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P30044

- PRDX5_HUMAN

UniProt

P30044 - PRDX5_HUMAN

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Protein

Peroxiredoxin-5, mitochondrial

Gene

PRDX5

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

Functioni

Reduces hydrogen peroxide and alkyl hydroperoxides with reducing equivalents provided through the thioredoxin system. Involved in intracellular redox signaling.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei100 – 1001Cysteine sulfenic acid (-SOH) intermediate1 Publication

GO - Molecular functioni

  1. antioxidant activity Source: UniProtKB
  2. cysteine-type endopeptidase inhibitor activity involved in apoptotic process Source: UniProtKB
  3. peroxidase activity Source: UniProtKB
  4. peroxiredoxin activity Source: UniProtKB
  5. peroxynitrite reductase activity Source: UniProtKB
  6. protein dimerization activity Source: UniProtKB
  7. receptor binding Source: UniProtKB
  8. RNA polymerase III regulatory region DNA binding Source: UniProtKB

GO - Biological processi

  1. cellular response to reactive oxygen species Source: UniProtKB
  2. hydrogen peroxide catabolic process Source: UniProtKB
  3. inflammatory response Source: UniProtKB
  4. NADPH oxidation Source: UniProtKB
  5. negative regulation of apoptotic process Source: UniProtKB
  6. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: GOC
  7. negative regulation of oxidoreductase activity Source: UniProtKB
  8. negative regulation of transcription from RNA polymerase III promoter Source: UniProtKB
  9. positive regulation of collagen biosynthetic process Source: UniProtKB
  10. reactive nitrogen species metabolic process Source: UniProtKB
  11. regulation of apoptosis involved in tissue homeostasis Source: UniProtKB
  12. 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

PeroxiBasei4448. HsPrxV.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxiredoxin-5, mitochondrial (EC:1.11.1.15)
Alternative name(s):
Alu corepressor 1
Antioxidant enzyme B166
Short name:
AOEB166
Liver tissue 2D-page spot 71B
PLP
Peroxiredoxin V
Short name:
Prx-V
Peroxisomal antioxidant enzyme
TPx type VI
Thioredoxin peroxidase PMP20
Thioredoxin reductase
Gene namesi
Name:PRDX5
Synonyms:ACR1
ORF Names:SBBI10
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:9355. PRDX5.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoplasmic vesicle Source: UniProtKB
  3. cytosol Source: UniProtKB
  4. extracellular space Source: UniProt
  5. extracellular vesicular exosome Source: UniProtKB
  6. intracellular membrane-bounded organelle Source: UniProtKB
  7. mitochondrial matrix Source: Reactome
  8. mitochondrion Source: UniProtKB
  9. nucleus Source: UniProtKB
  10. perinuclear region of cytoplasm Source: UniProtKB
  11. peroxisomal matrix Source: UniProtKB
  12. peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Peroxisome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi100 – 1001C → S: Complete loss of activity. 1 Publication
Mutagenesisi125 – 1251C → S: No change in activity. 1 Publication
Mutagenesisi204 – 2041C → S: Complete loss of activity. 1 Publication

Organism-specific databases

PharmGKBiPA33726.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5252MitochondrionSequence AnalysisAdd
BLAST
Chaini53 – 214162Peroxiredoxin-5, mitochondrialPRO_0000023793Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei75 – 751N6-acetyllysineBy similarity
Modified residuei83 – 831N6-acetyllysine; alternate1 Publication
Modified residuei83 – 831N6-succinyllysine; alternateBy similarity
Disulfide bondi100 ↔ 204Redox-active1 PublicationPROSITE-ProRule annotation
Modified residuei116 – 1161N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

MaxQBiP30044.
PaxDbiP30044.
PRIDEiP30044.

2D gel databases

OGPiP30044.
REPRODUCTION-2DPAGEIPI00759663.
SWISS-2DPAGEP30044.
UCD-2DPAGEP30044.

PTM databases

PhosphoSiteiP30044.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiP30044.
CleanExiHS_PRDX5.
ExpressionAtlasiP30044. baseline and differential.
GenevestigatoriP30044.

Organism-specific databases

HPAiCAB008661.
HPA037915.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi117352. 35 interactions.
IntActiP30044. 5 interactions.
MINTiMINT-5002532.
STRINGi9606.ENSP00000265462.

Structurei

Secondary structure

1
214
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi66 – 683Combined sources
Helixi72 – 743Combined sources
Beta strandi75 – 773Combined sources
Helixi78 – 814Combined sources
Turni82 – 843Combined sources
Beta strandi85 – 917Combined sources
Helixi98 – 1025Combined sources
Helixi104 – 1107Combined sources
Helixi112 – 1165Combined sources
Turni117 – 1193Combined sources
Beta strandi122 – 1298Combined sources
Helixi131 – 14010Combined sources
Turni144 – 1463Combined sources
Beta strandi148 – 1514Combined sources
Helixi156 – 1616Combined sources
Helixi167 – 1693Combined sources
Helixi170 – 1734Combined sources
Beta strandi181 – 1866Combined sources
Beta strandi189 – 1957Combined sources
Beta strandi199 – 2035Combined sources
Helixi207 – 2137Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H4OX-ray1.95A/B/C/D/E/F/G/H54-214[»]
1HD2X-ray1.50A54-214[»]
1OC3X-ray2.00A/B/C54-214[»]
1URMX-ray1.70A54-214[»]
2VL2X-ray1.92A/B/C54-214[»]
2VL3X-ray1.83A/B/C54-214[»]
2VL9X-ray2.70A/B/C/D54-214[»]
3MNGX-ray1.45A54-214[»]
4K7IX-ray2.25A/B/C54-214[»]
4K7NX-ray2.30A/B/C54-214[»]
4K7OX-ray1.98A/B/C54-214[»]
4MMMX-ray1.47A/C/E/G54-214[»]
ProteinModelPortaliP30044.
SMRiP30044. Positions 54-214.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30044.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini56 – 214159ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi212 – 2143Microbody targeting signalBy similarity

Sequence similaritiesi

Belongs to the peroxiredoxin 2 family.Curated
Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

eggNOGiCOG0678.
GeneTreeiENSGT00390000018173.
HOGENOMiHOG000255884.
HOVERGENiHBG053675.
InParanoidiP30044.
KOiK11187.
OMAiMSAWGKQ.
OrthoDBiEOG77Q4XX.
PhylomeDBiP30044.
TreeFamiTF105182.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR013740. Redoxin.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF08534. Redoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing and alternative initiation. Align

Isoform Mitochondrial (identifier: P30044-1) [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
MGLAGVCALR RSAGYILVGG AGGQSAAAAA RRYSEGEWAS GGVRSFSRAA
60 70 80 90 100
AAMAPIKVGD AIPAVEVFEG EPGNKVNLAE LFKGKKGVLF GVPGAFTPGC
110 120 130 140 150
SKTHLPGFVE QAEALKAKGV QVVACLSVND AFVTGEWGRA HKAEGKVRLL
160 170 180 190 200
ADPTGAFGKE TDLLLDDSLV SIFGNRRLKR FSMVVQDGIV KALNVEPDGT
210
GLTCSLAPNI ISQL
Length:214
Mass (Da):22,086
Last modified:January 11, 2011 - v4
Checksum:iDA1DEB21120254EE
GO
Isoform Cytoplasmic+peroxisomal (identifier: P30044-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-52: Missing.

Show »
Length:162
Mass (Da):17,031
Checksum:i370DF621012F880D
GO
Isoform 3 (identifier: P30044-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     102-145: Missing.

Note: No experimental confirmation available.

Show »
Length:170
Mass (Da):17,454
Checksum:i29984B81B33F82C1
GO
Isoform 4 (identifier: P30044-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     57-145: Missing.

Note: Produced by alternative splicing.

Show »
Length:125
Mass (Da):12,897
Checksum:iF3A1C1531E4E4A73
GO

Sequence cautioni

The sequence AAF17200.1 differs from that shown. Reason: Frameshift at positions 14 and 30. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti141 – 1411H → T in AAF04856. (PubMed:10679306)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti33 – 331Y → C.7 Publications
Corresponds to variant rs7938623 [ dbSNP | Ensembl ].
VAR_025049
Natural varianti157 – 1571F → L in a breast cancer sample; somatic mutation. 1 Publication
VAR_036406

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5252Missing in isoform Cytoplasmic+peroxisomal. 4 PublicationsVSP_018829Add
BLAST
Alternative sequencei57 – 14589Missing in isoform 4. 1 PublicationVSP_046682Add
BLAST
Alternative sequencei102 – 14544Missing in isoform 3. 1 PublicationVSP_045783Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF231705 mRNA. Translation: AAF78899.1.
AF124993 mRNA. Translation: AAF27531.1.
AF110731 mRNA. Translation: AAF03750.1.
AF197952 mRNA. Translation: AAF04856.1.
AJ249483 mRNA. Translation: CAB62210.1.
AF242525 mRNA. Translation: AAF99605.1.
AF112212 mRNA. Translation: AAF17200.1. Frameshift.
CR457203 mRNA. Translation: CAG33484.1.
DQ247769 Genomic DNA. Translation: ABB05181.1.
AP001453 Genomic DNA. No translation available.
AP003774 Genomic DNA. No translation available.
BC110983 mRNA. Translation: AAI10984.1.
BC113723 mRNA. Translation: AAI13724.1.
BC113725 mRNA. Translation: AAI13726.1.
BC143849 mRNA. Translation: AAI43850.1.
BC171733 mRNA. Translation: AAI71733.1.
CCDSiCCDS8069.1. [P30044-1]
CCDS8070.1. [P30044-3]
CCDS8071.1. [P30044-4]
RefSeqiNP_036226.1. NM_012094.4.
NP_857634.1. NM_181651.2.
NP_857635.1. NM_181652.2.
UniGeneiHs.502823.

Genome annotation databases

EnsembliENST00000265462; ENSP00000265462; ENSG00000126432. [P30044-1]
ENST00000347941; ENSP00000335363; ENSG00000126432. [P30044-4]
ENST00000352435; ENSP00000335334; ENSG00000126432. [P30044-3]
GeneIDi25824.
KEGGihsa:25824.
UCSCiuc001nzu.3. human. [P30044-1]

Polymorphism databases

DMDMi317373539.

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF231705 mRNA. Translation: AAF78899.1 .
AF124993 mRNA. Translation: AAF27531.1 .
AF110731 mRNA. Translation: AAF03750.1 .
AF197952 mRNA. Translation: AAF04856.1 .
AJ249483 mRNA. Translation: CAB62210.1 .
AF242525 mRNA. Translation: AAF99605.1 .
AF112212 mRNA. Translation: AAF17200.1 . Frameshift.
CR457203 mRNA. Translation: CAG33484.1 .
DQ247769 Genomic DNA. Translation: ABB05181.1 .
AP001453 Genomic DNA. No translation available.
AP003774 Genomic DNA. No translation available.
BC110983 mRNA. Translation: AAI10984.1 .
BC113723 mRNA. Translation: AAI13724.1 .
BC113725 mRNA. Translation: AAI13726.1 .
BC143849 mRNA. Translation: AAI43850.1 .
BC171733 mRNA. Translation: AAI71733.1 .
CCDSi CCDS8069.1. [P30044-1 ]
CCDS8070.1. [P30044-3 ]
CCDS8071.1. [P30044-4 ]
RefSeqi NP_036226.1. NM_012094.4.
NP_857634.1. NM_181651.2.
NP_857635.1. NM_181652.2.
UniGenei Hs.502823.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1H4O X-ray 1.95 A/B/C/D/E/F/G/H 54-214 [» ]
1HD2 X-ray 1.50 A 54-214 [» ]
1OC3 X-ray 2.00 A/B/C 54-214 [» ]
1URM X-ray 1.70 A 54-214 [» ]
2VL2 X-ray 1.92 A/B/C 54-214 [» ]
2VL3 X-ray 1.83 A/B/C 54-214 [» ]
2VL9 X-ray 2.70 A/B/C/D 54-214 [» ]
3MNG X-ray 1.45 A 54-214 [» ]
4K7I X-ray 2.25 A/B/C 54-214 [» ]
4K7N X-ray 2.30 A/B/C 54-214 [» ]
4K7O X-ray 1.98 A/B/C 54-214 [» ]
4MMM X-ray 1.47 A/C/E/G 54-214 [» ]
ProteinModelPortali P30044.
SMRi P30044. Positions 54-214.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117352. 35 interactions.
IntActi P30044. 5 interactions.
MINTi MINT-5002532.
STRINGi 9606.ENSP00000265462.

Chemistry

DrugBanki DB00995. Auranofin.

Protein family/group databases

PeroxiBasei 4448. HsPrxV.

PTM databases

PhosphoSitei P30044.

Polymorphism databases

DMDMi 317373539.

2D gel databases

OGPi P30044.
REPRODUCTION-2DPAGE IPI00759663.
SWISS-2DPAGE P30044.
UCD-2DPAGE P30044.

Proteomic databases

MaxQBi P30044.
PaxDbi P30044.
PRIDEi P30044.

Protocols and materials databases

DNASUi 25824.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000265462 ; ENSP00000265462 ; ENSG00000126432 . [P30044-1 ]
ENST00000347941 ; ENSP00000335363 ; ENSG00000126432 . [P30044-4 ]
ENST00000352435 ; ENSP00000335334 ; ENSG00000126432 . [P30044-3 ]
GeneIDi 25824.
KEGGi hsa:25824.
UCSCi uc001nzu.3. human. [P30044-1 ]

Organism-specific databases

CTDi 25824.
GeneCardsi GC11P064085.
HGNCi HGNC:9355. PRDX5.
HPAi CAB008661.
HPA037915.
MIMi 606583. gene.
neXtProti NX_P30044.
PharmGKBi PA33726.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0678.
GeneTreei ENSGT00390000018173.
HOGENOMi HOG000255884.
HOVERGENi HBG053675.
InParanoidi P30044.
KOi K11187.
OMAi MSAWGKQ.
OrthoDBi EOG77Q4XX.
PhylomeDBi P30044.
TreeFami TF105182.

Enzyme and pathway databases

Reactomei REACT_172715. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

ChiTaRSi PRDX5. human.
EvolutionaryTracei P30044.
GeneWikii PRDX5.
GenomeRNAii 25824.
NextBioi 35462441.
PROi P30044.
SOURCEi Search...

Gene expression databases

Bgeei P30044.
CleanExi HS_PRDX5.
ExpressionAtlasi P30044. baseline and differential.
Genevestigatori P30044.

Family and domain databases

Gene3Di 3.40.30.10. 1 hit.
InterProi IPR013740. Redoxin.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF08534. Redoxin. 1 hit.
[Graphical view ]
SUPFAMi SSF52833. SSF52833. 1 hit.
PROSITEi PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A novel human DNA-binding protein with sequence similarity to a subfamily of redox proteins which is able to repress RNA-polymerase-III-driven transcription of the Alu-family retroposons in vitro."
    Kropotov A., Sedova V., Ivanov V., Sazeeva N., Tomilin A., Krutilina R., Oei S.L., Griesenbeck J., Buchlow G., Tomilin N.
    Eur. J. Biochem. 260:336-346(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MITOCHONDRIAL), VARIANT CYS-33.
  2. "Characterization of human and murine PMP20 peroxisomal proteins that exhibit antioxidant activity in vitro."
    Yamashita H., Avraham S., Jiang S., London R., Van Veldhoven P.P., Subramani S., Rogers R.A., Avraham H.
    J. Biol. Chem. 274:29897-29904(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CYTOPLASMIC+PEROXISOMAL), CHARACTERIZATION.
  3. "Cloning and characterization of AOEB166, a novel mammalian antioxidant enzyme of the peroxiredoxin family."
    Knoops B., Clippe A., Bogard C., Arsalane K., Wattiez R., Hermans C., Duconseille E., Falmagne P., Bernard A.
    J. Biol. Chem. 274:30451-30458(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MITOCHONDRIAL), PROTEIN SEQUENCE OF 54-90, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, CHARACTERIZATION, VARIANT CYS-33.
    Tissue: Lung.
  4. "Mouse peroxiredoxin V is a thioredoxin peroxidase that inhibits p53-induced apoptosis."
    Zhou Y., Kok K.H., Chun A.C.S., Wong C.M., Wu H.W., Lin M.C.M., Fung P.C.W., Kung H.-F., Jin D.-Y.
    Biochem. Biophys. Res. Commun. 268:921-927(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CYTOPLASMIC+PEROXISOMAL), VARIANT CYS-33.
  5. "Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate."
    Seo M.S., Kang S.W., Kim K., Baines I.C., Lee T.H., Rhee S.G.
    J. Biol. Chem. 275:20346-20354(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS, CHARACTERIZATION.
  6. "A new type of human thiol peroxidase (Human TPx type VI)."
    Kim I.H., Jeong W.
    Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CYTOPLASMIC+PEROXISOMAL).
  7. Zhang W., Li N., Wan T., Cao X.
    Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MITOCHONDRIAL), VARIANT CYS-33.
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CYTOPLASMIC+PEROXISOMAL).
    Tissue: Adrenal gland.
  9. "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 (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM MITOCHONDRIAL), VARIANT CYS-33.
  10. NIEHS SNPs program
    Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT CYS-33.
  11. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  12. "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] (ISOFORMS MITOCHONDRIAL; 3 AND 4), VARIANT CYS-33.
    Tissue: Brain and Medulla oblongata.
  13. "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 54-63.
    Tissue: Liver.
  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-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Crystal structure of human peroxiredoxin 5, a novel type of mammalian peroxiredoxin at 1.5-A resolution."
    Declercq J.-P., Evrard C., Clippe A., Stricht D.V., Bernard A., Knoops B.
    J. Mol. Biol. 311:751-759(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
  17. "The crystal structures of oxidized forms of human peroxiredoxin 5 with an intramolecular disulfide bond confirm the proposed enzymatic mechanism for atypical 2-Cys peroxiredoxins."
    Smeets A., Marchand C., Linard D., Knoops B., Declercq J.P.
    Arch. Biochem. Biophys. 477:98-104(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 54-214, DISULFIDE BOND.
  18. "Structural evidence that peroxiredoxin catalytic power is based on transition-state stabilization."
    Hall A., Parsonage D., Poole L.B., Karplus P.A.
    J. Mol. Biol. 402:194-209(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 54-214 IN COMPLEX WITH DITHIOTHREITOL, ACTIVE SITE.
  19. Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-157.

Entry informationi

Entry nameiPRDX5_HUMAN
AccessioniPrimary (citable) accession number: P30044
Secondary accession number(s): A6NC19
, A6NG06, B7ZLJ4, B7ZVW3, Q14CK0, Q6IAF2, Q9UBU5, Q9UJU4, Q9UKX4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 11, 2011
Last modified: November 26, 2014
This is version 160 of the entry and version 4 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

Keywords - Technical termi

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

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3