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P00390

- GSHR_HUMAN

UniProt

P00390 - GSHR_HUMAN

Protein

Glutathione reductase, mitochondrial

Gene

GSR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 196 (01 Oct 2014)
      Sequence version 2 (11 Jul 2001)
      Previous versions | rss
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    Functioni

    Maintains high levels of reduced glutathione in the cytosol.

    Catalytic activityi

    2 glutathione + NADP+ = glutathione disulfide + NADPH.

    Cofactori

    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

    1. electron carrier activity Source: UniProtKB
    2. flavin adenine dinucleotide binding Source: InterPro
    3. glutathione-disulfide reductase activity Source: Reactome
    4. NADP binding Source: InterPro

    GO - Biological processi

    1. cell redox homeostasis Source: InterPro
    2. glutathione metabolic process Source: InterPro
    3. nucleobase-containing small molecule interconversion Source: Reactome
    4. nucleobase-containing small molecule metabolic process Source: Reactome
    5. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:HS02602-MONOMER.
    ReactomeiREACT_172715. Detoxification of Reactive Oxygen Species.
    REACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.
    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: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:4623. GSR.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt
    3. mitochondrial matrix Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

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

    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

    MaxQBiP00390.
    PaxDbiP00390.
    PRIDEiP00390.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00759575.

    PTM databases

    PhosphoSiteiP00390.

    Expressioni

    Gene expression databases

    ArrayExpressiP00390.
    BgeeiP00390.
    CleanExiHS_GSR.
    GenevestigatoriP00390.

    Organism-specific databases

    HPAiCAB008632.
    HPA001538.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked.1 Publication

    Protein-protein interaction databases

    BioGridi109191. 27 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 – 643
    Beta strandi66 – 705
    Helixi74 – 8512
    Beta strandi90 – 967
    Helixi100 – 1056
    Helixi107 – 12317
    Turni124 – 1307
    Helixi140 – 16425
    Beta strandi168 – 1725
    Beta strandi174 – 1763
    Beta strandi183 – 1864
    Beta strandi189 – 1924
    Beta strandi196 – 1983
    Beta strandi202 – 2043
    Turni209 – 2113
    Helixi215 – 2173
    Helixi221 – 2244
    Beta strandi232 – 2376
    Helixi241 – 25212
    Beta strandi256 – 2605
    Beta strandi262 – 2665
    Helixi272 – 28413
    Beta strandi288 – 2903
    Beta strandi293 – 3008
    Beta strandi302 – 31110
    Beta strandi319 – 33113
    Beta strandi335 – 3384
    Turni340 – 3434
    Helixi344 – 3474
    Beta strandi370 – 3723
    Helixi374 – 3774
    Helixi383 – 39816
    Beta strandi413 – 4153
    Beta strandi417 – 4193
    Beta strandi421 – 4255
    Helixi428 – 4358
    Helixi437 – 4393
    Beta strandi440 – 4478
    Helixi450 – 4545
    Beta strandi461 – 4688
    Turni469 – 4724
    Beta strandi473 – 4819
    Helixi484 – 49613
    Helixi501 – 5055
    Beta strandi511 – 5144
    Helixi515 – 5195

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000276712.
    HOVERGENiHBG004959.
    InParanoidiP00390.
    KOiK00383.
    OMAiGTNSDGF.
    OrthoDBiEOG7HHWS0.
    PhylomeDBiP00390.
    TreeFamiTF105353.

    Family and domain databases

    Gene3Di3.30.390.30. 1 hit.
    InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
    IPR013027. FAD_pyr_nucl-diS_OxRdtase.
    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]
    PRINTSiPR00368. FADPNR.
    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. Align

    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

    MALLPRALSA GAGPSWRRAA RAFRGFLLLL PEPAALTRAL SRAMACRQEP    50
    QPQGPPPAAG AVASYDYLVI GGGSGGLASA RRAAELGARA AVVESHKLGG 100
    TCVNVGCVPK KVMWNTAVHS EFMHDHADYG FPSCEGKFNW RVIKEKRDAY 150
    VSRLNAIYQN NLTKSHIEII RGHAAFTSDP KPTIEVSGKK YTAPHILIAT 200
    GGMPSTPHES QIPGASLGIT SDGFFQLEEL PGRSVIVGAG YIAVEMAGIL 250
    SALGSKTSLM IRHDKVLRSF DSMISTNCTE ELENAGVEVL KFSQVKEVKK 300
    TLSGLEVSMV TAVPGRLPVM TMIPDVDCLL WAIGRVPNTK DLSLNKLGIQ 350
    TDDKGHIIVD EFQNTNVKGI YAVGDVCGKA LLTPVAIAAG RKLAHRLFEY 400
    KEDSKLDYNN IPTVVFSHPP IGTVGLTEDE AIHKYGIENV KTYSTSFTPM 450
    YHAVTKRKTK CVMKMVCANK EEKVVGIHMQ GLGCDEMLQG FAVAVKMGAT 500
    KADFDNTVAI HPTSSEELVT LR 522
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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]

    Polymorphism databases

    DMDMi14916998.

    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS34877.1. [P00390-1 ]
    CCDS56530.1. [P00390-5 ]
    CCDS56531.1. [P00390-3 ]
    CCDS56532.1. [P00390-4 ]
    PIRi S08979. RDHUU.
    RefSeqi NP_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 ]
    UniGenei Hs.271510.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ALG NMR - A 480-503 [» ]
    1BWC X-ray 2.10 A 45-522 [» ]
    1DNC X-ray 1.70 A 45-522 [» ]
    1GRA X-ray 2.00 A 45-522 [» ]
    1GRB X-ray 1.85 A 45-522 [» ]
    1GRE X-ray 2.00 A 45-522 [» ]
    1GRF X-ray 2.00 A 45-522 [» ]
    1GRG X-ray 2.00 A 45-522 [» ]
    1GRH X-ray 3.00 A 45-522 [» ]
    1GRT X-ray 2.30 A 45-522 [» ]
    1GSN X-ray 1.70 A 45-522 [» ]
    1K4Q X-ray 1.90 A 62-522 [» ]
    1XAN X-ray 2.00 A 62-522 [» ]
    2AAQ X-ray 2.60 A 44-522 [» ]
    2GH5 X-ray 1.70 A/B 45-522 [» ]
    2GRT X-ray 2.70 A 62-522 [» ]
    3DJG X-ray 1.80 X 59-522 [» ]
    3DJJ X-ray 1.10 A 45-522 [» ]
    3DK4 X-ray 1.20 A 45-522 [» ]
    3DK8 X-ray 1.10 A 45-522 [» ]
    3DK9 X-ray 0.95 A 45-522 [» ]
    3GRS X-ray 1.54 A 45-522 [» ]
    3GRT X-ray 2.50 A 62-522 [» ]
    3SQP X-ray 2.21 A/B 45-522 [» ]
    4GR1 X-ray 2.40 A 45-522 [» ]
    4GRT X-ray 2.80 A 62-522 [» ]
    5GRT X-ray 2.40 A 62-522 [» ]
    ProteinModelPortali P00390.
    SMRi P00390. Positions 61-522.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109191. 27 interactions.
    IntActi P00390. 4 interactions.
    MINTi MINT-5000460.
    STRINGi 9606.ENSP00000221130.

    Chemistry

    BindingDBi P00390.
    ChEMBLi CHEMBL2755.
    DrugBanki DB00262. Carmustine.
    DB00143. Glutathione.
    DB00157. NADH.
    GuidetoPHARMACOLOGYi 2613.

    PTM databases

    PhosphoSitei P00390.

    Polymorphism databases

    DMDMi 14916998.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00759575.

    Proteomic databases

    MaxQBi P00390.
    PaxDbi P00390.
    PRIDEi P00390.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000221130 ; ENSP00000221130 ; ENSG00000104687 . [P00390-1 ]
    ENST00000537535 ; ENSP00000438845 ; ENSG00000104687 . [P00390-5 ]
    ENST00000541648 ; ENSP00000444559 ; ENSG00000104687 . [P00390-4 ]
    ENST00000546342 ; ENSP00000445516 ; ENSG00000104687 . [P00390-3 ]
    GeneIDi 2936.
    KEGGi hsa:2936.
    UCSCi uc003xih.2. human. [P00390-1 ]
    uc022ato.1. human. [P00390-4 ]
    uc022atp.1. human. [P00390-3 ]
    uc022atq.1. human. [P00390-5 ]

    Organism-specific databases

    CTDi 2936.
    GeneCardsi GC08M030535.
    HGNCi HGNC:4623. GSR.
    HPAi CAB008632.
    HPA001538.
    MIMi 138300. gene+phenotype.
    neXtProti NX_P00390.
    Orphaneti 90030. Hemolytic anemia due to glutathione reductase deficiency.
    PharmGKBi PA29014.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1249.
    HOGENOMi HOG000276712.
    HOVERGENi HBG004959.
    InParanoidi P00390.
    KOi K00383.
    OMAi GTNSDGF.
    OrthoDBi EOG7HHWS0.
    PhylomeDBi P00390.
    TreeFami TF105353.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS02602-MONOMER.
    Reactomei REACT_172715. Detoxification of Reactive Oxygen Species.
    REACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.
    SABIO-RK P00390.

    Miscellaneous databases

    EvolutionaryTracei P00390.
    GeneWikii Glutathione_reductase.
    GenomeRNAii 2936.
    NextBioi 11635.
    PROi P00390.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P00390.
    Bgeei P00390.
    CleanExi HS_GSR.
    Genevestigatori P00390.

    Family and domain databases

    Gene3Di 3.30.390.30. 1 hit.
    InterProi IPR016156. FAD/NAD-linked_Rdtase_dimer.
    IPR013027. FAD_pyr_nucl-diS_OxRdtase.
    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 ]
    Pfami PF00070. Pyr_redox. 1 hit.
    PF07992. Pyr_redox_2. 1 hit.
    PF02852. Pyr_redox_dim. 1 hit.
    [Graphical view ]
    PRINTSi PR00368. FADPNR.
    SUPFAMi SSF55424. SSF55424. 1 hit.
    TIGRFAMsi TIGR01421. gluta_reduc_1. 1 hit.
    PROSITEi PS00076. PYRIDINE_REDOX_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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.
    13. "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.
    14. "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.
    15. "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.
    16. "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: October 1, 2014
    This is version 196 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