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
SNRPD2
SMD2, SNRPD1, Sm-D2
small nuclear ribonucleoprotein D2 polypeptide 16.5kDa
GO Process (7)
GO Function (2)
GO Component (12)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- SMN-Sm protein complex [IDA]
- U1 snRNP [IDA]
- U12-type spliceosomal complex [IDA]
- U4 snRNP [IDA]
- catalytic step 2 spliceosome [IDA]
- cytosol [IDA, TAS]
- extracellular vesicular exosome [IDA]
- methylosome [IDA]
- nucleoplasm [TAS]
- pICln-Sm protein complex [IDA]
- small nuclear ribonucleoprotein complex [TAS]
- spliceosomal complex [TAS]
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