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P32119

- PRDX2_HUMAN

UniProt

P32119 - PRDX2_HUMAN

Protein

Peroxiredoxin-2

Gene

PRDX2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 170 (01 Oct 2014)
      Sequence version 5 (23 Jan 2007)
      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. It is not able to receive electrons 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.

    Catalytic activityi

    2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei51 – 511Cysteine sulfenic acid (-SOH) intermediate

    GO - Molecular functioni

    1. antioxidant activity Source: UniProtKB
    2. thioredoxin peroxidase activity Source: UniProtKB

    GO - Biological processi

    1. cellular response to oxidative stress Source: BHF-UCL
    2. hydrogen peroxide catabolic process Source: BHF-UCL
    3. negative regulation of apoptotic process Source: UniProtKB
    4. negative regulation of neuron apoptotic process Source: Ensembl
    5. regulation of apoptotic process Source: UniProtKB
    6. removal of superoxide radicals Source: BHF-UCL
    7. 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

    PeroxiBasei4475. Hs2CysPrx02.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peroxiredoxin-2 (EC:1.11.1.15)
    Alternative name(s):
    Natural killer cell-enhancing factor B
    Short name:
    NKEF-B
    PRP
    Thiol-specific antioxidant protein
    Short name:
    TSA
    Thioredoxin peroxidase 1
    Thioredoxin-dependent peroxide reductase 1
    Gene namesi
    Name:PRDX2
    Synonyms:NKEFB, TDPX1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:9353. PRDX2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33723.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 198197Peroxiredoxin-2PRO_0000135080Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Disulfide bondi51 – 51Interchain (with C-172); in linked formBy similarity
    Disulfide bondi172 – 172Interchain (with C-51); in linked formBy similarity

    Keywords - PTMi

    Acetylation, Disulfide bond

    Proteomic databases

    MaxQBiP32119.
    PaxDbiP32119.
    PRIDEiP32119.

    2D gel databases

    DOSAC-COBS-2DPAGEP32119.
    OGPiP32119.
    REPRODUCTION-2DPAGEIPI00027350.
    SWISS-2DPAGEP32119.
    UCD-2DPAGEP32119.

    PTM databases

    PhosphoSiteiP32119.

    Expressioni

    Gene expression databases

    ArrayExpressiP32119.
    BgeeiP32119.
    CleanExiHS_PRDX2.
    GenevestigatoriP32119.

    Organism-specific databases

    HPAiCAB008713.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked, upon oxidation. May be found as a toroid-shaped decamer composed of 5 dimers, depending on pH and calcium concentration. Interacts with TIPIN.1 Publication

    Protein-protein interaction databases

    BioGridi112860. 57 interactions.
    IntActiP32119. 27 interactions.
    MINTiMINT-3012817.
    STRINGi9606.ENSP00000301522.

    Structurei

    Secondary structure

    1
    198
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi16 – 216
    Beta strandi24 – 296
    Helixi30 – 334
    Beta strandi36 – 427
    Helixi50 – 6011
    Helixi62 – 665
    Turni67 – 693
    Beta strandi70 – 789
    Helixi80 – 878
    Helixi91 – 933
    Beta strandi103 – 1053
    Helixi110 – 1145
    Turni120 – 1223
    Beta strandi127 – 1326
    Beta strandi136 – 1449
    Helixi152 – 16817
    Helixi187 – 19711

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1QMVX-ray1.70A/B/C/D/E/F/G/H/I/J2-198[»]
    ProteinModelPortaliP32119.
    SMRiP32119. Positions 3-198.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP32119.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini6 – 164159ThioredoxinPROSITE-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.
    HOGENOMiHOG000022343.
    HOVERGENiHBG000286.
    InParanoidiP32119.
    KOiK03386.
    OMAiEGVIQHA.
    PhylomeDBiP32119.
    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: P32119-1) [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

    MASGNARIGK PAPDFKATAV VDGAFKEVKL SDYKGKYVVL FFYPLDFTFV    50
    CPTEIIAFSN RAEDFRKLGC EVLGVSVDSQ FTHLAWINTP RKEGGLGPLN 100
    IPLLADVTRR LSEDYGVLKT DEGIAYRGLF IIDGKGVLRQ ITVNDLPVGR 150
    SVDEALRLVQ AFQYTDEHGE VCPAGWKPGS DTIKPNVDDS KEYFSKHN 198
    Length:198
    Mass (Da):21,892
    Last modified:January 23, 2007 - v5
    Checksum:i1AC781D908B32B46
    GO
    Isoform 2 (identifier: P32119-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         87-198: INTPRKEGGL...DSKEYFSKHN → YEQGPKREVA...SLRMMTVISI

    Note: No experimental confirmation available. Due to intron retention. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Show »
    Length:142
    Mass (Da):15,819
    Checksum:iC1FE1157EED6EC5E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti59 – 668SNRAEDFR → TTVKRTSA in CAA80269. (PubMed:8144038)Curated
    Sequence conflicti82 – 821T → N in AAA50465. (PubMed:8026862)Curated
    Sequence conflicti105 – 1051A → G in AAA50465. (PubMed:8026862)Curated
    Sequence conflicti120 – 1201T → N in CAA80269. (PubMed:8144038)Curated
    Sequence conflicti126 – 1272YR → TT AA sequence (PubMed:8313871)Curated
    Sequence conflicti175 – 1751G → A in CAA80269. (PubMed:8144038)Curated
    Sequence conflicti180 – 1801S → R in CAA80269. (PubMed:8144038)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti153 – 1531D → E.1 Publication
    Corresponds to variant rs34012472 [ dbSNP | Ensembl ].
    VAR_025051

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei87 – 198112INTPR…FSKHN → YEQGPKREVAAKLTPSGPSS VASWPLLNLWNLRFPIVKIM ETLPPKSLRMMTVISI in isoform 2. 1 PublicationVSP_042924Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z22548 mRNA. Translation: CAA80269.1.
    L19185 mRNA. Translation: AAA50465.1.
    CR450356 mRNA. Translation: CAG29352.1.
    CR541789 mRNA. Translation: CAG46588.1.
    AK289485 mRNA. Translation: BAF82174.1.
    DQ231563 Genomic DNA. Translation: ABB02182.1.
    AC018761 Genomic DNA. No translation available.
    CH471106 Genomic DNA. Translation: EAW84311.1.
    BC000452 mRNA. Translation: AAH00452.1.
    BC003022 mRNA. Translation: AAH03022.1.
    BC039428 mRNA. Translation: AAH39428.1.
    X82321 mRNA. Translation: CAA57764.1.
    CCDSiCCDS12281.1. [P32119-1]
    PIRiI68897.
    RefSeqiNP_005800.3. NM_005809.5. [P32119-1]
    UniGeneiHs.432121.

    Genome annotation databases

    EnsembliENST00000301522; ENSP00000301522; ENSG00000167815. [P32119-1]
    GeneIDi7001.
    KEGGihsa:7001.
    UCSCiuc002mvd.4. human. [P32119-1]

    Polymorphism databases

    DMDMi2507169.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z22548 mRNA. Translation: CAA80269.1 .
    L19185 mRNA. Translation: AAA50465.1 .
    CR450356 mRNA. Translation: CAG29352.1 .
    CR541789 mRNA. Translation: CAG46588.1 .
    AK289485 mRNA. Translation: BAF82174.1 .
    DQ231563 Genomic DNA. Translation: ABB02182.1 .
    AC018761 Genomic DNA. No translation available.
    CH471106 Genomic DNA. Translation: EAW84311.1 .
    BC000452 mRNA. Translation: AAH00452.1 .
    BC003022 mRNA. Translation: AAH03022.1 .
    BC039428 mRNA. Translation: AAH39428.1 .
    X82321 mRNA. Translation: CAA57764.1 .
    CCDSi CCDS12281.1. [P32119-1 ]
    PIRi I68897.
    RefSeqi NP_005800.3. NM_005809.5. [P32119-1 ]
    UniGenei Hs.432121.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1QMV X-ray 1.70 A/B/C/D/E/F/G/H/I/J 2-198 [» ]
    ProteinModelPortali P32119.
    SMRi P32119. Positions 3-198.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112860. 57 interactions.
    IntActi P32119. 27 interactions.
    MINTi MINT-3012817.
    STRINGi 9606.ENSP00000301522.

    Protein family/group databases

    PeroxiBasei 4475. Hs2CysPrx02.

    PTM databases

    PhosphoSitei P32119.

    Polymorphism databases

    DMDMi 2507169.

    2D gel databases

    DOSAC-COBS-2DPAGE P32119.
    OGPi P32119.
    REPRODUCTION-2DPAGE IPI00027350.
    SWISS-2DPAGE P32119.
    UCD-2DPAGE P32119.

    Proteomic databases

    MaxQBi P32119.
    PaxDbi P32119.
    PRIDEi P32119.

    Protocols and materials databases

    DNASUi 7001.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000301522 ; ENSP00000301522 ; ENSG00000167815 . [P32119-1 ]
    GeneIDi 7001.
    KEGGi hsa:7001.
    UCSCi uc002mvd.4. human. [P32119-1 ]

    Organism-specific databases

    CTDi 7001.
    GeneCardsi GC19M012907.
    HGNCi HGNC:9353. PRDX2.
    HPAi CAB008713.
    MIMi 600538. gene.
    neXtProti NX_P32119.
    PharmGKBi PA33723.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0450.
    HOGENOMi HOG000022343.
    HOVERGENi HBG000286.
    InParanoidi P32119.
    KOi K03386.
    OMAi EGVIQHA.
    PhylomeDBi P32119.
    TreeFami TF105181.

    Enzyme and pathway databases

    Reactomei REACT_172715. Detoxification of Reactive Oxygen Species.

    Miscellaneous databases

    ChiTaRSi PRDX2. human.
    EvolutionaryTracei P32119.
    GeneWikii Peroxiredoxin_2.
    GenomeRNAii 7001.
    NextBioi 27342.
    PROi P32119.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P32119.
    Bgeei P32119.
    CleanExi HS_PRDX2.
    Genevestigatori P32119.

    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. "The thiol-specific antioxidant protein from human brain: gene cloning and analysis of conserved cysteine regions."
      Lim Y.-S., Cha M.-K., Kim H.-K., Kim I.-H.
      Gene 140:279-284(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    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] (ISOFORM 1).
    3. "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 2).
      Tissue: Cerebellum.
    4. "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] (ISOFORM 1).
    5. NIEHS SNPs program
      Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLU-153.
    6. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(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: Hypothalamus and Lung.
    9. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 8-26; 67-135 AND 140-150, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    10. "Thioredoxin-linked peroxidase from human red blood cell: evidence for the existence of thioredoxin and thioredoxin reductase in human red blood cell."
      Cha M.-K., Kim I.-H.
      Biochem. Biophys. Res. Commun. 217:900-907(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 8-24, CATALYTIC ACTIVITY.
      Tissue: Erythrocyte.
    11. Cited for: PROTEIN SEQUENCE OF 17-26; 93-103 AND 120-129.
      Tissue: Erythrocyte.
    12. "A two-dimensional gel database of human colon carcinoma proteins."
      Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.
      Electrophoresis 18:605-613(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 17-26; 111-135 AND 140-157.
      Tissue: Colon carcinoma.
    13. "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
      Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
      Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 17-25; 140-150 AND 163-185.
      Tissue: Keratinocyte.
    14. Oberbaeumer I.
      Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 35-198 (ISOFORM 1).
    15. "Proteomics analysis of cellular response to oxidative stress. Evidence for in vivo overoxidation of peroxiredoxins at their active site."
      Rabilloud T., Heller M., Gasnier F., Luche S., Rey C., Aebersold R., Benahmed M., Louisot P., Lunardi J.
      J. Biol. Chem. 277:19396-19401(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: OVEROXIDATION AT CYS-51.
    16. "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-51, IDENTIFICATION BY MASS SPECTROMETRY.
    17. "Mammalian TIMELESS and Tipin are evolutionarily conserved replication fork-associated factors."
      Gotter A.L., Suppa C., Emanuel B.S.
      J. Mol. Biol. 366:36-52(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TIPIN.
    18. "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].
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Crystal structure of decameric 2-Cys peroxiredoxin from human erythrocytes at 1.7 A resolution."
      Schroeder E., Littlechild J.A., Lebedev A.A., Errington N., Vagin A.A., Isupov M.N.
      Structure 8:605-615(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-198.

    Entry informationi

    Entry nameiPRDX2_HUMAN
    AccessioniPrimary (citable) accession number: P32119
    Secondary accession number(s): A8K0C0
    , P31945, P32118, P35701, Q6FHG4, Q92763, Q9UC23
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 170 of the entry and version 5 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-51 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-172-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-51 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 19
      Human chromosome 19: 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