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PRMT7

Chr 16q22.1

protein arginine methyltransferase 7

Aliases:
FLJ10640, KIAA1933
MANE:
ENST00000441236.3

Annotations refreshed 11 hours ago.

Predicted protein structure

Clinical relevance (Genomics England PanelApp)

Diagnostic Grade (Green)

  • DDG2P

    BIALLELIC, autosomal or pseudoautosomal
  • Early onset or syndromic epilepsy

    BIALLELIC, autosomal or pseudoautosomal
  • Fetal anomalies

    BIALLELIC, autosomal or pseudoautosomal
  • Intellectual disability

    BIALLELIC, autosomal or pseudoautosomal
  • Limb disorders

    BIALLELIC, autosomal or pseudoautosomal
  • Skeletal dysplasia

    BIALLELIC, autosomal or pseudoautosomal

Disease associations (Open Targets)

  • short stature-brachydactyly-obesity-global developmental delay syndrome

    0.80
  • hereditary disease

    0.51
  • Obesity

    0.43
  • brachydactyly

    0.43
  • Short stature

    0.43
  • Lumbar hyperlordosis

    0.43
  • Short metacarpal

    0.43
  • Hepatic steatosis

    0.43
  • Severe intellectual disability

    0.43
  • skeletal dysplasia

    0.43

Score is the Open Targets composite evidence score (0-1). Higher = stronger gene-disease association.

Protein function (UniProt)

Protein arginine N-methyltransferase 7

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

Data sources: HGNC (CC BY 4.0), AlphaFold (CC BY 4.0, Jumper et al. Nature 2021), Genomics England PanelApp (CC BY 4.0), ClinGen, Open Targets (CC0), UniProt.

Not for sole clinical decision-making. Always verify against primary sources.