PRMT3

Protein-coding gene in the species Homo sapiens
PRMT3
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2FYT, 3SMQ, 4HSG, 4QQN, 4RYL

Identifiers
AliasesPRMT3, HRMT1L3, protein arginine methyltransferase 3
External IDsOMIM: 603190; MGI: 1919224; HomoloGene: 24255; GeneCards: PRMT3; OMA:PRMT3 - orthologs
Gene location (Human)
Chromosome 11 (human)
Chr.Chromosome 11 (human)[1]
Chromosome 11 (human)
Genomic location for PRMT3
Genomic location for PRMT3
Band11p15.1Start20,387,558 bp[1]
End20,509,338 bp[1]
Gene location (Mouse)
Chromosome 7 (mouse)
Chr.Chromosome 7 (mouse)[2]
Chromosome 7 (mouse)
Genomic location for PRMT3
Genomic location for PRMT3
Band7|7 B4Start49,428,094 bp[2]
End49,508,013 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • ventricular zone

  • Achilles tendon

  • gonad

  • gingival epithelium

  • gastrocnemius muscle

  • left lobe of thyroid gland

  • germinal epithelium

  • right lobe of thyroid gland

  • islet of Langerhans

  • C1 segment
Top expressed in
  • genital tubercle

  • tail of embryo

  • condyle

  • cumulus cell

  • fossa

  • substantia nigra

  • Paneth cell

  • primitive streak

  • endothelial cell of lymphatic vessel

  • epiblast
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • metal ion binding
  • methyltransferase activity
  • transferase activity
  • protein binding
  • protein-arginine N-methyltransferase activity
  • nucleic acid binding
  • histone-arginine N-methyltransferase activity
  • protein-arginine omega-N asymmetric methyltransferase activity
  • ribosome binding
Cellular component
  • ribosome
  • cytoplasm
  • cytosol
  • nucleus
Biological process
  • methylation
  • negative regulation of protein ubiquitination
  • peptidyl-arginine N-methylation
  • protein methylation
  • regulation of transcription, DNA-templated
  • peptidyl-arginine methylation, to asymmetrical-dimethyl arginine
  • histone arginine methylation
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

10196

71974

Ensembl

ENSG00000185238

ENSMUSG00000030505

UniProt

O60678

Q922H1

RefSeq (mRNA)

NM_001145166
NM_001145167
NM_005788

NM_133740

RefSeq (protein)

NP_001138638
NP_001138639
NP_005779

NP_598501

Location (UCSC)Chr 11: 20.39 – 20.51 MbChr 7: 49.43 – 49.51 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Protein arginine N-methyltransferase 3 is an enzyme that in humans is encoded by the PRMT3 gene.[5][6]

Interactions

PRMT3 has been shown to interact with RPS2.[7]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000185238 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000030505 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Tang J, Gary JD, Clarke S, Herschman HR (July 1998). "PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation". The Journal of Biological Chemistry. 273 (27): 16935–45. doi:10.1074/jbc.273.27.16935. PMID 9642256.
  6. ^ "Entrez Gene: PRMT3 protein arginine methyltransferase 3".
  7. ^ Choi S, Jung CR, Kim JY, Im DS (September 2008). "PRMT3 inhibits ubiquitination of ribosomal protein S2 and together forms an active enzyme complex". Biochimica et Biophysica Acta (BBA) - General Subjects. 1780 (9): 1062–9. doi:10.1016/j.bbagen.2008.05.010. PMID 18573314.

Further reading

  • Singh V, Miranda TB, Jiang W, Frankel A, Roemer ME, Robb VA, et al. (October 2004). "DAL-1/4.1B tumor suppressor interacts with protein arginine N-methyltransferase 3 (PRMT3) and inhibits its ability to methylate substrates in vitro and in vivo". Oncogene. 23 (47): 7761–71. doi:10.1038/sj.onc.1208057. PMID 15334060.
  • Bachand F, Silver PA (July 2004). "PRMT3 is a ribosomal protein methyltransferase that affects the cellular levels of ribosomal subunits". The EMBO Journal. 23 (13): 2641–50. doi:10.1038/sj.emboj.7600265. PMC 449775. PMID 15175657.
  • Smith JJ, Rücknagel KP, Schierhorn A, Tang J, Nemeth A, Linder M, et al. (May 1999). "Unusual sites of arginine methylation in Poly(A)-binding protein II and in vitro methylation by protein arginine methyltransferases PRMT1 and PRMT3". The Journal of Biological Chemistry. 274 (19): 13229–34. doi:10.1074/jbc.274.19.13229. PMID 10224081.
  • v
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  • 1f3l: CRYSTAL STRUCTURE OF THE CONSERVED CORE OF PROTEIN ARGININE METHYLTRANSFERASE PRMT3
    1f3l: CRYSTAL STRUCTURE OF THE CONSERVED CORE OF PROTEIN ARGININE METHYLTRANSFERASE PRMT3
  • 1wir: Solution structure of the C2H2 zinc finger domain of the protein arginine N-methyltransferase 3 from Mus musculus
    1wir: Solution structure of the C2H2 zinc finger domain of the protein arginine N-methyltransferase 3 from Mus musculus
  • 2fyt: Human HMT1 hnRNP methyltransferase-like 3 (S. cerevisiae) protein
    2fyt: Human HMT1 hnRNP methyltransferase-like 3 (S. cerevisiae) protein
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