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P30044

- PRDX5_HUMAN

UniProt

P30044 - PRDX5_HUMAN

Protein

Peroxiredoxin-5, mitochondrial

Gene

PRDX5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 158 (01 Oct 2014)
      Sequence version 4 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    Reduces hydrogen peroxide and alkyl hydroperoxides with reducing equivalents provided through the thioredoxin system. Involved in intracellular redox signaling.

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei100 – 1001Cysteine sulfenic acid (-SOH) intermediate1 Publication

    GO - Molecular functioni

    1. antioxidant activity Source: UniProtKB
    2. cysteine-type endopeptidase inhibitor activity involved in apoptotic process Source: UniProtKB
    3. peroxidase activity Source: UniProtKB
    4. peroxiredoxin activity Source: UniProtKB
    5. peroxynitrite reductase activity Source: UniProtKB
    6. protein dimerization activity Source: UniProtKB
    7. receptor binding Source: UniProtKB
    8. RNA polymerase III regulatory region DNA binding Source: UniProtKB

    GO - Biological processi

    1. cellular response to reactive oxygen species Source: UniProtKB
    2. hydrogen peroxide catabolic process Source: UniProtKB
    3. inflammatory response Source: UniProtKB
    4. NADPH oxidation Source: UniProtKB
    5. negative regulation of apoptotic process Source: UniProtKB
    6. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: GOC
    7. negative regulation of oxidoreductase activity Source: UniProtKB
    8. negative regulation of transcription from RNA polymerase III promoter Source: UniProtKB
    9. positive regulation of collagen biosynthetic process Source: UniProtKB
    10. reactive nitrogen species metabolic process Source: UniProtKB
    11. regulation of apoptosis involved in tissue homeostasis Source: UniProtKB
    12. regulation of RNA biosynthetic process Source: UniProtKB
    13. response to oxidative stress Source: UniProtKB

    Keywords - Molecular functioni

    Antioxidant, Oxidoreductase, Peroxidase

    Enzyme and pathway databases

    ReactomeiREACT_172715. Detoxification of Reactive Oxygen Species.

    Protein family/group databases

    PeroxiBasei4448. HsPrxV.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peroxiredoxin-5, mitochondrial (EC:1.11.1.15)
    Alternative name(s):
    Alu corepressor 1
    Antioxidant enzyme B166
    Short name:
    AOEB166
    Liver tissue 2D-page spot 71B
    PLP
    Peroxiredoxin V
    Short name:
    Prx-V
    Peroxisomal antioxidant enzyme
    TPx type VI
    Thioredoxin peroxidase PMP20
    Thioredoxin reductase
    Gene namesi
    Name:PRDX5
    Synonyms:ACR1
    ORF Names:SBBI10
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:9355. PRDX5.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoplasmic vesicle Source: UniProtKB
    3. cytosol Source: UniProtKB
    4. extracellular space Source: UniProt
    5. extracellular vesicular exosome Source: UniProt
    6. intracellular membrane-bounded organelle Source: UniProtKB
    7. mitochondrial matrix Source: Reactome
    8. mitochondrion Source: UniProtKB
    9. nucleus Source: UniProtKB
    10. perinuclear region of cytoplasm Source: UniProtKB
    11. peroxisomal matrix Source: UniProtKB
    12. peroxisome Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion, Peroxisome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi100 – 1001C → S: Complete loss of activity. 1 Publication
    Mutagenesisi125 – 1251C → S: No change in activity. 1 Publication
    Mutagenesisi204 – 2041C → S: Complete loss of activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA33726.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 5252MitochondrionSequence AnalysisAdd
    BLAST
    Chaini53 – 214162Peroxiredoxin-5, mitochondrialPRO_0000023793Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei75 – 751N6-acetyllysineBy similarity
    Modified residuei83 – 831N6-acetyllysine; alternate1 Publication
    Modified residuei83 – 831N6-succinyllysine; alternateBy similarity
    Disulfide bondi100 ↔ 204Redox-active1 PublicationPROSITE-ProRule annotation
    Modified residuei116 – 1161N6-succinyllysineBy similarity

    Keywords - PTMi

    Acetylation, Disulfide bond

    Proteomic databases

    MaxQBiP30044.
    PaxDbiP30044.
    PRIDEiP30044.

    2D gel databases

    OGPiP30044.
    REPRODUCTION-2DPAGEIPI00759663.
    SWISS-2DPAGEP30044.
    UCD-2DPAGEP30044.

    PTM databases

    PhosphoSiteiP30044.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Gene expression databases

    ArrayExpressiP30044.
    BgeeiP30044.
    CleanExiHS_PRDX5.
    GenevestigatoriP30044.

    Organism-specific databases

    HPAiCAB008661.
    HPA037915.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    BioGridi117352. 35 interactions.
    IntActiP30044. 5 interactions.
    MINTiMINT-5002532.
    STRINGi9606.ENSP00000265462.

    Structurei

    Secondary structure

    1
    214
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi66 – 683
    Helixi72 – 743
    Beta strandi75 – 773
    Helixi78 – 814
    Turni82 – 843
    Beta strandi85 – 917
    Helixi98 – 1025
    Helixi104 – 1107
    Helixi112 – 1165
    Turni117 – 1193
    Beta strandi122 – 1298
    Helixi131 – 14010
    Turni144 – 1463
    Beta strandi148 – 1514
    Helixi156 – 1616
    Helixi167 – 1693
    Helixi170 – 1734
    Beta strandi181 – 1866
    Beta strandi189 – 1957
    Beta strandi199 – 2035
    Helixi207 – 2137

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1H4OX-ray1.95A/B/C/D/E/F/G/H54-214[»]
    1HD2X-ray1.50A54-214[»]
    1OC3X-ray2.00A/B/C54-214[»]
    1URMX-ray1.70A54-214[»]
    2VL2X-ray1.92A/B/C54-214[»]
    2VL3X-ray1.83A/B/C54-214[»]
    2VL9X-ray2.70A/B/C/D54-214[»]
    3MNGX-ray1.45A54-214[»]
    4K7IX-ray2.25A/B/C54-214[»]
    4K7NX-ray2.30A/B/C54-214[»]
    4K7OX-ray1.98A/B/C54-214[»]
    ProteinModelPortaliP30044.
    SMRiP30044. Positions 54-214.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP30044.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini56 – 214159ThioredoxinPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi212 – 2143Microbody targeting signalBy similarity

    Sequence similaritiesi

    Belongs to the peroxiredoxin 2 family.Curated
    Contains 1 thioredoxin domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Redox-active center, Transit peptide

    Phylogenomic databases

    eggNOGiCOG0678.
    HOGENOMiHOG000255884.
    HOVERGENiHBG053675.
    InParanoidiP30044.
    KOiK11187.
    OMAiMSAWGKQ.
    OrthoDBiEOG77Q4XX.
    PhylomeDBiP30044.
    TreeFamiTF105182.

    Family and domain databases

    Gene3Di3.40.30.10. 1 hit.
    InterProiIPR013740. Redoxin.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF08534. Redoxin. 1 hit.
    [Graphical view]
    SUPFAMiSSF52833. SSF52833. 1 hit.
    PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing and alternative initiation. Align

    Isoform Mitochondrial (identifier: P30044-1) [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

    MGLAGVCALR RSAGYILVGG AGGQSAAAAA RRYSEGEWAS GGVRSFSRAA    50
    AAMAPIKVGD AIPAVEVFEG EPGNKVNLAE LFKGKKGVLF GVPGAFTPGC 100
    SKTHLPGFVE QAEALKAKGV QVVACLSVND AFVTGEWGRA HKAEGKVRLL 150
    ADPTGAFGKE TDLLLDDSLV SIFGNRRLKR FSMVVQDGIV KALNVEPDGT 200
    GLTCSLAPNI ISQL 214
    Length:214
    Mass (Da):22,086
    Last modified:January 11, 2011 - v4
    Checksum:iDA1DEB21120254EE
    GO
    Isoform Cytoplasmic+peroxisomal (identifier: P30044-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-52: Missing.

    Show »
    Length:162
    Mass (Da):17,031
    Checksum:i370DF621012F880D
    GO
    Isoform 3 (identifier: P30044-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         102-145: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:170
    Mass (Da):17,454
    Checksum:i29984B81B33F82C1
    GO
    Isoform 4 (identifier: P30044-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         57-145: Missing.

    Note: Produced by alternative splicing.

    Show »
    Length:125
    Mass (Da):12,897
    Checksum:iF3A1C1531E4E4A73
    GO

    Sequence cautioni

    The sequence AAF17200.1 differs from that shown. Reason: Frameshift at positions 14 and 30.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti141 – 1411H → T in AAF04856. (PubMed:10679306)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti33 – 331Y → C.7 Publications
    Corresponds to variant rs7938623 [ dbSNP | Ensembl ].
    VAR_025049
    Natural varianti157 – 1571F → L in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036406

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5252Missing in isoform Cytoplasmic+peroxisomal. 4 PublicationsVSP_018829Add
    BLAST
    Alternative sequencei57 – 14589Missing in isoform 4. 1 PublicationVSP_046682Add
    BLAST
    Alternative sequencei102 – 14544Missing in isoform 3. 1 PublicationVSP_045783Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF231705 mRNA. Translation: AAF78899.1.
    AF124993 mRNA. Translation: AAF27531.1.
    AF110731 mRNA. Translation: AAF03750.1.
    AF197952 mRNA. Translation: AAF04856.1.
    AJ249483 mRNA. Translation: CAB62210.1.
    AF242525 mRNA. Translation: AAF99605.1.
    AF112212 mRNA. Translation: AAF17200.1. Frameshift.
    CR457203 mRNA. Translation: CAG33484.1.
    DQ247769 Genomic DNA. Translation: ABB05181.1.
    AP001453 Genomic DNA. No translation available.
    AP003774 Genomic DNA. No translation available.
    BC110983 mRNA. Translation: AAI10984.1.
    BC113723 mRNA. Translation: AAI13724.1.
    BC113725 mRNA. Translation: AAI13726.1.
    BC143849 mRNA. Translation: AAI43850.1.
    BC171733 mRNA. Translation: AAI71733.1.
    CCDSiCCDS8069.1. [P30044-1]
    CCDS8070.1. [P30044-3]
    CCDS8071.1. [P30044-4]
    RefSeqiNP_036226.1. NM_012094.4.
    NP_857634.1. NM_181651.2.
    NP_857635.1. NM_181652.2.
    UniGeneiHs.502823.

    Genome annotation databases

    EnsembliENST00000265462; ENSP00000265462; ENSG00000126432. [P30044-1]
    ENST00000347941; ENSP00000335363; ENSG00000126432. [P30044-4]
    ENST00000352435; ENSP00000335334; ENSG00000126432. [P30044-3]
    GeneIDi25824.
    KEGGihsa:25824.
    UCSCiuc001nzu.3. human. [P30044-1]

    Polymorphism databases

    DMDMi317373539.

    Keywords - Coding sequence diversityi

    Alternative initiation, Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF231705 mRNA. Translation: AAF78899.1 .
    AF124993 mRNA. Translation: AAF27531.1 .
    AF110731 mRNA. Translation: AAF03750.1 .
    AF197952 mRNA. Translation: AAF04856.1 .
    AJ249483 mRNA. Translation: CAB62210.1 .
    AF242525 mRNA. Translation: AAF99605.1 .
    AF112212 mRNA. Translation: AAF17200.1 . Frameshift.
    CR457203 mRNA. Translation: CAG33484.1 .
    DQ247769 Genomic DNA. Translation: ABB05181.1 .
    AP001453 Genomic DNA. No translation available.
    AP003774 Genomic DNA. No translation available.
    BC110983 mRNA. Translation: AAI10984.1 .
    BC113723 mRNA. Translation: AAI13724.1 .
    BC113725 mRNA. Translation: AAI13726.1 .
    BC143849 mRNA. Translation: AAI43850.1 .
    BC171733 mRNA. Translation: AAI71733.1 .
    CCDSi CCDS8069.1. [P30044-1 ]
    CCDS8070.1. [P30044-3 ]
    CCDS8071.1. [P30044-4 ]
    RefSeqi NP_036226.1. NM_012094.4.
    NP_857634.1. NM_181651.2.
    NP_857635.1. NM_181652.2.
    UniGenei Hs.502823.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1H4O X-ray 1.95 A/B/C/D/E/F/G/H 54-214 [» ]
    1HD2 X-ray 1.50 A 54-214 [» ]
    1OC3 X-ray 2.00 A/B/C 54-214 [» ]
    1URM X-ray 1.70 A 54-214 [» ]
    2VL2 X-ray 1.92 A/B/C 54-214 [» ]
    2VL3 X-ray 1.83 A/B/C 54-214 [» ]
    2VL9 X-ray 2.70 A/B/C/D 54-214 [» ]
    3MNG X-ray 1.45 A 54-214 [» ]
    4K7I X-ray 2.25 A/B/C 54-214 [» ]
    4K7N X-ray 2.30 A/B/C 54-214 [» ]
    4K7O X-ray 1.98 A/B/C 54-214 [» ]
    ProteinModelPortali P30044.
    SMRi P30044. Positions 54-214.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117352. 35 interactions.
    IntActi P30044. 5 interactions.
    MINTi MINT-5002532.
    STRINGi 9606.ENSP00000265462.

    Chemistry

    DrugBanki DB00995. Auranofin.

    Protein family/group databases

    PeroxiBasei 4448. HsPrxV.

    PTM databases

    PhosphoSitei P30044.

    Polymorphism databases

    DMDMi 317373539.

    2D gel databases

    OGPi P30044.
    REPRODUCTION-2DPAGE IPI00759663.
    SWISS-2DPAGE P30044.
    UCD-2DPAGE P30044.

    Proteomic databases

    MaxQBi P30044.
    PaxDbi P30044.
    PRIDEi P30044.

    Protocols and materials databases

    DNASUi 25824.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265462 ; ENSP00000265462 ; ENSG00000126432 . [P30044-1 ]
    ENST00000347941 ; ENSP00000335363 ; ENSG00000126432 . [P30044-4 ]
    ENST00000352435 ; ENSP00000335334 ; ENSG00000126432 . [P30044-3 ]
    GeneIDi 25824.
    KEGGi hsa:25824.
    UCSCi uc001nzu.3. human. [P30044-1 ]

    Organism-specific databases

    CTDi 25824.
    GeneCardsi GC11P064085.
    HGNCi HGNC:9355. PRDX5.
    HPAi CAB008661.
    HPA037915.
    MIMi 606583. gene.
    neXtProti NX_P30044.
    PharmGKBi PA33726.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0678.
    HOGENOMi HOG000255884.
    HOVERGENi HBG053675.
    InParanoidi P30044.
    KOi K11187.
    OMAi MSAWGKQ.
    OrthoDBi EOG77Q4XX.
    PhylomeDBi P30044.
    TreeFami TF105182.

    Enzyme and pathway databases

    Reactomei REACT_172715. Detoxification of Reactive Oxygen Species.

    Miscellaneous databases

    ChiTaRSi PRDX5. human.
    EvolutionaryTracei P30044.
    GeneWikii PRDX5.
    GenomeRNAii 25824.
    NextBioi 35462441.
    PROi P30044.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P30044.
    Bgeei P30044.
    CleanExi HS_PRDX5.
    Genevestigatori P30044.

    Family and domain databases

    Gene3Di 3.40.30.10. 1 hit.
    InterProi IPR013740. Redoxin.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF08534. Redoxin. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52833. SSF52833. 1 hit.
    PROSITEi PS51352. THIOREDOXIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel human DNA-binding protein with sequence similarity to a subfamily of redox proteins which is able to repress RNA-polymerase-III-driven transcription of the Alu-family retroposons in vitro."
      Kropotov A., Sedova V., Ivanov V., Sazeeva N., Tomilin A., Krutilina R., Oei S.L., Griesenbeck J., Buchlow G., Tomilin N.
      Eur. J. Biochem. 260:336-346(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MITOCHONDRIAL), VARIANT CYS-33.
    2. "Characterization of human and murine PMP20 peroxisomal proteins that exhibit antioxidant activity in vitro."
      Yamashita H., Avraham S., Jiang S., London R., Van Veldhoven P.P., Subramani S., Rogers R.A., Avraham H.
      J. Biol. Chem. 274:29897-29904(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CYTOPLASMIC+PEROXISOMAL), CHARACTERIZATION.
    3. "Cloning and characterization of AOEB166, a novel mammalian antioxidant enzyme of the peroxiredoxin family."
      Knoops B., Clippe A., Bogard C., Arsalane K., Wattiez R., Hermans C., Duconseille E., Falmagne P., Bernard A.
      J. Biol. Chem. 274:30451-30458(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MITOCHONDRIAL), PROTEIN SEQUENCE OF 54-90, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, CHARACTERIZATION, VARIANT CYS-33.
      Tissue: Lung.
    4. "Mouse peroxiredoxin V is a thioredoxin peroxidase that inhibits p53-induced apoptosis."
      Zhou Y., Kok K.H., Chun A.C.S., Wong C.M., Wu H.W., Lin M.C.M., Fung P.C.W., Kung H.-F., Jin D.-Y.
      Biochem. Biophys. Res. Commun. 268:921-927(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CYTOPLASMIC+PEROXISOMAL), VARIANT CYS-33.
    5. "Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate."
      Seo M.S., Kang S.W., Kim K., Baines I.C., Lee T.H., Rhee S.G.
      J. Biol. Chem. 275:20346-20354(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS, CHARACTERIZATION.
    6. "A new type of human thiol peroxidase (Human TPx type VI)."
      Kim I.H., Jeong W.
      Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CYTOPLASMIC+PEROXISOMAL).
    7. Zhang W., Li N., Wan T., Cao X.
      Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MITOCHONDRIAL), VARIANT CYS-33.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CYTOPLASMIC+PEROXISOMAL).
      Tissue: Adrenal gland.
    9. "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 (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM MITOCHONDRIAL), VARIANT CYS-33.
    10. NIEHS SNPs program
      Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT CYS-33.
    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] (ISOFORMS MITOCHONDRIAL; 3 AND 4), VARIANT CYS-33.
      Tissue: Brain and Medulla oblongata.
    13. "Human liver protein map: a reference database established by microsequencing and gel comparison."
      Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J.
      Electrophoresis 13:992-1001(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 54-63.
      Tissue: Liver.
    14. "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 LYS-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Crystal structure of human peroxiredoxin 5, a novel type of mammalian peroxiredoxin at 1.5-A resolution."
      Declercq J.-P., Evrard C., Clippe A., Stricht D.V., Bernard A., Knoops B.
      J. Mol. Biol. 311:751-759(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
    17. "The crystal structures of oxidized forms of human peroxiredoxin 5 with an intramolecular disulfide bond confirm the proposed enzymatic mechanism for atypical 2-Cys peroxiredoxins."
      Smeets A., Marchand C., Linard D., Knoops B., Declercq J.P.
      Arch. Biochem. Biophys. 477:98-104(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 54-214, DISULFIDE BOND.
    18. "Structural evidence that peroxiredoxin catalytic power is based on transition-state stabilization."
      Hall A., Parsonage D., Poole L.B., Karplus P.A.
      J. Mol. Biol. 402:194-209(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 54-214 IN COMPLEX WITH DITHIOTHREITOL, ACTIVE SITE.
    19. Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-157.

    Entry informationi

    Entry nameiPRDX5_HUMAN
    AccessioniPrimary (citable) accession number: P30044
    Secondary accession number(s): A6NC19
    , A6NG06, B7ZLJ4, B7ZVW3, Q14CK0, Q6IAF2, Q9UBU5, Q9UJU4, Q9UKX4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 158 of the entry and version 4 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 11
      Human chromosome 11: 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