Protein arginine methyltransferase 1

mammalian protein found in Homo sapiens
Protein protein Q21201642
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Summary

Protein arginine methyltransferase 1 is a protein[1]. It is known by 7 alternative names across languages and contexts.[2]

Key Facts

  • Subclass of: protein[3]
  • Part of: S-adenosyl-L-methionine-dependent methyltransferase[4], Protein arginine N-methyltransferase[5]
  • EC enzyme number: 2.1.1.321[6]
  • Molecular function: methyltransferase activity[7], histone methyltransferase activity[8], transferase activity[9], histone methyltransferase activity (H4-R3 specific)[10], methyl-CpG binding[11], mitogen-activated protein kinase p38 binding[12], protein binding[13], identical protein binding[14], enzyme binding[15], N-methyltransferase activity[16], protein-arginine omega-N asymmetric methyltransferase activity[17], RNA binding[18], protein methyltransferase activity[19], protein-arginine N-methyltransferase activity[20]
  • Cell component: cytoplasm[21], nucleoplasm[22], methylosome[23], nucleus[24], cytosol[25]
  • Biological process: positive regulation of p38MAPK cascade[26], positive regulation of hemoglobin biosynthetic process[27], histone H4-R3 methylation[28], positive regulation of erythrocyte differentiation[29], negative regulation of megakaryocyte differentiation[30], cell surface receptor signaling pathway[31], methylation[32], peptidyl-arginine methylation[33], histone methylation[34], neuron projection development[35], peptidyl-arginine N-methylation[36], peptidyl-arginine methylation, to asymmetrical-dimethyl arginine[37], DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest[38], regulation of transcription, DNA-templated[39]
  • Encoded by: PRMT1[40]
  • Found in taxon: Homo sapiens[41]

References

Programmatic citations — every numbered marker resolves to a verifiable graph row below.

Direct Wikidata claims

  1. [3] ↑ . UniProt. Retrieved . wikidata.org.
  2. [4] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  3. [5] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  4. [6] ↑ . ENZYME. Retrieved . wikidata.org.
  5. [7] ↑ . Identification and Characterization of Two Putative Human Arginine Methyltransferases (HRMT1L1 and HRMT1L2). Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  6. [8] ↑ . Kinetic analysis of human protein arginine N-methyltransferase 2: formation of monomethyl- and asymmetric dimethyl-arginine residues on histone H4. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  7. [9] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  8. [10] ↑ . 5-Hydroxymethylcytosine Plays a Critical Role in Glioblastomagenesis by Recruiting the CHTOP-Methylosome Complex. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  9. [11] ↑ . 5-Hydroxymethylcytosine Plays a Critical Role in Glioblastomagenesis by Recruiting the CHTOP-Methylosome Complex. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  10. [12] ↑ . Protein Arginine Methyltransferase 1 Interacts with and Activates p38α to Facilitate Erythroid Differentiation. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  11. [13] ↑ . PRMT1 mediated methylation of TAF15 is required for its positive gene regulatory function. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [14] ↑ . A proteome-scale map of the human interactome network. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [15] ↑ . Arginine methylation of ribosomal protein S3 affects ribosome assembly. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [16] ↑ . A protein-arginine methyltransferase binds to the intracytoplasmic domain of the IFNAR1 chain in the type I interferon receptor. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [17] ↑ . 5-Hydroxymethylcytosine Plays a Critical Role in Glioblastomagenesis by Recruiting the CHTOP-Methylosome Complex. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [18] ↑ . The mRNA-Bound Proteome and Its Global Occupancy Profile on Protein-Coding Transcripts. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [19] ↑ . FAM98A associates with DDX1-C14orf166-FAM98B in a novel complex involved in colorectal cancer progression.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [20] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [21] ↑ . A protein-arginine methyltransferase binds to the intracytoplasmic domain of the IFNAR1 chain in the type I interferon receptor. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [22] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [23] ↑ . 5-Hydroxymethylcytosine Plays a Critical Role in Glioblastomagenesis by Recruiting the CHTOP-Methylosome Complex. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [24] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [25] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [26] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [27] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  26. [28] ↑ . Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by the nuclear receptor coactivator PRMT1. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  27. [29] ↑ . Protein Arginine Methyltransferase 1 Interacts with and Activates p38α to Facilitate Erythroid Differentiation. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  28. [30] ↑ . Protein-arginine methyltransferase 1 suppresses megakaryocytic differentiation via modulation of the p38 MAPK pathway in K562 cells. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  29. [31] ↑ . A protein-arginine methyltransferase binds to the intracytoplasmic domain of the IFNAR1 chain in the type I interferon receptor. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  30. [32] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  31. [33] ↑ . Cross-talk between PRMT1-mediated methylation and ubiquitylation on RBM15 controls RNA splicing.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  32. [34] ↑ . Kinetic analysis of human protein arginine N-methyltransferase 2: formation of monomethyl- and asymmetric dimethyl-arginine residues on histone H4. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  33. [35] ↑ . PRMT1 and Btg2 regulates neurite outgrowth of Neuro2a cells. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  34. [36] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  35. [37] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  36. [38] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  37. [39] ↑ . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  38. [40] ↑ . UniProt. Retrieved . wikidata.org.
  39. [41] ↑ . UniProt. Retrieved . wikidata.org.

Class ancestry

  1. [1] ↑ . Wikidata. wikidata.org.

Aggregate / graph-position facts

  1. [2] ↑ . Wikidata aliases. wikidata.org.

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Edit History

Rolling log of changes to this entity's Wikidata record. Values shown reflect the current state of each edited property — follow the history link to see the precise diff for any edit.

  1. 13w ago · Boghog · 2026-07-24 view diff on Wikidata ↗
    Ec enzyme number → 2.1.1.321
    Imported from → —
    Wikidata description → mammalian protein found in Homo sapiens
    Encoded by → PRMT1
    + 10 other properties edited (see Wikidata diff for full list)
    "/* wbcreateclaim-create:1| */ Ec enzyme number: 2.1.1.319, [[:toollabs:quickstatements/#/batch/261491|batch #261491]]"
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