ID PRDX2_HUMAN Reviewed; 198 AA.
AC P32119; A8K0C0; P31945; P32118; P35701; Q6FHG4; Q92763; Q9UC23;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 5.
DT 27-MAR-2024, entry version 246.
DE RecName: Full=Peroxiredoxin-2;
DE EC=1.11.1.24 {ECO:0000269|PubMed:8554614, ECO:0000269|PubMed:9497357};
DE AltName: Full=Natural killer cell-enhancing factor B;
DE Short=NKEF-B;
DE AltName: Full=PRP;
DE AltName: Full=Thiol-specific antioxidant protein;
DE Short=TSA;
DE AltName: Full=Thioredoxin peroxidase 1;
DE AltName: Full=Thioredoxin-dependent peroxide reductase 1;
DE AltName: Full=Thioredoxin-dependent peroxiredoxin 2 {ECO:0000305};
GN Name=PRDX2; Synonyms=NKEFB, TDPX1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=8144038; DOI=10.1016/0378-1119(94)90558-4;
RA Lim Y.-S., Cha M.-K., Kim H.-K., Kim I.-H.;
RT "The thiol-specific antioxidant protein from human brain: gene cloning and
RT analysis of conserved cysteine regions.";
RL Gene 140:279-284(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8026862; DOI=10.1007/bf00188176;
RA Shau H., Butterfield L.H., Chiu R., Kim A.;
RT "Cloning and sequence analysis of candidate human natural killer-enhancing
RT factor genes.";
RL Immunogenetics 40:129-134(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLU-153.
RG NIEHS SNPs program;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hypothalamus, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 8-26; 67-135 AND 140-150, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [10]
RP PROTEIN SEQUENCE OF 8-24, AND CATALYTIC ACTIVITY.
RC TISSUE=Erythrocyte;
RX PubMed=8554614; DOI=10.1006/bbrc.1995.2856;
RA Cha M.-K., Kim I.-H.;
RT "Thioredoxin-linked peroxidase from human red blood cell: evidence for the
RT existence of thioredoxin and thioredoxin reductase in human red blood
RT cell.";
RL Biochem. Biophys. Res. Commun. 217:900-907(1995).
RN [11]
RP PROTEIN SEQUENCE OF 17-26; 93-103 AND 120-129.
RC TISSUE=Erythrocyte;
RX PubMed=8313871; DOI=10.1002/elps.11501401183;
RA Golaz O., Hughes G.J., Frutiger S., Paquet N., Bairoch A., Pasquali C.,
RA Sanchez J.-C., Tissot J.-D., Appel R.D., Walzer C., Balant L.,
RA Hochstrasser D.F.;
RT "Plasma and red blood cell protein maps: update 1993.";
RL Electrophoresis 14:1223-1231(1993).
RN [12]
RP PROTEIN SEQUENCE OF 17-26; 111-135 AND 140-157.
RC TISSUE=Colon carcinoma;
RX PubMed=9150948; DOI=10.1002/elps.1150180344;
RA Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.;
RT "A two-dimensional gel database of human colon carcinoma proteins.";
RL Electrophoresis 18:605-613(1997).
RN [13]
RP PROTEIN SEQUENCE OF 17-25; 140-150 AND 163-185.
RC TISSUE=Keratinocyte;
RX PubMed=1286667; DOI=10.1002/elps.11501301199;
RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
RA Vandekerckhove J.;
RT "Microsequences of 145 proteins recorded in the two-dimensional gel protein
RT database of normal human epidermal keratinocytes.";
RL Electrophoresis 13:960-969(1992).
RN [14]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 35-198 (ISOFORM 1).
RA Oberbaeumer I.;
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [15]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=9497357; DOI=10.1074/jbc.273.11.6297;
RA Kang S.W., Chae H.Z., Seo M.S., Kim K., Baines I.C., Rhee S.G.;
RT "Mammalian peroxiredoxin isoforms can reduce hydrogen peroxide generated in
RT response to growth factors and tumor necrosis factor-alpha.";
RL J. Biol. Chem. 273:6297-6302(1998).
RN [16]
RP OVEROXIDATION AT CYS-51.
RX PubMed=11904290; DOI=10.1074/jbc.m106585200;
RA Rabilloud T., Heller M., Gasnier F., Luche S., Rey C., Aebersold R.,
RA Benahmed M., Louisot P., Lunardi J.;
RT "Proteomics analysis of cellular response to oxidative stress. Evidence for
RT in vivo overoxidation of peroxiredoxins at their active site.";
RL J. Biol. Chem. 277:19396-19401(2002).
RN [17]
RP RETROREDUCTION OF CYS-51, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12853451; DOI=10.1074/jbc.m305161200;
RA Chevallet M., Wagner E., Luche S., van Dorsselaer A., Leize-Wagner E.,
RA Rabilloud T.;
RT "Regeneration of peroxiredoxins during recovery after oxidative stress:
RT only some overoxidized peroxiredoxins can be reduced during recovery after
RT oxidative stress.";
RL J. Biol. Chem. 278:37146-37153(2003).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [19]
RP INTERACTION WITH TIPIN.
RX PubMed=17141802; DOI=10.1016/j.jmb.2006.10.097;
RA Gotter A.L., Suppa C., Emanuel B.S.;
RT "Mammalian TIMELESS and Tipin are evolutionarily conserved replication
RT fork-associated factors.";
RL J. Mol. Biol. 366:36-52(2007).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22905912; DOI=10.1021/pr300539b;
RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P.,
RA Mariman E.C., Renes J.;
RT "Resveratrol-induced changes of the human adipocyte secretion profile.";
RL J. Proteome Res. 11:4733-4743(2012).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112 AND THR-182, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), AND SUBUNIT.
RX PubMed=10873855; DOI=10.1016/s0969-2126(00)00147-7;
RA Schroeder E., Littlechild J.A., Lebedev A.A., Errington N., Vagin A.A.,
RA Isupov M.N.;
RT "Crystal structure of decameric 2-Cys peroxiredoxin from human erythrocytes
RT at 1.7 A resolution.";
RL Structure 8:605-615(2000).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 46-198, AND DISULFIDE BONDS.
RX PubMed=27892488; DOI=10.1038/srep37610;
RA Kamariah N., Sek M.F., Eisenhaber B., Eisenhaber F., Grueber G.;
RT "Transition steps in peroxide reduction and a molecular switch for peroxide
RT robustness of prokaryotic peroxiredoxins.";
RL Sci. Rep. 6:37610-37610(2016).
CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC respectively. Plays a role in cell protection against oxidative stress
CC by detoxifying peroxides and as sensor of hydrogen peroxide-mediated
CC signaling events. Might participate in the signaling cascades of growth
CC factors and tumor necrosis factor-alpha by regulating the intracellular
CC concentrations of H(2)O(2). {ECO:0000269|PubMed:9497357}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-
CC disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC ChEBI:CHEBI:50058; EC=1.11.1.24;
CC Evidence={ECO:0000269|PubMed:8554614, ECO:0000269|PubMed:9497357};
CC -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation (PubMed:27892488).
CC 5 homodimers assemble to form a ring-like decamer (PubMed:27892488).
CC Interacts with TIPIN (PubMed:17141802). {ECO:0000269|PubMed:17141802,
CC ECO:0000269|PubMed:27892488}.
CC -!- INTERACTION:
CC P32119; P40763: STAT3; NbExp=4; IntAct=EBI-1266300, EBI-518675;
CC P32119; P10599: TXN; NbExp=2; IntAct=EBI-1266300, EBI-594644;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9497357}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P32119-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P32119-2; Sequence=VSP_042924;
CC -!- PTM: The enzyme can be inactivated by further oxidation of the cysteine
CC sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H) instead of its
CC condensation to a disulfide bond. It can be reactivated by forming a
CC transient disulfide bond with sulfiredoxin SRXN1, which reduces the
CC cysteine sulfinic acid in an ATP- and Mg-dependent manner.
CC {ECO:0000250|UniProtKB:Q06830, ECO:0000269|PubMed:11904290,
CC ECO:0000269|PubMed:12853451}.
CC -!- MISCELLANEOUS: The active site is a conserved redox-active cysteine
CC residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic
CC attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to
CC cysteine sulfenic acid (C(P)-SOH), which then reacts with another
CC cysteine residue, the resolving cysteine (C(R)), to form a disulfide
CC bridge. The disulfide is subsequently reduced by an appropriate
CC electron donor to complete the catalytic cycle. In this typical 2-Cys
CC peroxiredoxin, C(R) is provided by the other dimeric subunit to form an
CC intersubunit disulfide. The disulfide is subsequently reduced by
CC thioredoxin. {ECO:0000305|PubMed:27892488}.
CC -!- MISCELLANEOUS: [Isoform 2]: Due to intron retention. May be produced at
CC very low levels due to a premature stop codon in the mRNA, leading to
CC nonsense-mediated mRNA decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/prdx2/";
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DR EMBL; Z22548; CAA80269.1; -; mRNA.
DR EMBL; L19185; AAA50465.1; -; mRNA.
DR EMBL; CR450356; CAG29352.1; -; mRNA.
DR EMBL; CR541789; CAG46588.1; -; mRNA.
DR EMBL; AK289485; BAF82174.1; -; mRNA.
DR EMBL; DQ231563; ABB02182.1; -; Genomic_DNA.
DR EMBL; AC018761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471106; EAW84311.1; -; Genomic_DNA.
DR EMBL; BC000452; AAH00452.1; -; mRNA.
DR EMBL; BC003022; AAH03022.1; -; mRNA.
DR EMBL; BC039428; AAH39428.1; -; mRNA.
DR EMBL; X82321; CAA57764.1; -; mRNA.
DR CCDS; CCDS12281.1; -. [P32119-1]
DR PIR; I68897; I68897.
DR RefSeq; NP_005800.3; NM_005809.5. [P32119-1]
DR PDB; 1QMV; X-ray; 1.70 A; A/B/C/D/E/F/G/H/I/J=2-198.
DR PDB; 5B8A; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J=46-198.
DR PDB; 5B8B; X-ray; 3.10 A; A/B/C/D/E/F/G/H/I/J=46-163, A/B/C/D/E/F/G/H/I/J=80-198.
DR PDB; 5IJT; X-ray; 2.15 A; A/B/C/D/E/F/G/H/I/J=1-198.
DR PDB; 7KIZ; X-ray; 1.70 A; A/B/C/D/E/F/G/H/I/J=2-198.
DR PDB; 7KJ0; X-ray; 2.29 A; A/B/C/D/E/F/G/H/I/J=2-198.
DR PDB; 7KJ1; X-ray; 2.15 A; A/B/C/D/E/F/G/H/I/J=2-198.
DR PDBsum; 1QMV; -.
DR PDBsum; 5B8A; -.
DR PDBsum; 5B8B; -.
DR PDBsum; 5IJT; -.
DR PDBsum; 7KIZ; -.
DR PDBsum; 7KJ0; -.
DR PDBsum; 7KJ1; -.
DR AlphaFoldDB; P32119; -.
DR SMR; P32119; -.
DR BioGRID; 112860; 293.
DR DIP; DIP-39882N; -.
DR IntAct; P32119; 87.
DR MINT; P32119; -.
DR STRING; 9606.ENSP00000301522; -.
DR ChEMBL; CHEMBL4295744; -.
DR DrugBank; DB02153; 3-sulfino-L-alanine.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB04048; N-Carbamoyl-Alanine.
DR PeroxiBase; 4475; Hs2CysPrx02.
DR GlyCosmos; P32119; 2 sites, 1 glycan.
DR GlyGen; P32119; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P32119; -.
DR PhosphoSitePlus; P32119; -.
DR SwissPalm; P32119; -.
DR BioMuta; PRDX2; -.
DR DMDM; 2507169; -.
DR DOSAC-COBS-2DPAGE; P32119; -.
DR OGP; P32119; -.
DR REPRODUCTION-2DPAGE; IPI00027350; -.
DR SWISS-2DPAGE; P32119; -.
DR UCD-2DPAGE; P32119; -.
DR CPTAC; CPTAC-1445; -.
DR CPTAC; CPTAC-1446; -.
DR CPTAC; CPTAC-1447; -.
DR CPTAC; CPTAC-710; -.
DR CPTAC; CPTAC-727; -.
DR CPTAC; non-CPTAC-1143; -.
DR CPTAC; non-CPTAC-1144; -.
DR EPD; P32119; -.
DR jPOST; P32119; -.
DR MassIVE; P32119; -.
DR MaxQB; P32119; -.
DR PaxDb; 9606-ENSP00000301522; -.
DR PeptideAtlas; P32119; -.
DR PRIDE; P32119; -.
DR ProteomicsDB; 54836; -. [P32119-1]
DR ProteomicsDB; 54837; -. [P32119-2]
DR TopDownProteomics; P32119-1; -. [P32119-1]
DR ABCD; P32119; 13 sequenced antibodies.
DR Antibodypedia; 3283; 643 antibodies from 45 providers.
DR CPTC; P32119; 2 antibodies.
DR DNASU; 7001; -.
DR Ensembl; ENST00000301522.3; ENSP00000301522.2; ENSG00000167815.12. [P32119-1]
DR GeneID; 7001; -.
DR KEGG; hsa:7001; -.
DR MANE-Select; ENST00000301522.3; ENSP00000301522.2; NM_005809.6; NP_005800.3.
DR AGR; HGNC:9353; -.
DR CTD; 7001; -.
DR DisGeNET; 7001; -.
DR GeneCards; PRDX2; -.
DR HGNC; HGNC:9353; PRDX2.
DR HPA; ENSG00000167815; Low tissue specificity.
DR MIM; 600538; gene.
DR neXtProt; NX_P32119; -.
DR OpenTargets; ENSG00000167815; -.
DR PharmGKB; PA33723; -.
DR VEuPathDB; HostDB:ENSG00000167815; -.
DR eggNOG; KOG0852; Eukaryota.
DR GeneTree; ENSGT00940000155828; -.
DR HOGENOM; CLU_042529_21_0_1; -.
DR InParanoid; P32119; -.
DR OMA; VCTKELC; -.
DR OrthoDB; 47465at2759; -.
DR PhylomeDB; P32119; -.
DR TreeFam; TF105181; -.
DR BRENDA; 1.11.1.24; 2681.
DR PathwayCommons; P32119; -.
DR Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-HSA-8862803; Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models.
DR SignaLink; P32119; -.
DR BioGRID-ORCS; 7001; 66 hits in 1161 CRISPR screens.
DR ChiTaRS; PRDX2; human.
DR EvolutionaryTrace; P32119; -.
DR GeneWiki; Peroxiredoxin_2; -.
DR GenomeRNAi; 7001; -.
DR Pharos; P32119; Tbio.
DR PRO; PR:P32119; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P32119; Protein.
DR Bgee; ENSG00000167815; Expressed in lateral nuclear group of thalamus and 217 other cell types or tissues.
DR ExpressionAtlas; P32119; baseline and differential.
DR Genevisible; P32119; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016209; F:antioxidant activity; IDA:UniProtKB.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IDA:UniProtKB.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IDA:BHF-UCL.
DR GO; GO:0002357; P:defense response to tumor cell; IMP:ARUK-UCL.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR GO; GO:0045321; P:leukocyte activation; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR GO; GO:0031665; P:negative regulation of lipopolysaccharide-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0045581; P:negative regulation of T cell differentiation; IEA:Ensembl.
DR GO; GO:0030194; P:positive regulation of blood coagulation; IEA:Ensembl.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR GO; GO:0042981; P:regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0010310; P:regulation of hydrogen peroxide metabolic process; IEA:Ensembl.
DR GO; GO:0019430; P:removal of superoxide radicals; IDA:BHF-UCL.
DR GO; GO:0002536; P:respiratory burst involved in inflammatory response; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0006979; P:response to oxidative stress; IMP:UniProtKB.
DR GO; GO:0043029; P:T cell homeostasis; IEA:Ensembl.
DR GO; GO:0042098; P:T cell proliferation; IEA:Ensembl.
DR GO; GO:0048538; P:thymus development; IEA:Ensembl.
DR CDD; cd03015; PRX_Typ2cys; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10681:SF161; PEROXIREDOXIN-2; 1.
DR PANTHER; PTHR10681; THIOREDOXIN PEROXIDASE; 1.
DR Pfam; PF10417; 1-cysPrx_C; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR PIRSF; PIRSF000239; AHPC; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Antioxidant; Cytoplasm;
KW Direct protein sequencing; Disulfide bond; Oxidoreductase; Peroxidase;
KW Phosphoprotein; Redox-active center; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..198
FT /note="Peroxiredoxin-2"
FT /id="PRO_0000135080"
FT DOMAIN 6..164
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 51
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000305|PubMed:11904290"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 182
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT DISULFID 51
FT /note="Interchain (with C-172); in linked form"
FT /evidence="ECO:0000269|PubMed:27892488,
FT ECO:0007744|PDB:5B8A"
FT DISULFID 172
FT /note="Interchain (with C-51); in linked form"
FT /evidence="ECO:0000269|PubMed:27892488,
FT ECO:0007744|PDB:5B8A"
FT VAR_SEQ 87..198
FT /note="INTPRKEGGLGPLNIPLLADVTRRLSEDYGVLKTDEGIAYRGLFIIDGKGVL
FT RQITVNDLPVGRSVDEALRLVQAFQYTDEHGEVCPAGWKPGSDTIKPNVDDSKEYFSKH
FT N -> YEQGPKREVAAKLTPSGPSSVASWPLLNLWNLRFPIVKIMETLPPKSLRMMTVI
FT SI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042924"
FT VARIANT 153
FT /note="D -> E (in dbSNP:rs34012472)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_025051"
FT CONFLICT 59..66
FT /note="SNRAEDFR -> TTVKRTSA (in Ref. 1; CAA80269)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="T -> N (in Ref. 2; AAA50465)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="A -> G (in Ref. 2; AAA50465)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="T -> N (in Ref. 1; CAA80269)"
FT /evidence="ECO:0000305"
FT CONFLICT 126..127
FT /note="YR -> TT (in Ref. 11; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="G -> A (in Ref. 1; CAA80269)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="S -> R (in Ref. 1; CAA80269)"
FT /evidence="ECO:0000305"
FT STRAND 16..21
FT /evidence="ECO:0007829|PDB:1QMV"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:1QMV"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:1QMV"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:1QMV"
FT HELIX 50..60
FT /evidence="ECO:0007829|PDB:1QMV"
FT HELIX 62..66
FT /evidence="ECO:0007829|PDB:1QMV"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:1QMV"
FT STRAND 70..78
FT /evidence="ECO:0007829|PDB:1QMV"
FT HELIX 80..87
FT /evidence="ECO:0007829|PDB:1QMV"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:1QMV"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:1QMV"
FT HELIX 110..114
FT /evidence="ECO:0007829|PDB:1QMV"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:1QMV"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:5IJT"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:1QMV"
FT STRAND 136..144
FT /evidence="ECO:0007829|PDB:1QMV"
FT HELIX 152..168
FT /evidence="ECO:0007829|PDB:1QMV"
FT HELIX 187..197
FT /evidence="ECO:0007829|PDB:1QMV"
SQ SEQUENCE 198 AA; 21892 MW; 1AC781D908B32B46 CRC64;
MASGNARIGK PAPDFKATAV VDGAFKEVKL SDYKGKYVVL FFYPLDFTFV CPTEIIAFSN
RAEDFRKLGC EVLGVSVDSQ FTHLAWINTP RKEGGLGPLN IPLLADVTRR LSEDYGVLKT
DEGIAYRGLF IIDGKGVLRQ ITVNDLPVGR SVDEALRLVQ AFQYTDEHGE VCPAGWKPGS
DTIKPNVDDS KEYFSKHN
//
