RNASE7

Summary

RNASE7 (ribonuclease A family member 7, HGNC:19278) is a protein-coding gene on chromosome 14q11.2, encoding Ribonuclease 7 (Q9H1E1). Exhibits a potent RNase activity.

The protein encoded by this gene belongs to the pancreatic ribonuclease family, a subset of the ribonuclease A superfamily. The protein has broad-spectrum antimicrobial activity against bacteria and fungi.

Source: NCBI Gene 84659 — RefSeq curated summary.

At a glance

• MANE Select transcript: NM_032572

Identifiers

Gene identifiers

Field	Value
HGNC ID	HGNC:19278
Approved symbol	RNASE7
Name	ribonuclease A family member 7
Location	14q11.2
Locus type	gene with protein product
Status	Approved
Aliases	RAE1
Ensembl gene	ENSG00000165799
Ensembl biotype	protein_coding
OMIM	612484
Entrez	84659

Gene structure

Transcript identifiers

Ensembl transcripts: 2 — 1 protein_coding, 1 nonsense_mediated_decay

ENST00000298690, ENST00000481538

RefSeq mRNA: 1 — MANE Select: NM_032572 NM_032572

CCDS: CCDS41914

Canonical transcript exons

ENST00000298690 — 2 exons

Exon	Start	End
ENSE00001096676	21042953	21044233
ENSE00001309496	21042362	21042442

Expression profiles

Bgee: expression breadth ubiquitous, 107 present calls, max score 91.56.

FANTOM5 (CAGE): breadth tissue_specific, TPM avg 1.5228 / max 152.9456, expressed in 96 samples.

FANTOM5 promoters (4 alternative TSS)

Promoter ID	TPM avg	Samples expressed
138501	1.0283	87
138499	0.2514	65
138500	0.2022	59
138498	0.0408	26

Top tissues by expression

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

Tissue	Anatomy ID	Expression score	Quality
upper arm skin	UBERON:0004263	91.56	gold quality
amniotic fluid	UBERON:0000173	86.69	gold quality
gall bladder	UBERON:0002110	81.64	gold quality
skin of leg	UBERON:0001511	81.21	gold quality
oral cavity	UBERON:0000167	81.01	gold quality
lower esophagus mucosa	UBERON:0035834	80.89	gold quality
esophagus squamous epithelium	UBERON:0006920	78.42	gold quality
zone of skin	UBERON:0000014	76.78	gold quality
buccal mucosa cell	CL:0002336	75.76	gold quality
esophagus mucosa	UBERON:0002469	73.92	gold quality
skin of abdomen	UBERON:0001416	71.03	gold quality
tonsil	UBERON:0002372	65.72	gold quality
islet of Langerhans	UBERON:0000006	64.69	gold quality
minor salivary gland	UBERON:0001830	63.29	gold quality
vagina	UBERON:0000996	62.91	gold quality
penis	UBERON:0000989	62.87	gold quality
mouth mucosa	UBERON:0003729	62.75	gold quality
upper leg skin	UBERON:0004262	61.78	gold quality
saliva-secreting gland	UBERON:0001044	61.41	gold quality
pancreatic ductal cell	CL:0002079	60.22	silver quality
olfactory segment of nasal mucosa	UBERON:0005386	59.47	gold quality
primordial germ cell in gonad	CL:0000670 ∩ UBERON:0000991	57.99	gold quality
esophagus	UBERON:0001043	57.70	gold quality
right lobe of liver	UBERON:0001114	56.95	gold quality
tibialis anterior	UBERON:0001385	56.95	silver quality
rectum	UBERON:0001052	55.82	gold quality
pancreas	UBERON:0001264	55.10	gold quality
mammalian vulva	UBERON:0000997	54.95	silver quality
epithelial cell of pancreas	CL:0000083	54.68	gold quality
cardiac muscle of right atrium	UBERON:0003379	54.34	gold quality

Single-cell (SCXA)

Detected in 1 experiment(s), a significant marker in 0.

Experiment	Marker?	Max mean expression
E-ANND-3	no	2.29

Regulation

Is transcription factor: no

miRNA regulators (miRDB)

38 targeting RNASE7, 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-6758-5P	100.00	66.21	1470
HSA-MIR-6856-5P	100.00	65.47	1298
HSA-MIR-3065-5P	99.97	71.56	3281
HSA-MIR-4725-3P	99.96	69.53	2520
HSA-MIR-6780B-5P	99.96	69.60	2562
HSA-MIR-6772-5P	99.94	67.01	577
HSA-MIR-4760-3P	99.93	70.50	2385
HSA-MIR-4271	99.88	68.32	2244
HSA-MIR-4517	99.76	69.19	1867
HSA-MIR-4320	99.75	65.80	793
HSA-MIR-3059-5P	99.70	69.93	2491
HSA-MIR-1284	99.67	73.56	1353
HSA-MIR-3120-3P	99.54	70.28	2669
HSA-MIR-6505-3P	99.34	67.39	1071
HSA-MIR-4795-5P	99.11	66.90	876
HSA-MIR-4254	99.11	65.15	1315
HSA-MIR-670-3P	99.03	68.88	2404
HSA-MIR-3124-3P	98.87	68.95	2123
HSA-MIR-873-5P	98.84	66.90	1348
HSA-MIR-4451	98.82	68.17	1455
HSA-MIR-6501-3P	98.71	67.45	1480
HSA-MIR-6776-5P	98.54	67.43	1304
HSA-MIR-6873-5P	98.45	66.14	1417
HSA-MIR-6072	98.00	66.47	804
HSA-MIR-204-3P	97.80	66.84	1656
HSA-MIR-7111-3P	97.80	66.75	1467
HSA-MIR-4646-5P	97.70	66.84	1692
HSA-MIR-4637	97.69	68.14	632
HSA-MIR-8057	97.64	66.54	897
HSA-MIR-3157-5P	97.41	67.61	998

Literature-anchored findings (GeneRIF, showing 26)

• RNase 7 is an antimicrobial protein that plays an important role in the innate immune defense system of human epithelia. (PMID:12244054)
• proteases contribute indirectly to the defense function of the stratum corneum by releasing the RNase inhibitor mediated inhibition of RNase 5 and RNase 7. (PMID:19262607)
• Using phospholipid vesicles as membrane models, RNase 3 triggers first the vesicle aggregation, while RNase 7 induces leakage well before the aggregation step. (PMID:19366593)
• data indicate that RNase 7 contributes to the E. faecium-killing activity of skin extracts and suggest an important role for RNase 7 in the protection of human skin against E. faecium colonization (PMID:19641608)
• These findings suggest that antimicrobial peptides found at high baseline levels in healthy skin, such as RNase 7, confer protection against Staphylococcus aureus infection of the skin. (PMID:19919305)
• RNASE7 prevents staphylococcal skin infections (PMID:20668470)
• RNase 7 expression is increased in the urinary tract with infection and has antibacterial activity against uropathogens at micromolar concentrations. (PMID:23302724)
• a complex relationship between tear induction of miR-762, its modulation of innate defense genes, and P. aeruginosa internalization (PMID:23469087)
• Suggest that RNase 7 may function as antimicrobial peptide with a role in the differentiation and development of the primitive epidermis. (PMID:23545750)
• the influence of STAT3 on the IL-17A/IFN-gamma -mediated RNase 7 induction (PMID:23555696)
• Levels of psoriasin, RNase 7 and hBD-3 expression - assessed by immunohistochemistry - varied between different body localisations. (PMID:23614747)
• RNH1 bound to RNase 7 and suppressed its antimicrobial activity by blocking its ability to bind the cell wall of uropathogenic bacteria. (PMID:24107847)
• epidermal growth factor-dependent RNase 7 and human beta-defensin-3 expression upon infection with Trichophytum rubrum (PMID:24747887)
• This article provides an overview about the role of RNase 7 in cutaneous defense with focus on the molecular mechanism of the antimicrobial activity of RNase 7, the regulation of RNase 7 expression, and the role of RNase 7 in skin diseases. [review] (PMID:27089327)
• Insulin and PI3K/AKT signaling are essential for RNase 7 expression and increased infection risks in diabetic patients may be secondary to suppressed RNase 7 production. (PMID:27401534)
• Our results indicate that RNase 7 is an important factor released by keratinocytes to control the growth of P. aeruginosa on the skin surface. (PMID:27513608)
• RNase 7 has immunomodulatory functions on TH2 cells and decreases the production of TH2 cytokines in the skin. (PMID:28378334)
• RNase 7 may function as important effector molecule to control the growth of corynebacteria on human skin (PMID:29066761)
• RNase 7 exhibits potent immunomodulatory functions and supports the efficient recognition of microbial infections by human skin-infiltrating pDCs. (PMID:29157732)
• These data suggest that the induction of RNase 7 in response to Mycobacterium tuberculosis could have a role in anti-mycobacterial immunity. (PMID:29346642)
• RAE1 mediated ZEB1 expression promotes epithelial-mesenchymal transition in breast cancer. (PMID:30814639)
• RNase 7 has a role in kidney and bladder host defense against uropathogenic Escherichia coli (PMID:31239387)
• RNase 7 Promotes Sensing of Self-DNA by Human Keratinocytes and Activates an Antiviral Immune Response. (PMID:31978413)
• Involvement of RNase 7 in the malignant potential of oral squamous cell carcinoma cells. (PMID:32705284)
• Ribonuclease 7 polymorphism rs1263872 reduces antimicrobial activity and associates with pediatric urinary tract infections. (PMID:34779412)
• RNase 7 Inhibits Uropathogenic Escherichia coli-Induced Inflammation in Bladder Cells under a High-Glucose Environment by Regulating the JAK/STAT Signaling Pathway. (PMID:35563546)

Cross-species orthologs

0 orthologs

Paralogs (12): RNASE1 (ENSG00000129538), RNASE2 (ENSG00000169385), RNASE3 (ENSG00000169397), RNASE6 (ENSG00000169413), RNASE8 (ENSG00000173431), RNASE11 (ENSG00000173464), RNASE10 (ENSG00000182545), RNASE9 (ENSG00000188655), RNASE13 (ENSG00000206150), ANG (ENSG00000214274), RNASE12 (ENSG00000258436), RNASE4 (ENSG00000258818)

Protein

Protein identifiers

Ribonuclease 7 — Q9H1E1 (reviewed: Q9H1E1)

Alternative names: Skin-derived antimicrobial protein 2

All UniProt accessions (1): Q9H1E1

UniProt curated annotations — full annotation on UniProt →

Function. Exhibits a potent RNase activity. Has broad-spectrum antimicrobial activity against many pathogenic microorganisms including uropathogenic E.coli (UPEC), and remarkably potent activity (lethal dose of 90% < 30 nM) against a vancomycin resistant Enterococcus faecium. Causes loss of bacterial membrane integrity. Probably contributes to urinary tract sterility. Bactericidal activity is independent of RNase activity.

Subcellular location. Secreted.

Tissue specificity. Expressed in collecting ducts in kidney, and in apical uroepithelium in bladder (at protein level). Expressed in various epithelial tissues including skin, respiratory tract, genito-urinary tract and, at a low level, in the gut. Expressed in liver, kidney, skeletal muscle and heart.

Induction. Up-regulated in response to the cytokines IL1B, IFNG and TNF. Strongly up-regulated in response to the bacterium P.aeruginosa. Moderately up-regulated in response to S.aureus, E.coli and S.pyogenes. Up-regulated in kidney in response to infection.

Similarity. Belongs to the pancreatic ribonuclease family.

RefSeq proteins (1): NP_115961* (*=MANE)

Domains & families (InterPro)

ID	Name	Type
IPR001427	RNaseA	Family
IPR023411	RNaseA_AS	Active_site
IPR023412	RNaseA_domain	Domain
IPR036816	RNaseA-like_dom_sf	Homologous_superfamily

Pfam: PF00074

UniProt features (39 total): mutagenesis site 9, strand 7, binding site 6, disulfide bond 4, helix 3, sequence variant 2, region of interest 2, active site 2, signal peptide 1, chain 1, site 1, glycosylation site 1

Structure

Experimental structures (PDB)

3 structures.

PDB	Method	Resolution (Å)
9CSM	X-RAY DIFFRACTION	1.77
9CSN	X-RAY DIFFRACTION	2.07
2HKY	SOLUTION NMR

Predicted structure (AlphaFold)

Model	pLDDT	Fraction very-high
AF-Q9H1E1-F1	90.87	0.82

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 (3): 66 (critical for catalytic activity); 43 (proton acceptor); 151 (proton donor)

Ligand- & substrate-binding residues (6): 151; 154; 43; 66; 69; 70

Disulfide bonds (4): 51–109, 65–119, 83–134, 90–97

Glycosylation sites (1): 127

Mutagenesis-validated functional residues (9):

Position	Phenotype
29–32	significant loss of bactericidal activity. no effect on catalytic activity.
29	slight loss of bactericidal activity. no effect on catalytic activity.
31	significant loss of bactericidal activity. no effect on catalytic activity.
43	loss of catalytic activity. no effect on bactericidal activity.
60–63	no significant effect on bactericidal activity or catalytic activity.
66	loss of catalytic activity. no effect on bactericidal activity.
124–128	no significant effect on bactericidal activity or catalytic activity.
139–140	moderate loss of bactericidal activity. no effect on catalytic activity.
151	loss of catalytic activity. no effect on bactericidal activity.

Function

Pathways and Gene Ontology

Reactome pathways

3 pathways

ID	Pathway
R-HSA-6803157	Antimicrobial peptides
R-HSA-168249	Innate Immune System
R-HSA-168256	Immune System

MSigDB gene sets: 247 (showing top): GOBP_CHROMOSOME_ORGANIZATION, RODRIGUES_THYROID_CARCINOMA_ANAPLASTIC_UP, GOMF_ENDONUCLEASE_ACTIVITY, REACTOME_INTERACTIONS_OF_VPR_WITH_HOST_CELLULAR_PROTEINS, GOMF_RNA_NUCLEASE_ACTIVITY, REACTOME_INNATE_IMMUNE_SYSTEM, GOBP_ANTIMICROBIAL_HUMORAL_RESPONSE, GOBP_REGULATION_OF_MICROTUBULE_BASED_PROCESS, MORF_RAB5A, REACTOME_CYTOKINE_SIGNALING_IN_IMMUNE_SYSTEM, GOMF_NUCLEASE_ACTIVITY, ENK_UV_RESPONSE_KERATINOCYTE_UP, REACTOME_VIRAL_MESSENGER_RNA_SYNTHESIS, CHIANG_LIVER_CANCER_SUBCLASS_UNANNOTATED_DN, HEIDENBLAD_AMPLICON_8Q24_DN

GO Biological Process (8): antibacterial humoral response (GO:0019731), innate immune response (GO:0045087), defense response to Gram-negative bacterium (GO:0050829), defense response to Gram-positive bacterium (GO:0050830), defense response to fungus (GO:0050832), cytolysis in another organism (GO:0051715), antimicrobial humoral immune response mediated by antimicrobial peptide (GO:0061844), defense response to bacterium (GO:0042742)

GO Molecular Function (8): lipopolysaccharide binding (GO:0001530), nucleic acid binding (GO:0003676), endonuclease activity (GO:0004519), RNA nuclease activity (GO:0004540), hydrolase activity (GO:0016787), peptidoglycan binding (GO:0042834), nuclease activity (GO:0004518), protein binding (GO:0005515)

GO Cellular Component (3): extracellular region (GO:0005576), obsolete extracellular space (GO:0005615), cytoplasm (GO:0005737)

Reactome top-level categories

Rollup of top-2 pathways:

Category	Pathways
Innate Immune System	1
Immune System	1

GO top-level categories

Rollup of top GO terms by namespace:

Category	Terms
defense response to bacterium	3
antimicrobial humoral response	2
defense response	2
binding	2
nuclease activity	2
cellular anatomical structure	2
immune response	1
defense response to symbiont	1
response to fungus	1
cytolysis	1
killing of cells of another organism	1
response to bacterium	1
lipid binding	1
carbohydrate derivative binding	1
catalytic activity, acting on RNA	1
catalytic activity	1
glycosaminoglycan binding	1
catalytic activity, acting on a nucleic acid	1
intracellular anatomical structure	1

Protein interactions and networks

STRING

0 interactions, top by confidence (×1000):

IntAct

80 interactions, top by confidence:

A	B	Type	Score
PDIK1L	CTDSPL2	psi-mi:“MI:0914”(association)	0.840
CCNC	MED19	psi-mi:“MI:0914”(association)	0.640
ALDH3A1	RCCD1	psi-mi:“MI:0914”(association)	0.640
CFAP298	PEX7	psi-mi:“MI:0914”(association)	0.620
RNASE7	RNH1	psi-mi:“MI:0915”(physical association)	0.590
MORN3	ALOXE3	psi-mi:“MI:0914”(association)	0.560
ZSCAN12	A2ML1	psi-mi:“MI:0914”(association)	0.530
GMCL1	A2ML1	psi-mi:“MI:0914”(association)	0.530
TBC1D22B	A2ML1	psi-mi:“MI:0914”(association)	0.530
DNAAF19	KLK10	psi-mi:“MI:0914”(association)	0.530
KIR3DS1	PPL	psi-mi:“MI:0914”(association)	0.530
MMRN1	CTSV	psi-mi:“MI:0914”(association)	0.530
DPPA4	ALOX12B	psi-mi:“MI:0914”(association)	0.530
B3GALNT1	DUSP14	psi-mi:“MI:0914”(association)	0.530
MRPL38	DUSP14	psi-mi:“MI:0914”(association)	0.530
ZSWIM2	SEMG1	psi-mi:“MI:0914”(association)	0.530
DTL	DNAJA2	psi-mi:“MI:0914”(association)	0.530
ZIC1	CTSV	psi-mi:“MI:0914”(association)	0.530
MTHFD2L	MTHFD2	psi-mi:“MI:0914”(association)	0.530
PI4KA	A2ML1	psi-mi:“MI:0914”(association)	0.350
CDK15	A2ML1	psi-mi:“MI:0914”(association)	0.350
DDX19B	IGLL5	psi-mi:“MI:0914”(association)	0.350

BioGRID (84): RNASE7 (Affinity Capture-MS), RNASE7 (Affinity Capture-MS), RNASE7 (Affinity Capture-MS), RNASE7 (Affinity Capture-MS), RNASE7 (Affinity Capture-MS), RNH1 (Affinity Capture-MS), RNASE7 (Affinity Capture-MS), RNASE7 (Affinity Capture-MS), RNASE7 (Affinity Capture-MS), RNASE7 (Affinity Capture-MS), RNASE7 (Affinity Capture-MS), RNASE7 (Affinity Capture-MS), RNASE7 (Affinity Capture-MS), RNASE7 (Affinity Capture-MS), RNASE7 (Affinity Capture-MS)

ESM2 similar proteins: A1YLB9, O46525, O46526, O46527, O46528, O46529, O46530, O46531, O46532, O46533, O46534, P00683, P00684, P08904, P39873, P61823, P81649, Q8SPN3, Q8SPN4, Q8SPZ4, Q8SPZ5, Q8SPZ6, Q8SPZ7, Q8SPZ8, Q8SQ04, Q8SQ05, Q8SQ06, Q8SQ08, Q8SQ11, Q8SQ12, Q8TDE3, Q8VD84, Q8VD87, Q8VD89, Q8VD93, Q93091, Q9D244, Q9H1E1, Q9QYX2, Q9QYX3

Diamond homologs: A1YLB9, B3EWJ0, O18937, O35290, O35291, O35292, O46525, O46526, O46527, O46528, O46529, O46530, O46531, O46532, O46533, O46534, O55004, P00657, P00680, P00682, P00685, P03950, P08904, P10153, P12724, P15466, P15467, P15468, P16414, P24717, P34096, P47778, P47779, P47780, P47781, P47782, P47783, P47784, P47785, P47786

SIGNOR signaling

0 interactions.

Disease & clinical

Clinical variants and AI predictions

ClinVar

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

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

Top pathogenic / likely-pathogenic (0)

SpliceAI

2062 predictions. Top by Δscore:

Variant	Effect	Δscore
20:57351228:G:GT	donor_gain	1.0000
20:57354026:TTTTA:T	acceptor_loss	1.0000
20:57354027:TTTAG:T	acceptor_loss	1.0000
20:57354028:TTAGG:T	acceptor_loss	1.0000
20:57354029:TA:T	acceptor_loss	1.0000
20:57354031:G:T	acceptor_loss	1.0000
20:57354813:TGAT:T	donor_gain	1.0000
20:57354814:GAT:G	donor_gain	1.0000
20:57354814:GATG:G	donor_gain	1.0000
20:57354816:TGTA:T	donor_loss	1.0000
20:57354817:G:GG	donor_gain	1.0000
20:57354817:GT:G	donor_loss	1.0000
20:57354818:T:A	donor_loss	1.0000
20:57354819:AAGT:A	donor_loss	1.0000
20:57356435:T:A	acceptor_gain	1.0000
20:57356443:CAGG:C	acceptor_loss	1.0000
20:57356444:A:AC	acceptor_loss	1.0000
20:57356534:GTGAC:G	donor_gain	1.0000
20:57356535:TGACG:T	donor_loss	1.0000
20:57356536:GAC:G	donor_gain	1.0000
20:57356537:ACGTA:A	donor_loss	1.0000
20:57356538:CG:C	donor_loss	1.0000
20:57356539:G:GG	donor_gain	1.0000
20:57356539:GTAC:G	donor_loss	1.0000
20:57356540:T:G	donor_loss	1.0000
20:57367006:A:AG	acceptor_gain	1.0000
20:57367007:G:GG	acceptor_gain	1.0000
20:57368699:CCCTA:C	acceptor_loss	1.0000
20:57368700:CCTA:C	acceptor_loss	1.0000
20:57368701:CTAG:C	acceptor_loss	1.0000

AlphaMissense

1026 scored. Top likely-pathogenic:

Variant	Protein change	am_pathogenicity
14:21043203:T:C	F71L	0.962
14:21043205:C:A	F71L	0.962
14:21043205:C:G	F71L	0.962
14:21043107:T:C	F39L	0.916
14:21043109:T:A	F39L	0.916
14:21043109:T:G	F39L	0.916
14:21043204:T:G	F71C	0.914
14:21043190:A:C	K66N	0.889
14:21043190:A:T	K66N	0.889
14:21043290:A:C	S100R	0.874
14:21043292:C:A	S100R	0.874
14:21043292:C:G	S100R	0.874
14:21043185:T:A	C65S	0.853
14:21043186:G:C	C65S	0.853
14:21043317:T:A	C109S	0.827
14:21043318:G:C	C109S	0.827
14:21043108:T:G	F39C	0.824
14:21043204:T:C	F71S	0.816
14:21043189:A:T	K66I	0.815
14:21043218:T:C	F76L	0.807
14:21043220:C:A	F76L	0.807
14:21043220:C:G	F76L	0.807
14:21043118:G:C	Q42H	0.781
14:21043118:G:T	Q42H	0.781
14:21043347:T:A	C119S	0.780
14:21043348:G:C	C119S	0.780
14:21043392:T:A	C134S	0.775
14:21043393:G:C	C134S	0.775
14:21043239:T:A	C83S	0.767
14:21043240:G:C	C83S	0.767

dbSNP variants (sampled 300 via entrez): RS1000754233 (14:21044137 G>A), RS1001789922 (14:21040621 C>G), RS1002733456 (14:21040956 G>A,T), RS1002791703 (14:21041951 G>A), RS1003709252 (14:21042133 G>A), RS1004344330 (14:21042309 A>G), RS1004738692 (14:21042577 T>C), RS1005332663 (14:21044172 G>A), RS1006835678 (14:21044518 C>T), RS1007723958 (14:21041407 C>G), RS1008315851 (14:21042862 G>C), RS1008684782 (14:21041340 C>G,T), RS1009736381 (14:21044161 T>A,C), RS1011413767 (14:21041270 C>A), RS1011509053 (14:21041064 T>C)

Disease associations

OMIM: gene MIM:612484 | disease phenotypes:

GenCC curated gene-disease

Mondo (0):

Orphanet (0):

HPO phenotypes

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

GWAS associations

0 associations (top):

Drugs & pharmacology

Drug and pharmacology data

Is drug target: no

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

CTD chemical–gene interactions

20 total (human), top 20 by PubMed support.

Chemical	Actions (top 5)	PubMed papers
Aflatoxin B1	decreases methylation, increases expression	3
Particulate Matter	increases expression, increases abundance	3
sodium arsenite	increases expression	2
Benzo(a)pyrene	increases expression, increases methylation, affects methylation, decreases methylation	2
Formaldehyde	increases expression	2
Tobacco Smoke Pollution	increases expression	2
arsenite	increases methylation	1
hydroquinone	increases expression	1
perfluorooctane sulfonic acid	increases expression	1
CGP 52608	affects binding, increases reaction	1
abrine	increases expression	1
Resveratrol	affects cotreatment, decreases expression	1
Air Pollutants	increases abundance, increases expression	1
Estradiol	affects cotreatment, increases expression	1
Mustard Gas	increases expression	1
N-Nitrosopyrrolidine	increases expression	1
Plant Extracts	affects cotreatment, decreases expression	1
Tetrachlorodibenzodioxin	increases expression	1
Cadmium Chloride	increases expression	1
Lactic Acid	decreases expression	1

Clinical trials (associated diseases)

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