Version 5.4
Homo sapiens Gene: PRMT3
Summary
InnateDB Gene IDBG-35890.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol PRMT3
Gene Name protein arginine methyltransferase 3
Synonyms HRMT1L3
Species Homo sapiens
Ensembl Gene ENSG00000185238
Encoded Proteins
IDBP-35892
protein arginine methyltransferase 3
IDBP-35894
protein arginine methyltransferase 3
IDBP-369441
protein arginine methyltransferase 3
IDBP-590405
protein arginine methyltransferase 3
IDBP-600757
protein arginine methyltransferase 3
Protein Structure
Useful resources Stemformatics EHFPI ImmGen
Entrez Gene
Summary 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 11:20387530-20509294
Strand Forward strand
Band p15.1
Transcripts
ENST00000330796 ENSP00000329586
ENST00000331079 ENSP00000331879
ENST00000437750 ENSP00000397766
ENST00000525188 ENSP00000435151
ENST00000526583 ENSP00000434260
ENST00000529592
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 36 experimentally validated interaction(s) in this database.
Experimentally validated
Total 36 [view]
Protein-Protein 36 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
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
Mus musculus
Bos taurus
Gene ID
Gene Order
ENSMUSG00000030505
View Gene Order
ENSBTAG00000013421
Not yet available
Cross-References
SwissProt O60678
TrEMBL E9PLF6 E9PRB4
UniProt Splice Variant
Entrez Gene 10196
UniGene Hs.152337 Hs.701002
RefSeq NM_001145166 NM_001145167 NM_005788
HUGO HGNC:30163
OMIM 603190
CCDS CCDS44554 CCDS7853
HPRD
IMGT
EMBL AC025972 AC108005 AF059531 AK300591 BC037544 BC064831
GenPept AAC39837 AAH37544 AAH64831 BAG62289
RNA Seq Atlas 10196

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