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.
GO Process (4)
GO Function (2)
GO Component (1)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Saccharomyces cerevisiae (S288c)
PREY
TBF1
LPI16, L000002264, YPL128C
Telobox-containing general regulatory factor; binds TTAGGG repeats within subtelomeric anti-silencing regions (STARs), blocking silent chromatin propagation; binds majority of snoRNA gene promoters, required for full snoRNA expression; caps DSB flanked by long T2AG3 repeats and blocks checkpoint activation
GO Process (4)
GO Function (5)
GO Component (2)
Gene Ontology Biological Process
Gene Ontology Molecular Function- RNA polymerase II core promoter proximal region sequence-specific DNA binding [IDA]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity [IDA]
- chromatin insulator sequence binding [IDA]
- sequence-specific DNA binding [IDA]
- telomeric DNA binding [IDA]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding [IDA]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity [IDA]
- chromatin insulator sequence binding [IDA]
- sequence-specific DNA binding [IDA]
- telomeric DNA binding [IDA]
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.
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