PRMT3

gene
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Summary

PRMT3 (protein arginine methyltransferase 3, HGNC:30163) is a protein-coding gene on chromosome 11p15.1, encoding Protein arginine N-methyltransferase 3 (O60678). Protein-arginine N-methyltransferase that catalyzes both the monomethylation and asymmetric dimethylation of the guanidino nitrogens of arginine residues in target proteins, and therefore falls into the group of type I methyltransferases.

This gene belongs to the protein arginine methyltransferase (PRMT) family. The encoded enzyme catalyzes the methylation of guanidino nitrogens of arginyl residues of proteins. The enzyme acts on 40S ribosomal protein S2 (rpS2), which is its major in-vivo substrate, and is involved in the proper maturation of the 80S ribosome. Alternative splicing results in multiple transcript variants.

Source: NCBI Gene 10196 — RefSeq curated summary.

At a glance

  • GWAS associations: 4
  • Clinical variants (ClinVar): 85 total
  • Druggable target: yes — 1 molecules with ChEMBL bioactivity
  • MANE Select transcript: NM_005788

Identifiers

Gene identifiers

FieldValue
HGNC IDHGNC:30163
Approved symbolPRMT3
Nameprotein arginine methyltransferase 3
Location11p15.1
Locus typegene with protein product
StatusApproved
Ensembl geneENSG00000185238
Ensembl biotypeprotein_coding
OMIM603190
Entrez10196

Gene structure

Transcript identifiers

Ensembl transcripts: 13 — 9 protein_coding, 3 nonsense_mediated_decay, 1 retained_intron

ENST00000330796, ENST00000331079, ENST00000437750, ENST00000525188, ENST00000526583, ENST00000529592, ENST00000862431, ENST00000862432, ENST00000862433, ENST00000862434, ENST00000962519, ENST00000962520, ENST00000962521

RefSeq mRNA: 3 — MANE Select: NM_005788 NM_001145166, NM_001145167, NM_005788

CCDS: CCDS44554, CCDS7853

Canonical transcript exons

ENST00000331079 — 16 exons

ExonStartEnd
ENSE000012932422038801920388154
ENSE000021544312038771620387774
ENSE000021953472050830420509338
ENSE000034691682049391920493969
ENSE000035070932039757720397721
ENSE000035154472040791120408032
ENSE000035317852038974420389826
ENSE000035340332039580320395962
ENSE000035504562040291920402984
ENSE000035534032049416720494254
ENSE000035921792046446020464546
ENSE000035928262039289720392999
ENSE000036304152042676620426865
ENSE000036396952039221120392260
ENSE000036440962046198020462167
ENSE000036731292045213020452208

Expression profiles

Bgee: expression breadth ubiquitous, 269 present calls, max score 84.63.

FANTOM5 (CAGE): breadth ubiquitous, TPM avg 19.2870 / max 238.3430, expressed in 1808 samples.

FANTOM5 promoters (5 alternative TSS)

Promoter IDTPM avgSamples expressed
1134268.34731633
1134248.02031735
1134252.60121337
1134270.2408105
2062250.077525

Top tissues by expression

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

TissueAnatomy IDExpression scoreQuality
ventricular zoneUBERON:000305384.63gold quality
calcaneal tendonUBERON:000370184.55gold quality
primordial germ cell in gonadCL:0000670 ∩ UBERON:000099184.39gold quality
gingival epitheliumUBERON:000194984.29gold quality
gastrocnemiusUBERON:000138883.86gold quality
left lobe of thyroid glandUBERON:000112083.37gold quality
muscle of legUBERON:000138383.17gold quality
thyroid glandUBERON:000204682.96gold quality
germinal epithelium of ovaryUBERON:000130482.91gold quality
right lobe of thyroid glandUBERON:000111982.76gold quality
adrenal tissueUBERON:001830382.74gold quality
islet of LangerhansUBERON:000000682.16gold quality
C1 segment of cervical spinal cordUBERON:000646981.69gold quality
right adrenal gland cortexUBERON:003582781.21gold quality
left adrenal glandUBERON:000123481.19gold quality
right adrenal glandUBERON:000123381.13gold quality
left adrenal gland cortexUBERON:003582581.08gold quality
gingivaUBERON:000182881.01gold quality
palpebral conjunctivaUBERON:000181280.91gold quality
hindlimb stylopod muscleUBERON:000425280.79gold quality
stromal cell of endometriumCL:000225580.53gold quality
ganglionic eminenceUBERON:000402380.50gold quality
rectumUBERON:000105280.21gold quality
male germ line stem cell (sensu Vertebrata) in testisCL:0000089 ∩ UBERON:000047380.19gold quality
heart left ventricleUBERON:000208480.19gold quality
adrenal glandUBERON:000236980.17gold quality
esophagus mucosaUBERON:000246980.14gold quality
monocyteCL:000057680.08gold quality
right atrium auricular regionUBERON:000663180.05gold quality
mononuclear cellCL:000084279.96gold quality

Single-cell (SCXA)

Detected in 2 experiment(s), a significant marker in 1.

ExperimentMarker?Max mean expression
E-ANND-3yes5.06
E-MTAB-6058no165.44

Regulation

Is transcription factor: no

miRNA regulators (miRDB)

70 targeting PRMT3, top 30 by miRDB confidence (max_score; target_count = how many genes the miRNA targets in total — lower means more specific):

miRNAMax scoreAvg scoremiRNA target_count
HSA-MIR-5193100.0067.261744
HSA-MIR-188-3P100.0068.761240
HSA-MIR-6873-3P100.0071.422626
HSA-MIR-5692B100.0071.322622
HSA-MIR-5692C100.0071.322622
HSA-LET-7A-3P100.0074.033932
HSA-LET-7B-3P100.0074.083913
HSA-LET-7F-1-3P100.0074.023928
HSA-MIR-98-3P100.0074.083907
HSA-MIR-7110-3P100.0073.182486
HSA-MIR-428299.9975.366408
HSA-MIR-366299.9973.825684
HSA-MIR-60799.9773.625593
HSA-MIR-548AJ-3P99.9673.385345
HSA-MIR-548X-3P99.9673.385345
HSA-MIR-146A-5P99.9668.93988
HSA-MIR-146B-5P99.9669.13977
HSA-MIR-4666A-3P99.9671.713434
HSA-MIR-548J-3P99.9472.614881
HSA-MIR-1236-3P99.9468.041695
HSA-MIR-7153-5P99.9468.891006
HSA-MIR-548AE-3P99.9372.664867
HSA-MIR-548AH-3P99.9372.544872
HSA-MIR-548AM-3P99.9372.544872
HSA-MIR-548AQ-3P99.9372.664867
HSA-MIR-218-5P99.9372.222103
HSA-MIR-6508-5P99.9270.672465
HSA-MIR-374A-5P99.9071.342923
HSA-MIR-374B-5P99.9069.982734
HSA-MIR-548D-3P99.8770.674362

Literature-anchored findings (GeneRIF, showing 21)

  • PRMT3 is a ribosomal protein methyltransferase that affects the cellular level of ribosomal subunits. (PMID:15175657)
  • DAL-1/4.1B protein significantly inhibits PRMT3 methylation of cellular substrates, which may affect mechanism through which DAL-1/4.1B affects tumor cell growth. (PMID:15334060)
  • Type I Arginine Methyltransferases PRMT1 and PRMT-3 Act Distributively (PMID:19158082)
  • results suggest that the pathological mutation in the PABPN1 gene alters the protein conformation and induces a preferential interaction with type I PRMTs and Hsp70 chaperones (PMID:19641605)
  • The Tyr87Cys and Tyr87Glu-PRMT3 variants had markedly decreased affinity to ribosomal protein S2 and, consequently, reduced enzymatic activity compared to the wild-type enzyme. (PMID:21059412)
  • release of VHL30 from the E3 ligase complex, promotes the binding of VHL30 to a protein arginine methyltransferase, PRMT3 (PMID:21942715)
  • The crystal structure of PRMT3 in complex with an inhibitor as well as kinetic analysis reveals an allosteric site of inhibition. (PMID:22795084)
  • Mutational defects in PRMT3 is not the cause of frontotemporal lobar degeneration. (PMID:23635657)
  • results show that protein arginine methyl transferase (PRMT)-3 and -5 methylate NaV1.5 in vitro, interact with NaV1.5 in human embryonic kidney (HEK) cells, and increase NaV1.5 current density (PMID:23912080)
  • This work profilies substrates of protein arginine N-methyltransferase 3 with S-adenosyl-L-methionine analogues. (PMID:24320160)
  • PRMT3 translocation by palmitic acid is coupled to the binding of LXRalpha, which is responsible for the onset of fatty liver. (PMID:25187371)
  • Findings uncover the existence of an extra-ribosomal complex consisting of PDCD2L, RPS2, and PRMT3 and support a role for PDCD2L in the late maturation of 40S ribosomal subunits. (PMID:27697862)
  • ZNF277 and PRMT3 compete for uS5 binding, because overexpression of PRMT3 inhibited the formation of the ZNF277-uS5 complex, whereas depletion of cellular ZNF277 resulted in increased levels of uS5-PRMT3. (PMID:30530495)
  • PRMT3 is an essential regulator of mesenchymal stem cell-mediated osteogenesis and bone homeostasis. (PMID:31378783)
  • PRMT3 interacts with ALDH1A1 and regulates gene-expression by inhibiting retinoic acid signaling. (PMID:33495566)
  • Arginine methyltransferase PRMT3 promote tumorigenesis through regulating c-MYC stabilization in colorectal cancer. (PMID:33991650)
  • Decreased nitric oxide content mediated by asymmetrical dimethylarginine and protein l-arginine methyltransferase 3 in macrophages induces trophoblast apoptosis: a potential cause of recurrent miscarriage. (PMID:34647126)
  • Protein arginine methyltransferase 3: A crucial regulator in metabolic reprogramming and gene expression in cancers. (PMID:36400311)
  • PRMT3 regulates the progression of invasive micropapillary carcinoma of the breast. (PMID:36637351)
  • PRMT3-mediated arginine methylation of IGF2BP1 promotes oxaliplatin resistance in liver cancer. (PMID:37024475)
  • PRMT3-Mediated Arginine Methylation of METTL14 Promotes Malignant Progression and Treatment Resistance in Endometrial Carcinoma. (PMID:37973560)

Cross-species orthologs

7 orthologs

OrganismSymbolGene ID
danio_rerioprmt3ENSDARG00000019791
mus_musculusPrmt3ENSMUSG00000030505
rattus_norvegicusPrmt3ENSRNOG00000014829
drosophila_melanogasterArt9FBGN0038188
drosophila_melanogasterArt6FBGN0038189
drosophila_melanogasterArt3FBGN0038306
drosophila_melanogasterCG32152FBGN0052152

Paralogs (7): PRMT8 (ENSG00000111218), PRMT1 (ENSG00000126457), PRMT7 (ENSG00000132600), CARM1 (ENSG00000142453), PRMT2 (ENSG00000160310), PRMT9 (ENSG00000164169), PRMT6 (ENSG00000198890)

Protein

Protein identifiers

Protein arginine N-methyltransferase 3O60678 (reviewed: O60678)

Alternative names: Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 3

All UniProt accessions (3): E9PLF6, E9PRB4, O60678

UniProt curated annotations — full annotation on UniProt →

Function. Protein-arginine N-methyltransferase that catalyzes both the monomethylation and asymmetric dimethylation of the guanidino nitrogens of arginine residues in target proteins, and therefore falls into the group of type I methyltransferases. Catalyzes the asymmetric arginine dimethylation at multiple sites in the Arg/Gly-rich region of small ribosomal subunit protein uS5/RPS2. Also appears to methylate other ribosomal proteins. May regulate retinoic acid synthesis and signaling by inhibiting ALDH1A1 retinal dehydrogenase activity. Contributes to methylation of histone H4 ‘Arg-3’, a specific tag for epigenetic transcriptional activation. Mediates asymmetric arginine dimethylation of histone H4 ‘Arg-3’ (H4R3me2a) in the promoter region of miRNA miR-3648, to promote its transcription and osteogenesis.

Subunit / interactions. Monomer and homodimer. Interacts with EPB41L3 (via FERM domain); the interaction is direct and inhibits the protein-arginine N-methyltransferase activity of PRMT3. Interacts with the 40S ribosomal protein RPS2/uS5. Interacts with ALDH1A1; the interaction is direct, inhibits ALDH1A1 aldehyde dehydrogenase activity and is independent of the methyltransferase activity of PRMT3. Interacts (via zinc-finger) with ZNF200 (via C-terminus); the interaction is direct and required to localize PRMT3 to the nucleus and inhibit its proteasomal degradation.

Subcellular location. Cytoplasm. Cytosol. Nucleus.

Activity regulation. Inhibited by N-ethylmaleimide and high concentrations of zinc chloride. Allosterically inhibited by SGC707. Allosterically inhibited by (1-(benzo[d][1,2,3]thiadiazol- 6-yl)-3-(2-cyclohexenylethyl)urea) and derivatives thereof.

Domain organisation. The C2H2-type zinc-finger is responsible for substrate specificity.

Similarity. Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family.

Isoforms (2)

UniProt IDNamesCanonical?
O60678-11yes
O60678-22

RefSeq proteins (3): NP_001138638, NP_001138639, NP_005779* (*=MANE)

Domains & families (InterPro)

IDNameType
IPR013087Znf_C2H2_typeDomain
IPR025799Arg_MeTrfaseFamily
IPR029063SAM-dependent_MTases_sfHomologous_superfamily
IPR036236Znf_C2H2_sfHomologous_superfamily
IPR049009ANM3_Znf-C2H2Domain
IPR049482ANM3-like_C2H2_ZfDomain
IPR055135PRMT_domDomain

Pfam: PF06325, PF21137, PF21336, PF22528

Enzyme classification (BRENDA):

  • EC 2.1.1.319 — type I protein arginine methyltransferase (BRENDA: 13 organisms, 109 substrates, 121 inhibitors, 26 Km, 24 kcat entries)

Substrate kinetics (BRENDA)

16 substrates with measured Km, best-characterized 15. Km ranges are aggregated across organisms/conditions.

SubstrateKm (mM)Measurements
[HISTONE H2A]-L-ARGININE0.0005–0.1283
[HISTONE H3]-L-ARGININE0.001–0.02823
[HISTONE H4]-L-ARGININE0.0017–0.03883
[GRGGFGGRGGFRGGRGG]-L-ARGININE0.0003–0.00082
[HISTONE H4(1-22) PEPTIDE]-L-ARGININE30.0002–0.00082
FYSGFNS-DIMETHYL-R8-P-DIMETHYL-R10-GRVYATSWY0.02221
FYSGFNS-DIMETHYL-R8-PRG-DIMETHYL-R12-VYATSWY0.00071
FYSGFNS-DIMETHYL-R8-PRGRVYATSWY0.00061
FYSGFNSRP-DIMETHYL-R10-G-DIMETHYL-R12-VYATSWY0.0081
FYSGFNSRP-METHYL-R10-GRVYATSWY0.00071
[HISTONE H4(1-16) PEPTIDE]-L-ARGININE30.00031
[PABPN1 MUTANT DELTAC20]-L-ARGININE0.00041
[PABPN1 MUTANT DELTAC27]-L-ARGININE0.00011
[PABPN1 MUTANT DELTAC33]-L-ARGININE1
[PABPN1 MUTANT DELTAC40]-L-ARGININE0.00321

Catalyzed reactions (Rhea), 2 shown:

  • L-arginyl-[protein] + 2 S-adenosyl-L-methionine = N(omega),N(omega)-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine + 2 H(+) (RHEA:48096)
  • L-arginyl-[protein] + S-adenosyl-L-methionine = N(omega)-methyl-L-arginyl-[protein] + S-adenosyl-L-homocysteine + H(+) (RHEA:48100)

UniProt features (71 total): strand 16, helix 13, mutagenesis site 9, binding site 6, turn 5, modified residue 4, sequence variant 3, sequence conflict 3, region of interest 3, active site 2, initiator methionine 1, chain 1, site 1, domain 1, splice variant 1, zinc finger region 1, compositionally biased region 1

Structure

Experimental structures (PDB)

10 structures.

PDBMethodResolution (Å)
8SHRX-RAY DIFFRACTION1.92
2FYTX-RAY DIFFRACTION2
3SMQX-RAY DIFFRACTION2
8G2GX-RAY DIFFRACTION2.02
8G2FX-RAY DIFFRACTION2.06
4QQNX-RAY DIFFRACTION2.08
8SHBX-RAY DIFFRACTION2.09
4RYLX-RAY DIFFRACTION2.1
8SIOX-RAY DIFFRACTION2.2
4HSGX-RAY DIFFRACTION2.3

Predicted structure (AlphaFold)

ModelpLDDTFraction very-high
AF-O60678-F185.630.69

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): 87 (not phosphorylated); 329; 338

Ligand- & substrate-binding residues (6): 239; 263; 285; 313; 314; 343

Post-translational modifications (4): 2, 25, 27, 171

Mutagenesis-validated functional residues (9):

PositionPhenotype
87markedly reduced affinity for rps2.
87no effect on interaction with rps2.
338loss of catalytic activity. no effect on aldh1a1 activity regulation.
403reduces catalytic activity.
464loss of interaction with aldh1a1.
465loss of interaction with aldh1a1.
466loss of interaction with aldh1a1.
468loss of interaction with aldh1a1.

Function

Pathways and Gene Ontology

Reactome pathways

6 pathways

IDPathway
R-HSA-3214858RMTs methylate histone arginines
R-HSA-8876725Protein methylation
R-HSA-3247509Chromatin modifying enzymes
R-HSA-392499Metabolism of proteins
R-HSA-4839726Chromatin organization
R-HSA-597592Post-translational protein modification

MSigDB gene sets: 317 (showing top): RNGTGGGC_UNKNOWN, E2F_Q4_01, GOBP_NEGATIVE_REGULATION_OF_LIPID_METABOLIC_PROCESS, GCANCTGNY_MYOD_Q6, AREB6_03, GOBP_REGULATION_OF_HORMONE_LEVELS, GOBP_NEGATIVE_REGULATION_OF_LIPID_BIOSYNTHETIC_PROCESS, GOBP_OSTEOBLAST_DIFFERENTIATION, MEF2_02, TAL1ALPHAE47_01, GOBP_MONOCARBOXYLIC_ACID_METABOLIC_PROCESS, GOBP_KETONE_METABOLIC_PROCESS, GOBP_ORGANIC_ACID_BIOSYNTHETIC_PROCESS, GOBP_REGULATION_OF_VITAMIN_METABOLIC_PROCESS, SRF_Q5_01

GO Biological Process (8): chromatin remodeling (GO:0006338), regulation of DNA-templated transcription (GO:0006355), negative regulation of protein ubiquitination (GO:0031397), methylation (GO:0032259), positive regulation of osteoblast differentiation (GO:0045669), transcription initiation-coupled chromatin remodeling (GO:0045815), negative regulation of retinoic acid biosynthetic process (GO:1900053), peptidyl-arginine methylation (GO:0018216)

GO Molecular Function (10): methyltransferase activity (GO:0008168), zinc ion binding (GO:0008270), protein-arginine N-methyltransferase activity (GO:0016274), protein-arginine omega-N monomethyltransferase activity (GO:0035241), protein-arginine omega-N asymmetric methyltransferase activity (GO:0035242), histone methyltransferase activity (GO:0042054), histone H4R3 methyltransferase activity (GO:0044020), protein binding (GO:0005515), transferase activity (GO:0016740), metal ion binding (GO:0046872)

GO Cellular Component (4): nucleus (GO:0005634), cytoplasm (GO:0005737), cytosol (GO:0005829), membrane (GO:0016020)

Reactome top-level categories

Rollup of top-4 pathways:

CategoryPathways
Chromatin modifying enzymes1
Post-translational protein modification1
Chromatin organization1
Metabolism of proteins1

GO top-level categories

Rollup of top GO terms by namespace:

CategoryTerms
protein-arginine N-methyltransferase activity3
cellular anatomical structure3
protein methyltransferase activity2
chromatin organization1
DNA-templated transcription1
regulation of gene expression1
regulation of RNA biosynthetic process1
protein ubiquitination1
regulation of protein ubiquitination1
negative regulation of protein modification by small protein conjugation or removal1
metabolic process1
osteoblast differentiation1
positive regulation of cell differentiation1
regulation of osteoblast differentiation1
transcription initiation at RNA polymerase II promoter1
positive regulation of gene expression, epigenetic1
retinoic acid biosynthetic process1
negative regulation of hormone metabolic process1
negative regulation of isoprenoid metabolic process1
negative regulation of vitamin metabolic process1
negative regulation of lipid biosynthetic process1
regulation of retinoic acid biosynthetic process1
protein methylation1
peptidyl-arginine modification1
transferase activity, transferring one-carbon groups1
transition metal ion binding1
arginine N-methyltransferase activity1
histone modifying activity1
histone H4 methyltransferase activity1
binding1
catalytic activity1
cation binding1
intracellular membrane-bounded organelle1
intracellular anatomical structure1
cytoplasm1

Protein interactions and networks

STRING

2474 interactions, top by confidence (×1000):

Protein AProtein BPartner UniProtScore
PRMT3EPB41L3Q9Y2J2914
PRMT3PRMT5O14744892
PRMT3RPS2P15880843
PRMT3PRMT1Q99873838
PRMT3CARM1Q86X55790
PRMT3SETD7Q8WTS6708
PRMT3SUV39H2Q9H5I1637
PRMT3HNRNPA1P09651624
PRMT3EZH2Q15910615
PRMT3HNRNPDLO14979608
PRMT3PDCD2LQ9BRP1591
PRMT3KMT5AQ9NQR1585
PRMT3SMYD3Q9H7B4581
PRMT3WDR77Q9BQA1576
PRMT3KDM1AO60341562

IntAct

75 interactions, top by confidence:

ABTypeScore
PRMT3RPS2psi-mi:“MI:0915”(physical association)0.810
RPS2PRMT3psi-mi:“MI:0915”(physical association)0.810
PRMT3RPS2psi-mi:“MI:0914”(association)0.810
DYNLL2BLTP3Bpsi-mi:“MI:0914”(association)0.640
PRMT3PIH1D2psi-mi:“MI:0915”(physical association)0.560
PRMT3BEND7psi-mi:“MI:0915”(physical association)0.560
PRMT3MEOX2psi-mi:“MI:0915”(physical association)0.560
FKBP6EEF2Kpsi-mi:“MI:0914”(association)0.530
RPS2MPHOSPH10psi-mi:“MI:0914”(association)0.530
TSKSRGPD8psi-mi:“MI:0914”(association)0.530
PDCD2LPRMT3psi-mi:“MI:0914”(association)0.530
DDX21MED19psi-mi:“MI:2364”(proximity)0.480
SCN5APRMT3psi-mi:“MI:2364”(proximity)0.470
SCN5APRMT3psi-mi:“MI:0915”(physical association)0.470
SH2D1BPRMT3psi-mi:“MI:0915”(physical association)0.400
HNRNPKPRMT3psi-mi:“MI:0915”(physical association)0.400
PPARDPRMT3psi-mi:“MI:0915”(physical association)0.370
PRMT3RASSF2psi-mi:“MI:0915”(physical association)0.370
Ranbp2POM121Cpsi-mi:“MI:0914”(association)0.350
HNRNPDARHGAP32psi-mi:“MI:0914”(association)0.350
JUNTPM3psi-mi:“MI:0914”(association)0.350
Xpo1IFT56psi-mi:“MI:0914”(association)0.350
HSCBRBP5psi-mi:“MI:0914”(association)0.350
ORF2PRMT3psi-mi:“MI:0914”(association)0.350
PARP8PRMT3psi-mi:“MI:0914”(association)0.350
PRMT3CSTApsi-mi:“MI:0914”(association)0.350
Mpsi-mi:“MI:0914”(association)0.350

BioGRID (248): RPS2 (Biochemical Activity), PRMT3 (Affinity Capture-MS), PRMT3 (Affinity Capture-MS), PRMT3 (Affinity Capture-MS), PRMT3 (Affinity Capture-MS), PRMT3 (Affinity Capture-MS), PRMT3 (Affinity Capture-MS), PRMT3 (Affinity Capture-MS), PRMT3 (Proximity Label-MS), PRMT3 (Affinity Capture-MS), PRMT3 (Affinity Capture-MS), PRMT3 (Affinity Capture-MS), PRMT3 (Two-hybrid), PRMT3 (Affinity Capture-MS), PRMT3 (Affinity Capture-MS)

ESM2 similar proteins: A0JMU5, A1A4L5, A2AV36, A2Y8B9, B0X4N1, B3DLB3, B3M1E1, B3MF31, B3P4N5, B4GZ20, B4HJC0, B4I8G2, B4JXV2, B4KA23, B4LVS8, B4NKI9, B4P925, B4PVH6, B4QI55, B4QVW6, B6DMK2, D9IVE5, O14727, O60678, O70467, O88879, Q0V9P1, Q16NS8, Q29B63, Q3EBC8, Q3U213, Q3U3W5, Q4SBY6, Q5RAY7, Q5ZIB9, Q6P2P2, Q6P5U7, Q6PCI6, Q7QIL2, Q80VJ4

Diamond homologs: A0A3Q0KHE7, A0A411EW25, A0JMU5, A2AV36, A2Y953, A2YPT7, A2Z0C0, A3KPF2, A6QQV6, A8IEF3, B0JYW5, B0W3L6, B3DLB3, B3M1E1, B3P4N5, B4GZ20, B4HJC0, B4JXV2, B4KA23, B4LVS8, B4MNL1, B4NKI9, B4PVH6, B4QVW6, D9IVE5, O13648, O60678, O70467, O82210, P38074, P55345, Q08A71, Q0J2C6, Q174R2, Q28F07, Q29B63, Q3U3W5, Q4AE70, Q54EF2, Q54HI0

SIGNOR signaling

1 interactions.

AEffectBMechanism
PRMT3“down-regulates activity”ALDH1A1binding

Disease & clinical

Clinical variants and AI predictions

ClinVar

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

ClassificationCount (floor)
Pathogenic0
Likely pathogenic0
Uncertain significance63
Likely benign1
Benign1

Top pathogenic / likely-pathogenic (0)

SpliceAI

3604 predictions. Top by Δscore:

VariantEffectΔscore
11:20388153:AG:Adonor_loss1.0000
11:20388154:GG:Gdonor_loss1.0000
11:20388156:T:Adonor_loss1.0000
11:20395798:TTTA:Tacceptor_loss1.0000
11:20395799:TTA:Tacceptor_loss1.0000
11:20395800:TA:Tacceptor_loss1.0000
11:20395801:A:AGacceptor_gain1.0000
11:20395802:G:Aacceptor_loss1.0000
11:20395802:G:GAacceptor_gain1.0000
11:20395802:GAT:Gacceptor_gain1.0000
11:20395937:GCAC:Gdonor_gain1.0000
11:20395960:G:GTdonor_gain1.0000
11:20395960:GAA:Gdonor_gain1.0000
11:20395963:G:GGdonor_gain1.0000
11:20402914:CCTAG:Cacceptor_loss1.0000
11:20402915:CTAGG:Cacceptor_loss1.0000
11:20402916:TAG:Tacceptor_loss1.0000
11:20402918:G:Aacceptor_loss1.0000
11:20402982:AAGG:Adonor_loss1.0000
11:20402984:GGT:Gdonor_loss1.0000
11:20402985:G:GCdonor_loss1.0000
11:20402986:T:Adonor_loss1.0000
11:20407900:A:AGacceptor_gain1.0000
11:20407901:A:Gacceptor_gain1.0000
11:20407904:A:AGacceptor_gain1.0000
11:20407910:GGTA:Gacceptor_gain1.0000
11:20408028:ATAAG:Adonor_loss1.0000
11:20408029:TAAG:Tdonor_loss1.0000
11:20408030:AAG:Adonor_loss1.0000
11:20408033:GT:Gdonor_loss1.0000

AlphaMissense

3522 scored. Top likely-pathogenic:

VariantProtein changeam_pathogenicity
11:20402944:G:CR244P1.000
11:20397714:T:CM233T0.999
11:20402919:G:CD236H0.999
11:20407915:T:AV259D0.999
11:20426858:A:TE329V0.999
11:20426860:T:AW330R0.999
11:20426860:T:CW330R0.999
11:20452130:G:CG332R0.999
11:20452145:T:CF337L0.999
11:20452147:T:AF337L0.999
11:20452147:T:GF337L0.999
11:20452149:A:TE338V0.999
11:20493934:T:CF455L0.999
11:20493936:T:AF455L0.999
11:20493936:T:GF455L0.999
11:20494206:T:AW480R0.999
11:20494206:T:CW480R0.999
11:20494208:G:CW480C0.999
11:20494208:G:TW480C0.999
11:20392942:T:AW115R0.998
11:20392942:T:CW115R0.998
11:20397714:T:GM233R0.998
11:20397715:G:AM233I0.998
11:20397715:G:CM233I0.998
11:20397715:G:TM233I0.998
11:20402920:A:CD236A0.998
11:20402920:A:TD236V0.998
11:20407939:G:AG267E0.998
11:20407957:C:AA273D0.998
11:20407990:T:AV284D0.998

dbSNP variants (sampled 300 via entrez): RS1000120912 (11:20440533 T>G), RS1000124689 (11:20456608 T>C), RS1000200330 (11:20397043 C>G), RS1000230690 (11:20493896 A>C,G), RS1000232884 (11:20407489 T>G), RS1000265163 (11:20479328 T>A), RS1000283276 (11:20493583 A>G,T), RS1000283931 (11:20450279 T>G), RS1000347358 (11:20395443 A>C), RS1000378301 (11:20480876 G>C), RS1000413527 (11:20414018 A>G), RS1000426964 (11:20443761 G>A), RS1000430153 (11:20499827 C>T), RS1000435857 (11:20443467 C>A,G), RS1000463858 (11:20487392 C>T)

Disease associations

OMIM: gene MIM:603190 | disease phenotypes:

GenCC curated gene-disease

Mondo (0):

Orphanet (0):

HPO phenotypes

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

GWAS associations

4 associations (top):

StudyTraitp-value
GCST002754_2Response to inhaled glucocorticoid treatment in asthma (change in FEV1)6.000000e-11
GCST005024_106Pursuit maintenance gain8.000000e-06
GCST008447_2Number of alcoholic drinks required to feel an effect (long-term average)6.000000e-10
GCST009738_2Carotid intima media thickness (maximum)3.000000e-08

EFO canonical traits (2, from GWAS)

EFO IDTrait name
EFO:0005921FEV change measurement
EFO:0008433pursuit maintenance gain measurement

Drugs & pharmacology

Drug and pharmacology data

Is drug target: yes

ChEMBL targets (1): CHEMBL5891 (SINGLE PROTEIN)

Molecules with ChEMBL bioactivity

1 molecules (phase ≥1), by development phase (incl. off-target/promiscuous compounds). Patent mentions across the top 20 by phase: 1,522 (via chembl_molecule»patent_compound — counts attach to the compound, not the gene–compound relationship, so off-target/promiscuous molecules can dominate).

MoleculeNamePhasePatents
CHEMBL1088977ADEMETIONINE31,522

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

GtoPdb / IUPHAR curated pharmacology

(IUPHAR/BPS Guide to Pharmacology — expert-curated)

Target class: enzyme — 2.1.1.- Protein arginine N-methyltransferases

Most potent curated ligand interactions (3 total), top 3:

LigandActionAffinityParameter
SGC707Negative7.28pKd
MS023Inhibition7.26pKi
compound 1 [PMID: 22795084]Inhibition5.6pIC50

Binding affinities (BindingDB)

2 measured of 5 human assays (5 total across all organisms); most potent 2 below. Values come from heterogeneous assays and are not directly comparable.

LigandMeasureValue
MS023 (Compound 3)KI23 nM
N1-Methyl-N1-((4-(3-(trifluoromethyl)phenyl)-1H-pyrrol-3-yl)methyl)ethane-1,2-diamine (Compound 2)KI120 nM

ChEMBL bioactivities

125 potent at pChembl≥5 of 146 total, top 50 by pChembl (potency: 10 = 0.1 nM, 6 = 1 µM).

pChemblTypeValueUnitMolecule
8.77IC501.7nMCHEMBL5559689
8.40IC504nMCHEMBL3901808
8.00IC5010nMCHEMBL4079503
7.77IC5017nMCHEMBL4076640
7.72IC5019nMCHEMBL4061429
7.72IC5019nMCHEMBL4077534
7.72IC5019nMCHEMBL4072005
7.66IC5022nMCHEMBL4094513
7.66IC5022nMCHEMBL4061085
7.66IC5022nMCHEMBL4071410
7.62IC5024nMCHEMBL4062783
7.51IC5031nMCHEMBL4072005
7.46IC5035nMCHEMBL4086964
7.44IC5036nMCHEMBL4095787
7.34IC5046nMCHEMBL4082966
7.28Kd53nMCHEMBL4072005
7.26IC5055nMCHEMBL4105488
7.26Ki55nMCHEMBL3901808
7.21IC5061nMCHEMBL4097428
7.18IC5066nMCHEMBL4072005
7.08IC5084nMCHEMBL4087094
7.07Kd85nMCHEMBL4072005
7.06IC5087nMCHEMBL4082359
7.04IC5091nMCHEMBL4072005
6.96IC50110nMS-ADENOSYLHOMOCYSTEINE
6.94IC50114nMCHEMBL4065941
6.92IC50119nMCHEMBL3901808
6.92IC50119nMCHEMBL5633822
6.87IC50134nMCHEMBL4077534
6.87IC50134nMCHEMBL4071410
6.87IC50134nMCHEMBL2325198
6.82IC50150nMCHEMBL4090733
6.80IC50158nMCHEMBL4074611
6.78IC50166nMCHEMBL4097411
6.71IC50194nMCHEMBL4059940
6.65IC50225nMCHEMBL4072005
6.64IC50230nMCHEMBL2325198
6.62IC50240nMCHEMBL4062783
6.54IC50292nMCHEMBL4063230
6.54IC50291nMCHEMBL4101037
6.53IC50295nMCHEMBL4081032
6.52IC50300nMCHEMBL2325177
6.49IC50321nMCHEMBL5613745
6.49IC50321nMCHEMBL5613785
6.49IC50321nMCHEMBL5612658
6.44IC50360nMCHEMBL2325197
6.38IC50421nMCHEMBL4104833
6.32IC50480nMCHEMBL2325183
6.32IC50477nMCHEMBL4084879
6.32IC50476nMCHEMBL4100373

PubChem BioAssay actives

121 with measured affinity, of 370 total; 50 most potent distinct compounds. Largely complementary to BindingDB; screening values are coarse (µM, 4 dp), so sub-nM hits tie at the floor.

CompoundAssayTypeValueUnit
N’-[[5-[4,4-bis(ethoxymethyl)cyclohexyl]-1H-pyrazol-4-yl]methyl]-N,N’-dimethylethane-1,2-diamine2069866: Inhibition of N-terminal GST-tagged human PRMT3 (2 to end residues) expressed in Escherichia coli using SAM and Histone (1 to 21 residues) as substrate preincubated for 60 mins followed by substrate addition and measured after 40 mins by Topcount reader based analysisic500.0017uM
N’-methyl-N’-[[4-(4-propan-2-yloxyphenyl)-1H-pyrrol-3-yl]methyl]ethane-1,2-diamine1319863: Inhibition of human PRMT3 assessed as inhibition of methylation activity using biotin-labeled peptide as substrate and [3H]-SAM by scintillation proximity assayic500.0040uM
1-(3-fluoroisoquinolin-6-yl)-3-(2-oxo-2-pyrrolidin-1-ylethyl)urea1472768: Inhibition of PRMT3 (unknown origin) using C-terminally biotinylated histone H4 as substrate in presence of [3H]S-adenosylmethionine by scintillation proximity assayic500.0100uM
1-[2-(azepan-1-yl)-2-oxoethyl]-3-isoquinolin-6-ylurea1472768: Inhibition of PRMT3 (unknown origin) using C-terminally biotinylated histone H4 as substrate in presence of [3H]S-adenosylmethionine by scintillation proximity assayic500.0170uM
1-(8-chloroisoquinolin-6-yl)-3-(2-oxo-2-pyrrolidin-1-ylethyl)urea1472768: Inhibition of PRMT3 (unknown origin) using C-terminally biotinylated histone H4 as substrate in presence of [3H]S-adenosylmethionine by scintillation proximity assayic500.0190uM
1-(7-fluoroisoquinolin-6-yl)-3-(2-oxo-2-pyrrolidin-1-ylethyl)urea1472768: Inhibition of PRMT3 (unknown origin) using C-terminally biotinylated histone H4 as substrate in presence of [3H]S-adenosylmethionine by scintillation proximity assayic500.0190uM
1-isoquinolin-6-yl-3-(2-oxo-2-pyrrolidin-1-ylethyl)urea1472768: Inhibition of PRMT3 (unknown origin) using C-terminally biotinylated histone H4 as substrate in presence of [3H]S-adenosylmethionine by scintillation proximity assayic500.0190uM
1-[2-(8-azabicyclo[3.2.1]octan-8-yl)-2-oxoethyl]-3-isoquinolin-6-ylurea1472768: Inhibition of PRMT3 (unknown origin) using C-terminally biotinylated histone H4 as substrate in presence of [3H]S-adenosylmethionine by scintillation proximity assayic500.0220uM
1-[2-(2,5-dimethylpyrrolidin-1-yl)-2-oxoethyl]-3-isoquinolin-6-ylurea1472768: Inhibition of PRMT3 (unknown origin) using C-terminally biotinylated histone H4 as substrate in presence of [3H]S-adenosylmethionine by scintillation proximity assayic500.0220uM
N’-[[2-(2-chlorophenyl)sulfanylphenyl]methyl]-N’-methylethane-1,2-diamine1471457: Inhibition of PRMT3 (unknown origin) incubated for 15 mins followed by substrate addition measured after 60 mins by AlphaLisa methodic500.0220uM
1-isoquinolin-6-yl-3-[2-oxo-2-(3,3,4,4-tetrafluoropyrrolidin-1-yl)ethyl]urea1472768: Inhibition of PRMT3 (unknown origin) using C-terminally biotinylated histone H4 as substrate in presence of [3H]S-adenosylmethionine by scintillation proximity assayic500.0240uM
1-[2-(4,4-difluoropiperidin-1-yl)-2-oxoethyl]-3-isoquinolin-6-ylurea1472768: Inhibition of PRMT3 (unknown origin) using C-terminally biotinylated histone H4 as substrate in presence of [3H]S-adenosylmethionine by scintillation proximity assayic500.0350uM
1-(7-methylisoquinolin-6-yl)-3-(2-oxo-2-pyrrolidin-1-ylethyl)urea1472768: Inhibition of PRMT3 (unknown origin) using C-terminally biotinylated histone H4 as substrate in presence of [3H]S-adenosylmethionine by scintillation proximity assayic500.0360uM
1-[2-(7-azabicyclo[2.2.1]heptan-7-yl)-2-oxoethyl]-3-isoquinolin-6-ylurea1472768: Inhibition of PRMT3 (unknown origin) using C-terminally biotinylated histone H4 as substrate in presence of [3H]S-adenosylmethionine by scintillation proximity assayic500.0460uM
1-[2-(3,3a,4,5,6,6a-hexahydro-1H-cyclopenta[c]pyrrol-2-yl)-2-oxoethyl]-3-isoquinolin-6-ylurea1472768: Inhibition of PRMT3 (unknown origin) using C-terminally biotinylated histone H4 as substrate in presence of [3H]S-adenosylmethionine by scintillation proximity assayic500.0550uM
1-[2-(azetidin-1-yl)-2-oxoethyl]-3-isoquinolin-6-ylurea1472768: Inhibition of PRMT3 (unknown origin) using C-terminally biotinylated histone H4 as substrate in presence of [3H]S-adenosylmethionine by scintillation proximity assayic500.0610uM
1-isoquinolin-6-yl-3-(2-oxo-2-piperidin-1-ylethyl)urea1472768: Inhibition of PRMT3 (unknown origin) using C-terminally biotinylated histone H4 as substrate in presence of [3H]S-adenosylmethionine by scintillation proximity assayic500.0840uM
N-cyclopentyl-2-(isoquinolin-6-ylcarbamoylamino)-N-methylacetamide1472768: Inhibition of PRMT3 (unknown origin) using C-terminally biotinylated histone H4 as substrate in presence of [3H]S-adenosylmethionine by scintillation proximity assayic500.0870uM
(2S)-2-amino-4-[[(2S,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methylsulfanyl]butanoic acid1689512: Inhibition of recombinant human PRMT8 using histone H4 as substrate by hotspot assayic500.1100uM
N,N-diethyl-2-(isoquinolin-6-ylcarbamoylamino)acetamide1472768: Inhibition of PRMT3 (unknown origin) using C-terminally biotinylated histone H4 as substrate in presence of [3H]S-adenosylmethionine by scintillation proximity assayic500.1140uM
N’-[[4-(4-propan-2-yloxyphenyl)-1H-pyrrol-3-yl]methyl]ethane-1,2-diamine2138374: Inhibition of PRMT3 (unknown origin)ic500.1190uM
1-(1,2,3-benzothiadiazol-6-yl)-3-(2-oxo-2-piperidin-1-ylethyl)urea1472768: Inhibition of PRMT3 (unknown origin) using C-terminally biotinylated histone H4 as substrate in presence of [3H]S-adenosylmethionine by scintillation proximity assayic500.1340uM
2-(isoquinolin-6-ylcarbamoylamino)-N,N-dimethylacetamide1472768: Inhibition of PRMT3 (unknown origin) using C-terminally biotinylated histone H4 as substrate in presence of [3H]S-adenosylmethionine by scintillation proximity assayic500.1500uM
N-cyclopropyl-2-(isoquinolin-6-ylcarbamoylamino)acetamide1472768: Inhibition of PRMT3 (unknown origin) using C-terminally biotinylated histone H4 as substrate in presence of [3H]S-adenosylmethionine by scintillation proximity assayic500.1580uM
methyl (2S)-1-[2-(isoquinolin-6-ylcarbamoylamino)acetyl]pyrrolidine-2-carboxylate1472768: Inhibition of PRMT3 (unknown origin) using C-terminally biotinylated histone H4 as substrate in presence of [3H]S-adenosylmethionine by scintillation proximity assayic500.1660uM
1-(1-methylisoquinolin-6-yl)-3-(2-oxo-2-pyrrolidin-1-ylethyl)urea1472768: Inhibition of PRMT3 (unknown origin) using C-terminally biotinylated histone H4 as substrate in presence of [3H]S-adenosylmethionine by scintillation proximity assayic500.1940uM
1-[2-[1-(aminomethyl)cyclohexyl]ethyl]-3-isoquinolin-6-ylurea1472768: Inhibition of PRMT3 (unknown origin) using C-terminally biotinylated histone H4 as substrate in presence of [3H]S-adenosylmethionine by scintillation proximity assayic500.2910uM
N-cyclopentyl-2-(isoquinolin-6-ylcarbamoylamino)acetamide1472768: Inhibition of PRMT3 (unknown origin) using C-terminally biotinylated histone H4 as substrate in presence of [3H]S-adenosylmethionine by scintillation proximity assayic500.2920uM
1-(2-cyclopentylethyl)-3-isoquinolin-6-ylurea1472768: Inhibition of PRMT3 (unknown origin) using C-terminally biotinylated histone H4 as substrate in presence of [3H]S-adenosylmethionine by scintillation proximity assayic500.2950uM
1-(1,2,3-benzothiadiazol-6-yl)-3-[(4-nitrophenyl)methyl]urea729422: Inhibition of PRMT3 (unknown origin) using histone H4 (1 to 24) as substrate after 1 hr by scintillation proximity assay in presence of [3H]-S-adenosylmethionineic500.3000uM
2-[2-[[(2S,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methylsulfanyl]ethyl]-1-phenylguanidine2127550: Inhibition of human PRMT3 using Histone H3 as substrate and SAM as cofactor by radiometric HotSpot assayic500.3210uM
2-[2-[[(2S,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methylsulfanyl]ethyl]-1-(2-bromophenyl)guanidine2127582: Inhibition of PRMT3 (unknown origin)ic500.3210uM
1-(1,2,3-benzothiadiazol-6-yl)-3-[2-(4-fluorophenyl)-2-oxoethyl]urea729422: Inhibition of PRMT3 (unknown origin) using histone H4 (1 to 24) as substrate after 1 hr by scintillation proximity assay in presence of [3H]-S-adenosylmethionineic500.3600uM
1-[2-(cyclohexen-1-yl)ethyl]-3-isoquinolin-6-ylurea1472768: Inhibition of PRMT3 (unknown origin) using C-terminally biotinylated histone H4 as substrate in presence of [3H]S-adenosylmethionine by scintillation proximity assayic500.4210uM
2-(isoquinolin-6-ylcarbamoylamino)-N-methoxy-N-methylacetamide1472768: Inhibition of PRMT3 (unknown origin) using C-terminally biotinylated histone H4 as substrate in presence of [3H]S-adenosylmethionine by scintillation proximity assayic500.4760uM
N-cyclohexyl-2-(isoquinolin-6-ylcarbamoylamino)acetamide1472768: Inhibition of PRMT3 (unknown origin) using C-terminally biotinylated histone H4 as substrate in presence of [3H]S-adenosylmethionine by scintillation proximity assayic500.4770uM
1-(1,2,3-benzothiadiazol-6-yl)-3-phenacylurea729422: Inhibition of PRMT3 (unknown origin) using histone H4 (1 to 24) as substrate after 1 hr by scintillation proximity assay in presence of [3H]-S-adenosylmethionineic500.4800uM
1-(1,2,3-benzothiadiazol-6-yl)-3-(2-cyclohexyl-2-hydroxyethyl)urea729422: Inhibition of PRMT3 (unknown origin) using histone H4 (1 to 24) as substrate after 1 hr by scintillation proximity assay in presence of [3H]-S-adenosylmethionineic500.4900uM
N’-[[2-[4,4-bis(methoxymethyl)cyclohexyl]oxyphenyl]methyl]-N,N’-dimethylethane-1,2-diamine;dihydrochloride2069842: Inhibition of PRMT3 (unknown origin) by AlphaLISA assayic500.4930uM
1-(2-cyclohexylethyl)-3-isoquinolin-6-ylurea1472768: Inhibition of PRMT3 (unknown origin) using C-terminally biotinylated histone H4 as substrate in presence of [3H]S-adenosylmethionine by scintillation proximity assayic500.5400uM
N’-methyl-N’-[[4-[3-(trifluoromethyl)phenyl]-1H-pyrrol-3-yl]methyl]ethane-1,2-diamine1801573: PRMT Biochemical Assays from Article 10.1021/acschembio.5b00839: “A Potent, Selective, and Cell-Active Inhibitor of Human Type I Protein Arginine Methyltransferases.”ki0.5500uM
1-(1-oxo-3H-2-benzofuran-5-yl)-3-(2-oxo-2-piperidin-1-ylethyl)urea1472768: Inhibition of PRMT3 (unknown origin) using C-terminally biotinylated histone H4 as substrate in presence of [3H]S-adenosylmethionine by scintillation proximity assayic500.7570uM
1-isoquinolin-6-yl-3-(2-phenylethyl)urea1472768: Inhibition of PRMT3 (unknown origin) using C-terminally biotinylated histone H4 as substrate in presence of [3H]S-adenosylmethionine by scintillation proximity assayic500.8330uM
1-(1,2,3-benzothiadiazol-6-yl)-3-(2-cyclohexyl-2-oxoethyl)urea729422: Inhibition of PRMT3 (unknown origin) using histone H4 (1 to 24) as substrate after 1 hr by scintillation proximity assay in presence of [3H]-S-adenosylmethionineic500.8400uM
1-(1,2,3-benzothiadiazol-6-yl)-3-[(4-methylsulfonylphenyl)methyl]urea729422: Inhibition of PRMT3 (unknown origin) using histone H4 (1 to 24) as substrate after 1 hr by scintillation proximity assay in presence of [3H]-S-adenosylmethionineic500.8500uM
(2S)-2-amino-4-[[(2S,3S,4R,5R)-5-(4-amino-5-cyanopyrrolo[2,3-d]pyrimidin-7-yl)-3,4-dihydroxyoxolan-2-yl]methylsulfanyl]butanoic acid1636911: Inhibition of PRMT3 (unknown origin)ic500.8700uM
(2S)-1-[[2-[[3-chloro-4-(1,3-thiazol-2-yl)phenyl]methoxy]phenyl]methyl-methylamino]-3-(methylamino)propan-2-ol2104090: Inhibition of PRMT3 (unknown origin)ic500.9420uM
1-(2-oxo-2-piperidin-1-ylethyl)-3-quinazolin-7-ylurea1472768: Inhibition of PRMT3 (unknown origin) using C-terminally biotinylated histone H4 as substrate in presence of [3H]S-adenosylmethionine by scintillation proximity assayic500.9670uM
1-(1,2,3-benzothiadiazol-6-yl)-3-(2-cyclohexylethyl)urea729422: Inhibition of PRMT3 (unknown origin) using histone H4 (1 to 24) as substrate after 1 hr by scintillation proximity assay in presence of [3H]-S-adenosylmethionineic501.0000uM
(2S)-2-amino-4-[[(2S,3S,4R,5R)-5-(4-amino-5-bromopyrrolo[2,3-d]pyrimidin-7-yl)-3,4-dihydroxyoxolan-2-yl]methylsulfanyl]butanoic acid738921: Inhibition of PRMT3 (unknown origin) using [3H]SAM assessed as inhibition of biotinylated-H4 (1 to 24 amino acid residues) methylation after 1 hr by scintillation proximity assayki1.1500uM

CTD chemical–gene interactions

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

ChemicalActions (top 5)PubMed papers
sodium arsenitedecreases expression, affects cotreatment, increases abundance, increases expression3
Air Pollutantsdecreases expression, increases abundance, increases expression2
Arsenicincreases abundance, increases expression, decreases expression, affects cotreatment2
Dexamethasonedecreases expression, affects cotreatment2
Particulate Matterincreases abundance, increases expression, decreases expression2
aristolochic acid Idecreases expression1
SGC707affects folding, affects binding, decreases activity1
FR900359affects phosphorylation1
bisphenol Faffects cotreatment, decreases expression1
dicrotophosdecreases expression1
triphenyl phosphateaffects expression1
trichostatin Aaffects expression1
arseniteaffects binding, increases reaction1
cobaltous chloridedecreases expression1
manganese chlorideaffects cotreatment, increases abundance, increases expression1
potassium chromate(VI)affects cotreatment, decreases expression1
1-nitropyreneincreases expression1
epigallocatechin gallateaffects cotreatment, decreases expression1
di-n-butylphosphoric acidaffects expression1
Resveratrolaffects cotreatment, increases expression1
Sunitinibincreases expression1
Benzo(a)pyreneincreases methylation1
Dichlorodiphenyl Dichloroethyleneincreases expression1
Doxorubicindecreases expression1
Enzyme Inhibitorsincreases O-linked glycosylation, decreases activity1
Estradiolincreases expression1
Ethyl Methanesulfonatedecreases expression1
Formaldehydedecreases expression1
Indomethacinaffects cotreatment, decreases expression1
Ivermectindecreases expression1

ChEMBL screening assays

148 unique, capped per target: 145 binding, 3 functional

Representative assays (with source publication via chembl_document):

Assay IDTypeDescriptionSource paper
CHEMBL1037276BindingInhibition of PRMT3Benzo[d]imidazole inhibitors of Coactivator Associated Arginine Methyltransferase 1 (CARM1)–Hit to Lead studies. — Bioorg Med Chem Lett
CHEMBL5444955FunctionalAffinity Phenotypic Cellular interaction: (Western Blot (inhibitor of H4R3 methylation in MCF-7 cells)) EUB0000261b PRMT3Affinity Phenotypic Cellular Literature for EUbOPEN Chemogenomic Library

Cellosaurus cell lines

3 cell lines: 3 cancer cell line

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

CellosaurusNameCategorySex
CVCL_KW00InCELL Hunter A549 PRMT3 MethyltransferaseCancer cell lineMale
CVCL_TH12HAP1 PRMT3 (-) 1Cancer cell lineMale
CVCL_TH13HAP1 PRMT3 (-) 2Cancer cell lineMale

Clinical trials (associated diseases)

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

No linked Atlas pages yet — the cross-entity mesh grows as the corpus expands.