BAIT

HMT1

HCP1, ODP1, RMT1, protein-arginine omega-N methyltransferase HMT1, L000002808, L000001296, YBR034C
Nuclear SAM-dependent mono- and asymmetric methyltransferase; modifies hnRNPs, including Npl3p and Hrp1p, affecting their activity and nuclear export; methylates U1 snRNP protein Snp1p and ribosomal protein Rps2p; interacts genetically with genes encoding components of Rpd3(L) and this interaction is important for Rpd3 recruitment to the subtelomeric region.
Saccharomyces cerevisiae (S288c)
PREY

RPS2

RPS4, SUP138, SUP38, SUP44, ribosomal 40S subunit protein S2, rp12, Ys5, S5, S4, S2, L000002205, YGL123W
Protein component of the small (40S) subunit; essential for control of translational accuracy; phosphorylation by C-terminal domain kinase I (CTDK-I) enhances translational accuracy; methylated on one or more arginine residues by Hmt1p; homologous to mammalian ribosomal protein S2 and bacterial S5
GO Process (2)
GO Function (2)
GO Component (2)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)

Biochemical Activity (Methylation)

An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation.

Publication

Yeast proteins Gar1p, Nop1p, Npl3p, Nsr1p, and Rps2p are natively methylated and are substrates of the arginine methyltransferase Hmt1p.

Yagoub D, Hart-Smith G, Moecking J, Erce MA, Wilkins MR

The Hmt1 methyltransferase is the predominant arginine methyltransferase in Saccharomyces cerevisiae. There are 18 substrate proteins described for this methyltransferase, however native sites of methylation have only been identified on two of these proteins. Here we used peptide immunoaffinity enrichment, followed by LC-ETD-MS/MS, to discover 21 native sites of arginine methylation on five putative Hmt1 substrate proteins, namely Gar1p (H/ACA ... [more]

Proteomics Sep. 01, 2015; 15(18);3209-18 [Pubmed: 26081071]

Throughput

  • Low Throughput

Additional Notes

  • Table 3

Curated By

  • BioGRID