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HSL7 protein arginine N-methyltransferase [ Saccharomyces cerevisiae S288C ]

Gene ID: 852431, updated on 2-Nov-2024

Summary

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Official Symbol
HSL7
Official Full Name
protein arginine N-methyltransferase
Primary source
SGD:S000000337
Locus tag
YBR133C
See related
AllianceGenome:SGD:S000000337; FungiDB:YBR133C; VEuPathDB:YBR133C
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Saccharomyces cerevisiae S288C (strain: S288C)
Lineage
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary
Enables protein-arginine omega-N monomethyltransferase activity and protein-arginine omega-N symmetric methyltransferase activity. Involved in G2/M transition of mitotic cell cycle; protein catabolic process; and regulation of cell cycle. Located in cellular bud neck septin collar; cellular bud neck septin ring; and outer plaque of spindle pole body. Orthologous to human PRMT5 (protein arginine methyltransferase 5). [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

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See HSL7 in Genome Data Viewer
Location:
chromosome: II
Exon count:
1
Sequence:
Chromosome: II; NC_001134.8 (501804..504287, complement)

Chromosome II - NC_001134.8Genomic Context describing neighboring genes Neighboring gene Ccz1p Neighboring gene Agp2p Neighboring gene cyclin-dependent protein kinase regulatory subunit CKS1 Neighboring gene protein kinase MEC1

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_001134.8

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Hsl7p, the yeast homologue of human JBP1, is a protein methyltransferase. Lee JH, et al. Biochem Biophys Res Commun, 2000 Jul 21. PMID 10903903
  2. Role of Hsl7 in morphology and pathogenicity and its interaction with other signaling components in the plant pathogen Ustilago maydis. Lovely CB, et al. Eukaryot Cell, 2011 Jul. PMID 21622903, Free PMC Article
  3. Feedback control of Swe1p degradation in the yeast morphogenesis checkpoint. King K, et al. Mol Biol Cell, 2013 Apr. PMID 23389636, Free PMC Article
  4. Arginine methylation in yeast proteins during stationary-phase growth and heat shock. Lakowski TM, et al. Amino Acids, 2015 Dec. PMID 26189025
  5. Cell-cycle regulatory proteins Hsl7p/Skb1p belong to the protein methyltransferase superfamily. Ma XJ. Trends Biochem Sci, 2000 Jan. PMID 10637604

See all (78) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Hsl7 has a repressive role in transcription. Hsl7 is responsible for in vivo symmetric dimethylation of histone H4 arginine 3 in a transcriptionally repressed state.
    Title: Yeast symmetric arginine methyltransferase Hsl7 has a repressive role in transcription.
  2. Hsl7p interaction with Hsl1p is not needed for degradation of septin-Swe1p fusion protein.
    Title: Roles of Hsl1p and Hsl7p in Swe1p degradation: beyond septin tethering.
  3. Hsl7 can display type II type II protein arginine methyltransferase activity.
    Title: Hsl7 is a substrate-specific type II protein arginine methyltransferase in yeast.
Submit: New GeneRIF Correction

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 SGD

Function Evidence Code Pubs
enables histone arginine N-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 IEA
Inferred from Electronic Annotation
more info
  
enables protein-arginine omega-N monomethyltransferase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables protein-arginine omega-N symmetric methyltransferase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables protein-arginine omega-N symmetric methyltransferase activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in G2/M transition of mitotic cell cycle IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in cell division IEA
Inferred from Electronic Annotation
more info
  
involved_in chromatin remodeling IEA
Inferred from Electronic Annotation
more info
  
involved_in methylation IEA
Inferred from Electronic Annotation
more info
  
involved_in peptidyl-arginine N-methylation IEA
Inferred from Electronic Annotation
more info
  
involved_in protein catabolic process 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 cell cycle IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Component Evidence Code Pubs
located_in cellular bud neck HDA PubMed 
located_in cellular bud neck IDA
Inferred from Direct Assay
more info
 PubMed 
located_in cellular bud neck IEA
Inferred from Electronic Annotation
more info
  
located_in cellular bud neck septin collar IDA
Inferred from Direct Assay
more info
 PubMed 
located_in cellular bud neck septin ring IDA
Inferred from Direct Assay
more info
 PubMed 
located_in cellular bud neck septin ring IMP
Inferred from Mutant Phenotype
more info
 PubMed 
located_in cytoplasm HDA PubMed 
is_active_in cytosol IBA
Inferred from Biological aspect of Ancestor
more info
  
is_active_in nucleus IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in outer plaque of spindle pole body IDA
Inferred from Direct Assay
more info
 PubMed 

General protein information

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Preferred Names
protein arginine N-methyltransferase
NP_009691.1
  • Protein arginine N-methyltransferase; exhibits septin and Hsl1p-dependent localization to the bud neck in budded cells and periodic Hsl1p-dependent phosphorylation; required with Hsl1p, and Elm1p for the mother-bud neck recruitment, phosphorylation, and degradation of Swe1p; responsible for symmetric dimethylation of histone H4 on Arg3; relocalizes away from bud neck upon DNA replication stress; human homolog PRMT5 can complement yeast hsl7 mutant

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_001134.8 Reference assembly

    Range
    501804..504287 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001178481.1 → NP_009691.1  TPA: protein arginine N-methyltransferase [Saccharomyces cerevisiae S288C]

    See identical proteins and their annotated locations for NP_009691.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    A2NP39, D6VQD0, P38274
    UniProtKB/TrEMBL
    B3LN23, G2W9D7, N1P6Q3
    Conserved Domains (3) summary
    pfam05185
    Location:316 → 493
    PRMT5; PRMT5 arginine-N-methyltransferase
    pfam17285
    Location:38 → 308
    PRMT5_TIM; PRMT5 TIM barrel domain
    pfam17286
    Location:496 → 690
    PRMT5_C; PRMT5 oligomerization domain
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P38274.1

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