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
JAK3
JAK-3, JAK3_HUMAN, JAKL, L-JAK, LJAK
Janus kinase 3
GO Process (30)
GO Function (5)
GO Component (2)
Gene Ontology Biological Process
- B cell differentiation [IBA, ISS]
- JAK-STAT cascade involved in growth hormone signaling pathway [TAS]
- STAT protein import into nucleus [TAS]
- T cell homeostasis [IBA, ISS, TAS]
- cell migration [IBA]
- enzyme linked receptor protein signaling pathway [ISS]
- erythrocyte differentiation [IBA]
- inflammatory response [IBA]
- innate immune response [IBA]
- interleukin-4-mediated signaling pathway [IDA]
- intracellular signal transduction [ISS]
- negative regulation of FasL biosynthetic process [ISS]
- negative regulation of T cell activation [ISS]
- negative regulation of T-helper 1 cell differentiation [ISS]
- negative regulation of dendritic cell cytokine production [ISS]
- negative regulation of interleukin-10 production [ISS]
- negative regulation of interleukin-12 production [ISS]
- negative regulation of thymocyte apoptotic process [ISS]
- peptidyl-tyrosine autophosphorylation [IBA]
- peptidyl-tyrosine phosphorylation [ISS]
- positive regulation of T cell proliferation [IBA]
- protein phosphorylation [TAS]
- regulation of T cell apoptotic process [ISS]
- regulation of apoptotic process [IBA]
- response to interleukin-15 [TAS]
- response to interleukin-2 [TAS]
- response to interleukin-4 [IDA]
- response to interleukin-9 [TAS]
- transmembrane receptor protein tyrosine kinase signaling pathway [IBA]
- tyrosine phosphorylation of STAT protein [IBA, TAS]
Gene Ontology Molecular Function
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