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P32119 (PRDX2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 168. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peroxiredoxin-2

EC=1.11.1.15
Alternative name(s):
Natural killer cell-enhancing factor B
Short name=NKEF-B
PRP
Thiol-specific antioxidant protein
Short name=TSA
Thioredoxin peroxidase 1
Thioredoxin-dependent peroxide reductase 1
Gene names
Name:PRDX2
Synonyms:NKEFB, TDPX1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length198 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system. It is not able to receive electrons from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2.

Catalytic activity

2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH. Ref.10

Subunit structure

Homodimer; disulfide-linked, upon oxidation. May be found as a toroid-shaped decamer composed of 5 dimers, depending on pH and calcium concentration. Interacts with TIPIN. Ref.17

Subcellular location

Cytoplasm.

Miscellaneous

The active site is the redox-active Cys-51 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-172-SH of the other subunit to form an intermolecular disulfide with a concomitant homodimer formation. The enzyme may be subsequently regenerated by reduction of the disulfide by thioredoxin.

Inactivated upon oxidative stress by overoxidation of Cys-51 to Cys-SO2H and Cys-SO3H. Cys-SO2H is retroreduced to Cys-SOH after removal of H2O2, while Cys-SO3H may be irreversibly oxidized.

Sequence similarities

Belongs to the AhpC/TSA family.

Contains 1 thioredoxin domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P32119-1)

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.
Isoform 2 (identifier: P32119-2)

The sequence of this isoform differs from the canonical sequence as follows:
     87-198: INTPRKEGGL...DSKEYFSKHN → YEQGPKREVA...SLRMMTVISI
Note: No experimental confirmation available. Due to intron retention. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.18
Chain2 – 198197Peroxiredoxin-2
PRO_0000135080

Regions

Domain6 – 164159Thioredoxin

Sites

Active site511Cysteine sulfenic acid (-SOH) intermediate

Amino acid modifications

Modified residue21N-acetylalanine Ref.18
Disulfide bond51Interchain (with C-172); in linked form By similarity
Disulfide bond172Interchain (with C-51); in linked form By similarity

Natural variations

Alternative sequence87 – 198112INTPR…FSKHN → YEQGPKREVAAKLTPSGPSS VASWPLLNLWNLRFPIVKIM ETLPPKSLRMMTVISI in isoform 2.
VSP_042924
Natural variant1531D → E. Ref.5
Corresponds to variant rs34012472 [ dbSNP | Ensembl ].
VAR_025051

Experimental info

Sequence conflict59 – 668SNRAEDFR → TTVKRTSA in CAA80269. Ref.1
Sequence conflict821T → N in AAA50465. Ref.2
Sequence conflict1051A → G in AAA50465. Ref.2
Sequence conflict1201T → N in CAA80269. Ref.1
Sequence conflict126 – 1272YR → TT AA sequence Ref.11
Sequence conflict1751G → A in CAA80269. Ref.1
Sequence conflict1801S → R in CAA80269. Ref.1

Secondary structure

................................ 198
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 5.
Checksum: 1AC781D908B32B46

FASTA19821,892
        10         20         30         40         50         60 
MASGNARIGK PAPDFKATAV VDGAFKEVKL SDYKGKYVVL FFYPLDFTFV CPTEIIAFSN 

        70         80         90        100        110        120 
RAEDFRKLGC EVLGVSVDSQ FTHLAWINTP RKEGGLGPLN IPLLADVTRR LSEDYGVLKT 

       130        140        150        160        170        180 
DEGIAYRGLF IIDGKGVLRQ ITVNDLPVGR SVDEALRLVQ AFQYTDEHGE VCPAGWKPGS 

       190 
DTIKPNVDDS KEYFSKHN 

« Hide

Isoform 2 [UniParc].

Checksum: C1FE1157EED6EC5E
Show »

FASTA14215,819

References

« Hide 'large scale' references
[1]"The thiol-specific antioxidant protein from human brain: gene cloning and analysis of conserved cysteine regions."
Lim Y.-S., Cha M.-K., Kim H.-K., Kim I.-H.
Gene 140:279-284(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"Cloning and sequence analysis of candidate human natural killer-enhancing factor genes."
Shau H., Butterfield L.H., Chiu R., Kim A.
Immunogenetics 40:129-134(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Cerebellum.
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]NIEHS SNPs program
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLU-153.
[6]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Hypothalamus and Lung.
[9]Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 8-26; 67-135 AND 140-150, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[10]"Thioredoxin-linked peroxidase from human red blood cell: evidence for the existence of thioredoxin and thioredoxin reductase in human red blood cell."
Cha M.-K., Kim I.-H.
Biochem. Biophys. Res. Commun. 217:900-907(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 8-24, CATALYTIC ACTIVITY.
Tissue: Erythrocyte.
[11]"Plasma and red blood cell protein maps: update 1993."
Golaz O., Hughes G.J., Frutiger S., Paquet N., Bairoch A., Pasquali C., Sanchez J.-C., Tissot J.-D., Appel R.D., Walzer C., Balant L., Hochstrasser D.F.
Electrophoresis 14:1223-1231(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 17-26; 93-103 AND 120-129.
Tissue: Erythrocyte.
[12]"A two-dimensional gel database of human colon carcinoma proteins."
Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.
Electrophoresis 18:605-613(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 17-26; 111-135 AND 140-157.
Tissue: Colon carcinoma.
[13]"Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 17-25; 140-150 AND 163-185.
Tissue: Keratinocyte.
[14]Oberbaeumer I.
Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 35-198 (ISOFORM 1).
[15]"Proteomics analysis of cellular response to oxidative stress. Evidence for in vivo overoxidation of peroxiredoxins at their active site."
Rabilloud T., Heller M., Gasnier F., Luche S., Rey C., Aebersold R., Benahmed M., Louisot P., Lunardi J.
J. Biol. Chem. 277:19396-19401(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: OVEROXIDATION AT CYS-51.
[16]"Regeneration of peroxiredoxins during recovery after oxidative stress: only some overoxidized peroxiredoxins can be reduced during recovery after oxidative stress."
Chevallet M., Wagner E., Luche S., van Dorsselaer A., Leize-Wagner E., Rabilloud T.
J. Biol. Chem. 278:37146-37153(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: RETROREDUCTION OF CYS-51, IDENTIFICATION BY MASS SPECTROMETRY.
[17]"Mammalian TIMELESS and Tipin are evolutionarily conserved replication fork-associated factors."
Gotter A.L., Suppa C., Emanuel B.S.
J. Mol. Biol. 366:36-52(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TIPIN.
[18]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[19]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Crystal structure of decameric 2-Cys peroxiredoxin from human erythrocytes at 1.7 A resolution."
Schroeder E., Littlechild J.A., Lebedev A.A., Errington N., Vagin A.A., Isupov M.N.
Structure 8:605-615(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-198.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z22548 mRNA. Translation: CAA80269.1.
L19185 mRNA. Translation: AAA50465.1.
CR450356 mRNA. Translation: CAG29352.1.
CR541789 mRNA. Translation: CAG46588.1.
AK289485 mRNA. Translation: BAF82174.1.
DQ231563 Genomic DNA. Translation: ABB02182.1.
AC018761 Genomic DNA. No translation available.
CH471106 Genomic DNA. Translation: EAW84311.1.
BC000452 mRNA. Translation: AAH00452.1.
BC003022 mRNA. Translation: AAH03022.1.
BC039428 mRNA. Translation: AAH39428.1.
X82321 mRNA. Translation: CAA57764.1.
CCDSCCDS12281.1. [P32119-1]
PIRI68897.
RefSeqNP_005800.3. NM_005809.5. [P32119-1]
UniGeneHs.432121.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QMVX-ray1.70A/B/C/D/E/F/G/H/I/J2-198[»]
ProteinModelPortalP32119.
SMRP32119. Positions 3-198.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112860. 58 interactions.
IntActP32119. 27 interactions.
MINTMINT-3012817.
STRING9606.ENSP00000301522.

Protein family/group databases

PeroxiBase4475. Hs2CysPrx02.

PTM databases

PhosphoSiteP32119.

Polymorphism databases

DMDM2507169.

2D gel databases

DOSAC-COBS-2DPAGEP32119.
OGPP32119.
REPRODUCTION-2DPAGEIPI00027350.
SWISS-2DPAGEP32119.
UCD-2DPAGEP32119.

Proteomic databases

MaxQBP32119.
PaxDbP32119.
PRIDEP32119.

Protocols and materials databases

DNASU7001.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000301522; ENSP00000301522; ENSG00000167815. [P32119-1]
ENST00000435703; ENSP00000408905; ENSG00000167815. [P32119-2]
GeneID7001.
KEGGhsa:7001.
UCSCuc002mvd.4. human. [P32119-1]

Organism-specific databases

CTD7001.
GeneCardsGC19M012907.
HGNCHGNC:9353. PRDX2.
HPACAB008713.
MIM600538. gene.
neXtProtNX_P32119.
PharmGKBPA33723.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0450.
HOGENOMHOG000022343.
HOVERGENHBG000286.
InParanoidP32119.
KOK03386.
OMAEGVIQHA.
PhylomeDBP32119.
TreeFamTF105181.

Enzyme and pathway databases

ReactomeREACT_120956. Cellular responses to stress.

Gene expression databases

ArrayExpressP32119.
BgeeP32119.
CleanExHS_PRDX2.
GenevestigatorP32119.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
PIRSFPIRSF000239. AHPC. 1 hit.
SUPFAMSSF52833. SSF52833. 1 hit.
PROSITEPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPRDX2. human.
EvolutionaryTraceP32119.
GeneWikiPeroxiredoxin_2.
GenomeRNAi7001.
NextBio27342.
PROP32119.
SOURCESearch...

Entry information

Entry namePRDX2_HUMAN
AccessionPrimary (citable) accession number: P32119
Secondary accession number(s): A8K0C0 expand/collapse secondary AC list , P31945, P32118, P35701, Q6FHG4, Q92763, Q9UC23
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 168 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM