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P32119

- PRDX2_HUMAN

UniProt

P32119 - PRDX2_HUMAN

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Protein

Peroxiredoxin-2

Gene

PRDX2

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

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
Complete GO annotation...

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: UniProtKB
Complete GO annotation...

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

BgeeiP32119.
CleanExiHS_PRDX2.
ExpressionAtlasiP32119. baseline and differential.
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

        10         20         30         40         50
MASGNARIGK PAPDFKATAV VDGAFKEVKL SDYKGKYVVL FFYPLDFTFV
60 70 80 90 100
CPTEIIAFSN RAEDFRKLGC EVLGVSVDSQ FTHLAWINTP RKEGGLGPLN
110 120 130 140 150
IPLLADVTRR LSEDYGVLKT DEGIAYRGLF IIDGKGVLRQ ITVNDLPVGR
160 170 180 190
SVDEALRLVQ AFQYTDEHGE VCPAGWKPGS DTIKPNVDDS KEYFSKHN
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

Bgeei P32119.
CleanExi HS_PRDX2.
ExpressionAtlasi P32119. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 171 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

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