF228703 Genomic DNA. Translation: AAF37572.1.
AF228703 Genomic DNA. Translation: AAF37573.1.
AF228704 mRNA. Translation: AAF37574.1.
AY338490 Genomic DNA. Translation: AAP88037.1. Different initiation.
AB519179 mRNA. Translation: BAI43437.1.
AB519180 mRNA. Translation: BAI43438.1.
AB519181 mRNA. Translation: BAI43439.1.
AC009314 Genomic DNA. No translation available.
AC103959 Genomic DNA. No translation available.
AF215848 Genomic DNA. No translation available.
CH471080 Genomic DNA. Translation: EAW63443.1.
CH471080 Genomic DNA. Translation: EAW63445.1.
BC069244 mRNA. Translation: AAH69244.1.
CCDSiCCDS34877.1. [P00390-1]
CCDS56530.1. [P00390-5]
CCDS56531.1. [P00390-3]
CCDS56532.1. [P00390-4]
PIRiS08979. RDHUU.
RefSeqiNP_000628.2. NM_000637.3. [P00390-1]
NP_001182031.1. NM_001195102.1. [P00390-3]
NP_001182032.1. NM_001195103.1. [P00390-4]
NP_001182033.1. NM_001195104.1. [P00390-5]
UniGeneiHs.271510.

Genome annotation databases

EnsembliENST00000221130; ENSP00000221130; ENSG00000104687. [P00390-1]
ENST00000537535; ENSP00000438845; ENSG00000104687. [P00390-5]
ENST00000541648; ENSP00000444559; ENSG00000104687. [P00390-4]
ENST00000546342; ENSP00000445516; ENSG00000104687. [P00390-3]
GeneIDi2936.
KEGGihsa:2936.
UCSCiuc003xih.2. human. [P00390-1]
uc022ato.1. human. [P00390-4]
uc022atp.1. human. [P00390-3]
uc022atq.1. human. [P00390-5]

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Wikipedia

Glutathione reductase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15722 mRNA. Translation: CAA33744.1.
AF228703 Genomic DNA. Translation: AAF37572.1.
AF228703 Genomic DNA. Translation: AAF37573.1.
AF228704 mRNA. Translation: AAF37574.1.
AY338490 Genomic DNA. Translation: AAP88037.1. Different initiation.
AB519179 mRNA. Translation: BAI43437.1.
AB519180 mRNA. Translation: BAI43438.1.
AB519181 mRNA. Translation: BAI43439.1.
AC009314 Genomic DNA. No translation available.
AC103959 Genomic DNA. No translation available.
AF215848 Genomic DNA. No translation available.
CH471080 Genomic DNA. Translation: EAW63443.1.
CH471080 Genomic DNA. Translation: EAW63445.1.
BC069244 mRNA. Translation: AAH69244.1.
CCDSiCCDS34877.1. [P00390-1]
CCDS56530.1. [P00390-5]
CCDS56531.1. [P00390-3]
CCDS56532.1. [P00390-4]
PIRiS08979. RDHUU.
RefSeqiNP_000628.2. NM_000637.3. [P00390-1]
NP_001182031.1. NM_001195102.1. [P00390-3]
NP_001182032.1. NM_001195103.1. [P00390-4]
NP_001182033.1. NM_001195104.1. [P00390-5]
UniGeneiHs.271510.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ALGNMR-A480-503[»]
1BWCX-ray2.10A45-522[»]
1DNCX-ray1.70A45-522[»]
1GRAX-ray2.00A45-522[»]
1GRBX-ray1.85A45-522[»]
1GREX-ray2.00A45-522[»]
1GRFX-ray2.00A45-522[»]
1GRGX-ray2.00A45-522[»]
1GRHX-ray3.00A45-522[»]
1GRTX-ray2.30A45-522[»]
1GSNX-ray1.70A45-522[»]
1K4QX-ray1.90A62-522[»]
1XANX-ray2.00A62-522[»]
2AAQX-ray2.60A44-522[»]
2GH5X-ray1.70A/B45-522[»]
2GRTX-ray2.70A62-522[»]
3DJGX-ray1.80X59-522[»]
3DJJX-ray1.10A45-522[»]
3DK4X-ray1.20A45-522[»]
3DK8X-ray1.10A45-522[»]
3DK9X-ray0.95A45-522[»]
3GRSX-ray1.54A45-522[»]
3GRTX-ray2.50A62-522[»]
3SQPX-ray2.21A/B45-522[»]
4GR1X-ray2.40A45-522[»]
4GRTX-ray2.80A62-522[»]
5GRTX-ray2.40A62-522[»]
ProteinModelPortaliP00390.
SMRiP00390. Positions 61-522.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109191. 26 interactions.
IntActiP00390. 4 interactions.
MINTiMINT-5000460.
STRINGi9606.ENSP00000221130.

Chemistry

BindingDBiP00390.
ChEMBLiCHEMBL2755.
DrugBankiDB00262. Carmustine.
DB03147. Flavin adenine dinucleotide.
DB00143. Glutathione.
GuidetoPHARMACOLOGYi2613.

PTM databases

PhosphoSiteiP00390.

Polymorphism and mutation databases

BioMutaiGSR.
DMDMi14916998.

2D gel databases

REPRODUCTION-2DPAGEIPI00759575.

Proteomic databases

PaxDbiP00390.
PRIDEiP00390.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000221130; ENSP00000221130; ENSG00000104687. [P00390-1]
ENST00000537535; ENSP00000438845; ENSG00000104687. [P00390-5]
ENST00000541648; ENSP00000444559; ENSG00000104687. [P00390-4]
ENST00000546342; ENSP00000445516; ENSG00000104687. [P00390-3]
GeneIDi2936.
KEGGihsa:2936.
UCSCiuc003xih.2. human. [P00390-1]
uc022ato.1. human. [P00390-4]
uc022atp.1. human. [P00390-3]
uc022atq.1. human. [P00390-5]

Organism-specific databases

CTDi2936.
GeneCardsiGC08M030535.
HGNCiHGNC:4623. GSR.
HPAiCAB008632.
HPA001538.
MIMi138300. gene+phenotype.
neXtProtiNX_P00390.
Orphaneti90030. Hemolytic anemia due to glutathione reductase deficiency.
PharmGKBiPA29014.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1249.
GeneTreeiENSGT00390000007578.
HOGENOMiHOG000276712.
HOVERGENiHBG004959.
InParanoidiP00390.
KOiK00383.
OMAiSFDPMII.
OrthoDBiEOG7HHWS0.
PhylomeDBiP00390.
TreeFamiTF105353.

Enzyme and pathway databases

BioCyciMetaCyc:HS02602-MONOMER.
BRENDAi1.8.1.7. 2681.
ReactomeiREACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.
REACT_264249. Detoxification of Reactive Oxygen Species.
REACT_355377. TP53 Regulates Metabolic Genes.
SABIO-RKP00390.

Miscellaneous databases

EvolutionaryTraceiP00390.
GeneWikiiGlutathione_reductase.
GenomeRNAii2936.
NextBioi11635.
PROiP00390.
SOURCEiSearch...

Gene expression databases

BgeeiP00390.
CleanExiHS_GSR.
ExpressionAtlasiP00390. baseline and differential.
GenevisibleiP00390. HS.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR006322. Glutathione_Rdtase_euk/bac.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view]
PfamiPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01421. gluta_reduc_1. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequencing of mammalian glutathione reductase cDNA."
    Tutic M., Lu X.A., Schirmer R.H., Werner D.
    Eur. J. Biochem. 188:523-528(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CYTOPLASMIC).
    Tissue: Placenta.
  2. "Structural organization of the human glutathione reductase (GSR) gene: determination of correct cDNA sequence and identification of a mitochondrial leader sequence."
    Kelner M.J., Montoya M.A.
    Biochem. Biophys. Res. Commun. 269:366-368(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM MITOCHONDRIAL), ALTERNATIVE INITIATION.
  3. NIEHS SNPs program
    Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CYS-153; SER-232; VAL-261 AND ASP-297.
  4. "Expression of glutathione reductase splice variants in human tissues."
    Satoh N., Watanabe N., Kanda A., Sugaya-Fukazawa M., Hisatomi H.
    Biochem. Genet. 48:816-821(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
  5. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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 MITOCHONDRIAL).
    Tissue: Lung.
  8. "Glutathione reductase from human erythrocytes. The sequences of the NADPH domain and of the interface domain."
    Krauth-Siegel R.L., Blatterspiel R., Saleh M., Schiltz E., Schirmer R.H., Untucht-Grau R.
    Eur. J. Biochem. 121:259-267(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 45-522.
  9. "Glutathione reductase from human erythrocytes. Isolation of the enzyme and sequence analysis of the redox-active peptide."
    Krohne-Ehrich G., Schirmer R.H., Untucht-Grau R.
    Eur. J. Biochem. 80:65-71(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 98-110.
    Tissue: Erythrocyte.
  10. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. "Three-dimensional structure of glutathione reductase at 2-A resolution."
    Thieme R., Pai E.F., Schirmer R.H., Schulz G.E.
    J. Mol. Biol. 152:763-782(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2 ANGSTROMS) OF 45-522.
  14. "Refined structure of glutathione reductase at 1.54-A resolution."
    Karplus P.A., Schulz G.E.
    J. Mol. Biol. 195:701-729(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 45-522.
  15. "Kinetics and crystallographic analysis of human glutathione reductase in complex with a xanthene inhibitor."
    Savvides S.N., Karplus P.A.
    J. Biol. Chem. 271:8101-8107(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 62-522, DISULFIDE BONDS.
  16. "Glutathione reductase turned into trypanothione reductase: structural analysis of an engineered change in substrate specificity."
    Stoll V.S., Simpson S.J., Krauth-Siegel R.L., Walsh C.T., Pai E.F.
    Biochemistry 36:6437-6447(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 62-522.
  17. "Enzyme inactivation through sulfhydryl oxidation by physiologic NO-carriers."
    Becker K., Savvides S.N., Keese M., Schirmer R.H., Karplus P.A.
    Nat. Struct. Biol. 5:267-271(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 62-522.

Entry informationi

Entry nameiGSHR_HUMAN
AccessioniPrimary (citable) accession number: P00390
Secondary accession number(s): C8KIL8
, C8KIL9, C8KIM0, D3DSV3, Q7Z5C9, Q9NP63
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 11, 2001
Last modified: June 24, 2015
This is version 204 of the entry and version 2 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 active site is a redox-active disulfide bond.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: 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

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 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.