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P30048

- PRDX3_HUMAN

UniProt

P30048 - PRDX3_HUMAN

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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

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 C-terminus binding Source: UniProtKB
  5. protein kinase binding Source: UniProtKB
  6. 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiP30048.
CleanExiHS_PRDX3.
ExpressionAtlasiP30048. baseline and differential.
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. 45 interactions.
IntActiP30048. 34 interactions.
MINTiMINT-195453.
STRINGi9606.ENSP00000298510.

Structurei

3D structure databases

ProteinModelPortaliP30048.
SMRiP30048. Positions 63-256.
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.
GeneTreeiENSGT00390000004653.
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

        10         20         30         40         50
MAAAVGRLLR ASVARHVSAI PWGISATAAL RPAACGRTSL TNLLCSGSSQ
60 70 80 90 100
AKLFSTSSSC HAPAVTQHAP YFKGTAVVNG EFKDLSLDDF KGKYLVLFFY
110 120 130 140 150
PLDFTFVCPT EIVAFSDKAN EFHDVNCEVV AVSVDSHFSH LAWINTPRKN
160 170 180 190 200
GGLGHMNIAL LSDLTKQISR DYGVLLEGSG LALRGLFIID PNGVIKHLSV
210 220 230 240 250
NDLPVGRSVE ETLRLVKAFQ YVETHGEVCP ANWTPDSPTI KPSPAASKEY

FQKVNQ
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:
EMBLi
GenBanki
DDBJi
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.
CCDSiCCDS7611.1. [P30048-1]
RefSeqiNP_006784.1. NM_006793.4. [P30048-1]
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:
EMBLi
GenBanki
DDBJi
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 CCDS7611.1. [P30048-1 ]
RefSeqi NP_006784.1. NM_006793.4. [P30048-1 ]
UniGenei Hs.523302.

3D structure databases

ProteinModelPortali P30048.
SMRi P30048. Positions 63-256.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116136. 45 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 GC10M120928.
H-InvDB HIX0035477.
HGNCi HGNC:9354. PRDX3.
HPAi CAB008656.
MIMi 604769. gene.
neXtProti NX_P30048.
PharmGKBi PA33724.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0450.
GeneTreei ENSGT00390000004653.
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

Bgeei P30048.
CleanExi HS_PRDX3.
ExpressionAtlasi P30048. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 177 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

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