BAIT
UBE2M
UBC-RS2, UBC12, hUbc12
ubiquitin-conjugating enzyme E2M
GO Process (4)
GO Function (6)
GO Component (3)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Homo sapiens
PREY
PRMT1
ANM1, HCP1, HRMT1L2, IR1B4
protein arginine methyltransferase 1
GO Process (9)
GO Function (8)
GO Component (3)
Gene Ontology Biological Process
- cell surface receptor signaling pathway [TAS]
- histone H4-R3 methylation [IDA]
- histone methylation [IDA]
- negative regulation of megakaryocyte differentiation [IDA]
- neuron projection development [IMP]
- peptidyl-arginine methylation [IDA]
- peptidyl-arginine methylation, to asymmetrical-dimethyl arginine [IBA]
- protein methylation [TAS]
- regulation of transcription, DNA-templated [IBA]
Gene Ontology Molecular Function- N-methyltransferase activity [IDA, IMP]
- histone methyltransferase activity [IDA]
- histone methyltransferase activity (H4-R3 specific) [IDA]
- identical protein binding [IPI]
- methyltransferase activity [TAS]
- poly(A) RNA binding [IDA]
- protein binding [IPI]
- protein-arginine omega-N asymmetric methyltransferase activity [IBA]
- N-methyltransferase activity [IDA, IMP]
- histone methyltransferase activity [IDA]
- histone methyltransferase activity (H4-R3 specific) [IDA]
- identical protein binding [IPI]
- methyltransferase activity [TAS]
- poly(A) RNA binding [IDA]
- protein binding [IPI]
- protein-arginine omega-N asymmetric methyltransferase activity [IBA]
Homo sapiens
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
Blocking an N-terminal acetylation-dependent protein interaction inhibits an E3 ligase.
N-terminal acetylation is an abundant modification influencing protein functions. Because ∼80% of mammalian cytosolic proteins are N-terminally acetylated, this modification is potentially an untapped target for chemical control of their functions. Structural studies have revealed that, like lysine acetylation, N-terminal acetylation converts a positively charged amine into a hydrophobic handle that mediates protein interactions; hence, this modification may be a ... [more]
Nat. Chem. Biol. Aug. 01, 2017; 13(8);850-857 [Pubmed: 28581483]
Throughput
- High Throughput
Curated By
- BioGRID