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
HNRNPK
CSBP, HNRPK, TUNP, RP11-575L7.1
heterogeneous nuclear ribonucleoprotein K
GO Process (10)
GO Function (6)
GO Component (7)
Gene Ontology Biological Process
- RNA processing [TAS]
- RNA splicing [TAS]
- gene expression [TAS]
- mRNA splicing, via spliceosome [IC, TAS]
- positive regulation of low-density lipoprotein particle receptor biosynthetic process [IMP]
- positive regulation of receptor-mediated endocytosis [IMP]
- positive regulation of transcription from RNA polymerase II promoter [IMP]
- regulation of lipid transport by positive regulation of transcription from RNA polymerase II promoter [IMP]
- regulation of low-density lipoprotein particle clearance [IMP]
- signal transduction [TAS]
Gene Ontology Molecular Function- RNA binding [TAS]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding [IMP]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [IMP]
- poly(A) RNA binding [IDA]
- protein binding [IPI]
- single-stranded DNA binding [TAS]
- RNA binding [TAS]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding [IMP]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [IMP]
- poly(A) RNA binding [IDA]
- protein binding [IPI]
- single-stranded DNA binding [TAS]
Gene Ontology Cellular Component
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