PRDX2

Summary

PRDX2 (peroxiredoxin 2, HGNC:9353) is a protein-coding gene on chromosome 19p13.13, encoding Peroxiredoxin-2 (P32119). Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively.

This gene encodes a member of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. The encoded protein plays an antioxidant protective role in cells, and it may contribute to the antiviral activity of CD8(+) T-cells. The crystal structure of this protein has been resolved to 2.7 angstroms. This protein prevents hemolytic anemia from oxidative stress by stabilizing hemoglobin, thus making this gene a therapeutic target for patients with hemolytic anemia. This protein may have a proliferative effect and play a role in cancer development or progression. Related pseudogenes have been identified on chromosomes 5, 6, 10 and 13.

Source: NCBI Gene 7001 — RefSeq curated summary.

At a glance

• GWAS associations: 1
• Clinical variants (ClinVar): 20 total
• Druggable target: yes
• MANE Select transcript: NM_005809

Identifiers

Gene identifiers

Field	Value
HGNC ID	HGNC:9353
Approved symbol	PRDX2
Name	peroxiredoxin 2
Location	19p13.13
Locus type	gene with protein product
Status	Approved
Aliases	PRP, NKEFB, TSA, PRXII, PRX2, MGC4104
Ensembl gene	ENSG00000167815
Ensembl biotype	protein_coding
OMIM	600538
Entrez	7001

Gene structure

Transcript identifiers

Ensembl transcripts: 10 — 6 protein_coding, 4 retained_intron

ENST00000301522, ENST00000334482, ENST00000466174, ENST00000477555, ENST00000478908, ENST00000498785, ENST00000866178, ENST00000866180, ENST00000866181, ENST00000955165

RefSeq mRNA: 1 — MANE Select: NM_005809 NM_005809

CCDS: CCDS12281

Canonical transcript exons

ENST00000301522 — 6 exons

Exon	Start	End
ENSE00001117400	12800177	12800299
ENSE00001718527	12799859	12799989
ENSE00001899489	12801740	12801800
ENSE00003533436	12801159	12801270
ENSE00003574969	12800916	12801069
ENSE00003644940	12796823	12797166

Expression profiles

Bgee: expression breadth ubiquitous, 304 present calls, max score 99.86.

FANTOM5 (CAGE): breadth ubiquitous, TPM avg 192.8225 / max 5871.7591, expressed in 1800 samples.

FANTOM5 promoters (6 alternative TSS)

Promoter ID	TPM avg	Samples expressed
179391	123.5253	1789
179393	29.9508	1738
179392	29.1224	1726
179394	9.1503	1630
179390	0.8358	402
179389	0.2380	100

Top tissues by expression

304 total, by Bgee expression score (0-100, higher = more expressed):

Tissue	Anatomy ID	Expression score	Quality
lateral nuclear group of thalamus	UBERON:0002736	99.86	gold quality
substantia nigra pars compacta	UBERON:0001965	99.84	gold quality
trabecular bone tissue	UBERON:0002483	99.84	gold quality
substantia nigra pars reticulata	UBERON:0001966	99.81	gold quality
lateral globus pallidus	UBERON:0002476	99.71	gold quality
pons	UBERON:0000988	99.70	gold quality
heart right ventricle	UBERON:0002080	99.65	gold quality
apex of heart	UBERON:0002098	99.64	gold quality
right adrenal gland cortex	UBERON:0035827	99.64	gold quality
right adrenal gland	UBERON:0001233	99.63	gold quality
left adrenal gland	UBERON:0001234	99.59	gold quality
adrenal cortex	UBERON:0001235	99.58	gold quality
left adrenal gland cortex	UBERON:0035825	99.57	gold quality
superior vestibular nucleus	UBERON:0007227	99.54	gold quality
embryo	UBERON:0000922	99.49	gold quality
adrenal gland	UBERON:0002369	99.48	gold quality
prefrontal cortex	UBERON:0000451	99.47	gold quality
cardiac ventricle	UBERON:0002082	99.47	gold quality
heart left ventricle	UBERON:0002084	99.47	gold quality
ganglionic eminence	UBERON:0004023	99.45	gold quality
right frontal lobe	UBERON:0002810	99.44	gold quality
right atrium auricular region	UBERON:0006631	99.44	gold quality
Brodmann (1909) area 10	UBERON:0013541	99.43	gold quality
penis	UBERON:0000989	99.42	gold quality
mammalian vulva	UBERON:0000997	99.42	gold quality
cerebellar vermis	UBERON:0004720	99.41	gold quality
cardiac atrium	UBERON:0002081	99.40	gold quality
right hemisphere of cerebellum	UBERON:0014890	99.40	gold quality
pituitary gland	UBERON:0000007	99.39	gold quality
cerebellar cortex	UBERON:0002129	99.37	gold quality

Single-cell (SCXA)

Detected in 26 experiment(s), a significant marker in 17.

Experiment	Marker?	Max mean expression
E-MTAB-10042	yes	7131.29
E-MTAB-7407	yes	6350.25
E-GEOD-130473	yes	5140.73
E-CURD-112	yes	4116.43
E-HCAD-24	yes	3629.86
E-HCAD-4	yes	3590.30
E-CURD-122	yes	3522.79
E-MTAB-8205	yes	2106.04
E-CURD-6	yes	2088.35
E-GEOD-81383	yes	501.34
E-HCAD-6	yes	55.81
E-HCAD-10	yes	49.70
E-MTAB-9221	yes	16.15
E-HCAD-9	yes	9.72
E-MTAB-9067	yes	8.05

Regulation

Is transcription factor: no

Upstream regulators (CollecTRI, top): ARNT, EPAS1, HIF1A

miRNA regulators (miRDB)

11 targeting PRDX2, top 30 by miRDB confidence (max_score; target_count = how many genes the miRNA targets in total — lower means more specific):

miRNA	Max score	Avg score	miRNA target_count
HSA-MIR-6783-3P	99.89	67.92	2059
HSA-MIR-6756-5P	99.82	67.97	2466
HSA-MIR-6766-5P	99.68	67.70	2325
HSA-MIR-3612	99.45	66.02	1333
HSA-MIR-650	99.45	65.77	1309
HSA-MIR-4318	99.38	66.94	1505
HSA-MIR-3922-3P	99.25	64.96	1136
HSA-MIR-3176	99.25	64.35	954
HSA-MIR-4443	98.02	66.25	1928
HSA-MIR-6515-5P	97.08	65.48	1219
HSA-MIR-7847-3P	96.63	64.58	952

Literature-anchored findings (GeneRIF, showing 40)

• Protein levels of Prx-I and Prx-II were significantly increased in Alzheimer Disease and Down Syndrome. (PMID:11771746)
• Proteomics analysis of cellular response to oxidative stress. Evidence for in vivo overoxidation of peroxiredoxins at their active site (PMID:11904290)
• 2-Cys Prxs act in a mutually nonredundant and sometimes stress-specific fashion to protect human cells from oxidant injury. The substantial resistance of human cells to hydroperoxides may result in part from the additive action of multiple Prxs (PMID:12080185)
• Peroxiredoxin 2 levels are significantly increased in the frontal cortex of patients with Down syndrome, Alzheimer and Pick’s disease and provides evidence for existence of compensatory response in increased cell loss. (PMID:12650976)
• decreased expression of PRDX2 may contribute to the altered redox state in Down syndrome at levels comparable to that of the increased expression of SOD1 (PMID:12943237)
• Prx II can be used as a novel marker of vascular tumors and preferential expression of Prx II is found in benign vascular tumors. (PMID:12963914)
• results show that sestrins, a family of proteins whose expression is modulated by p53, are required for regeneration of peroxiredoxins containing Cys-SO(2)H (PMID:15105503)
• Prx I and Prx II are induced at the early and late stage of differentiation of normal human epidermal keratinocytes. (PMID:15864612)
• loss of IDPc and Prx-II during tumor development may involve in tumor progression and metastasis (PMID:15936593)
• PDX2 was involved in malignant transformation of human bronchial epithelial cell induced by crystalline nickel sulfide. (PMID:16188094)
• in the erythrocyte Prx2 is extremely efficient at scavenging H(2)O(2) noncatalytically (PMID:17105810)
• We propose a model in which Prxs function as peroxide dosimeters in subcellular processes that involve redox cycling, with hyperoxidation controlling structural transitions that alert cells of perturbations in peroxide homeostasis. (PMID:17145963)
• peroxiredoxin 2 has a tertiary structure that facilitates reaction of the active site thiol with hydrogen peroxide while restricting its reactivity with other thiol reagents (PMID:17329258)
• Human Prdx1 and Prdx2 possess unique functions and regulatory mechanisms and that Cys(83) bestows a distinctive identity to Prdx1. (PMID:17519234)
• PrxII might play an important role in hepatocarcinogenesis and might be used as a molecular target for HCC prevention and treatment. (PMID:17524271)
• observation of increased SNO-Prx2 in human Parkinson’s disease (PD) brains, and S-nitrosylation of Prx2 inhibited both its enzymatic activity and protective function from oxidative stress (PMID:18003920)
• Peroxiredoxin II (PRXII) exclusively expressed in bronchiolitis obliterans syndrome. (PMID:18022079)
• Significantly decreased expression of Prx-2, -3, and -5 in FED may suggest an alteration in the ability of endothelial cells to withstand oxidant-induced damage and may be closely related to the pathogenesis of this disease. (PMID:18378575)
• study reports identification of Prx2 in the erythrocyte membrane from hereditary spherocytosis patients; presence of Prx2 in erythrocyte membranes was linked to higher levels of oxidative stress, as reflected by increased membrane bound hemoglobin (PMID:18387321)
• 2-cysteine peroxiredoxins from Homo sapiens, Arabidopsis thaliana, and Pisum sativum as well as a carboxy-terminally truncated variant were subjected to isothermal titration calorimetry analysis. (PMID:18553980)
• Silencing of PRDX2 caused decreased rates of Hep3B cell growth and clone formation, increased rates of cell apoptosis, and increased the levels of endogenous ROS and MDA. (PMID:18578994)
• analysis of a protein thiosulfinate intermediate in the reduction of cysteine sulfinic acid in peroxiredoxin by human sulfiredoxin (PMID:18593714)
• The results suggest that Prx II oxidation does not relate to the pathogenesis of IPF/UIP (PMID:18606608)
• peroxiredoxin (Prx) I and Prx II are specific targets of HDAC6 (PMID:18606987)
• inhibiting peroxiredoxin II sensitizes glioma cells to oxidative stress (PMID:18718523)
• Prx2 is a key antioxidant enzyme for the erythrocyte and reveal red blood cells as active oxidant scrubbers in the bloodstream. (PMID:19061854)
• These results indicate that both nipradilol and timolol possess a novel mechanism of action and function as potent protective agents against oxidative stress. (PMID:19151395)
• Using shotgun mass spectrometry, we found this protein differentially expressed in the dorsolateral prefrontal cortex from patients with schizophrenia. (PMID:19165527)
• Prx II is more susceptible than Prx I to hyperoxidation and that the majority of the hyperoxidized Prx II formation is reversible. However, the hyperoxidized Prx I showed much less reversibility (PMID:19286652)
• Conclude that Prx II and III are upregulated in response to the development of cervical cancer. (PMID:19424615)
• Deglutathionylation of 2-Cys Prx is specifically catalyzed by Srx. (PMID:19561357)
• Resutls show that three of five autoantibodies, FKBP52, PPIA, and PRDX2, showed significantly increased reactivity in primary breast cancer and CIS compared with healthy controls. (PMID:19584157)
• P. falciparum imports the human redox-active protein peroxiredoxin 2 (hPrx-2, hTPx1) into its cytosol. (PMID:19666612)
• Exposure to Chloramines and hypochlorous acid inflammatory oxidants will result in Prx2 oxidation and could compromise the erythrocyte’s ability to resist damaging oxidative insult. (PMID:19716412)
• could act as an autoantigen of a streptococcal-induced autoimmune response and represents a target of the exaggerated T cell response in psoriasis. (PMID:20363977)
• Data suggest that anti-Prx2 autoantibodies would be a useful marker for systemic vasculitis and would be involved in the inflammatory processes of systemic vasculitis. (PMID:20646000)
• PRDX2 was up-regulated in women older than 38 years, and its expression in cumulus cells was associated with embryo quality (PMID:20721618)
• Addition of an uncharged derivative of leucine hydroperoxide to intact erythrocytes caused Prx2 oxidation with no concomitant loss in glutathione. (PMID:20840079)
• proteomic profiling used to identify the target proteins of miR-122a in hepatocellular carcinoma; PRDXII was identified to be the new target of miR-122a (PMID:20859956)
• High PRDX2 expression in the cytoplasm is associated with uterine cervix carcinogenesis. (PMID:21119665)

Cross-species orthologs

5 orthologs

Organism	Symbol	Gene ID
mus_musculus	Prdx2	ENSMUSG00000005161
rattus_norvegicus	Prdx2	ENSRNOG00000003520
drosophila_melanogaster	Prx6c	FBGN0033518
drosophila_melanogaster	Prx6b	FBGN0033520
drosophila_melanogaster	CG12896	FBGN0033521

Paralogs (4): PRDX1 (ENSG00000117450), PRDX6 (ENSG00000117592), PRDX4 (ENSG00000123131), PRDX3 (ENSG00000165672)

Protein

Protein identifiers

Peroxiredoxin-2 — P32119 (reviewed: P32119)

Alternative names: Natural killer cell-enhancing factor B, PRP, Thiol-specific antioxidant protein, Thioredoxin peroxidase 1, Thioredoxin-dependent peroxide reductase 1, Thioredoxin-dependent peroxiredoxin 2

All UniProt accessions (3): A6NIW5, P32119, V9HW12

UniProt curated annotations — full annotation on UniProt →

Function. Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2).

Subunit / interactions. Homodimer; disulfide-linked, upon oxidation. 5 homodimers assemble to form a ring-like decamer. Interacts with TIPIN.

Subcellular location. Cytoplasm.

Post-translational modifications. The enzyme can be inactivated by further oxidation of the cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H) instead of its condensation to a disulfide bond. It can be reactivated by forming a transient disulfide bond with sulfiredoxin SRXN1, which reduces the cysteine sulfinic acid in an ATP- and Mg-dependent manner. Acetylation increases resistance to transition to high molecular-mass complexes. Deacetylated by HDAC6 which decreases reducing activity.

Miscellaneous. The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this typical 2-Cys peroxiredoxin, C(R) is provided by the other dimeric subunit to form an intersubunit disulfide. The disulfide is subsequently reduced by thioredoxin. 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.

Similarity. Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.

Isoforms (2)

UniProt ID	Names	Canonical?
P32119-1	1	yes
P32119-2	2

RefSeq proteins (1): NP_005800* (*=MANE)

Domains & families (InterPro)

ID	Name	Type
IPR000866	AhpC/TSA	Domain
IPR013766	Thioredoxin_domain	Domain
IPR019479	Peroxiredoxin_C	Domain
IPR024706	Peroxiredoxin_AhpC-typ	Family
IPR036249	Thioredoxin-like_sf	Homologous_superfamily
IPR050217	Peroxiredoxin	Family

Pfam: PF00578, PF10417

Enzyme classification (BRENDA):

• EC 1.11.1.24 — thioredoxin-dependent peroxiredoxin (BRENDA: 72 organisms, 110 substrates, 31 inhibitors, 72 Km, 50 kcat entries)

Substrate kinetics (BRENDA)

13 substrates with measured Km, best-characterized 13. Km ranges are aggregated across organisms/conditions.

Substrate	Km (mM)	Measurements
H2O2	0.0004–11.7	23
CUMENE HYDROPEROXIDE	0.0066–0.191	8
THIOREDOXIN	0.001–0.0794	7
TERT-BUTYL HYDROPEROXIDE	—	5
THIOREDOXIN A	0.0009–0.0122	5
THIOREDOXIN B	0.0022–0.0208	5
T-BUTYL HYDROPEROXIDE	0.072–0.193	4
THIOREDOXIN Q	0.0007–0.0028	4
REDUCED THIOREDOXIN	0.0024–0.004	2
REDUCED THIOREDOXIN A	0.0079–0.0087	2
ETHYL HYDROPEROXIDE	0.0045	1
LINOLEIC ACID HYDROPEROXIDE	0.117	1
TRYPAREDOXIN 2	0.0319	1

Catalyzed reactions (Rhea), 1 shown:

• a hydroperoxide + [thioredoxin]-dithiol = an alcohol + [thioredoxin]-disulfide + H2O (RHEA:62620)

UniProt features (38 total): strand 8, helix 8, sequence conflict 7, modified residue 4, turn 2, disulfide bond 2, initiator methionine 1, chain 1, splice variant 1, sequence variant 1, mutagenesis site 1, domain 1, active site 1

Structure

Experimental structures (PDB)

7 structures.

PDB	Method	Resolution (Å)
1QMV	X-RAY DIFFRACTION	1.7
7KIZ	X-RAY DIFFRACTION	1.7
5IJT	X-RAY DIFFRACTION	2.15
7KJ1	X-RAY DIFFRACTION	2.15
7KJ0	X-RAY DIFFRACTION	2.29
5B8A	X-RAY DIFFRACTION	2.7
5B8B	X-RAY DIFFRACTION	3.1

Predicted structure (AlphaFold)

Model	pLDDT	Fraction very-high
AF-P32119-F1	97.87	0.99

Functional residue map

Curated UniProt residues grouped by drug-discovery relevance — catalytic, ligand-binding, modification, and mutation-validated positions. Source: UniProtKB sequence features.

Catalytic / active sites (1): 51 (cysteine sulfenic acid (-soh) intermediate)

Post-translational modifications (4): 2, 112, 182, 196

Disulfide bonds (2): 51, 172

Mutagenesis-validated functional residues (1):

Position	Phenotype
196	abolishes acetylation.

Function

Pathways and Gene Ontology

Reactome pathways

3 pathways

ID	Pathway
R-HSA-3299685	Detoxification of Reactive Oxygen Species
R-HSA-5628897	TP53 Regulates Metabolic Genes
R-HSA-8862803	Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer’s disease models

MSigDB gene sets: 361 (showing top): GOBP_REGULATION_OF_CELL_ACTIVATION, GOBP_NEGATIVE_REGULATION_OF_CELL_DEVELOPMENT, GNF2_PRDX2, GOBP_REGULATION_OF_WOUND_HEALING, GOBP_INFLAMMATORY_RESPONSE, GOBP_CELLULAR_RESPONSE_TO_LIPID, GOBP_REGULATION_OF_COAGULATION, JAEGER_METASTASIS_DN, CHIARETTI_T_ALL_REFRACTORY_TO_THERAPY, ENK_UV_RESPONSE_KERATINOCYTE_UP, GOBP_CELLULAR_RESPONSE_TO_BIOTIC_STIMULUS, GOBP_HYDROGEN_PEROXIDE_CATABOLIC_PROCESS, STARK_PREFRONTAL_CORTEX_22Q11_DELETION_DN, GOBP_POSITIVE_REGULATION_OF_COAGULATION, GOBP_POSITIVE_REGULATION_OF_MAPK_CASCADE

GO Biological Process (24): defense response to tumor cell (GO:0002357), respiratory burst involved in inflammatory response (GO:0002536), response to oxidative stress (GO:0006979), regulation of hydrogen peroxide metabolic process (GO:0010310), removal of superoxide radicals (GO:0019430), positive regulation of blood coagulation (GO:0030194), negative regulation of lipopolysaccharide-mediated signaling pathway (GO:0031665), response to lipopolysaccharide (GO:0032496), cellular response to oxidative stress (GO:0034599), T cell proliferation (GO:0042098), hydrogen peroxide catabolic process (GO:0042744), regulation of apoptotic process (GO:0042981), T cell homeostasis (GO:0043029), negative regulation of apoptotic process (GO:0043066), positive regulation of MAPK cascade (GO:0043410), leukocyte activation (GO:0045321), cell redox homeostasis (GO:0045454), negative regulation of T cell differentiation (GO:0045581), thymus development (GO:0048538), extrinsic apoptotic signaling pathway (GO:0097191), negative regulation of extrinsic apoptotic signaling pathway in absence of ligand (GO:2001240), hydrogen peroxide metabolic process (GO:0042743), cellular oxidant detoxification (GO:0098869), negative regulation of extrinsic apoptotic signaling pathway (GO:2001237)

GO Molecular Function (7): thioredoxin peroxidase activity (GO:0008379), antioxidant activity (GO:0016209), peroxidase activity (GO:0004601), protein binding (GO:0005515), oxidoreductase activity (GO:0016491), peroxiredoxin activity (GO:0051920), thioredoxin-dependent peroxiredoxin activity (GO:0140824)

GO Cellular Component (3): cytoplasm (GO:0005737), cytosol (GO:0005829), extracellular exosome (GO:0070062)

Reactome top-level categories

Rollup of top-3 pathways:

Category	Pathways
Cellular response to chemical stress	1
Transcriptional Regulation by TP53	1
Neurodegenerative Diseases	1

GO top-level categories

Rollup of top GO terms by namespace:

Category	Terms
hydrogen peroxide metabolic process	2
cellular oxidant detoxification	2
apoptotic process	2
cellular anatomical structure	2
response to tumor cell	1
defense response	1
production of molecular mediator involved in inflammatory response	1
respiratory burst involved in defense response	1
inflammatory response	1
response to stress	1
regulation of reactive oxygen species metabolic process	1
superoxide metabolic process	1
cellular response to superoxide	1
blood coagulation	1
regulation of blood coagulation	1
positive regulation of coagulation	1
positive regulation of wound healing	1
positive regulation of hemostasis	1
negative regulation of response to biotic stimulus	1
negative regulation of signal transduction	1
lipopolysaccharide-mediated signaling pathway	1
regulation of lipopolysaccharide-mediated signaling pathway	1
negative regulation of response to external stimulus	1
response to molecule of bacterial origin	1
response to lipid	1
response to oxygen-containing compound	1
response to oxidative stress	1
cellular response to chemical stress	1
T cell activation	1
lymphocyte proliferation	1
catabolic process	1
regulation of programmed cell death	1
lymphocyte homeostasis	1
regulation of apoptotic process	1
negative regulation of programmed cell death	1
MAPK cascade	1
regulation of MAPK cascade	1
positive regulation of intracellular signal transduction	1
cell activation	1
immune system process	1

Protein interactions and networks

STRING

0 interactions, top by confidence (×1000):

IntAct

168 interactions, top by confidence:

A	B	Type	Score
PPP2R1A	STRN	psi-mi:“MI:0914”(association)	0.880
PPP2R1B	STRN	psi-mi:“MI:0914”(association)	0.730
CCT2	TXNDC9	psi-mi:“MI:0914”(association)	0.730
CFTR	ESYT2	psi-mi:“MI:0914”(association)	0.710
CFTR	ESYT2	psi-mi:“MI:2364”(proximity)	0.710
PDCL3	PEX7	psi-mi:“MI:0914”(association)	0.640
PRDX2	TXN	psi-mi:“MI:0914”(association)	0.560
TXN	PRDX2	psi-mi:“MI:0915”(physical association)	0.560
PRDX2	PRDX3	psi-mi:“MI:0914”(association)	0.510
PRDX2	STAT3	psi-mi:“MI:0915”(physical association)	0.500
CFTR	PLEKHG3	psi-mi:“MI:0914”(association)	0.480
CFTR	CNOT1	psi-mi:“MI:0914”(association)	0.480
DDX21	MED19	psi-mi:“MI:2364”(proximity)	0.480
PRDX2	BAD	psi-mi:“MI:0915”(physical association)	0.440
BAD	PRDX2	psi-mi:“MI:0403”(colocalization)	0.440

BioGRID (397): PRDX2 (Affinity Capture-MS), ANXA2 (Co-fractionation), DUT (Co-fractionation), MSH6 (Co-fractionation), PCBP1 (Co-fractionation), PDCD6IP (Co-fractionation), PRDX2 (Co-fractionation), PRDX2 (Co-fractionation), PRDX2 (Co-fractionation), PRDX2 (Co-fractionation), PRDX2 (Co-fractionation), PRDX2 (Co-fractionation), PRDX2 (Co-fractionation), PRDX2 (Co-fractionation), PRDX2 (Co-fractionation)

ESM2 similar proteins: A0A0K3AUJ9, A0A2Z5VKM8, K0J4Q8, O04005, O74887, P0A0B5, P0A0B6, P0A0B7, P0CB50, P0CU34, P21762, P23161, P32119, P34760, P35700, P35704, P51272, P52574, P56876, P80239, P80602, P91883, P99074, Q04120, Q06830, Q17172, Q1XDL4, Q26695, Q2FJN4, Q2PFZ3, Q2YVK2, Q55624, Q5E947, Q5HIR5, Q5HRY1, Q5RC63, Q61171, Q63716, Q6B4U9, Q6DV14

Diamond homologs: A0A0K3AUJ9, A0A2Z5VKM8, A0R1V9, A2BJD9, A3DKL1, A5IIX7, A8A9P0, K0J4Q8, O08807, O24364, O34564, O67024, O74887, P0A0B5, P0A0B6, P0A0B7, P0A251, P0A252, P0AE08, P0AE09, P0AE10, P0AE11, P0CB50, P0CU34, P19476, P20108, P21762, P23161, P26830, P30048, P32119, P34760, P35700, P35704, P35705, P48822, P49537, P51272, P52552, P56876

SIGNOR signaling

2 interactions.

A	Effect	B	Mechanism
LCK	“down-regulates activity”	PRDX2	phosphorylation
ABL1	“down-regulates activity”	PRDX2	phosphorylation

Enriched among interaction partners

Reactome pathways and GO biological processes over-represented among this gene’s 189 IntAct physical interaction partners (hypergeometric vs the genome-wide background, BH-FDR, gene-set size 15–500, ranked by fold). A functional readout of the neighbourhood — distinct from this gene’s own memberships above, and biased toward well-studied / hub proteins, so read it as themes rather than proof.

Reactome pathways:

Pathway	Partners	Fold	FDR
Dengue Virus Genome Translation and Replication	5	11.3×	6e-03
Intrinsic Pathway for Apoptosis	5	10.5×	8e-03
Loss of Nlp from mitotic centrosomes	9	10.2×	6e-05
Loss of proteins required for interphase microtubule organization from the centrosome	9	10.2×	6e-05
AURKA Activation by TPX2	9	9.8×	6e-05
Regulation of PLK1 Activity at G2/M Transition	10	9.1×	6e-05
Centrosome maturation	5	9.1×	1e-02
Recruitment of mitotic centrosome proteins and complexes	9	8.7×	1e-04

GO biological processes:

GO term	Partners	Fold	FDR
centriole replication	6	26.0×	6e-05
extrinsic apoptotic signaling pathway via death domain receptors	6	14.2×	2e-03
intrinsic apoptotic signaling pathway	6	12.7×	3e-03
autophagosome maturation	6	12.5×	3e-03
mitophagy	6	11.3×	3e-03
microtubule cytoskeleton organization	8	5.7×	1e-02

Disease & clinical

Clinical variants and AI predictions

ClinVar

20 variants total. Per-class counts are floors (≥ shown; pagination cap):

Classification	Count (floor)
Pathogenic	0
Likely pathogenic	0
Uncertain significance	12
Likely benign	0
Benign	0

Top pathogenic / likely-pathogenic (0)

SpliceAI

880 predictions. Top by Δscore:

Variant	Effect	Δscore
19:12799854:CTCA:C	donor_loss	1.0000
19:12799855:TCAC:T	donor_loss	1.0000
19:12799856:CACCT:C	donor_loss	1.0000
19:12799857:A:C	donor_loss	1.0000
19:12800172:AGTAC:A	donor_loss	1.0000
19:12800173:GTA:G	donor_loss	1.0000
19:12800174:TA:T	donor_loss	1.0000
19:12800175:A:AT	donor_loss	1.0000
19:12800176:C:A	donor_loss	1.0000
19:12800195:T:C	donor_gain	1.0000
19:12800295:TGATC:T	acceptor_gain	1.0000
19:12800297:ATCCT:A	acceptor_loss	1.0000
19:12800298:TC:T	acceptor_gain	1.0000
19:12800298:TCC:T	acceptor_loss	1.0000
19:12800299:CC:C	acceptor_gain	1.0000
19:12800300:C:CC	acceptor_gain	1.0000
19:12800301:T:C	acceptor_loss	1.0000
19:12800306:G:GC	acceptor_gain	1.0000
19:12800913:TAC:T	donor_loss	1.0000
19:12800914:A:AC	donor_gain	1.0000
19:12800914:A:AT	donor_loss	1.0000
19:12800915:C:CC	donor_gain	1.0000
19:12800915:CCAAG:C	donor_gain	1.0000
19:12800941:C:CT	donor_gain	1.0000
19:12800942:C:CT	donor_gain	1.0000
19:12800952:C:CA	donor_gain	1.0000
19:12800961:T:TA	donor_gain	1.0000
19:12800961:TC:T	donor_gain	1.0000
19:12801065:CTTCC:C	acceptor_gain	1.0000
19:12801067:TCC:T	acceptor_gain	1.0000

AlphaMissense

1292 scored. Top likely-pathogenic:

Variant	Protein change	am_pathogenicity
19:12800177:C:A	R127M	1.000
19:12801026:A:C	F49L	0.999
19:12801026:A:T	F49L	0.999
19:12801028:A:G	F49L	0.999
19:12801032:G:C	F47L	0.999
19:12801032:G:T	F47L	0.999
19:12801034:A:G	F47L	0.999
19:12797152:A:G	W176R	0.998
19:12797152:A:T	W176R	0.998
19:12800177:C:G	R127T	0.998
19:12800917:A:G	W86R	0.998
19:12800917:A:T	W86R	0.998
19:12800930:G:C	F81L	0.998
19:12800930:G:T	F81L	0.998
19:12800932:A:G	F81L	0.998
19:12801012:T:A	E54V	0.998
19:12801022:A:G	C51R	0.998
19:12797150:C:A	W176C	0.997
19:12797150:C:G	W176C	0.997
19:12799894:A:T	V159D	0.997
19:12800926:G:C	H83D	0.997
19:12800941:C:G	D78H	0.997
19:12801020:G:C	C51W	0.997
19:12801021:C:T	C51Y	0.997
19:12801030:G:A	T48I	0.997
19:12797162:A:C	C172W	0.996
19:12799922:G:T	R150S	0.996
19:12799938:A:C	N144K	0.996
19:12799938:A:T	N144K	0.996
19:12799989:C:A	R127S	0.996

dbSNP variants (sampled 300 via entrez): RS1000287165 (19:12803528 C>T), RS1000657412 (19:12803148 A>T), RS1002013450 (19:12798628 G>A), RS1002440054 (19:12798604 G>A), RS1002574924 (19:12803197 G>A), RS1002931061 (19:12802882 G>A,C,T), RS1003011698 (19:12797402 C>A,G,T), RS1003101785 (19:12801451 A>C), RS1003134178 (19:12801784 C>G,T), RS1003951585 (19:12802099 C>G,T), RS1004451441 (19:12796955 C>A), RS1004747572 (19:12802331 G>A,T), RS1004765009 (19:12802371 GGC>G), RS1004780112 (19:12802740 G>A,C), RS1005209427 (19:12799191 G>A)

Disease associations

OMIM: gene MIM:600538 | disease phenotypes:

GenCC curated gene-disease

Mondo (0):

Orphanet (0):

HPO phenotypes

0 total (0 of 0 shown, HPO-id order):

GWAS associations

1 associations (top):

Study	Trait	p-value
GCST90002401_252	Platelet distribution width	3.000000e-21

EFO canonical traits (1, from GWAS)

EFO ID	Trait name
EFO:0007984	platelet component distribution width

Drugs & pharmacology

Drug and pharmacology data

Is drug target: yes

ChEMBL targets (1): CHEMBL4295744 (SINGLE PROTEIN)

PharmGKB: 1 entry (VIP=true, CPIC=false)

ChEMBL bioactivities

4 potent at pChembl≥5 of 4 total, top 4 by pChembl (potency: 10 = 0.1 nM, 6 = 1 µM).

pChembl	Type	Value	Unit	Molecule
5.16	Kd	6924	nM	CHEMBL5653589
5.16	ED50	6924	nM	CHEMBL5653589
5.10	Kd	7995	nM	CHEMBL3752910
5.10	ED50	7995	nM	CHEMBL3752910

PubChem BioAssay actives

2 with measured affinity, of 27 total; 2 most potent distinct compounds. Largely complementary to BindingDB; screening values are coarse (µM, 4 dp), so sub-nM hits tie at the floor.

Compound	Assay	Type	Value	Unit
4-methyl-3-[(2-methyl-6-pyridin-3-ylpyrazolo[3,4-d]pyrimidin-4-yl)amino]-N-[3-(trifluoromethyl)phenyl]benzamide	2149062: Binding affinity to human PRDX2 incubated for 45 mins by Kinobead based pull down assay	kd	6.9239	uM
4-methyl-3-[(1-methyl-6-pyridin-3-ylpyrazolo[3,4-d]pyrimidin-4-yl)amino]-N-[3-(trifluoromethyl)phenyl]benzamide	2149062: Binding affinity to human PRDX2 incubated for 45 mins by Kinobead based pull down assay	kd	7.9953	uM

CTD chemical–gene interactions

100 total (human), top 30 by PubMed support.

Chemical	Actions (top 5)	PubMed papers
bisphenol A	affects expression, decreases expression, decreases methylation, increases expression	4
sodium arsenite	increases expression	4
Hydrogen Peroxide	increases expression, increases oxidation, decreases response to substance	4
Valproic Acid	increases methylation, affects expression, decreases expression	4
Cisplatin	increases expression, affects response to substance, decreases response to substance	3
bisphenol F	increases expression, affects cotreatment, decreases expression	2
ochratoxin A	increases acetylation, increases expression	2
S-(1,2-dichlorovinyl)cysteine	decreases expression, decreases reaction, increases expression	2
Aerosols	decreases expression	2
Benzo(a)pyrene	increases expression, decreases reaction, decreases expression	2
Cocaine	affects expression, decreases expression	2
Doxorubicin	affects expression, decreases response to substance	2
Estradiol	decreases expression	2
Formaldehyde	decreases reaction, increases activity, increases expression, decreases expression	2
Lead	affects expression, decreases expression	2
Paraquat	increases expression, affects cotreatment	2
Quercetin	decreases reaction, affects cotreatment, increases expression, decreases expression	2
Tobacco Smoke Pollution	affects expression	2
Cyclosporine	decreases expression	2
tert-Butylhydroperoxide	decreases expression, increases expression	2
Nanotubes, Carbon	increases expression, affects expression	2
Particulate Matter	increases expression, increases response to substance, decreases expression	2
dicrotophos	increases expression	1
uranyl acetate	affects expression	1
cumene hydroperoxide	increases expression	1
deoxynivalenol	decreases expression	1
lead acetate	affects cotreatment, increases expression	1
pyrogallol 1,3-dimethyl ether	affects cotreatment, affects localization, increases expression	1
4-vinyl-1-cyclohexene dioxide	increases expression	1
arsenite	affects binding, increases reaction	1

ChEMBL screening assays

20 unique, capped per target: 20 binding

Representative assays (with source publication via chembl_document):

Assay ID	Type	Description	Source paper
CHEMBL4144685	Binding	Binding affinity to wild type recombinant human N-terminal 6His-tagged peroxiredoxin-2 expressed in Escherichia coli BL21 after 1 hr by LC-MS/MS analysis	ent-Jungermannenone C Triggers Reactive Oxygen Species-Dependent Cell Differentiation in Leukemia Cells. — J Nat Prod

Cellosaurus cell lines

6 cell lines: 5 cancer cell line, 1 transformed cell line

First 10 cell lines (id-ordered, not curated):

Cellosaurus	Name	Category	Sex
CVCL_B3ES	Abcam HEK293T PRDX2 KO	Transformed cell line	Female
CVCL_KT96	HeLa SilenciX PRDX2	Cancer cell line	Female
CVCL_TG44	HAP1 PRDX2 (-) 1	Cancer cell line	Male
CVCL_TG45	HAP1 PRDX2 (-) 2	Cancer cell line	Male
CVCL_TG46	HAP1 PRDX2 (-) 3	Cancer cell line	Male
CVCL_TG47	HAP1 PRDX2 (-) 4	Cancer cell line	Male

Clinical trials (associated diseases)

0 trials via MONDO — disease-level, not drug-specific.