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P30048

- PRDX3_HUMAN

UniProt

P30048 - PRDX3_HUMAN

Protein

Thioredoxin-dependent peroxide reductase, mitochondrial

Gene

PRDX3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 175 (01 Oct 2014)
      Sequence version 3 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Involved in redox regulation of the cell. Protects radical-sensitive enzymes from oxidative damage by a radical-generating system. Acts synergistically with MAP3K13 to regulate the activation of NF-kappa-B in the cytosol.1 Publication

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei108 – 1081Cysteine sulfenic acid (-SOH) intermediateBy similarity

    GO - Molecular functioni

    1. alkyl hydroperoxide reductase activity Source: UniProtKB
    2. cysteine-type endopeptidase inhibitor activity involved in apoptotic process Source: UniProtKB
    3. kinase binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein C-terminus binding Source: UniProtKB
    6. protein kinase binding Source: UniProtKB
    7. thioredoxin peroxidase activity Source: ParkinsonsUK-UCL

    GO - Biological processi

    1. cellular response to oxidative stress Source: ParkinsonsUK-UCL
    2. cellular response to reactive oxygen species Source: UniProtKB
    3. hydrogen peroxide catabolic process Source: UniProtKB
    4. maternal placenta development Source: Ensembl
    5. mitochondrion organization Source: UniProtKB
    6. myeloid cell differentiation Source: UniProtKB
    7. negative regulation of apoptotic process Source: UniProtKB
    8. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: GOC
    9. negative regulation of kinase activity Source: UniProtKB
    10. peptidyl-cysteine oxidation Source: ParkinsonsUK-UCL
    11. positive regulation of cell proliferation Source: UniProtKB
    12. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    13. regulation of mitochondrial membrane potential Source: UniProtKB
    14. response to hydrogen peroxide Source: UniProtKB
    15. response to lipopolysaccharide Source: UniProtKB
    16. 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

    PeroxiBasei4492. Hs2CysPrx03.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thioredoxin-dependent peroxide reductase, mitochondrial (EC:1.11.1.15)
    Alternative name(s):
    Antioxidant protein 1
    Short name:
    AOP-1
    HBC189
    Peroxiredoxin III
    Short name:
    Prx-III
    Peroxiredoxin-3
    Protein MER5 homolog
    Gene namesi
    Name:PRDX3
    Synonyms:AOP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:9354. PRDX3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: ParkinsonsUK-UCL
    3. early endosome Source: UniProtKB
    4. extracellular vesicular exosome Source: UniProt
    5. mitochondrial matrix Source: Reactome
    6. mitochondrion Source: UniProtKB

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi146 – 1461T → A: Impairs phosphorylation. 1 Publication

    Organism-specific databases

    PharmGKBiPA33724.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 6262MitochondrionAdd
    BLAST
    Chaini63 – 256194Thioredoxin-dependent peroxide reductase, mitochondrialPRO_0000023782Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei83 – 831N6-succinyllysineBy similarity
    Modified residuei91 – 911N6-acetyllysine; alternate1 Publication
    Modified residuei91 – 911N6-succinyllysine; alternateBy similarity
    Disulfide bondi108 – 108Interchain (with C-229); in linked formBy similarity
    Modified residuei146 – 1461Phosphothreonine1 Publication
    Disulfide bondi229 – 229Interchain (with C-108); in linked formBy similarity

    Post-translational modificationi

    Phosphorylated by LRRK2; phosphorylation reduces perodixase activity.1 Publication

    Keywords - PTMi

    Acetylation, Disulfide bond, Phosphoprotein

    Proteomic databases

    MaxQBiP30048.
    PaxDbiP30048.
    PeptideAtlasiP30048.
    PRIDEiP30048.

    2D gel databases

    OGPiP30048.
    SWISS-2DPAGEP30048.
    UCD-2DPAGEP30048.

    PTM databases

    PhosphoSiteiP30048.

    Expressioni

    Gene expression databases

    ArrayExpressiP30048.
    BgeeiP30048.
    CleanExiHS_PRDX3.
    GenevestigatoriP30048.

    Organism-specific databases

    HPAiCAB008656.

    Interactioni

    Subunit structurei

    Dodecameric ring assembled from homodimeric units; disulfide-linked, upon oxidation. The rings have an approximate diameter of 150 A and a central hole of 70 A. 3-5% of the rings are interlocked by pairs. Binds MAP3K13. Interacts with NEK6. Interacts with LRRK2.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LRRK2Q5S00712EBI-748336,EBI-5323863

    Protein-protein interaction databases

    BioGridi116136. 41 interactions.
    IntActiP30048. 34 interactions.
    MINTiMINT-195453.
    STRINGi9606.ENSP00000298510.

    Structurei

    3D structure databases

    ProteinModelPortaliP30048.
    SMRiP30048. Positions 63-223.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini63 – 221159ThioredoxinPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Redox-active center, Transit peptide

    Phylogenomic databases

    eggNOGiCOG0450.
    HOVERGENiHBG000286.
    InParanoidiP30048.
    KOiK03386.
    OMAiPDEACPA.
    OrthoDBiEOG7T1RCD.
    PhylomeDBiP30048.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P30048-1) [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

    MAAAVGRLLR ASVARHVSAI PWGISATAAL RPAACGRTSL TNLLCSGSSQ    50
    AKLFSTSSSC HAPAVTQHAP YFKGTAVVNG EFKDLSLDDF KGKYLVLFFY 100
    PLDFTFVCPT EIVAFSDKAN EFHDVNCEVV AVSVDSHFSH LAWINTPRKN 150
    GGLGHMNIAL LSDLTKQISR DYGVLLEGSG LALRGLFIID PNGVIKHLSV 200
    NDLPVGRSVE ETLRLVKAFQ YVETHGEVCP ANWTPDSPTI KPSPAASKEY 250
    FQKVNQ 256
    Length:256
    Mass (Da):27,693
    Last modified:November 1, 1997 - v3
    Checksum:i8BEB7F5E55BFE9BE
    GO
    Isoform 2 (identifier: P30048-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         51-68: Missing.

    Note: No experimental confirmation available. Gene prediction based on EST data.

    Show »
    Length:238
    Mass (Da):25,839
    Checksum:i28657F36943A2355
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti31 – 311R → W in AAH08435. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti55 – 551S → R.1 Publication
    Corresponds to variant rs34698541 [ dbSNP | Ensembl ].
    VAR_025052
    Natural varianti170 – 1701R → Q.
    Corresponds to variant rs11554902 [ dbSNP | Ensembl ].
    VAR_059546
    Natural varianti218 – 2181A → T.1 Publication
    VAR_025053
    Natural varianti234 – 2341T → I.1 Publication
    Corresponds to variant rs35697338 [ dbSNP | Ensembl ].
    VAR_025054

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei51 – 6818Missing in isoform 2. CuratedVSP_054050Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D49396 mRNA. Translation: BAA08389.1.
    AK313169 mRNA. Translation: BAG35987.1.
    CR450344 mRNA. Translation: CAG29340.1.
    BT020007 mRNA. Translation: AAV38810.1.
    DQ298752 Genomic DNA. Translation: ABB84468.1.
    AL355861 Genomic DNA. Translation: CAI15802.1.
    CH471066 Genomic DNA. Translation: EAW49399.1.
    BC002685 mRNA. Translation: AAH02685.1.
    BC007062 mRNA. Translation: AAH07062.1.
    BC008435 mRNA. Translation: AAH08435.1.
    BC009601 mRNA. Translation: AAH09601.1.
    BC021691 mRNA. Translation: AAH21691.1.
    BC022373 mRNA. Translation: AAH22373.1.
    BC059169 mRNA. Translation: AAH59169.1.
    BC111397 mRNA. Translation: AAI11398.1.
    CCDSiCCDS44484.1. [P30048-2]
    CCDS7611.1. [P30048-1]
    RefSeqiNP_006784.1. NM_006793.3. [P30048-1]
    NP_054817.2. NM_014098.3. [P30048-2]
    UniGeneiHs.523302.

    Genome annotation databases

    EnsembliENST00000298510; ENSP00000298510; ENSG00000165672. [P30048-1]
    GeneIDi10935.
    KEGGihsa:10935.
    UCSCiuc001lec.3. human. [P30048-1]

    Polymorphism databases

    DMDMi2507171.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D49396 mRNA. Translation: BAA08389.1 .
    AK313169 mRNA. Translation: BAG35987.1 .
    CR450344 mRNA. Translation: CAG29340.1 .
    BT020007 mRNA. Translation: AAV38810.1 .
    DQ298752 Genomic DNA. Translation: ABB84468.1 .
    AL355861 Genomic DNA. Translation: CAI15802.1 .
    CH471066 Genomic DNA. Translation: EAW49399.1 .
    BC002685 mRNA. Translation: AAH02685.1 .
    BC007062 mRNA. Translation: AAH07062.1 .
    BC008435 mRNA. Translation: AAH08435.1 .
    BC009601 mRNA. Translation: AAH09601.1 .
    BC021691 mRNA. Translation: AAH21691.1 .
    BC022373 mRNA. Translation: AAH22373.1 .
    BC059169 mRNA. Translation: AAH59169.1 .
    BC111397 mRNA. Translation: AAI11398.1 .
    CCDSi CCDS44484.1. [P30048-2 ]
    CCDS7611.1. [P30048-1 ]
    RefSeqi NP_006784.1. NM_006793.3. [P30048-1 ]
    NP_054817.2. NM_014098.3. [P30048-2 ]
    UniGenei Hs.523302.

    3D structure databases

    ProteinModelPortali P30048.
    SMRi P30048. Positions 63-223.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116136. 41 interactions.
    IntActi P30048. 34 interactions.
    MINTi MINT-195453.
    STRINGi 9606.ENSP00000298510.

    Protein family/group databases

    PeroxiBasei 4492. Hs2CysPrx03.

    PTM databases

    PhosphoSitei P30048.

    Polymorphism databases

    DMDMi 2507171.

    2D gel databases

    OGPi P30048.
    SWISS-2DPAGE P30048.
    UCD-2DPAGE P30048.

    Proteomic databases

    MaxQBi P30048.
    PaxDbi P30048.
    PeptideAtlasi P30048.
    PRIDEi P30048.

    Protocols and materials databases

    DNASUi 10935.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000298510 ; ENSP00000298510 ; ENSG00000165672 . [P30048-1 ]
    GeneIDi 10935.
    KEGGi hsa:10935.
    UCSCi uc001lec.3. human. [P30048-1 ]

    Organism-specific databases

    CTDi 10935.
    GeneCardsi GC10M120917.
    H-InvDB HIX0035477.
    HGNCi HGNC:9354. PRDX3.
    HPAi CAB008656.
    MIMi 604769. gene.
    neXtProti NX_P30048.
    PharmGKBi PA33724.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0450.
    HOVERGENi HBG000286.
    InParanoidi P30048.
    KOi K03386.
    OMAi PDEACPA.
    OrthoDBi EOG7T1RCD.
    PhylomeDBi P30048.
    TreeFami TF105181.

    Enzyme and pathway databases

    Reactomei REACT_172715. Detoxification of Reactive Oxygen Species.

    Miscellaneous databases

    ChiTaRSi PRDX3. human.
    GeneWikii PRDX3.
    GenomeRNAii 10935.
    NextBioi 41537.
    PROi P30048.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P30048.
    Bgeei P30048.
    CleanExi HS_PRDX3.
    Genevestigatori P30048.

    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. "Mammalian antioxidant protein complements alkylhydroperoxide reductase (ahpC) mutation in Escherichia coli."
      Tsuji K., Copeland N.G., Jenkins N.A., Obinata M.
      Biochem. J. 307:377-381(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Blood.
    2. "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] (ISOFORM 1).
      Tissue: Lung.
    3. "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] (ISOFORM 1).
    4. "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] (ISOFORM 1).
    5. NIEHS SNPs program
      Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-55; THR-218 AND ILE-234.
    6. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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 1).
      Tissue: Bone marrow, Skeletal muscle, Testis, Urinary bladder and Uterus.
    9. "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 63-72 (ISOFORM 1).
      Tissue: Liver.
    10. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 74-93; 149-166 AND 171-214 (ISOFORM 1), 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-108.
    12. "Mixed lineage kinase LZK and antioxidant protein-1 activate NF-kappaB synergistically."
      Masaki M., Ikeda A., Shiraki E., Oka S., Kawasaki T.
      Eur. J. Biochem. 270:76-83(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MAP3K13.
    13. "Reconstitution of the mitochondrial PrxIII antioxidant defence pathway: general properties and factors affecting PrxIII activity and oligomeric state."
      Cao Z., Bhella D., Lindsay J.G.
      J. Mol. Biol. 372:1022-1033(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    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-91, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Characterization of hNek6 interactome reveals an important role for its short N-terminal domain and colocalization with proteins at the centrosome."
      Vaz Meirelles G., Ferreira Lanza D.C., da Silva J.C., Santana Bernachi J., Paes Leme A.F., Kobarg J.
      J. Proteome Res. 9:6298-6316(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NEK6.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Mutations in LRRK2 increase phosphorylation of peroxiredoxin 3 exacerbating oxidative stress-induced neuronal death."
      Angeles D.C., Gan B.H., Onstead L., Zhao Y., Lim K.L., Dachsel J., Melrose H., Farrer M., Wszolek Z.K., Dickson D.W., Tan E.K.
      Hum. Mutat. 32:1390-1397(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LRRK2, PHOSPHORYLATION AT THR-146, MUTAGENESIS OF THR-146.

    Entry informationi

    Entry nameiPRDX3_HUMAN
    AccessioniPrimary (citable) accession number: P30048
    Secondary accession number(s): B2R7Z0
    , D3DRC9, E9PH29, P35690, Q0D2H1, Q13776, Q5T5V2, Q96HK4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 175 of the entry and version 3 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-108 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-229-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.
    Irreversibly inactivated by overoxidation of Cys-108 (to Cys-SO3H) upon oxidative stress.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3