prmt-1 Protein arginine N-methyltransferase 1 [Caenorhabditis elegans] - Gene

Summary

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Official Symbol: prmt-1
Official Full Name: Protein arginine N-methyltransferase 1
Primary source: WormBase:WBGene00013766
Locus tag: CELE_Y113G7B.17
See related: AllianceGenome:WB:WBGene00013766
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Caenorhabditis elegans (strain: Bristol N2)
Lineage: Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis
Summary: Enables S-adenosyl-L-methionine binding activity and protein methyltransferase activity. Involved in several processes, including heat acclimation; positive regulation of protein localization to nucleus; and regulation of dauer entry. Located in cytoplasm. Is expressed in several structures, including intestine; muscle cell; nervous system; pharynx; and vulval cell. Orthologous to several human genes including PRMT8 (protein arginine methyltransferase 8). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See prmt-1 in Genome Data Viewer

Location:: chromosome: V

Exon count:: 3

Sequence:: Chromosome: V; NC_003283.11 (20267377..20269711, complement)

Chromosome V - NC_003283.11 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_003283.11

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

It show the morphological and functional phenotypes of single or double null alleles of prmt-1 in Caenorhabditis elegans. The prmt-1;prmt-5 double mutants are viable, and exhibit short body length and small brood size compared to N2 and each of the single mutants.
Title: Simultaneous ablation of prmt-1 and prmt-5 abolishes asymmetric and symmetric arginine dimethylations in Caenorhabditis elegans.

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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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Markers

Y113G7B.17 (e-PCR)
- UniSTS:321809

Homology

Orthologs from OrthoDB

Gene Ontology Provided by WormBase

Function	Evidence Code	Pubs
enables S-adenosyl-L-methionine binding	IDA Inferred from Direct Assay more info	PubMed
enables histone H2A methyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables histone H4 methyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables histone methyltransferase activity	IBA Inferred from Biological aspect of Ancestor more info
enables methyltransferase activity	IEA Inferred from Electronic Annotation more info
enables protein-arginine N-methyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables protein-arginine N-methyltransferase activity	IEA Inferred from Electronic Annotation more info
enables protein-arginine omega-N asymmetric methyltransferase activity	IBA Inferred from Biological aspect of Ancestor more info
enables protein-arginine omega-N asymmetric methyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables protein-arginine omega-N asymmetric methyltransferase activity	IEA Inferred from Electronic Annotation more info
enables protein-arginine omega-N monomethyltransferase activity	IBA Inferred from Biological aspect of Ancestor more info
enables protein-arginine omega-N monomethyltransferase activity	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in chromatin remodeling	IBA Inferred from Biological aspect of Ancestor more info
involved_in heat acclimation	IGI Inferred from Genetic Interaction more info	PubMed
involved_in methylation	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of protein binding	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in peptidyl-arginine methylation	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of gene expression	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of protein localization to nucleus	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in regulation of DNA-templated transcription	IBA Inferred from Biological aspect of Ancestor more info
involved_in regulation of dauer entry	IGI Inferred from Genetic Interaction more info	PubMed
involved_in regulation of gene expression	IGI Inferred from Genetic Interaction more info	PubMed
involved_in regulation of lipid storage	IGI Inferred from Genetic Interaction more info	PubMed
involved_in response to UV	IGI Inferred from Genetic Interaction more info	PubMed
involved_in response to oxidative stress	IGI Inferred from Genetic Interaction more info	PubMed
involved_in response to starvation	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
located_in endoplasmic reticulum	HDA more info	PubMed
is_active_in nucleus	IBA Inferred from Biological aspect of Ancestor more info
located_in nucleus	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: Protein arginine N-methyltransferase 1

NP_507909.1

Confirmed by transcript evidence

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

NC_003283.11 Reference assembly

Range

20267377..20269711 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_075508.8 → NP_507909.1 Protein arginine N-methyltransferase 1 [Caenorhabditis elegans]

See identical proteins and their annotated locations for NP_507909.1

Status: REVIEWED

UniProtKB/Swiss-Prot

Q9U2X0

Conserved Domains (1) summary

cd02440
Location:66 → 169

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). ...