HPM1 protein-histidine N-methyltransferase [Saccharomyces cerevisiae S288C] - Gene

Summary

Official Symbol: HPM1
Official Full Name: protein-histidine N-methyltransferase
Primary source: SGD:S000001372
Locus tag: YIL110W
See related: AllianceGenome:SGD:S000001372; FungiDB:YIL110W; VEuPathDB:YIL110W
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: MNI1
Summary: Enables protein-L-histidine N-tele-methyltransferase activity. Involved in peptidyl-histidine methylation, to form tele-methylhistidine; positive regulation of translational fidelity; and ribosomal large subunit assembly. Located in cytoplasm and nucleus. Orthologous to human METTL18 (methyltransferase 18, RPL3 N3(tau)-histidine). [provided by Alliance of Genome Resources, Dec 2024]
NEW: Try the new Gene table
Try the new Transcript table

Chromosome IX - NC_001141.2 Genomic Context describing neighboring genes

Go to nucleotide: Graphics FASTA GenBank

Differential Proteome and Interactome Analysis Reveal the Basis of Pleiotropy Associated With the Histidine Methyltransferase Hpm1p.
Title: Differential Proteome and Interactome Analysis Reveal the Basis of Pleiotropy Associated With the Histidine Methyltransferase Hpm1p.
Hpm1 is a multifunctional methyltransferase with independent roles in ribosome biogenesis and translation.
Title: Methylation of yeast ribosomal protein Rpl3 promotes translational elongation fidelity.
3-methylhistidine modification of Rpl3 is dependent upon the YIL110W methyltransferase.
Title: A novel 3-methylhistidine modification of yeast ribosomal protein Rpl3 is dependent upon the YIL110W methyltransferase.

Submit: New GeneRIF Correction

Products	Interactant	Other Gene	Complex	Source	Pubs	Description

Function	Evidence Code	Pubs
enables S-adenosylmethionine-dependent methyltransferase activity	IEA Inferred from Electronic Annotation more info
enables methyltransferase activity	IEA Inferred from Electronic Annotation more info
enables protein-L-histidine N-tele-methyltransferase activity	IBA Inferred from Biological aspect of Ancestor more info
enables protein-L-histidine N-tele-methyltransferase activity	IEA Inferred from Electronic Annotation more info
enables protein-L-histidine N-tele-methyltransferase activity	IMP Inferred from Mutant Phenotype more info	PubMed

Process	Evidence Code	Pubs
involved_in methylation	IEA Inferred from Electronic Annotation more info
involved_in peptidyl-histidine methylation, to form tele-methylhistidine	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of translational fidelity	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in regulation of translation	IBA Inferred from Biological aspect of Ancestor more info
involved_in ribosomal large subunit assembly	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasm	HDA more info	PubMed
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
located_in nucleus	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

NP_012156.1

AdoMet-dependent methyltransferase; involved in a novel 3-methylhistidine modification of multiple proteins, including ribosomal protein Rpl3p; seven beta-strand MTase family member; null mutant exhibits a weak vacuolar protein sorting defect and caspofungin resistance