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Q06830

- PRDX1_HUMAN

UniProt

Q06830 - PRDX1_HUMAN

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Protein

Peroxiredoxin-1

Gene

PRDX1

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 but not from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2. Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation (By similarity).By similarity

Catalytic activityi

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

Sites

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

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Antioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

ReactomeiREACT_172715. Detoxification of Reactive Oxygen Species.

Protein family/group databases

PeroxiBasei4501. Hs2CysPrx01.

Names & Taxonomyi

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

Organism-specific databases

HGNCiHGNC:9352. PRDX1.

Subcellular locationi

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

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

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

Organism-specific databases

PharmGKBiPA33722.

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiQ06830.
PaxDbiQ06830.
PRIDEiQ06830.

2D gel databases

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

PTM databases

PhosphoSiteiQ06830.

Expressioni

Inductioni

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

Gene expression databases

BgeeiQ06830.
CleanExiHS_PRDX1.
GenevestigatoriQ06830.

Organism-specific databases

HPAiCAB004682.
HPA007730.

Interactioni

Subunit structurei

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

Binary interactionsi

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

Protein-protein interaction databases

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

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ06830.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

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

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG0450.
GeneTreeiENSGT00390000004653.
HOVERGENiHBG000286.
InParanoidiQ06830.
KOiK13279.
OMAiEMKIPLV.
OrthoDBiEOG7T1RCD.
PhylomeDBiQ06830.
TreeFamiTF105181.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

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

Q06830 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSGNAKIGH PAPNFKATAV MPDGQFKDIS LSDYKGKYVV FFFYPLDFTF
60 70 80 90 100
VCPTEIIAFS DRAEEFKKLN CQVIGASVDS HFCHLAWVNT PKKQGGLGPM
110 120 130 140 150
NIPLVSDPKR TIAQDYGVLK ADEGISFRGL FIIDDKGILR QITVNDLPVG
160 170 180 190
RSVDETLRLV QAFQFTDKHG EVCPAGWKPG SDTIKPDVQK SKEYFSKQK
Length:199
Mass (Da):22,110
Last modified:June 1, 1994 - v1
Checksum:i8F68E56D75BF5304
GO

Sequence cautioni

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

Experimental Info

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

Natural variant

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

Sequence databases

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

Genome annotation databases

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

Polymorphism databases

DMDMi548453.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

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

Sequence databases

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

3D structure databases

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

Protein-protein interaction databases

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

Chemistry

ChEMBLi CHEMBL5315.

Protein family/group databases

PeroxiBasei 4501. Hs2CysPrx01.

PTM databases

PhosphoSitei Q06830.

Polymorphism databases

DMDMi 548453.

2D gel databases

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

Proteomic databases

MaxQBi Q06830.
PaxDbi Q06830.
PRIDEi Q06830.

Protocols and materials databases

DNASUi 5052.
Structural Biology Knowledgebase Search...

Genome annotation databases

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

Organism-specific databases

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

Phylogenomic databases

eggNOGi COG0450.
GeneTreei ENSGT00390000004653.
HOVERGENi HBG000286.
InParanoidi Q06830.
KOi K13279.
OMAi EMKIPLV.
OrthoDBi EOG7T1RCD.
PhylomeDBi Q06830.
TreeFami TF105181.

Enzyme and pathway databases

Reactomei REACT_172715. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

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

Gene expression databases

Bgeei Q06830.
CleanExi HS_PRDX1.
Genevestigatori Q06830.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "A human cDNA corresponding to a gene overexpressed during cell proliferation encodes a product sharing homology with amoebic and bacterial proteins."
    Prosperi M.T., Ferbus D., Karczinski I., Goubin G.
    J. Biol. Chem. 268:11050-11056(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloning and sequence analysis of candidate human natural killer-enhancing factor genes."
    Shau H., Butterfield L.H., Chiu R., Kim A.
    Immunogenetics 40:129-134(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. NIEHS SNPs program
    Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLY-62.
  6. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
    Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
    , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
    Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Urinary bladder.
  10. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 17-35; 93-136; 141-151 AND 159-190, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  11. "A method for detection of overoxidation of cysteines: peroxiredoxins are oxidized in vivo at the active-site cysteine during oxidative stress."
    Wagner E., Luche S., Penna L., Chevallet M., van Dorsselaer A., Leize-Wagner E., Rabilloud T.
    Biochem. J. 366:777-785(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: OVEROXIDATION AT CYS-52.
  12. "Regulation of peroxiredoxin I activity by Cdc2-mediated phosphorylation."
    Chang T.-S., Jeong W., Choi S.Y., Yu S., Kang S.W., Rhee S.G.
    J. Biol. Chem. 277:25370-25376(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-90, MUTAGENESIS OF THR-90.
  13. "Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid."
    Yang K.S., Kang S.W., Woo H.A., Hwang S.C., Chae H.Z., Kim K., Rhee S.G.
    J. Biol. Chem. 277:38029-38036(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: OVEROXIDATION AT CYS-52.
  14. "Regeneration of peroxiredoxins during recovery after oxidative stress: only some overoxidized peroxiredoxins can be reduced during recovery after oxidative stress."
    Chevallet M., Wagner E., Luche S., van Dorsselaer A., Leize-Wagner E., Rabilloud T.
    J. Biol. Chem. 278:37146-37153(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: RETROREDUCTION OF CYS-52, IDENTIFICATION BY MASS SPECTROMETRY.
  15. "Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation."
    Woo H.A., Chae H.Z., Hwang S.C., Yang K.S., Kang S.W., Kim K., Rhee S.G.
    Science 300:653-656(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: RETROREDUCTION OF CYS-52, IDENTIFICATION BY MASS SPECTROMETRY.
  16. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Melanoma.
  17. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2; LYS-7; LYS-16; LYS-27 AND LYS-35, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPRDX1_HUMAN
AccessioniPrimary (citable) accession number: Q06830
Secondary accession number(s): B5BU26
, D3DPZ8, P35703, Q2V576, Q5T154, Q5T155
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: October 29, 2014
This is version 165 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

The active site is the redox-active Cys-52 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-173-SH of the other subunit to form an intermolecular disulfide with a concomitant homodimer formation. The enzyme may be subsequently regenerated by reduction of the disulfide by thioredoxin.
Inactivated upon oxidative stress by overoxidation of Cys-52 to Cys-SO2H and Cys-SO3H. Cys-SO2H is retroreduced to Cys-SOH after removal of H2O2, while Cys-SO3H may be irreversibly oxidized.

Keywords - Technical termi

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

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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