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P30041

- PRDX6_HUMAN

UniProt

P30041 - PRDX6_HUMAN

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Protein

Peroxiredoxin-6

Gene

PRDX6

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. Can reduce H2O2 and short chain organic, fatty acid, and phospholipid hydroperoxides. May play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury.

Catalytic activityi

2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.
2 glutathione + H2O2 = glutathione disulfide + 2 H2O.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei32 – 321For phospholipase activity
Active sitei47 – 471Cysteine sulfenic acid (-SOH) intermediate

GO - Molecular functioni

  1. antioxidant activity Source: UniProtKB
  2. glutathione peroxidase activity Source: UniProtKB-EC
  3. peroxiredoxin activity Source: UniProtKB-EC
  4. phospholipase A2 activity Source: UniProtKB

GO - Biological processi

  1. hydrogen peroxide catabolic process Source: Ensembl
  2. phospholipid catabolic process Source: UniProtKB
  3. response to oxidative stress Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Hydrolase, Oxidoreductase, Peroxidase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Enzyme and pathway databases

BRENDAi1.11.1.15. 2681.
ReactomeiREACT_172715. Detoxification of Reactive Oxygen Species.

Protein family/group databases

PeroxiBasei4426. Hs1CysPrx01.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxiredoxin-6 (EC:1.11.1.15)
Alternative name(s):
1-Cys peroxiredoxin
Short name:
1-Cys PRX
24 kDa protein
Acidic calcium-independent phospholipase A2 (EC:3.1.1.-)
Short name:
aiPLA2
Antioxidant protein 2
Liver 2D page spot 40
Non-selenium glutathione peroxidase (EC:1.11.1.9)
Short name:
NSGPx
Red blood cells page spot 12
Gene namesi
Name:PRDX6
Synonyms:AOP2, KIAA0106
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:16753. PRDX6.

Subcellular locationi

Cytoplasm 2 Publications. Lysosome By similarity. Cytoplasmic vesicle By similarity
Note: Also found in lung secretory organelles.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoplasmic vesicle Source: UniProtKB-KW
  3. cytosol Source: UniProtKB
  4. extracellular space Source: UniProt
  5. extracellular vesicular exosome Source: UniProtKB
  6. lysosome Source: UniProtKB-KW
  7. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Lysosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi32 – 321S → A: Loss of AIPLA2 activity, but no effect on NSGPX activity.
Mutagenesisi47 – 471C → S: Loss of NSGPX activity, but no effect on AIPLA2 activity.

Organism-specific databases

PharmGKBiPA134992760.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed4 Publications
Chaini2 – 224223Peroxiredoxin-6PRO_0000135102Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei44 – 441Phosphothreonine2 Publications
Disulfide bondi47 – 47Interchain; in linked formBy similarity
Modified residuei63 – 631N6-acetyllysine1 Publication
Modified residuei89 – 891Phosphotyrosine1 Publication
Modified residuei209 – 2091N6-acetyllysine; alternate1 Publication
Modified residuei209 – 2091N6-succinyllysine; alternateBy similarity

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiP30041.
PaxDbiP30041.
PeptideAtlasiP30041.
PRIDEiP30041.

2D gel databases

DOSAC-COBS-2DPAGEP30041.
OGPiP30041.
REPRODUCTION-2DPAGEIPI00220301.
P30041.
SWISS-2DPAGEP30041.

PTM databases

PhosphoSiteiP30041.

Expressioni

Gene expression databases

BgeeiP30041.
CleanExiHS_PRDX6.
ExpressionAtlasiP30041. baseline and differential.
GenevestigatoriP30041.

Organism-specific databases

HPAiCAB008663.
HPA006983.

Interactioni

Subunit structurei

Homotetramer. Interacts with GSTP1; mediates PRDX6 glutathionylation and regeneration. May interact with HTR2A (By similarity). Interacts with APEX1 and STH. May interact with FAM168B.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P299913EBI-2255129,EBI-8826747From a different organism.
GSTP1P092112EBI-2255129,EBI-353467

Protein-protein interaction databases

BioGridi114956. 50 interactions.
IntActiP30041. 19 interactions.
MINTiMINT-4999165.
STRINGi9606.ENSP00000342026.

Structurei

Secondary structure

1
224
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi15 – 184Combined sources
Beta strandi21 – 244Combined sources
Helixi25 – 295Combined sources
Beta strandi32 – 409Combined sources
Helixi45 – 6218Combined sources
Turni63 – 653Combined sources
Beta strandi66 – 749Combined sources
Helixi76 – 8914Combined sources
Beta strandi102 – 1043Combined sources
Helixi109 – 1135Combined sources
Beta strandi124 – 1263Combined sources
Beta strandi133 – 1375Combined sources
Beta strandi141 – 1488Combined sources
Helixi157 – 17317Combined sources
Beta strandi175 – 1773Combined sources
Beta strandi187 – 1893Combined sources
Helixi195 – 2017Combined sources
Beta strandi219 – 2213Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PRXX-ray2.00A/B1-224[»]
ProteinModelPortaliP30041.
SMRiP30041. Positions 5-224.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30041.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 169165ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG0450.
HOGENOMiHOG000022346.
HOVERGENiHBG105234.
InParanoidiP30041.
KOiK11188.
OMAiDMIDYQD.
OrthoDBiEOG7CNZGP.
PhylomeDBiP30041.
TreeFamiTF105183.

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.

P30041-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPGGLLLGDV APNFEANTTV GRIRFHDFLG DSWGILFSHP RDFTPVCTTE
60 70 80 90 100
LGRAAKLAPE FAKRNVKLIA LSIDSVEDHL AWSKDINAYN CEEPTEKLPF
110 120 130 140 150
PIIDDRNREL AILLGMLDPA EKDEKGMPVT ARVVFVFGPD KKLKLSILYP
160 170 180 190 200
ATTGRNFDEI LRVVISLQLT AEKRVATPVD WKDGDSVMVL PTIPEEEAKK
210 220
LFPKGVFTKE LPSGKKYLRY TPQP
Length:224
Mass (Da):25,035
Last modified:January 23, 2007 - v3
Checksum:i017D955F0FEEDFBC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14662 mRNA. Translation: BAA03496.1.
DQ230990 Genomic DNA. Translation: ABB02185.1.
AL139142 Genomic DNA. Translation: CAI20936.1.
AK289352 mRNA. Translation: BAF82041.1.
CH471067 Genomic DNA. Translation: EAW90944.1.
BC035857 mRNA. Translation: AAH35857.1.
BC053550 mRNA. Translation: AAH53550.1.
AJ844621 mRNA. Translation: CAH59743.1.
CCDSiCCDS1307.1.
RefSeqiNP_004896.1. NM_004905.2.
UniGeneiHs.120.
Hs.731505.

Genome annotation databases

EnsembliENST00000340385; ENSP00000342026; ENSG00000117592.
GeneIDi9588.
KEGGihsa:9588.
UCSCiuc001giy.1. human.

Polymorphism databases

DMDMi1718024.

Cross-referencesi

Web resourcesi

NIEHS SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14662 mRNA. Translation: BAA03496.1 .
DQ230990 Genomic DNA. Translation: ABB02185.1 .
AL139142 Genomic DNA. Translation: CAI20936.1 .
AK289352 mRNA. Translation: BAF82041.1 .
CH471067 Genomic DNA. Translation: EAW90944.1 .
BC035857 mRNA. Translation: AAH35857.1 .
BC053550 mRNA. Translation: AAH53550.1 .
AJ844621 mRNA. Translation: CAH59743.1 .
CCDSi CCDS1307.1.
RefSeqi NP_004896.1. NM_004905.2.
UniGenei Hs.120.
Hs.731505.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1PRX X-ray 2.00 A/B 1-224 [» ]
ProteinModelPortali P30041.
SMRi P30041. Positions 5-224.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114956. 50 interactions.
IntActi P30041. 19 interactions.
MINTi MINT-4999165.
STRINGi 9606.ENSP00000342026.

Protein family/group databases

PeroxiBasei 4426. Hs1CysPrx01.

PTM databases

PhosphoSitei P30041.

Polymorphism databases

DMDMi 1718024.

2D gel databases

DOSAC-COBS-2DPAGE P30041.
OGPi P30041.
REPRODUCTION-2DPAGE IPI00220301.
P30041.
SWISS-2DPAGE P30041.

Proteomic databases

MaxQBi P30041.
PaxDbi P30041.
PeptideAtlasi P30041.
PRIDEi P30041.

Protocols and materials databases

DNASUi 9588.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000340385 ; ENSP00000342026 ; ENSG00000117592 .
GeneIDi 9588.
KEGGi hsa:9588.
UCSCi uc001giy.1. human.

Organism-specific databases

CTDi 9588.
GeneCardsi GC01P173446.
H-InvDB HIX0028696.
HGNCi HGNC:16753. PRDX6.
HPAi CAB008663.
HPA006983.
MIMi 602316. gene.
neXtProti NX_P30041.
PharmGKBi PA134992760.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0450.
HOGENOMi HOG000022346.
HOVERGENi HBG105234.
InParanoidi P30041.
KOi K11188.
OMAi DMIDYQD.
OrthoDBi EOG7CNZGP.
PhylomeDBi P30041.
TreeFami TF105183.

Enzyme and pathway databases

BRENDAi 1.11.1.15. 2681.
Reactomei REACT_172715. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

ChiTaRSi PRDX6. human.
EvolutionaryTracei P30041.
GeneWikii PRDX6.
GenomeRNAii 9588.
NextBioi 35979.
PROi P30041.
SOURCEi Search...

Gene expression databases

Bgeei P30041.
CleanExi HS_PRDX6.
ExpressionAtlasi P30041. baseline and differential.
Genevestigatori P30041.

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. "Identification of a human cDNA clone for lysosomal type Ca2+-independent phospholipase A2 and properties of the expressed protein."
    Kim T.-S., Sundaresh C.S., Feinstein S.I., Dodia C., Skach W.R., Jain M.K., Nagase T., Seki N., Ishikawa K., Nomura N., Fisher A.B.
    J. Biol. Chem. 272:2542-2550(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The human homologue of a bovine non-selenium glutathione peroxidase is a novel keratinocyte growth factor-regulated gene."
    Frank S., Munz B., Werner S.
    Oncogene 14:915-921(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1."
    Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.
    DNA Res. 2:37-43(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Bone marrow.
  4. "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].
  5. NIEHS SNPs program
    Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. "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].
  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].
    Tissue: Fetal brain and Testis.
  9. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-22.
    Tissue: Platelet.
  10. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-22; 25-53; 85-106; 133-142; 145-155; 163-173 AND 175-199, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  11. "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 2-15.
    Tissue: Liver.
  12. Cited for: PROTEIN SEQUENCE OF 2-13.
    Tissue: Erythrocyte.
  13. "DNA probes built and sequenced for microarrays hybridisations."
    Dominguez O., Lombardia L.
    Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 14-99.
  14. "Characterization of a mammalian peroxiredoxin that contains one conserved cysteine."
    Kang S.W., Baines I.C., Rhee S.G.
    J. Biol. Chem. 273:6303-6311(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, MUTAGENESIS.
  15. "1-Cys peroxiredoxin, a bifunctional enzyme with glutathione peroxidase and phospholipase A2 activities."
    Chen J.-W., Dodia C., Feinstein S.I., Jain M.K., Fisher A.B.
    J. Biol. Chem. 275:28421-28427(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, MUTAGENESIS.
  16. "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-47.
  17. "Saitohin, which is nested in the tau locus and confers allele-specific susceptibility to several neurodegenerative diseases, interacts with peroxiredoxin 6."
    Gao L., Tse S.-W., Conrad C., Andreadis A.
    J. Biol. Chem. 280:39268-39272(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH STH.
  18. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-89, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-44, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. "APE1/Ref-1 interacts with NPM1 within nucleoli and plays a role in the rRNA quality control process."
    Vascotto C., Fantini D., Romanello M., Cesaratto L., Deganuto M., Leonardi A., Radicella J.P., Kelley M.R., D'Ambrosio C., Scaloni A., Quadrifoglio F., Tell G.
    Mol. Cell. Biol. 29:1834-1854(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH APEX1, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
  21. "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-63 AND LYS-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-44, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "The novel protein MANI modulates neurogenesis and neurite-cone growth."
    Mishra M., Akatsu H., Heese K.
    J. Cell. Mol. Med. 15:1713-1725(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FAM168B.
  25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "Crystal structure of a novel human peroxidase enzyme at 2.0-A resolution."
    Choi H.-J., Kang S.W., Yang C.-H., Rhee S.G., Ryu S.-E.
    Nat. Struct. Biol. 5:400-406(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Entry informationi

Entry nameiPRDX6_HUMAN
AccessioniPrimary (citable) accession number: P30041
Secondary accession number(s): A8JZY7
, P32077, Q5TAH4, Q5ZEZ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 162 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-47 oxidized to Cys-SOH. Unlike 2-Cys peroxiredoxins, PRDX6 conserves only this peroxidatic cysteine. To regenerate and activate the enzyme, the oxidized form is directly reduced to cysteine by glutathione and not thioredoxin.
Irreversibly inactivated by overoxidation of Cys-47 (to Cys-SO3H) upon oxidative stress.

Keywords - Technical termi

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

Documents

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

External Data

Dasty 3