Version 5.4
Mus musculus Gene: Prmt3
Summary
InnateDB Gene IDBG-188018.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Prmt3
Gene Name protein arginine N-methyltransferase 3
Synonyms 2010005E20Rik; 2410018A17Rik; AL033309; Hrmt1l3
Species Mus musculus
Ensembl Gene ENSMUSG00000030505
Encoded Proteins
IDBP-188020
protein arginine N-methyltransferase 3
IDBP-534434
protein arginine N-methyltransferase 3
IDBP-532981
protein arginine N-methyltransferase 3
IDBP-542288
protein arginine N-methyltransferase 3
IDBP-540406
protein arginine N-methyltransferase 3
Protein Structure
Useful resources Stemformatics EHFPI ImmGen
Entrez Gene
Summary This gene does not have any Entrez summary - the following is the summary from its human ortholog ENSG00000185238:
Type I protein arginine N-methyltransferases (PRMTs), such as PRMT3, catalyze the formation of asymmetric N(G),N(G)-dimethylarginine (ADMA) residues in proteins (Tang et al., 1998 [PubMed 9642256]).[supplied by OMIM, Mar 2008]
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. [provided by RefSeq, Aug 2013]
Gene Information
Type Protein coding
Genomic Location Chromosome 7:49778346-49858265
Strand Forward strand
Band B4
Transcripts
ENSMUST00000032715 ENSMUSP00000032715
ENSMUST00000140656 ENSMUSP00000124114
ENSMUST00000147401 ENSMUSP00000115155
ENSMUST00000152127
ENSMUST00000148996
ENSMUST00000145666
ENSMUST00000146052 ENSMUSP00000117241
ENSMUST00000130907 ENSMUSP00000114676
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 1 experimentally validated interaction(s) in this database.
They are also associated with 10 interaction(s) predicted by orthology.
Experimentally validated
Total 1 [view]
Protein-Protein 1 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 10 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0005515 protein binding
GO:0008168 methyltransferase activity
GO:0008276 protein methyltransferase activity
GO:0008469 histone-arginine N-methyltransferase activity
GO:0016274 protein-arginine N-methyltransferase activity
GO:0016740 transferase activity
GO:0035242 protein-arginine omega-N asymmetric methyltransferase activity
GO:0046872 metal ion binding
GO:0072341 modified amino acid binding
Biological Process
GO:0006355 regulation of transcription, DNA-templated
GO:0006479 protein methylation
GO:0008152 metabolic process
GO:0018216 peptidyl-arginine methylation
GO:0019919 peptidyl-arginine methylation, to asymmetrical-dimethyl arginine
GO:0031397 negative regulation of protein ubiquitination
GO:0034969 histone arginine methylation
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005840 ribosome
Orthologs
Species
Homo sapiens
Bos taurus
Gene ID
Gene Order
ENSG00000185238
View Gene Order
ENSBTAG00000013421
Not yet available
Cross-References
SwissProt
TrEMBL
UniProt Splice Variant
Entrez Gene
UniGene Mm.397402
RefSeq NM_133740
OMIM
CCDS CCDS21307
HPRD
IMGT
MGI ID
MGI Symbol
EMBL
GenPept
RNA Seq Atlas

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca