P32119 (PRDX2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	198 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Redox-active center
Molecular function	Antioxidant Oxidoreductase Peroxidase
PTM	Acetylation Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	hydrogen peroxide catabolic process Traceable author statement PubMed 18606987. Source: BHF-UCL negative regulation of apoptotic process Traceable author statement PubMed 16130169. Source: UniProtKB negative regulation of neuron apoptotic process Inferred from electronic annotation. Source: Compara removal of superoxide radicals Inferred from direct assay PubMed 20978343. Source: BHF-UCL
Cellular_component	cytoplasm Traceable author statement PubMed 16130169. Source: UniProtKB cytosol Inferred from electronic annotation. Source: Compara
Molecular_function	thioredoxin peroxidase activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 198

197

Peroxiredoxin-2

PRO_0000135080

Regions

Domain

6 – 164

159

Thioredoxin

Sites

Active site

51

1

Cysteine sulfenic acid (-SOH) intermediate

Amino acid modifications

Modified residue

2

1

N-acetylalanine By similarity

Disulfide bond

51

Interchain (with C-172); in linked form By similarity

Disulfide bond

172

Interchain (with C-51); in linked form By similarity

Natural variations

Alternative sequence

87 – 198

112

INTPR…FSKHN → YEQGPKREVAAKLTPSGPSS VASWPLLNLWNLRFPIVKIM ETLPPKSLRMMTVISI in isoform 2.

VSP_042924

Natural variant

153

1

D → E. Ref.5
Corresponds to variant rs34012472 [ dbSNP | Ensembl ].

VAR_025051

Experimental info

Sequence conflict

59 – 66

8

SNRAEDFR → TTVKRTSA in CAA80269. Ref.1

Sequence conflict

82

1

T → N in AAA50465. Ref.2

Sequence conflict

105

1

A → G in AAA50465. Ref.2

Sequence conflict

120

1

T → N in CAA80269. Ref.1

Sequence conflict

126 – 127

2

YR → TT AA sequence Ref.11

Sequence conflict

175

1

G → A in CAA80269. Ref.1

Sequence conflict

180

1

S → R in CAA80269. Ref.1

Secondary structure

1

.

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198

Helix Strand Turn

Details...

Beta strand

16 – 21

6

Beta strand

24 – 29

6

Helix

30 – 33

4

Beta strand

36 – 42

7

Helix

50 – 60

11

Helix

62 – 66

5

Turn

67 – 69

3

Beta strand

70 – 78

9

Helix

80 – 87

8

Helix

91 – 93

3

Beta strand

103 – 105

3

Helix

110 – 114

5

Turn

120 – 122

3

Beta strand

127 – 132

6

Beta strand

136 – 144

9

Helix

152 – 168

17

Helix

187 – 197

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 5. Checksum: 1AC781D908B32B46	FASTA	198	21,892
	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
	Isoform 2 [UniParc]. Checksum: C1FE1157EED6EC5E	FASTA	142	15,819
	10 20 30 40 50 60 MASGNARIGK PAPDFKATAV VDGAFKEVKL SDYKGKYVVL FFYPLDFTFV CPTEIIAFSN 70 80 90 100 110 120 RAEDFRKLGC EVLGVSVDSQ FTHLAWYEQG PKREVAAKLT PSGPSSVASW PLLNLWNLRF 130 140 PIVKIMETLP PKSLRMMTVI SI

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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, 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, 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]	"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].
[19]	"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

NIEHS-SNPs

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.

IPI

IPI00027350.
IPI00375401.

PIR

I68897.

RefSeq

NP_005800.3. NM_005809.4.
NP_859428.1. NM_181738.1.

UniGene

Hs.432121.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QMV	X-ray	1.70	A/B/C/D/E/F/G/H/I/J	2-198	[»]

ProteinModelPortal

P32119.

ModBase

Search...

Protein-protein interaction databases

IntAct

P32119. 26 interactions.

MINT

MINT-3012817.

STRING

9606.ENSP00000301522.

Protein family/group databases

PeroxiBase

4475. Hs2CysPrx02.

PTM databases

PhosphoSite

P32119.

Polymorphism databases

DMDM

2507169.

2D gel databases

DOSAC-COBS-2DPAGE

P32119.

OGP

P32119.

REPRODUCTION-2DPAGE

IPI00027350.

SWISS-2DPAGE

P32119.

UCD-2DPAGE

P32119.

Proteomic databases

PaxDb

P32119.

PRIDE

P32119.

Protocols and materials databases

DNASU

7001.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000301522; ENSP00000301522; ENSG00000167815.
ENST00000435703; ENSP00000408905; ENSG00000167815.

GeneID

7001.

KEGG

hsa:7001.

UCSC

uc002mvd.3. human.

Organism-specific databases

CTD

7001.

GeneCards

GC19M012907.

HGNC

HGNC:9353. PRDX2.

HPA

CAB008713.

MIM

600538. gene.

neXtProt

NX_P32119.

PharmGKB

PA33723.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0450.

HOGENOM

HOG000022343.

HOVERGEN

HBG000286.

InParanoid

P32119.

KO

K03386.

OMA

INDGGVG.

OrthoDB

EOG4V6ZHJ.

PhylomeDB

P32119.

Gene expression databases

ArrayExpress

P32119.

Bgee

P32119.

CleanEx

HS_PRDX2.

Genevestigator

P32119.

GermOnline

ENSG00000167815. Homo sapiens.

Family and domain databases

Gene3D

3.40.30.10. 1 hit.

InterPro

IPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]

Pfam

PF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]

PIRSF

PIRSF000239. AHPC. 1 hit.

SUPFAM

SSF52833. Thiordxn-like_fd. 1 hit.

PROSITE

PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

PRDX2. human.

EvolutionaryTrace

P32119.

GenomeRNAi

7001.

NextBio

27342.

SOURCE

Search...

Entry information

Entry name

PRDX2_HUMAN

Accession

Primary (citable) accession number: P32119
Secondary accession number(s): A8K0C0 , P31945, P32118, P35701, Q6FHG4, Q92763, Q9UC23

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 156 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.