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P35754

- GLRX1_HUMAN

UniProt

P35754 - GLRX1_HUMAN

Protein

Glutaredoxin-1

Gene

GLRX

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

    Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins.

    GO - Molecular functioni

    1. electron carrier activity Source: InterPro
    2. glutathione disulfide oxidoreductase activity Source: ProtInc
    3. protein disulfide oxidoreductase activity Source: InterPro
    4. protein N-terminus binding Source: UniProtKB

    GO - Biological processi

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

    Keywords - Biological processi

    Electron transport, Transport

    Enzyme and pathway databases

    BioCyciMetaCyc:HS04268-MONOMER.
    ReactomeiREACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.
    SABIO-RKP35754.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutaredoxin-1
    Alternative name(s):
    Thioltransferase-1
    Short name:
    TTase-1
    Gene namesi
    Name:GLRX
    Synonyms:GRX
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:4330. GLRX.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. extracellular vesicular exosome Source: UniProt
    3. mitochondrion Source: Ensembl
    4. nucleus Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28731.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 106105Glutaredoxin-1PRO_0000141600Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei9 – 91N6-succinyllysineBy similarity
    Disulfide bondi23 ↔ 26Redox-active
    Disulfide bondi79 ↔ 83

    Keywords - PTMi

    Acetylation, Disulfide bond

    Proteomic databases

    MaxQBiP35754.
    PaxDbiP35754.
    PeptideAtlasiP35754.
    PRIDEiP35754.

    2D gel databases

    UCD-2DPAGEP35754.

    PTM databases

    PhosphoSiteiP35754.

    Expressioni

    Gene expression databases

    BgeeiP35754.
    CleanExiHS_GLRX.
    GenevestigatoriP35754.

    Organism-specific databases

    HPAiCAB008634.

    Interactioni

    Protein-protein interaction databases

    BioGridi109007. 8 interactions.
    IntActiP35754. 4 interactions.
    MINTiMINT-4649604.
    STRINGi9606.ENSP00000237858.

    Structurei

    Secondary structure

    1
    106
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 74
    Beta strandi15 – 195
    Helixi24 – 3512
    Helixi40 – 423
    Beta strandi43 – 475
    Turni48 – 514
    Helixi54 – 6411
    Beta strandi72 – 754
    Beta strandi78 – 825
    Helixi83 – 9210
    Helixi94 – 1029

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B4QNMR-A2-106[»]
    1JHBNMR-A1-106[»]
    ProteinModelPortaliP35754.
    SMRiP35754. Positions 2-106.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP35754.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 106104GlutaredoxinPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    eggNOGiCOG0695.
    HOGENOMiHOG000095204.
    HOVERGENiHBG000283.
    InParanoidiP35754.
    KOiK03676.
    OMAiDAKYLTI.
    OrthoDBiEOG7QRQWZ.
    PhylomeDBiP35754.
    TreeFamiTF326994.

    Family and domain databases

    Gene3Di3.40.30.10. 1 hit.
    InterProiIPR011767. GLR_AS.
    IPR002109. 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.
    PROSITEiPS00195. GLUTAREDOXIN_1. 1 hit.
    PS51354. GLUTAREDOXIN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P35754-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAQEFVNCKI QPGKVVVFIK PTCPYCRRAQ EILSQLPIKQ GLLEFVDITA    50
    TNHTNEIQDY LQQLTGARTV PRVFIGKDCI GGCSDLVSLQ QSGELLTRLK 100
    QIGALQ 106
    Length:106
    Mass (Da):11,776
    Last modified:January 23, 2007 - v2
    Checksum:iBB86FED55967EBE2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti96 – 961L → V in BAA04769. (PubMed:8018729)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti47 – 471D → Y.
    Corresponds to variant rs4767 [ dbSNP | Ensembl ].
    VAR_049189

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D21238 mRNA. Translation: BAA04769.1.
    X76648 mRNA. Translation: CAA54094.1.
    AF069668 mRNA. Translation: AAC35798.1.
    AF115105, AF115104 Genomic DNA. Translation: AAC98318.1.
    AF162769 mRNA. Translation: AAD43353.1.
    BT006689 mRNA. Translation: AAP35335.1.
    CR450312 mRNA. Translation: CAG29308.1.
    CR542165 mRNA. Translation: CAG46962.1.
    AK311868 mRNA. Translation: BAG34809.1.
    DQ026062 Genomic DNA. Translation: AAY29058.1.
    CH471084 Genomic DNA. Translation: EAW96056.1.
    BC005304 mRNA. Translation: AAH05304.1.
    BC010965 mRNA. Translation: AAH10965.1.
    BC106075 mRNA. Translation: AAI06076.1.
    CCDSiCCDS4078.1.
    PIRiS68701. S47472.
    RefSeqiNP_001112362.1. NM_001118890.1.
    NP_001230587.1. NM_001243658.1.
    NP_001230588.1. NM_001243659.1.
    NP_002055.1. NM_002064.2.
    UniGeneiHs.28988.

    Genome annotation databases

    EnsembliENST00000237858; ENSP00000237858; ENSG00000173221.
    ENST00000379979; ENSP00000369314; ENSG00000173221.
    ENST00000505427; ENSP00000427353; ENSG00000173221.
    ENST00000508780; ENSP00000422708; ENSG00000173221.
    ENST00000512469; ENSP00000424636; ENSG00000173221.
    GeneIDi2745.
    KEGGihsa:2745.
    UCSCiuc003kln.4. human.

    Polymorphism databases

    DMDMi1346143.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D21238 mRNA. Translation: BAA04769.1 .
    X76648 mRNA. Translation: CAA54094.1 .
    AF069668 mRNA. Translation: AAC35798.1 .
    AF115105 , AF115104 Genomic DNA. Translation: AAC98318.1 .
    AF162769 mRNA. Translation: AAD43353.1 .
    BT006689 mRNA. Translation: AAP35335.1 .
    CR450312 mRNA. Translation: CAG29308.1 .
    CR542165 mRNA. Translation: CAG46962.1 .
    AK311868 mRNA. Translation: BAG34809.1 .
    DQ026062 Genomic DNA. Translation: AAY29058.1 .
    CH471084 Genomic DNA. Translation: EAW96056.1 .
    BC005304 mRNA. Translation: AAH05304.1 .
    BC010965 mRNA. Translation: AAH10965.1 .
    BC106075 mRNA. Translation: AAI06076.1 .
    CCDSi CCDS4078.1.
    PIRi S68701. S47472.
    RefSeqi NP_001112362.1. NM_001118890.1.
    NP_001230587.1. NM_001243658.1.
    NP_001230588.1. NM_001243659.1.
    NP_002055.1. NM_002064.2.
    UniGenei Hs.28988.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B4Q NMR - A 2-106 [» ]
    1JHB NMR - A 1-106 [» ]
    ProteinModelPortali P35754.
    SMRi P35754. Positions 2-106.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109007. 8 interactions.
    IntActi P35754. 4 interactions.
    MINTi MINT-4649604.
    STRINGi 9606.ENSP00000237858.

    Chemistry

    DrugBanki DB00143. Glutathione.

    PTM databases

    PhosphoSitei P35754.

    Polymorphism databases

    DMDMi 1346143.

    2D gel databases

    UCD-2DPAGE P35754.

    Proteomic databases

    MaxQBi P35754.
    PaxDbi P35754.
    PeptideAtlasi P35754.
    PRIDEi P35754.

    Protocols and materials databases

    DNASUi 2745.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000237858 ; ENSP00000237858 ; ENSG00000173221 .
    ENST00000379979 ; ENSP00000369314 ; ENSG00000173221 .
    ENST00000505427 ; ENSP00000427353 ; ENSG00000173221 .
    ENST00000508780 ; ENSP00000422708 ; ENSG00000173221 .
    ENST00000512469 ; ENSP00000424636 ; ENSG00000173221 .
    GeneIDi 2745.
    KEGGi hsa:2745.
    UCSCi uc003kln.4. human.

    Organism-specific databases

    CTDi 2745.
    GeneCardsi GC05M095087.
    HGNCi HGNC:4330. GLRX.
    HPAi CAB008634.
    MIMi 600443. gene.
    neXtProti NX_P35754.
    PharmGKBi PA28731.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0695.
    HOGENOMi HOG000095204.
    HOVERGENi HBG000283.
    InParanoidi P35754.
    KOi K03676.
    OMAi DAKYLTI.
    OrthoDBi EOG7QRQWZ.
    PhylomeDBi P35754.
    TreeFami TF326994.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS04268-MONOMER.
    Reactomei REACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.
    SABIO-RK P35754.

    Miscellaneous databases

    EvolutionaryTracei P35754.
    GeneWikii GLRX.
    GenomeRNAii 2745.
    NextBioi 10820.
    PROi P35754.
    SOURCEi Search...

    Gene expression databases

    Bgeei P35754.
    CleanExi HS_GLRX.
    Genevestigatori P35754.

    Family and domain databases

    Gene3Di 3.40.30.10. 1 hit.
    InterProi IPR011767. GLR_AS.
    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 PS00195. GLUTAREDOXIN_1. 1 hit.
    PS51354. GLUTAREDOXIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    2. "Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin."
      Padilla C.A., Martinez-Galisteo E., Barcena J.A., Spyrou G., Holmgren A.
      Eur. J. Biochem. 227:27-34(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Spleen.
    3. "Purification, cloning and expression of dehydroascorbic acid-reducing activity from human neutrophils: identification as glutaredoxin."
      Park J.B., Levine M.
      Biochem. J. 315:931-938(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    4. "The human glutaredoxin gene: determination of its organization, transcription start point, and promoter analysis."
      Park J.B., Levine M.
      Gene 197:189-193(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Human lens thioltransferase: cloning, purification, and function."
      Qiao F., Xing K.Y., Liu A., Ehlers N., Raghavachari N., Lou M.F.
      Invest. Ophthalmol. Vis. Sci. 42:743-751(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Lens.
    6. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    7. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    8. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    9. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    10. NIEHS SNPs program
      Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    11. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    12. "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].
      Tissue: Liver, Skin and Urinary bladder.
    13. "The primary structure and properties of thioltransferase (glutaredoxin) from human red blood cells."
      Papov V.V., Gravina S.A., Mieyal J.J., Biemann K.
      Protein Sci. 3:428-434(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-106.
      Tissue: Blood.
    14. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "The NMR solution structure of human glutaredoxin in the fully reduced form."
      Sun C., Berardi M.J., Bushweller J.H.
      J. Mol. Biol. 280:687-701(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    17. "Reactivity of the human thioltransferase (glutaredoxin) C7S, C25S, C78S, C82S mutant and NMR solution structure of its glutathionyl mixed disulfide intermediate reflect catalytic specificity."
      Yang Y., Jao S.C., Nanduri S., Starke D.W., Mieyal J.J., Qin J.
      Biochemistry 37:17145-17156(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.

    Entry informationi

    Entry nameiGLRX1_HUMAN
    AccessioniPrimary (citable) accession number: P35754
    Secondary accession number(s): B2R4L2, Q3KQS1, Q6ICT1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 147 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

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 5
      Human chromosome 5: 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