HMT1 protein-arginine omega-N methyltransferase HMT1 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: HMT1
Official Full Name: protein-arginine omega-N methyltransferase HMT1
Primary source: SGD:S000000238
Locus tag: YBR034C
See related: AllianceGenome:SGD:S000000238; FungiDB:YBR034C; VEuPathDB:YBR034C
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Also known as: HCP1; ODP1; RMT1
Summary: Enables protein-arginine omega-N asymmetric methyltransferase activity and protein-arginine omega-N monomethyltransferase activity. Involved in several processes, including folic acid biosynthetic process; mRNA export from nucleus; and regulation of DNA-templated transcription. Located in nucleus. Orthologous to several human genes including PRMT1 (protein arginine methyltransferase 1). [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

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See HMT1 in Genome Data Viewer

Location:: chromosome: II

Exon count:: 1

Sequence:: Chromosome: II; NC_001134.8 (304930..305976, complement)

Chromosome II - NC_001134.8 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001134.8

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Experimental evolution reveals a general role for the Hmt1 in heterogeneity noise buffering.
Title: Experimental evolution reveals a general role for the methyltransferase Hmt1 in noise buffering.
this is the first study to reveal an association between Hmt1p and phosphate homeostasis and one which suggests a regulatory link between S-adenosyl methionine and intracellular phosphate
Title: Knockout of the Hmt1p Arginine Methyltransferase in Saccharomyces cerevisiae Leads to the Dysregulation of Phosphate-associated Genes and Processes.
This study investigated the enzyme-substrate interaction between Hmt1p and nucleolar protein Npl3p, using chemical cross linking/mass spectrometry. This method can capture transient interprotein interactions that occur during the process of methylation, involving a disordered region in Npl3p with tandem SRGG repeats, and we confirm that Hmt1p and Npl3p exist as homomultimers.
Title: Characterization of the Interaction between Arginine Methyltransferase Hmt1 and Its Substrate Npl3: Use of Multiple Cross-Linkers, Mass Spectrometric Approaches, and Software Platforms.
Data suggest that Hmt1-based arginine methylation is required for Scd6 localization and function.
Title: Analysis of the Physiological Activities of Scd6 through Its Interaction with Hmt1.
Arginine methylation is a widespread modification, with Hmt1 being the major arginine methyltransferase in S. cerevisiae.
Title: Protein substrates of the arginine methyltransferase Hmt1 identified by proteome arrays.
Studied and discovered 21 native sites of arginine methylation on five putative Hmt1 substrate proteins (Gar1p, Nop1p, Npl3p, Nsr1p, Rps2p).
Title: Yeast proteins Gar1p, Nop1p, Npl3p, Nsr1p, and Rps2p are natively methylated and are substrates of the arginine methyltransferase Hmt1p.
the methyltransferase activity of Hmt1 on histone H3R2 requires reciprocal contributions from two Hmt1 molecules, suggesting an intermolecular trans-complementary mechanism by which Hmt1 dimer methylates its substrates
Title: Yeast Hmt1 catalyses asymmetric dimethylation of histone H3 arginine 2 in vitro.
Carried out a proteomic profiling experiment to comprehensively identify the physical interactors of Hmt1, the budding yeast homolog for human PRMT1. Snf2 was experimentally confirmed as a robust substrate of Hmt1 in vitro.
Title: Proteomic analysis of interactors for yeast protein arginine methyltransferase Hmt1 reveals novel substrate and insights into additional biological roles.
Interactions between HMT1 and genes encoding components of the histone deacetylase complex Rpd3L, are reported.
Title: Recruitment of Rpd3 to the telomere depends on the protein arginine methyltransferase Hmt1.
These results are suggestive of a role for Rmt1 in modifying the function of Rps2 in a manner distinct from that occurring in S. pombe and mammalian cells.
Title: Rmt1 catalyzes zinc-finger independent arginine methylation of ribosomal protein Rps2 in Saccharomyces cerevisiae.

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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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Homology

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
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	IBA Inferred from Biological aspect of Ancestor more info
enables protein-arginine N-methyltransferase activity	IEA Inferred from Electronic Annotation 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	IMP Inferred from Mutant Phenotype more info	PubMed
enables protein-arginine omega-N monomethyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables protein-arginine omega-N monomethyltransferase 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 folic acid biosynthetic process	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in mRNA export from nucleus	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in methylation	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of termination of DNA-templated transcription	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in peptidyl-arginine methylation	IDA Inferred from Direct Assay more info	PubMed
involved_in peptidyl-arginine methylation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of transcription elongation by RNA polymerase II	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in regulation of DNA-templated transcription	IBA Inferred from Biological aspect of Ancestor more info

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

General protein information

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Preferred Names: protein-arginine omega-N methyltransferase HMT1

NP_009590.1

Nuclear SAM-dependent mono- and asymmetric methyltransferase; modifies hnRNPs, including Npl3p and Hrp1p, affecting their activity and nuclear export; methylates U1 snRNP protein Snp1p, ribosomal protein Rps2p, and histones H3 and H4; interacts genetically with genes encoding components of Rpd3(L) and this interaction is important for Rpd3 recruitment to the subtelomeric region

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_001134.8 Reference assembly

Range

304930..305976 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001178382.1 → NP_009590.1 TPA: protein-arginine omega-N methyltransferase HMT1 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_009590.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VQ34, P38074

UniProtKB/TrEMBL

A6ZKX8, B3LNB1, C7GXX8, D3UED0, G2W939, N1PAR4

Conserved Domains (1) summary

cl17173
Location:56 → 130

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). ...