PRMT7

gene
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Also known as FLJ10640KIAA1933

Summary

PRMT7 (protein arginine methyltransferase 7, HGNC:25557) is a protein-coding gene on chromosome 16q22.1, encoding Protein arginine N-methyltransferase 7 (Q9NVM4). Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA.

This gene encodes a member of the protein arginine N-methyltransferase family of proteins. The encoded enzyme transfers single methyl groups to arginine residues to generate monomethylarginines on histone proteins as well as other protein substrates. This enzyme plays a role in a wide range of biological processes, including neuronal differentiation, male germ line imprinting, small nuclear ribonucleoprotein biogenesis, and regulation of the Wnt signaling pathway. Mutations in this gene underlie multiple related syndromes in human patients characterized by intellectual disability, short stature and other features. The encoded protein may promote breast cancer cell invasion and metastasis in human patients.

Source: NCBI Gene 54496 — RefSeq curated summary.

At a glance

  • Gene–disease (curated): short stature-brachydactyly-obesity-global developmental delay syndrome (Strong, GenCC)
  • GWAS associations: 13
  • Clinical variants (ClinVar): 361 total — 21 pathogenic, 20 likely-pathogenic
  • Phenotypes (HPO): 89
  • Druggable target: yes — 1 molecules with ChEMBL bioactivity
  • MANE Select transcript: NM_019023

Identifiers

Gene identifiers

FieldValue
HGNC IDHGNC:25557
Approved symbolPRMT7
Nameprotein arginine methyltransferase 7
Location16q22.1
Locus typegene with protein product
StatusApproved
AliasesFLJ10640, KIAA1933
Ensembl geneENSG00000132600
Ensembl biotypeprotein_coding
OMIM610087
Entrez54496

Gene structure

Transcript identifiers

Ensembl transcripts: 84 — 42 protein_coding, 19 nonsense_mediated_decay, 13 retained_intron, 10 protein_coding_CDS_not_defined

ENST00000339507, ENST00000441236, ENST00000449359, ENST00000561806, ENST00000562050, ENST00000562381, ENST00000562456, ENST00000563443, ENST00000563520, ENST00000563562, ENST00000563608, ENST00000564050, ENST00000564441, ENST00000565356, ENST00000565745, ENST00000565761, ENST00000565983, ENST00000566341, ENST00000566430, ENST00000566687, ENST00000566708, ENST00000567542, ENST00000568463, ENST00000568975, ENST00000569047, ENST00000569571, ENST00000675132, ENST00000685109, ENST00000685141, ENST00000686053, ENST00000686346, ENST00000686904, ENST00000687444, ENST00000687558, ENST00000687654, ENST00000688470, ENST00000688969, ENST00000689486, ENST00000689637, ENST00000690311, ENST00000690432, ENST00000690932, ENST00000691663, ENST00000691804, ENST00000691833, ENST00000691961, ENST00000692283, ENST00000692621, ENST00000692632, ENST00000692760, ENST00000692867, ENST00000692966, ENST00000693200, ENST00000693309, ENST00000693670, ENST00000897111, ENST00000897112, ENST00000897113, ENST00000897114, ENST00000897115, ENST00000897116, ENST00000897117, ENST00000897118, ENST00000926970, ENST00000926971, ENST00000926972, ENST00000926973, ENST00000926974, ENST00000926975, ENST00000926976, ENST00000926977, ENST00000926978, ENST00000926979, ENST00000926980, ENST00000926981, ENST00000950163, ENST00000950164, ENST00000950165, ENST00000950166, ENST00000950167, ENST00000950168, ENST00000950169, ENST00000950170, ENST00000950171

RefSeq mRNA: 10 — MANE Select: NM_019023 NM_001184824, NM_001290018, NM_001351143, NM_001351144, NM_001378018, NM_001378020, NM_001378021, NM_001378022, NM_001378023, NM_019023

CCDS: CCDS10866, CCDS54033, CCDS92184, CCDS92187

Canonical transcript exons

ENST00000441236 — 19 exons

ExonStartEnd
ENSE000011115586834834268348431
ENSE000015165536831204268312176
ENSE000034582406832906668329174
ENSE000034717596833978868339968
ENSE000035184156835349268353566
ENSE000035226916833932268339563
ENSE000035349906832142668321462
ENSE000035473786833745968337571
ENSE000035507886835670168356797
ENSE000035638766835572368355883
ENSE000035711216834614568346280
ENSE000035955686835224868352409
ENSE000035965986834721168347294
ENSE000035976406834763168347678
ENSE000036148576834567568345802
ENSE000036795416831589768316074
ENSE000036929056832468368324832
ENSE000037517796835705468358584
ENSE000039001476831101968311099

Expression profiles

Bgee: expression breadth ubiquitous, 186 present calls, max score 97.50.

FANTOM5 (CAGE): breadth ubiquitous, TPM avg 18.8410 / max 160.4231, expressed in 1798 samples.

FANTOM5 promoters (4 alternative TSS)

Promoter IDTPM avgSamples expressed
15473617.54921794
1547390.8597136
1547370.2470124
1547380.185289

Top tissues by expression

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

TissueAnatomy IDExpression scoreQuality
right hemisphere of cerebellumUBERON:001489097.50gold quality
cerebellar hemisphereUBERON:000224597.24gold quality
cerebellar cortexUBERON:000212996.98gold quality
right frontal lobeUBERON:000281094.50gold quality
right uterine tubeUBERON:000130294.38gold quality
apex of heartUBERON:000209893.70gold quality
cerebellumUBERON:000203793.67gold quality
hindlimb stylopod muscleUBERON:000425293.46gold quality
tibial nerveUBERON:000132393.22gold quality
sural nerveUBERON:001548893.09gold quality
ventricular zoneUBERON:000305393.08gold quality
right ovaryUBERON:000211892.96gold quality
left ovaryUBERON:000211992.84gold quality
ganglionic eminenceUBERON:000402392.75gold quality
adenohypophysisUBERON:000219692.64gold quality
body of uterusUBERON:000985392.27gold quality
right adrenal glandUBERON:000123392.24gold quality
right adrenal gland cortexUBERON:003582792.00gold quality
gastrocnemiusUBERON:000138891.94gold quality
cortical plateUBERON:000534391.87gold quality
muscle of legUBERON:000138391.86gold quality
anterior cingulate cortexUBERON:000983591.86gold quality
left adrenal gland cortexUBERON:003582591.79gold quality
muscle layer of sigmoid colonUBERON:003580591.77gold quality
cingulate cortexUBERON:000302791.70gold quality
left adrenal glandUBERON:000123491.57gold quality
right lobe of thyroid glandUBERON:000111991.32gold quality
endocervixUBERON:000045891.29gold quality
right lobe of liverUBERON:000111491.24gold quality
colonic epitheliumUBERON:000039791.18gold quality

Single-cell (SCXA)

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

ExperimentMarker?Max mean expression
E-ANND-3yes5.10
E-MTAB-7303no460.92

Regulation

Is transcription factor: no

Upstream regulators (CollecTRI, top): CTCFL, KMT2B, TCF3

Literature-anchored findings (GeneRIF, showing 24)

  • both domains are required for functionality (PMID:15044439)
  • PRMT7 (like PRMT5) is a Type II methyltransferase capable of producing symmetric dimethylarginine modifications in proteins. (PMID:15494416)
  • that in human cells, PRMT5 and PRMT7 are required for Sm protein sDMA modification, and that Sm protein symmetric dimethylarginine modification is required for snRNP biogenesis in human cells. (PMID:17709427)
  • Here the authors report that H3R2 is also symmetrically dimethylated (H3R2me2s) by PRMT5 and PRMT7 and present in euchromatic regions. (PMID:22231400)
  • Human protein arginine methyltransferase 7 (PRMT7) is a type III enzyme forming omega-NG-monomethylated arginine residues. (PMID:22241471)
  • reducing expression of individual PRMT7 target DNA repair genes showed that only the catalytic subunit of DNA polymerase, POLD1, was able to resensitize PRMT7 knock-down cells to DNA-damaging agents. (PMID:22761421)
  • results define PRMT7 as an inducer of breast cancer metastasis and present the opportunity for applying PRMT7-targeted therapeutics to treat highly invasive breast cancers (PMID:25136067)
  • Data indicate that two acidic residues within the double E loop, Asp-147 and Glu-149, confer specificity to protein arginine methyltransferase 7 (PRMT7. (PMID:25294873)
  • Upregulation of PRMT7 in breast cancer may have a significant role in promoting cell invasion through the regulation of MMP9. (PMID:25605249)
  • Loss of PRMT7 causes decreases in arginine methylation throughout the proteome.Loss of the arginine methyltranserase PRMT7 causes syndromic intellectual disability with microcephaly and brachydactyly. (PMID:27718516)
  • The authors showed that ASS1 mutations linked to type I citrullinemia disrupt the ASS1-PRMT7 interaction, which might explain the molecular pathogenesis of the disease. (PMID:28587924)
  • These kinetic studies suggest a biochemical explanation for the interplay between PRMT5- and PRMT7-mediated methylation of the same substrate at different residues and also suggest a general model for regulation of PRMTs. (PMID:28874563)
  • Our findings expand the clinical and molecular spectrum of homozygous PRMT7 mutations, associated to the SBIDDS syndrome, showing a possible correlation between the type of mutation and the severity of the phenotype. (PMID:28902392)
  • Our patients provide additional clinical and pathological data and expand the phenotypic manifestations associated with PRMT7 homozygote/compound heterozygote mutations to include brain calcifications and delayed myelination, and congenital orbital tumor. (PMID:30513135)
  • PRMT7 promotes the growth of renal cell carcinoma through modulating the beta-catenin/C-MYC axis. (PMID:31926310)
  • Pharmacological inhibition of PRMT7 links arginine monomethylation to the cellular stress response. (PMID:32409666)
  • Profiling PRMT methylome reveals roles of hnRNPA1 arginine methylation in RNA splicing and cell growth. (PMID:33782401)
  • The role of protein arginine methyltransferase 7 in human developmentally arrested embryos cultured in vitro. (PMID:34041522)
  • Arginine monomethylation by PRMT7 controls MAVS-mediated antiviral innate immunity. (PMID:34171297)
  • An enhancer variant at 16q22.1 predisposes to hepatocellular carcinoma via regulating PRMT7 expression. (PMID:35264579)
  • The arginine methyltransferase PRMT7 promotes extravasation of monocytes resulting in tissue injury in COPD. (PMID:35288557)
  • Short stature in PRMT7 Mutations: first evidence of response to growth hormone treatment. (PMID:36348013)
  • Biallelic PRMT7 pathogenic variants are associated with a recognizable syndromic neurodevelopmental disorder with short stature, obesity, and craniofacial and digital abnormalities. (PMID:36399134)
  • The exquisite specificity of human protein arginine methyltransferase 7 (PRMT7) toward Arg-X-Arg sites. (PMID:37216364)

Cross-species orthologs

5 orthologs

OrganismSymbolGene ID
danio_rerioprmt7ENSDARG00000051902
mus_musculusPrmt7ENSMUSG00000060098
rattus_norvegicusPrmt7ENSRNOG00000000258
drosophila_melanogasterArt7FBGN0034817
caenorhabditis_elegansprmt-7WBGENE00012298

Paralogs (7): PRMT8 (ENSG00000111218), PRMT1 (ENSG00000126457), CARM1 (ENSG00000142453), PRMT2 (ENSG00000160310), PRMT9 (ENSG00000164169), PRMT3 (ENSG00000185238), PRMT6 (ENSG00000198890)

Protein

Protein identifiers

Protein arginine N-methyltransferase 7Q9NVM4 (reviewed: Q9NVM4)

Alternative names: Histone-arginine N-methyltransferase PRMT7, [Myelin basic protein]-arginine N-methyltransferase PRMT7

All UniProt accessions (20): Q9NVM4, A0A6Q8PFP4, A0A8I5KPP4, A0A8I5KPT4, A0A8I5KQA6, A0A8I5KRA7, A0A8I5KRU8, A0A8I5KRV0, A0A8I5KRW2, A0A8I5KWG5, A0A8I5KXS9, A0A8I5KYD6, A0A8I5KZ05, A0A8I5KZ92, A0A8I5QKQ0, A0A8I5QKZ3, H3BNC0, H3BPZ8, H3BRD3, H3BSS9

UniProt curated annotations — full annotation on UniProt →

Function. Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Specifically mediates the symmetric dimethylation of histone H4 ‘Arg-3’ to form H4R3me2s. Plays a role in gene imprinting by being recruited by CTCFL at the H19 imprinted control region (ICR) and methylating histone H4 to form H4R3me2s, possibly leading to recruit DNA methyltransferases at these sites. May also play a role in embryonic stem cell (ESC) pluripotency. Also able to mediate the arginine methylation of histone H2A and myelin basic protein (MBP) in vitro; the relevance of such results is however unclear in vivo.

Subunit / interactions. Homodimer and heterodimer. Interacts with CTCFL. Interacts with PRMT5 and SNRPD3.

Subcellular location. Cytoplasm. Cytosol. Nucleus.

Disease relevance. Short stature, brachydactyly, impaired intellectual developmental, and seizures (SBIDDS) [MIM:617157] An autosomal recessive disease characterized by developmental delay, learning disabilities, mild intellectual disability, delayed speech, and skeletal abnormalities. Skeletal features include short stature, brachydactyly, and short metacarpals and metatarsals. The disease is caused by variants affecting the gene represented in this entry.

Miscellaneous. May be involved in etoposide-induced cytotoxicity, a chemotherapeutic agent frequently used for testicular cancer and small-cell lung cancer that can cause cytotoxicity in the treatment of other cancers. Down-regulation confers increased sensitivity to the Top1 inhibitor camptothecin (CPT).

Similarity. Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT7 subfamily.

Isoforms (4)

UniProt IDNamesCanonical?
Q9NVM4-11yes
Q9NVM4-22
Q9NVM4-33
Q9NVM4-44

RefSeq proteins (10): NP_001171753, NP_001276947, NP_001338072, NP_001338073, NP_001364947, NP_001364949, NP_001364950, NP_001364951, NP_001364952, NP_061896* (*=MANE)

Domains & families (InterPro)

IDNameType
IPR014644MeTrfase_PRMT7Family
IPR025799Arg_MeTrfaseFamily
IPR029063SAM-dependent_MTases_sfHomologous_superfamily
IPR055135PRMT_domDomain

Pfam: PF06325, PF22528

Enzyme classification (BRENDA):

  • EC 2.1.1.321 — type III protein arginine methyltransferase (BRENDA: 7 organisms, 78 substrates, 27 inhibitors, 15 Km, 2 kcat entries)

Substrate kinetics (BRENDA)

10 substrates with measured Km, best-characterized 10. Km ranges are aggregated across organisms/conditions.

SubstrateKm (mM)Measurements
ACTEYL-KKDGKKRKRSRKESY-AMIDE0.0006–0.0172
ACTEYL-KKGGRGRGGKKY-AMIDE0.0007–0.00622
ACTEYL-KKGGRGRKGKKY-AMIDE0.0005–0.00242
ACTEYL-KKGGRKRGGKKY-AMIDE0.0006–0.00692
ACTEYL-KKGKRGRGGKKY-AMIDE0.0006–0.00332
ACTEYL-KKGGRERGGKKY-AMIDE0.00281
ACTEYL-KKGGRGGGGKKY-AMIDE0.00141
S-ADENOSYL-L-HOMOCYSTEINE0.00161
[HEAT SHOCK PROTEIN A8]-L-ARGININE4690.01061
[HISTONE H2B PEPTIDE 23-37]-L-ARGININE0.00691

Catalyzed reactions (Rhea), 1 shown:

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

UniProt features (18 total): splice variant 5, sequence conflict 4, sequence variant 3, domain 2, active site 2, chain 1, modified residue 1

Structure

Experimental structures (PDB)

0 structures.

Predicted structure (AlphaFold)

ModelpLDDTFraction very-high
AF-Q9NVM4-F193.190.83

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 (2): 144; 153

Post-translational modifications (1): 32

Function

Pathways and Gene Ontology

Reactome pathways

3 pathways

IDPathway
R-HSA-3214858RMTs methylate histone arginines
R-HSA-3247509Chromatin modifying enzymes
R-HSA-4839726Chromatin organization

MSigDB gene sets: 346 (showing top): GSE18804_SPLEEN_MACROPHAGE_VS_BRAIN_TUMORAL_MACROPHAGE_DN, GSE45365_NK_CELL_VS_BCELL_DN, BUYTAERT_PHOTODYNAMIC_THERAPY_STRESS_DN, chr16q22, GRAESSMANN_APOPTOSIS_BY_DOXORUBICIN_DN, GOBP_PROTEIN_RNA_COMPLEX_ORGANIZATION, GOBP_RNA_SPLICING, GOBP_GENOMIC_IMPRINTING, GOBP_CELLULAR_PROCESS_INVOLVED_IN_REPRODUCTION_IN_MULTICELLULAR_ORGANISM, GOBP_DEVELOPMENTAL_PROCESS_INVOLVED_IN_REPRODUCTION, GOBP_CHROMATIN_REMODELING, GOBP_METHYLATION, GOBP_RIBONUCLEOPROTEIN_COMPLEX_BIOGENESIS, CUI_TCF21_TARGETS_2_UP, GOBP_EPIGENETIC_REGULATION_OF_GENE_EXPRESSION

GO Biological Process (9): spliceosomal snRNP assembly (GO:0000387), chromatin remodeling (GO:0006338), regulation of DNA-templated transcription (GO:0006355), peptidyl-arginine methylation (GO:0018216), genomic imprinting (GO:0071514), chromatin organization (GO:0006325), protein methylation (GO:0006479), cell differentiation (GO:0030154), methylation (GO:0032259)

GO Molecular Function (13): S-adenosylmethionine-dependent methyltransferase activity (GO:0008757), protein-arginine N-methyltransferase activity (GO:0016274), protein-arginine omega-N monomethyltransferase activity (GO:0035241), protein-arginine omega-N symmetric methyltransferase activity (GO:0035243), histone methyltransferase activity (GO:0042054), histone binding (GO:0042393), ribonucleoprotein complex binding (GO:0043021), histone H4R3 methyltransferase activity (GO:0044020), histone H4 methyltransferase activity (GO:0140939), protein binding (GO:0005515), methyltransferase activity (GO:0008168), protein methyltransferase activity (GO:0008276), transferase activity (GO:0016740)

GO Cellular Component (5): fibrillar center (GO:0001650), nucleus (GO:0005634), nucleoplasm (GO:0005654), cytosol (GO:0005829), cytoplasm (GO:0005737)

Reactome top-level categories

Rollup of top-2 pathways:

CategoryPathways
Chromatin modifying enzymes1
Chromatin organization1

GO top-level categories

Rollup of top GO terms by namespace:

CategoryTerms
cellular anatomical structure4
protein-arginine N-methyltransferase activity3
methyltransferase activity2
protein methyltransferase activity2
mRNA splicing, via spliceosome1
protein-RNA complex assembly1
chromatin organization1
DNA-templated transcription1
regulation of gene expression1
regulation of RNA biosynthetic process1
protein methylation1
peptidyl-arginine modification1
germ cell development1
epigenetic programming of gene expression1
cellular component organization1
protein alkylation1
macromolecule methylation1
cellular developmental process1
metabolic process1
arginine N-methyltransferase activity1
histone modifying activity1
protein binding1
protein-containing complex binding1
histone H4 methyltransferase activity1
histone methyltransferase activity1
binding1
transferase activity, transferring one-carbon groups1
catalytic activity, acting on a protein1
catalytic activity1
nucleolus1
intracellular membrane-bounded organelle1
nuclear lumen1
cytoplasm1
intracellular anatomical structure1

Protein interactions and networks

STRING

1922 interactions, top by confidence (×1000):

Protein AProtein BPartner UniProtScore
PRMT7PRMT5O14744963
PRMT7CTCFLQ8NI51857
PRMT7H4C7Q99525709
PRMT7H4C16P02304691
PRMT7FBLP22087680
PRMT7SNRPD3P43331665
PRMT7PRMT8Q9NR22663
PRMT7WDR77Q9BQA1629
PRMT7SMYD3Q9H7B4611
PRMT7SF3B2Q13435570
PRMT7PRMT1Q99873565
PRMT7YY1P25490506
PRMT7DNMT1P26358496
PRMT7PRMT3O60678481
PRMT7SMURF1Q9HCE7477

IntAct

45 interactions, top by confidence:

ABTypeScore
EIF2S1EIF2S3psi-mi:“MI:0914”(association)0.820
EIF2S2EIF2S1psi-mi:“MI:0914”(association)0.810
EIF2S1PRMT7psi-mi:“MI:0915”(physical association)0.670
PRMT7ASS1psi-mi:“MI:0915”(physical association)0.640
PRMT7ASS1psi-mi:“MI:0407”(direct interaction)0.640
PRMT7ASS1psi-mi:“MI:0403”(colocalization)0.640
ZNF438PRMT7psi-mi:“MI:0915”(physical association)0.560
NFKBIDPRMT7psi-mi:“MI:0915”(physical association)0.560
POT1PRMT7psi-mi:“MI:0915”(physical association)0.370
ECE1PRMT7psi-mi:“MI:0915”(physical association)0.370
PRMT7H3-5psi-mi:“MI:0915”(physical association)0.370
PRMT7MNDApsi-mi:“MI:0915”(physical association)0.370
PRMT7ZBTB24psi-mi:“MI:0915”(physical association)0.370
PRMT7SSR3psi-mi:“MI:0914”(association)0.350
PIK3CGUTRNpsi-mi:“MI:0914”(association)0.350
rl10_rl10l_humanFBN2psi-mi:“MI:0914”(association)0.350
TAFA3FUOMpsi-mi:“MI:0914”(association)0.350
C1QTNF8VWA8psi-mi:“MI:0914”(association)0.350
EIF2S2TOR1Bpsi-mi:“MI:0914”(association)0.350
SMAD7PSMG1psi-mi:“MI:0914”(association)0.350
THAP8SNAP29psi-mi:“MI:0914”(association)0.350
EZREEF2Kpsi-mi:“MI:2364”(proximity)0.270

BioGRID (69): PRMT7 (Affinity Capture-MS), PRMT7 (Affinity Capture-MS), PRMT7 (Co-fractionation), SSR3 (Affinity Capture-MS), REPS2 (Affinity Capture-MS), GANAB (Affinity Capture-MS), ICE1 (Affinity Capture-MS), PRMT7 (Affinity Capture-MS), PRMT7 (Affinity Capture-MS), PRMT7 (Affinity Capture-MS), PRMT7 (Affinity Capture-MS), PRMT7 (Affinity Capture-MS), PRMT7 (Affinity Capture-MS), PRMT7 (Negative Genetic), PRMT7 (Proximity Label-MS)

ESM2 similar proteins: A0A1W2PQ27, A0A1W2PQ64, A0A1W2PQC6, A0A1W2PQD8, A0A1W2PQJ5, A0A1W2PR75, A2AV36, A4QN59, A6QQV6, D4A1F2, F1RA39, G5E8F4, J9SQF3, O00142, O42868, O55239, O95050, O95932, O97972, P0CR76, P0CR77, P10938, P40261, P40936, P53538, Q01841, Q22453, Q32LP9, Q4R7D0, Q566Y1, Q5M9G7, Q5RFR7, Q5U4E8, Q5XG58, Q62160, Q6C195, Q6CQ61, Q6DE00, Q6FMU7, Q6PCI6

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

0 interactions.

Disease & clinical

Clinical variants and AI predictions

ClinVar

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

ClassificationCount (floor)
Pathogenic21
Likely pathogenic20
Uncertain significance152
Likely benign104
Benign19

Top pathogenic / likely-pathogenic (30)

Variant IDHGVSClassification
1098280NM_019023.5(PRMT7):c.622del (p.Gln208fs)Pathogenic
1119980NM_019023.5(PRMT7):c.1097G>A (p.Cys366Tyr)Pathogenic
1323497NM_019023.5(PRMT7):c.98C>A (p.Ser33Ter)Pathogenic
2577129NM_019023.5(PRMT7):c.967C>T (p.Gln323Ter)Pathogenic
266020NM_019023.5(PRMT7):c.1276-1G>APathogenic
2754073NM_019023.5(PRMT7):c.847del (p.Asp283fs)Pathogenic
3069131NM_019023.5(PRMT7):c.1168C>T (p.Arg390Ter)Pathogenic
3236051NM_019023.5(PRMT7):c.1173C>G (p.Tyr391Ter)Pathogenic
3254663NM_019023.5(PRMT7):c.1678del (p.Glu560fs)Pathogenic
3366822NM_019023.5(PRMT7):c.477T>A (p.Tyr159Ter)Pathogenic
3651536NM_019023.5(PRMT7):c.194del (p.Lys65fs)Pathogenic
3775502NM_019023.5(PRMT7):c.82C>T (p.Gln28Ter)Pathogenic
3893271NM_019023.5(PRMT7):c.1105C>T (p.Gln369Ter)Pathogenic
427216NC_000016.9:g.68345747_68361056delPathogenic
4685006NM_019023.5(PRMT7):c.2008del (p.Tyr670fs)Pathogenic
522559NM_019023.5(PRMT7):c.431_432del (p.Glu144fs)Pathogenic
522593NM_019023.5(PRMT7):c.1239_1246dup (p.Val416fs)Pathogenic
523434NM_019023.5(PRMT7):c.1713C>A (p.Cys571Ter)Pathogenic
951784NM_019023.5(PRMT7):c.77del (p.Tyr26fs)Pathogenic
984615NM_019023.5(PRMT7):c.148C>T (p.Gln50Ter)Pathogenic
986005NM_019023.5(PRMT7):c.1402C>T (p.Gln468Ter)Pathogenic
1098281NM_019023.5(PRMT7):c.927G>T (p.Gln309His)Likely pathogenic
1305249NM_019023.5(PRMT7):c.391+5G>CLikely pathogenic
1332826NM_019023.5(PRMT7):c.457dup (p.Glu153fs)Likely pathogenic
1334191NM_019023.5(PRMT7):c.347T>A (p.Ile116Asn)Likely pathogenic
1693267NM_019023.5(PRMT7):c.1220G>A (p.Cys407Tyr)Likely pathogenic
1693268NM_019023.5(PRMT7):c.1323+2T>GLikely pathogenic
1878579NM_019023.5(PRMT7):c.1335_1338dup (p.His447Ter)Likely pathogenic
266022NM_019023.5(PRMT7):c.95G>C (p.Arg32Thr)Likely pathogenic
266023NM_019023.5(PRMT7):c.1159A>G (p.Arg387Gly)Likely pathogenic

SpliceAI

3801 predictions. Top by Δscore:

VariantEffectΔscore
16:68321463:G:GGdonor_gain1.0000
16:68337457:A:AGacceptor_gain1.0000
16:68337457:AGAG:Aacceptor_gain1.0000
16:68337458:G:GGacceptor_gain1.0000
16:68337458:GAGG:Gacceptor_gain1.0000
16:68345667:C:CAacceptor_gain1.0000
16:68345670:TTCA:Tacceptor_loss1.0000
16:68345672:CAGTG:Cacceptor_loss1.0000
16:68345673:A:AGacceptor_gain1.0000
16:68345673:AGT:Aacceptor_gain1.0000
16:68345673:AGTG:Aacceptor_gain1.0000
16:68345674:G:GAacceptor_gain1.0000
16:68345674:GT:Gacceptor_gain1.0000
16:68345674:GTG:Gacceptor_gain1.0000
16:68345674:GTGG:Gacceptor_gain1.0000
16:68345674:GTGGC:Gacceptor_gain1.0000
16:68345675:T:TAacceptor_gain1.0000
16:68345799:CCAG:Cdonor_loss1.0000
16:68345800:CAG:Cdonor_loss1.0000
16:68345801:AG:Adonor_loss1.0000
16:68345802:GG:Gdonor_loss1.0000
16:68345803:G:Adonor_loss1.0000
16:68345804:T:Adonor_loss1.0000
16:68346131:A:AGacceptor_gain1.0000
16:68346132:T:Gacceptor_gain1.0000
16:68346137:T:Aacceptor_gain1.0000
16:68346138:G:Aacceptor_gain1.0000
16:68346140:CCTA:Cacceptor_loss1.0000
16:68346141:CTAG:Cacceptor_loss1.0000
16:68346143:A:AGacceptor_gain1.0000

AlphaMissense

4591 scored. Top likely-pathogenic:

VariantProtein changeam_pathogenicity
16:68321461:G:CR44T0.999
16:68321462:A:CR44S0.999
16:68321462:A:TR44S0.999
16:68337498:A:TE144V0.999
16:68345687:T:AW314R0.999
16:68345687:T:CW314R0.999
16:68321443:T:CM38T0.998
16:68321452:A:TD41V0.998
16:68321461:G:TR44I0.998
16:68324753:T:AV68D0.998
16:68324756:T:CL69P0.998
16:68324777:G:AG76E0.998
16:68337507:A:TD147V0.998
16:68339885:T:AW282R0.998
16:68339885:T:CW282R0.998
16:68345675:T:AW310R0.998
16:68345675:T:CW310R0.998
16:68345689:G:CW314C0.998
16:68345689:G:TW314C0.998
16:68321444:G:AM38I0.997
16:68321444:G:CM38I0.997
16:68321444:G:TM38I0.997
16:68321451:G:CD41H0.997
16:68324692:T:GY48D0.997
16:68324765:G:AG72D0.997
16:68324771:G:AG74D0.997
16:68329090:G:CA103P0.997
16:68337489:T:CL141P0.997
16:68337516:T:CL150P0.997
16:68339338:T:AV174E0.997

dbSNP variants (sampled 300 via entrez): RS1000124069 (16:68355015 A>C), RS1000154493 (16:68341084 G>A,C), RS1000160210 (16:68311550 C>T), RS1000234417 (16:68309252 G>A), RS1000240434 (16:68320182 G>A), RS1000307455 (16:68335673 T>A), RS1000365002 (16:68351903 A>G), RS1000385968 (16:68346917 C>T), RS1000453835 (16:68341625 T>C), RS1000561467 (16:68324290 A>G), RS1000573334 (16:68360194 G>A), RS1000578104 (16:68318741 C>T), RS1000697778 (16:68350628 C>A,T), RS1000729382 (16:68356188 T>C), RS1000734892 (16:68319141 G>C)

Disease associations

OMIM: gene MIM:610087 | disease phenotypes: MIM:617157, MIM:619191

GenCC curated gene-disease

DiseaseClassificationInheritance
short stature-brachydactyly-obesity-global developmental delay syndromeStrongAutosomal recessive

Mondo (9): short stature-brachydactyly-obesity-global developmental delay syndrome (MONDO:0014944), fatty liver disease (MONDO:0004790), acanthosis nigricans (MONDO:0007035), obesity disorder (MONDO:0011122), skeletal dysplasia (MONDO:0018230), renal hypoplasia (MONDO:0019637), brachydactyly (MONDO:0021004), hyperlipidemia (MONDO:0021187), epilepsy, progressive myoclonic, 12 (MONDO:0030936)

Orphanet (6): Short stature-brachydactyly-obesity-global developmental delay syndrome (Orphanet:464288), Primary bone dysplasia (Orphanet:364526), Obesity due to melanocortin 4 receptor deficiency (Orphanet:71529), Renal hypoplasia (Orphanet:93101), NON RARE IN EUROPE: Acanthosis nigricans (Orphanet:924), NON RARE IN EUROPE: Non rare obesity (Orphanet:521399)

HPO phenotypes

89 total (30 of 89 shown, HPO-id order):

HPOTerm
HP:0000007Autosomal recessive inheritance
HP:0000010Recurrent urinary tract infections
HP:0000028Cryptorchidism
HP:0000076Vesicoureteral reflux
HP:0000089Renal hypoplasia
HP:0000212Gingival overgrowth
HP:0000218High palate
HP:0000233Thin vermilion border
HP:0000248Brachycephaly
HP:0000252Microcephaly
HP:0000272Malar flattening
HP:0000278Retrognathia
HP:0000286Epicanthus
HP:0000316Hypertelorism
HP:0000343Long philtrum
HP:0000384Preauricular skin tag
HP:0000407Sensorineural hearing impairment
HP:0000431Wide nasal bridge
HP:0000455Broad nasal tip
HP:0000457Depressed nasal ridge
HP:0000463Anteverted nares
HP:0000470Short neck
HP:0000483Astigmatism
HP:0000486Strabismus
HP:0000490Deeply set eye
HP:0000508Ptosis
HP:0000588Optic disc coloboma
HP:0000589Coloboma
HP:0000592Blue sclerae
HP:0000620Dacryocystitis

GWAS associations

13 associations (top):

StudyTraitp-value
GCST000756_2Magnesium levels2.000000e-06
GCST002783_278Body mass index4.000000e-07
GCST002783_633Body mass index1.000000e-06
GCST004904_185Body mass index3.000000e-08
GCST006249_87Serum metabolite levels6.000000e-11
GCST008152_39Weight4.000000e-07
GCST008362_60Birth weight7.000000e-06
GCST008362_61Birth weight1.000000e-08
GCST008363_126Offspring birth weight8.000000e-08
GCST008906_1Schizophrenia3.000000e-06
GCST010002_113Refractive error2.000000e-14
GCST012231_138A body shape index8.000000e-09
GCST012232_25Lipoprotein (a) levels3.000000e-12

EFO canonical traits (7, from GWAS)

EFO IDTrait name
EFO:0004845magnesium measurement
EFO:0004340body mass index
EFO:0004338body weight
EFO:0004344birth weight
EFO:0005939parental genotype effect measurement
EFO:0007789BMI-adjusted waist circumference
EFO:0006925lipoprotein A measurement

MeSH disease descriptors (4)

DescriptorNameTree numbers
D000052Acanthosis NigricansC17.800.621.430.530.100
D059327BrachydactylyC05.660.585.262; C16.131.621.585.262
D005234Fatty LiverC06.552.241
D006949HyperlipidemiasC18.452.584.500.500

Drugs & pharmacology

Drug and pharmacology data

Is drug target: yes

ChEMBL targets (1): CHEMBL3562175 (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 (1 total), top 1:

LigandActionAffinityParameter
DS-437Inhibition5.22pIC50

ChEMBL bioactivities

56 potent at pChembl≥5 of 68 total, top 50 by pChembl (potency: 10 = 0.1 nM, 6 = 1 µM).

pChemblTypeValueUnitMolecule
9.40IC500.4nMCHEMBL6103457
7.11IC5077nMCHEMBL5303356
6.96IC50110nMS-ADENOSYLHOMOCYSTEINE
6.66IC50220nMCHEMBL5206272
6.65IC50226nMCHEMBL5202088
6.53IC50294nMCHEMBL5562317
6.50IC50320nMCHEMBL5199380
6.50Kd320nMCHEMBL6132636
6.39IC50410nMCHEMBL5180108
6.31IC50491nMADEMETIONINE
6.30IC50500nMCHEMBL6132636
6.27IC50540nMCHEMBL5408585
6.26IC50550nMCHEMBL5170047
6.26IC50555nMCHEMBL5613785
6.21IC50610nMCHEMBL6149781
6.20IC50631nMCHEMBL5186617
6.03IC50940nMCHEMBL6170788
6.00IC501000nMCHEMBL538693
5.90IC501270nMCHEMBL6149873
5.78IC501680nMCHEMBL5173678
5.78IC501670nMCHEMBL6172522
5.73IC501850nMCHEMBL6142991
5.71IC501960nMCHEMBL6166289
5.68IC502100nMCHEMBL5561462
5.64IC502300nMCHEMBL5563222
5.62IC502400nMCHEMBL5560678
5.62IC502400nMCHEMBL5613745
5.62IC502400nMCHEMBL5094158
5.60IC502500nMCHEMBL5527953
5.60IC502500nMCHEMBL5185202
5.59IC502550nMCHEMBL6133309
5.59IC502580nMCHEMBL6143398
5.59IC502570nMCHEMBL6171993
5.58IC502630nMCHEMBL6168787
5.49IC503230nMCHEMBL6173686
5.47IC503410nMCHEMBL6150027
5.46IC503440nMCHEMBL6169590
5.42IC503810nMCHEMBL6145743
5.34IC504560nMCHEMBL6142311
5.33IC504680nMCHEMBL5191769
5.33IC504710nMCHEMBL6151762
5.30IC505000nMCHEMBL6134055
5.27IC505370nMCHEMBL6144701
5.26IC505490nMCHEMBL6168599
5.25IC505600nMCHEMBL5396270
5.22IC506000nMCHEMBL3577854
5.15Kd7120nMCHEMBL6134055
5.13IC507490nMCHEMBL6171072
5.12IC507500nMCHEMBL2169919
5.10IC507980nMCHEMBL6152768

PubChem BioAssay actives

26 with measured affinity, of 143 total; 24 most potent distinct compounds. Largely complementary to BindingDB; screening values are coarse (µM, 4 dp), so sub-nM hits tie at the floor.

CompoundAssayTypeValueUnit
(2R,3R,4S,5S)-2-(6-aminopurin-9-yl)-5-[4-[[4-(4-chlorophenyl)phenyl]methylamino]butylsulfanylmethyl]oxolane-3,4-diol2074379: Inhibition of full-length PRMT7 (unknown origin) expressed in Sf9 cells using biotinylated H2B as substrate incubated for 60 mins in presence of 3H-SAM by Topcount plate reader analysisic500.0025uM
(2R,3R,4S,5S)-2-(6-aminopurin-9-yl)-5-[4-[[3-(4-chlorophenyl)phenyl]methylamino]butylsulfanylmethyl]oxolane-3,4-diol1882377: Inhibition of PRMT7 (unknown origin)ic500.0025uM
(2R,3R,4S,5S)-2-(6-aminopurin-9-yl)-5-[3-[(4-phenylphenyl)methylamino]propylsulfanylmethyl]oxolane-3,4-diol2074379: Inhibition of full-length PRMT7 (unknown origin) expressed in Sf9 cells using biotinylated H2B as substrate incubated for 60 mins in presence of 3H-SAM by Topcount plate reader analysisic500.0025uM
(2S)-2-amino-4-[[(2S,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methylsulfanyl]butanoic acid1689511: Inhibition of recombinant human PRMT7 using GST-GAR as substrate by hotspot assayic500.1100uM
methyl 6-[5-[[N’-[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl]carbamimidoyl]amino]pentylcarbamoylamino]-4-hydroxynaphthalene-2-carboxylate1883074: Inhibition of human full length recombinant his-tagged PRMT7 (2 to 692 residues) using GST-GAR as substrate incubated for 20 mins in presence of [3H]-SAM by radioisotope-based filter assayic500.2200uM
methyl 6-[4-[[amino-[2-[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]ethylamino]methylidene]amino]butylcarbamoylamino]-4-hydroxynaphthalene-2-carboxylate1883074: Inhibition of human full length recombinant his-tagged PRMT7 (2 to 692 residues) using GST-GAR as substrate incubated for 20 mins in presence of [3H]-SAM by radioisotope-based filter assayic500.2260uM
methyl 6-[3-[[N’-[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl]carbamimidoyl]amino]propylcarbamoylamino]-4-hydroxynaphthalene-2-carboxylate1883074: Inhibition of human full length recombinant his-tagged PRMT7 (2 to 692 residues) using GST-GAR as substrate incubated for 20 mins in presence of [3H]-SAM by radioisotope-based filter assayic500.3200uM
methyl 7-[6-[[N’-[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl]carbamimidoyl]amino]hexylcarbamoylamino]-4-hydroxynaphthalene-2-carboxylate1883074: Inhibition of human full length recombinant his-tagged PRMT7 (2 to 692 residues) using GST-GAR as substrate incubated for 20 mins in presence of [3H]-SAM by radioisotope-based filter assayic500.4100uM
methyl 6-[2-[[N’-[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl]carbamimidoyl]amino]ethylcarbamoylamino]-4-hydroxynaphthalene-2-carboxylate2012350: Inhibition of N-terminal/C-terminal His-tagged human recombinant full-length PRMT7 (2 to 692 residues) using histone GST-GAR as substrate and 3H-SAM as cosubstrate incubated for 60 mins by scintillation counter analysisic500.5400uM
methyl 6-[4-[[N’-[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl]carbamimidoyl]amino]butylcarbamoylamino]-4-hydroxynaphthalene-2-carboxylate1883074: Inhibition of human full length recombinant his-tagged PRMT7 (2 to 692 residues) using GST-GAR as substrate incubated for 20 mins in presence of [3H]-SAM by radioisotope-based filter assayic500.5500uM
2-[2-[[(2S,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methylsulfanyl]ethyl]-1-(2-bromophenyl)guanidine2127585: Inhibition of PRMT7 (unknown origin)ic500.5550uM
methyl 6-[7-[[N’-[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl]carbamimidoyl]amino]heptylcarbamoylamino]-4-hydroxynaphthalene-2-carboxylate1883074: Inhibition of human full length recombinant his-tagged PRMT7 (2 to 692 residues) using GST-GAR as substrate incubated for 20 mins in presence of [3H]-SAM by radioisotope-based filter assayic500.6310uM
(2S,3S,4R,5R)-2-(3-aminopropylsulfanylmethyl)-5-(6-aminopurin-9-yl)oxolane-3,4-diol2074379: Inhibition of full-length PRMT7 (unknown origin) expressed in Sf9 cells using biotinylated H2B as substrate incubated for 60 mins in presence of 3H-SAM by Topcount plate reader analysisic501.0000uM
methyl 6-[4-[[N’-[(E)-3-[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]prop-2-enyl]carbamimidoyl]amino]butylcarbamoylamino]-4-hydroxynaphthalene-2-carboxylate1883074: Inhibition of human full length recombinant his-tagged PRMT7 (2 to 692 residues) using GST-GAR as substrate incubated for 20 mins in presence of [3H]-SAM by radioisotope-based filter assayic501.6800uM
7-N-[5-fluoro-2-(3,4,5-trimethoxyphenyl)pyrimidin-4-yl]-3-methylnaphthalene-1,7-diamine2074382: Inhibition of PRMT7 (unknown origin)ic502.1000uM
7-N-[2-(1,3-benzodioxol-5-yl)-5-fluoropyrimidin-4-yl]-3-methylnaphthalene-1,7-diamine2074382: Inhibition of PRMT7 (unknown origin)ic502.3000uM
7-N-[2-(1-benzofuran-2-yl)-5-fluoropyrimidin-4-yl]-3-methylnaphthalene-1,7-diamine2074382: Inhibition of PRMT7 (unknown origin)ic502.4000uM
2-[2-[[(2S,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methylsulfanyl]ethyl]-1-phenylguanidine2127552: Inhibition of human PRMT7 using GST-GAR as substrate and SAM as cofactor by radiometric HotSpot assayic502.4000uM
7-N-[2-(2,3-dihydro-1,4-benzodioxin-6-yl)-5-fluoropyrimidin-4-yl]-3-methylnaphthalene-1,7-diamine2074382: Inhibition of PRMT7 (unknown origin)ic502.5000uM
methyl 6-[4-[[N’-[3-[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]propyl]carbamimidoyl]amino]butylcarbamoylamino]-4-hydroxynaphthalene-2-carboxylate1883074: Inhibition of human full length recombinant his-tagged PRMT7 (2 to 692 residues) using GST-GAR as substrate incubated for 20 mins in presence of [3H]-SAM by radioisotope-based filter assayic504.6800uM
methyl 6-[3-[[N’-[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl]carbamimidoyl]amino]propylcarbamoylamino]-4-hydroxy-8-(trifluoromethyl)naphthalene-2-carboxylate2012350: Inhibition of N-terminal/C-terminal His-tagged human recombinant full-length PRMT7 (2 to 692 residues) using histone GST-GAR as substrate and 3H-SAM as cosubstrate incubated for 60 mins by scintillation counter analysisic505.6000uM
1-[2-[[(2S,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methylsulfanyl]ethyl]-3-ethylurea1226186: Inhibition of human full length PRMT7 expressed in Sf9 cells assessed as inhibition of H2B[23-37] methylationic506.0000uM
1-[3-[[(2R,3S,4R,5R)-5-(4-aminopyrrolo[2,3-d]pyrimidin-7-yl)-3,4-dihydroxyoxolan-2-yl]methyl-propan-2-ylamino]propyl]-3-(4-tert-butylphenyl)urea1226183: Inhibition of human full length PRMT7 expressed in Sf9 cellsic507.5000uM
(2S)-2-[[(2S)-5-amino-2-[[2-[[(2S)-2-amino-5-(diaminomethylideneamino)pentanoyl]amino]acetyl]amino]pentanoyl]amino]-5-[[N’-[3-[[(2S,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methylsulfanyl]propyl]carbamimidoyl]amino]pentanoic acid2127552: Inhibition of human PRMT7 using GST-GAR as substrate and SAM as cofactor by radiometric HotSpot assayic508.3000uM

CTD chemical–gene interactions

25 total (human), top 25 by PubMed support.

ChemicalActions (top 5)PubMed papers
sodium arseniteaffects expression, decreases expression, increases expression3
Ribavirindecreases expression2
pirinixic acidaffects binding, decreases expression, increases activity1
tris(1,3-dichloro-2-propyl)phosphatedecreases expression1
jinfukangincreases expression1
NSC 689534affects binding, decreases expression1
Resveratrolaffects cotreatment, increases expression1
Leflunomidedecreases expression1
Atrazinedecreases expression1
Berberineincreases expression1
Copperaffects binding, decreases expression1
Dichlorodiphenyl Dichloroethyleneincreases expression1
Doxorubicindecreases expression1
Estradiolaffects cotreatment, affects expression1
Plant Extractsaffects cotreatment, increases expression1
Progesteroneaffects expression, affects cotreatment1
S-Adenosylhomocysteinedecreases activity1
Silicon Dioxidedecreases methylation1
Tetrachlorodibenzodioxinaffects expression1
Thiramdecreases expression1
8-Bromo Cyclic Adenosine Monophosphatedecreases expression1
Cyclosporinedecreases expression1
Aflatoxin B1increases methylation1
Cadmium Chloridedecreases expression1
Copper Sulfatedecreases expression1

ChEMBL screening assays

100 unique, capped per target: 98 binding, 2 functional

Representative assays (with source publication via chembl_document):

Assay IDTypeDescriptionSource paper
CHEMBL3578932BindingInhibition of human full length PRMT7 expressed in Sf9 cellsDiscovery of a Dual PRMT5-PRMT7 Inhibitor. — ACS Med Chem Lett
CHEMBL5445483FunctionalAffinity Phenotypic Cellular interaction: (HSP70 monomethylation in C2C12 cells) EUB0000236b PRMT7Affinity 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_B7YWAbcam Raji PRMT7 KOCancer cell lineMale
CVCL_B9ZMAbcam THP-1 PRMT7 KOCancer cell lineMale
CVCL_C7BBAbcam PC-3 PRMT7 KOCancer cell lineMale

Clinical trials (associated diseases)

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

TrialPhaseStatusTitle
NCT00160407PHASE4COMPLETEDOrlistat (Xenical) in the Treatment of Overweight Patients With Nonalcoholic Steatohepatitis (NASH)
NCT00207311PHASE4COMPLETEDStudy for the Treatment of Significant Steatosis With Xenical Followed by Treatment of Hepatitis C With Pegasys/Copegus
NCT00274495PHASE4TERMINATEDAssessing the Efficacy and Safety of Rosiglitazone Added to Standard Therapy for Hepatitis C Genotype 1 With Fatty Liver
NCT00736385PHASE4TERMINATEDMetformin for the Treatment of Nonalcoholic Fatty Liver Disease (NAFLD)
NCT00742326PHASE4TERMINATEDPioglitazone to Treat Fatty Liver in Patients With HIV and Hepatitis C Infections
NCT01720719PHASE4UNKNOWNAtorvastatin Versus Vitamin E in Treatment of Non-alcoholic Fatty Liver Disease
NCT01761318PHASE4COMPLETEDEffect of Liraglutide on Cardiovascular Endpoints in Diabetes Mellitus Type 2 Patients
NCT02102646PHASE4COMPLETEDMRI Substudy; Metabolic Changes Due to Iatrogenic Hypogonadism
NCT02210715PHASE4COMPLETEDRaltegravir-based Antiretroviral Versus Maintaining Any Other Antiretroviral Therapy in HIV Mono-infected Patients
NCT02660047PHASE4COMPLETEDEffect of Liraglutide on Cardiovascular Endpoints in Diabetes Mellitus Type 2 Patients of South Asian Descent
NCT02669641PHASE4UNKNOWNComplex Imaging Assessment of Steatosis
NCT03374358PHASE4COMPLETEDEffect on Liver Fat and Metabolic Parameters When Switching a Protease Inhibitor or Efavirenz to Raltegravir
NCT03646292PHASE4COMPLETEDAntidiabetic Drugs for Steatotic Liver Disease
NCT03851627PHASE4RECRUITINGEffects of Testosterone Undecanoate vs Placebo on Intrahepatic Fat Content in Overweight/Obese Men With T2DM or Prediabetes and Hypogonadism
NCT05898841PHASE4COMPLETEDStudy to Evaluate the Efficacy and Safety of a Rilpivarine-based Antiretroviral Tratment Regimen in HIV- Infected Patients With Liver Metabolic Disease Who Maintain Udetectable HIV Viral Load
NCT06989723PHASE4RECRUITINGPioglitazone and Empagliflozin for Fatty Liver Disease in Type 2 Diabetes
NCT02438020PHASE4UNKNOWNStudy of Efficacy of Metformin in the Treatment of Acanthosis Nigricans in Children With Obesity
NCT00076362PHASE4COMPLETEDPediatric Hypothalamic Obesity
NCT00079547PHASE4COMPLETEDThe Safety and Effectiveness of Low and High Carbohydrate Diets
NCT00115063PHASE4TERMINATEDLOSS- Louisiana Obese Subjects Study
NCT00134303PHASE4COMPLETEDTrial Comparing Metformin Versus Placebo in Non Alcoholic Steatohepatitis (NASH) Patients Receiving Bariatric Surgery for Obesity
NCT00143936PHASE4COMPLETEDThe Safety and Efficacy of Low and High Carbohydrate Diets
NCT00143962PHASE4COMPLETEDComparison of Two Approaches to Weight Loss Follow-Up Study
NCT00152360PHASE4COMPLETEDThe Effect of Xenical on Weight and Risk Factors
NCT00176306PHASE4COMPLETEDLevofloxacin Pharmacokinetics (PK) in the Severely Obese
NCT00203450PHASE4COMPLETEDZonegran for the Treatment of Weight Gain Associated With Psychotropic Medication Use: A Placebo-Controlled Trial
NCT00205504PHASE4COMPLETEDOral Contraceptives in the Metabolic Syndrome
NCT00229229PHASE4TERMINATEDComparison of 4 Diets in the Management of Overweight Patients With Vascular Disease
NCT00234988PHASE4COMPLETEDA Phase IV, Multi-Center, Open-Label Trial of Sibutramine in Combination With a Hypocaloric Diet in Obese and Overweight Thai Subjects.
NCT00264589PHASE4COMPLETEDExercise Training and Cardiovascular Function in Obesity and in Type 2 Diabetes
NCT00288873PHASE4COMPLETEDCharacterization of Hyperparathyroidism and Vitamin D Deficiency in Obesity
NCT00298857PHASE4TERMINATEDA Pharmacokinetic Study to Compare the Dosing of Valproic Acid in Subjects With Different Body Weights
NCT00315146PHASE4COMPLETEDOptimizing Body Composition for Function in Older Adults
NCT00319202PHASE4TERMINATEDClinical Trial to Assess the Effects of Candesartan on the Carbohydrate Metabolism of Obese Subjects
NCT00327912PHASE4UNKNOWNLaparoscopic Roux-en-Y Gastric Bypass Versus Laparoscopic Biliopancreatic Diversion (BPD)- Duodenal Switch for Superobesity
NCT00352287PHASE4COMPLETEDStudy to Determine the Effects of Human Growth Hormone and Pioglitazone in Overweight, Prediabetic Adults
NCT00353054PHASE4COMPLETEDEffect of Calcium/Vitamin D Supplementation on Body Weight and Fat Loss.
NCT00390637PHASE4COMPLETEDDiet, Obesity and Genes (DiOGenes)
NCT00415688PHASE4COMPLETEDLifestyle Modification for Obesity-Related Type 2 Diabetes
NCT00433641PHASE4COMPLETEDWeight Loss in Response to Sibutramine (MERIDIA) is Influenced by the Inherited Genes