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

SIP1

L000001890, YDR422C
Alternate beta-subunit of the Snf1p kinase complex; may confer substrate specificity; vacuolar protein containing KIS (Kinase-Interacting Sequence) and ASC (Association with Snf1 kinase Complex) domains involved in protein interactions
Kinome Project (Sc)
GO Process (3)
GO Function (1)
GO Component (2)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)

Affinity Capture-MS

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.

Publication

Proteomic analysis of interactors for yeast protein arginine methyltransferase hmt1 reveals novel substrate and insights into additional biological roles.

Jackson CA, Yadav N, Min S, Li J, Milliman EJ, Qu J, Chen YC, Yu MC

Protein arginine methylation is a post-translational modification catalyzed by an evolutionarily conserved family of enzymes called protein arginine methyltransferases (PRMTs), with PRMT1 being the most conserved member of this enzyme family. This modification has emerged to be an important regulator of protein functions. To better understand the role of PRMTs in cellular pathways and functions, we have carried out a ... [more]

Proteomics Sep. 20, 2012; 0(0); [Pubmed: 22997150]

Throughput

  • High Throughput

Curated By

  • BioGRID