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Q06830

- PRDX1_HUMAN

UniProt

Q06830 - PRDX1_HUMAN

Protein

Peroxiredoxin-1

Gene

PRDX1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 164 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      Previous versions | rss
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    Functioni

    Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2. Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation By similarity.By similarity

    Catalytic activityi

    2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei52 – 521Cysteine sulfenic acid (-SOH) intermediate

    GO - Molecular functioni

    1. heme binding Source: Ensembl
    2. peroxidase activity Source: MGI
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: IntAct
    5. thioredoxin peroxidase activity Source: BHF-UCL

    GO - Biological processi

    1. cell proliferation Source: ProtInc
    2. erythrocyte homeostasis Source: Ensembl
    3. hydrogen peroxide catabolic process Source: BHF-UCL
    4. natural killer cell mediated cytotoxicity Source: Ensembl
    5. regulation of NF-kappaB import into nucleus Source: Ensembl
    6. regulation of stress-activated MAPK cascade Source: Ensembl
    7. removal of superoxide radicals Source: Ensembl
    8. retina homeostasis Source: UniProt
    9. skeletal system development Source: ProtInc

    Keywords - Molecular functioni

    Antioxidant, Oxidoreductase, Peroxidase

    Enzyme and pathway databases

    ReactomeiREACT_172715. Detoxification of Reactive Oxygen Species.

    Protein family/group databases

    PeroxiBasei4501. Hs2CysPrx01.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peroxiredoxin-1 (EC:1.11.1.15)
    Alternative name(s):
    Natural killer cell-enhancing factor A
    Short name:
    NKEF-A
    Proliferation-associated gene protein
    Short name:
    PAG
    Thioredoxin peroxidase 2
    Thioredoxin-dependent peroxide reductase 2
    Gene namesi
    Name:PRDX1
    Synonyms:PAGA, PAGB, TDPX2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:9352. PRDX1.

    Subcellular locationi

    Cytoplasm 1 Publication. Melanosome 1 Publication
    Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. cytosol Source: Reactome
    3. extracellular space Source: UniProt
    4. extracellular vesicular exosome Source: UniProt
    5. melanosome Source: UniProtKB-SubCell
    6. mitochondrial matrix Source: Ensembl
    7. nuclear euchromatin Source: Ensembl
    8. nucleolus Source: Ensembl
    9. nucleus Source: UniProt
    10. peroxisomal matrix Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi90 – 901T → A: Abolishes phosphorylation by CDK1; 30% reduction in enzymatic activity. 1 Publication
    Mutagenesisi90 – 901T → D: 87% reduction in enzymatic activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA33722.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 199198Peroxiredoxin-1PRO_0000135076Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei7 – 71N6-acetyllysine1 Publication
    Modified residuei16 – 161N6-acetyllysine1 Publication
    Modified residuei27 – 271N6-acetyllysine1 Publication
    Modified residuei35 – 351N6-acetyllysine; alternate1 Publication
    Modified residuei35 – 351N6-succinyllysine; alternateBy similarity
    Disulfide bondi52 – 52Interchain (with C-173); in linked form
    Modified residuei90 – 901Phosphothreonine; by CDK11 Publication
    Modified residuei136 – 1361N6-acetyllysineBy similarity
    Disulfide bondi173 – 173Interchain (with C-52); in linked form

    Post-translational modificationi

    Phosphorylated on Thr-90 during the M-phase, which leads to a more than 80% decrease in enzymatic activity.1 Publication

    Keywords - PTMi

    Acetylation, Disulfide bond, Phosphoprotein

    Proteomic databases

    MaxQBiQ06830.
    PaxDbiQ06830.
    PRIDEiQ06830.

    2D gel databases

    DOSAC-COBS-2DPAGEQ06830.
    OGPiQ06830.
    SWISS-2DPAGEQ06830.
    UCD-2DPAGEQ06830.

    PTM databases

    PhosphoSiteiQ06830.

    Expressioni

    Inductioni

    Constitutively expressed in most human cells; is induced to higher levels upon serum stimulation in untransformed and transformed cells.

    Gene expression databases

    BgeeiQ06830.
    CleanExiHS_PRDX1.
    GenevestigatoriQ06830.

    Organism-specific databases

    HPAiCAB004682.
    HPA007730.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked, upon oxidation By similarity. May form heterodimers with AOP2. Interacts with GDPD5; forms a mixed-disulfide with GDPD5 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARP102753EBI-353193,EBI-608057
    PTENP604847EBI-353193,EBI-696162

    Protein-protein interaction databases

    BioGridi111089. 91 interactions.
    DIPiDIP-33152N.
    IntActiQ06830. 39 interactions.
    MINTiMINT-4999060.
    STRINGi9606.ENSP00000262746.

    Structurei

    Secondary structure

    1
    199
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi16 – 205
    Beta strandi26 – 305
    Helixi31 – 344
    Beta strandi37 – 437
    Helixi54 – 618
    Helixi63 – 686
    Beta strandi71 – 799
    Helixi81 – 888
    Helixi92 – 943
    Beta strandi104 – 1063
    Helixi111 – 1155
    Turni121 – 1233
    Beta strandi124 – 1263
    Beta strandi128 – 1336
    Beta strandi137 – 1459
    Helixi153 – 16816
    Beta strandi169 – 1713
    Helixi181 – 1833

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2RIIX-ray2.60A/B1-199[»]
    3HY2X-ray2.10A/B1-199[»]
    ProteinModelPortaliQ06830.
    SMRiQ06830. Positions 3-187.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ06830.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini6 – 165160ThioredoxinPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the AhpC/TSA family.Curated
    Contains 1 thioredoxin domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    eggNOGiCOG0450.
    HOVERGENiHBG000286.
    InParanoidiQ06830.
    KOiK13279.
    OMAiEMKIPLV.
    OrthoDBiEOG7T1RCD.
    PhylomeDBiQ06830.
    TreeFamiTF105181.

    Family and domain databases

    Gene3Di3.40.30.10. 1 hit.
    InterProiIPR000866. AhpC/TSA.
    IPR024706. Peroxiredoxin_AhpC-typ.
    IPR019479. Peroxiredoxin_C.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF10417. 1-cysPrx_C. 1 hit.
    PF00578. AhpC-TSA. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000239. AHPC. 1 hit.
    SUPFAMiSSF52833. SSF52833. 1 hit.
    PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q06830-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSGNAKIGH PAPNFKATAV MPDGQFKDIS LSDYKGKYVV FFFYPLDFTF    50
    VCPTEIIAFS DRAEEFKKLN CQVIGASVDS HFCHLAWVNT PKKQGGLGPM 100
    NIPLVSDPKR TIAQDYGVLK ADEGISFRGL FIIDDKGILR QITVNDLPVG 150
    RSVDETLRLV QAFQFTDKHG EVCPAGWKPG SDTIKPDVQK SKEYFSKQK 199
    Length:199
    Mass (Da):22,110
    Last modified:June 1, 1994 - v1
    Checksum:i8F68E56D75BF5304
    GO

    Sequence cautioni

    The sequence CAI13097.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti147 – 1471L → P(PubMed:8026862)Curated
    Sequence conflicti149 – 1502VG → CC(PubMed:8026862)Curated
    Sequence conflicti189 – 1891Q → P(PubMed:8026862)Curated
    Sequence conflicti191 – 1911S → T(PubMed:8026862)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti62 – 621R → G.1 Publication
    Corresponds to variant rs34034070 [ dbSNP | Ensembl ].
    VAR_025050

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X67951 mRNA. Translation: CAA48137.1.
    L19184 mRNA. Translation: AAA50464.1.
    BT019740 mRNA. Translation: AAV38545.1.
    CR407652 mRNA. Translation: CAG28580.1.
    DQ297142 Genomic DNA. Translation: ABB84465.1.
    AB451262 mRNA. Translation: BAG70076.1.
    AB451388 mRNA. Translation: BAG70202.1.
    AL451136 Genomic DNA. Translation: CAI13095.1.
    AL451136 Genomic DNA. Translation: CAI13096.1.
    AL451136 Genomic DNA. Translation: CAI13097.1. Sequence problems.
    CH471059 Genomic DNA. Translation: EAX06975.1.
    CH471059 Genomic DNA. Translation: EAX06976.1.
    CH471059 Genomic DNA. Translation: EAX06978.1.
    CH471059 Genomic DNA. Translation: EAX06979.1.
    CH471059 Genomic DNA. Translation: EAX06980.1.
    CH471059 Genomic DNA. Translation: EAX06981.1.
    CH471059 Genomic DNA. Translation: EAX06982.1.
    BC007063 mRNA. Translation: AAH07063.1.
    BC021683 mRNA. Translation: AAH21683.1.
    CCDSiCCDS522.1.
    PIRiA46711.
    RefSeqiNP_001189360.1. NM_001202431.1.
    NP_002565.1. NM_002574.3.
    NP_859047.1. NM_181696.2.
    NP_859048.1. NM_181697.2.
    UniGeneiHs.180909.
    Hs.731900.

    Genome annotation databases

    EnsembliENST00000262746; ENSP00000262746; ENSG00000117450.
    ENST00000319248; ENSP00000361152; ENSG00000117450.
    GeneIDi5052.
    KEGGihsa:5052.
    UCSCiuc001coa.3. human.

    Polymorphism databases

    DMDMi548453.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X67951 mRNA. Translation: CAA48137.1 .
    L19184 mRNA. Translation: AAA50464.1 .
    BT019740 mRNA. Translation: AAV38545.1 .
    CR407652 mRNA. Translation: CAG28580.1 .
    DQ297142 Genomic DNA. Translation: ABB84465.1 .
    AB451262 mRNA. Translation: BAG70076.1 .
    AB451388 mRNA. Translation: BAG70202.1 .
    AL451136 Genomic DNA. Translation: CAI13095.1 .
    AL451136 Genomic DNA. Translation: CAI13096.1 .
    AL451136 Genomic DNA. Translation: CAI13097.1 . Sequence problems.
    CH471059 Genomic DNA. Translation: EAX06975.1 .
    CH471059 Genomic DNA. Translation: EAX06976.1 .
    CH471059 Genomic DNA. Translation: EAX06978.1 .
    CH471059 Genomic DNA. Translation: EAX06979.1 .
    CH471059 Genomic DNA. Translation: EAX06980.1 .
    CH471059 Genomic DNA. Translation: EAX06981.1 .
    CH471059 Genomic DNA. Translation: EAX06982.1 .
    BC007063 mRNA. Translation: AAH07063.1 .
    BC021683 mRNA. Translation: AAH21683.1 .
    CCDSi CCDS522.1.
    PIRi A46711.
    RefSeqi NP_001189360.1. NM_001202431.1.
    NP_002565.1. NM_002574.3.
    NP_859047.1. NM_181696.2.
    NP_859048.1. NM_181697.2.
    UniGenei Hs.180909.
    Hs.731900.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2RII X-ray 2.60 A/B 1-199 [» ]
    3HY2 X-ray 2.10 A/B 1-199 [» ]
    ProteinModelPortali Q06830.
    SMRi Q06830. Positions 3-187.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111089. 91 interactions.
    DIPi DIP-33152N.
    IntActi Q06830. 39 interactions.
    MINTi MINT-4999060.
    STRINGi 9606.ENSP00000262746.

    Chemistry

    ChEMBLi CHEMBL5315.

    Protein family/group databases

    PeroxiBasei 4501. Hs2CysPrx01.

    PTM databases

    PhosphoSitei Q06830.

    Polymorphism databases

    DMDMi 548453.

    2D gel databases

    DOSAC-COBS-2DPAGE Q06830.
    OGPi Q06830.
    SWISS-2DPAGE Q06830.
    UCD-2DPAGE Q06830.

    Proteomic databases

    MaxQBi Q06830.
    PaxDbi Q06830.
    PRIDEi Q06830.

    Protocols and materials databases

    DNASUi 5052.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262746 ; ENSP00000262746 ; ENSG00000117450 .
    ENST00000319248 ; ENSP00000361152 ; ENSG00000117450 .
    GeneIDi 5052.
    KEGGi hsa:5052.
    UCSCi uc001coa.3. human.

    Organism-specific databases

    CTDi 5052.
    GeneCardsi GC01M045976.
    HGNCi HGNC:9352. PRDX1.
    HPAi CAB004682.
    HPA007730.
    MIMi 176763. gene.
    neXtProti NX_Q06830.
    PharmGKBi PA33722.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0450.
    HOVERGENi HBG000286.
    InParanoidi Q06830.
    KOi K13279.
    OMAi EMKIPLV.
    OrthoDBi EOG7T1RCD.
    PhylomeDBi Q06830.
    TreeFami TF105181.

    Enzyme and pathway databases

    Reactomei REACT_172715. Detoxification of Reactive Oxygen Species.

    Miscellaneous databases

    ChiTaRSi PRDX1. human.
    EvolutionaryTracei Q06830.
    GeneWikii Peroxiredoxin_1.
    GenomeRNAii 5052.
    NextBioi 19468.
    PROi Q06830.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q06830.
    CleanExi HS_PRDX1.
    Genevestigatori Q06830.

    Family and domain databases

    Gene3Di 3.40.30.10. 1 hit.
    InterProi IPR000866. AhpC/TSA.
    IPR024706. Peroxiredoxin_AhpC-typ.
    IPR019479. Peroxiredoxin_C.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF10417. 1-cysPrx_C. 1 hit.
    PF00578. AhpC-TSA. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000239. AHPC. 1 hit.
    SUPFAMi SSF52833. SSF52833. 1 hit.
    PROSITEi PS51352. THIOREDOXIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A human cDNA corresponding to a gene overexpressed during cell proliferation encodes a product sharing homology with amoebic and bacterial proteins."
      Prosperi M.T., Ferbus D., Karczinski I., Goubin G.
      J. Biol. Chem. 268:11050-11056(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Cloning and sequence analysis of candidate human natural killer-enhancing factor genes."
      Shau H., Butterfield L.H., Chiu R., Kim A.
      Immunogenetics 40:129-134(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "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].
    5. NIEHS SNPs program
      Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLY-62.
    6. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
      Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
      , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
      Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    7. "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].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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: Urinary bladder.
    10. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 17-35; 93-136; 141-151 AND 159-190, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    11. "A method for detection of overoxidation of cysteines: peroxiredoxins are oxidized in vivo at the active-site cysteine during oxidative stress."
      Wagner E., Luche S., Penna L., Chevallet M., van Dorsselaer A., Leize-Wagner E., Rabilloud T.
      Biochem. J. 366:777-785(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: OVEROXIDATION AT CYS-52.
    12. "Regulation of peroxiredoxin I activity by Cdc2-mediated phosphorylation."
      Chang T.-S., Jeong W., Choi S.Y., Yu S., Kang S.W., Rhee S.G.
      J. Biol. Chem. 277:25370-25376(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-90, MUTAGENESIS OF THR-90.
    13. "Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid."
      Yang K.S., Kang S.W., Woo H.A., Hwang S.C., Chae H.Z., Kim K., Rhee S.G.
      J. Biol. Chem. 277:38029-38036(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: OVEROXIDATION AT CYS-52.
    14. "Regeneration of peroxiredoxins during recovery after oxidative stress: only some overoxidized peroxiredoxins can be reduced during recovery after oxidative stress."
      Chevallet M., Wagner E., Luche S., van Dorsselaer A., Leize-Wagner E., Rabilloud T.
      J. Biol. Chem. 278:37146-37153(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: RETROREDUCTION OF CYS-52, IDENTIFICATION BY MASS SPECTROMETRY.
    15. "Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation."
      Woo H.A., Chae H.Z., Hwang S.C., Yang K.S., Kang S.W., Kim K., Rhee S.G.
      Science 300:653-656(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: RETROREDUCTION OF CYS-52, IDENTIFICATION BY MASS SPECTROMETRY.
    16. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    17. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2; LYS-7; LYS-16; LYS-27 AND LYS-35, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPRDX1_HUMAN
    AccessioniPrimary (citable) accession number: Q06830
    Secondary accession number(s): B5BU26
    , D3DPZ8, P35703, Q2V576, Q5T154, Q5T155
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 164 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 active site is the redox-active Cys-52 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-173-SH of the other subunit to form an intermolecular disulfide with a concomitant homodimer formation. The enzyme may be subsequently regenerated by reduction of the disulfide by thioredoxin.
    Inactivated upon oxidative stress by overoxidation of Cys-52 to Cys-SO2H and Cys-SO3H. Cys-SO2H is retroreduced to Cys-SOH after removal of H2O2, while Cys-SO3H may be irreversibly oxidized.

    Keywords - Technical termi

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