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rmt1 protein arginine N-methyltransferase Rmt1 [ Schizosaccharomyces pombe (fission yeast) ]

Gene ID: 2543492, updated on 18-Sep-2024

Summary

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Official Symbol
rmt1
Official Full Name
protein arginine N-methyltransferase Rmt1
Primary source
PomBase:SPAC890.07c
Locus tag
SPOM_SPAC890.07C
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Schizosaccharomyces pombe (strain: 972h-)
Lineage
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces
Also known as
prmt1
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Genomic context

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See rmt1 in Genome Data Viewer
Location:
chromosome: I
Exon count:
9
Sequence:
Chromosome: I; NC_003424.3 (5015959..5017919, complement)

Chromosome I - NC_003424.3Genomic Context describing neighboring genes Neighboring gene ncRNA Neighboring gene ncRNA Neighboring gene nucleoporin, WD repeat Nup155 Neighboring gene ncRNA Neighboring gene ncRNA Neighboring gene 60S ribosomal protein eL31

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_003424.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. A proline-tyrosine nuclear localization signal (PY-NLS) is required for the nuclear import of fission yeast PAB2, but not of human PABPN1. Mallet PL, et al. Traffic, 2013 Mar. PMID 23279110
  2. PRMT3 is a ribosomal protein methyltransferase that affects the cellular levels of ribosomal subunits. Bachand F, et al. EMBO J, 2004 Jul 7. PMID 15175657, Free PMC Article
  3. Regulation of the nuclear poly(A)-binding protein by arginine methylation in fission yeast. Perreault A, et al. J Biol Chem, 2007 Mar 9. PMID 17213188
  4. Genetic interactions and functional analyses of the fission yeast gsk3 and amk2 single and double mutants defective in TORC1-dependent processes. Rallis C, et al. Sci Rep, 2017 Mar 10. PMID 28281664, Free PMC Article
  5. ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe. Matsuyama A, et al. Nat Biotechnol, 2006 Jul. PMID 16823372

See all (11) citations in PubMed

GeneRIFs: Gene References Into Functions

Pathways from PubChem

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Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Homology

Gene Ontology Provided by PomBase

Function Evidence Code Pubs
enables histone methyltransferase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables protein-arginine N-methyltransferase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables protein-arginine omega-N asymmetric methyltransferase activity IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Process Evidence Code Pubs
involved_in chromatin remodeling IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in regulation of DNA-templated transcription IBA
Inferred from Biological aspect of Ancestor
more info
  
Component Evidence Code Pubs
is_active_in cytosol HDA PubMed 
is_active_in nucleus HDA PubMed 
is_active_in nucleus IBA
Inferred from Biological aspect of Ancestor
more info
  
is_active_in nucleus IDA
Inferred from Direct Assay
more info
 PubMed 

General protein information

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Preferred Names
protein arginine N-methyltransferase Rmt1

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_003424.3 Reference assembly

    Range
    5015959..5017919 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001020254.4 → NP_594825.2  protein arginine N-methyltransferase Rmt1 [Schizosaccharomyces pombe]

    See identical proteins and their annotated locations for NP_594825.2

    Status: PROVISIONAL

    UniProtKB/Swiss-Prot
    Q9URX7
    Conserved Domains (1) summary
    cd02440
    Location:58 → 158
    AdoMet_MTases; S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). ...
Nucleotide Protein
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