UBE2M
Gene Ontology Biological Process
Gene Ontology Molecular Function
CALR
Gene Ontology Biological Process
- activation of signaling protein activity involved in unfolded protein response [TAS]
- antigen processing and presentation of exogenous peptide antigen via MHC class I [TAS]
- antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [TAS]
- antigen processing and presentation of peptide antigen via MHC class I [TAS]
- cell cycle arrest [IGI]
- cellular calcium ion homeostasis [TAS]
- cellular protein metabolic process [TAS]
- cellular senescence [IGI]
- endoplasmic reticulum unfolded protein response [TAS]
- glucocorticoid receptor signaling pathway [TAS]
- negative regulation of intracellular steroid hormone receptor signaling pathway [IDA]
- negative regulation of neuron differentiation [IDA]
- negative regulation of retinoic acid receptor signaling pathway [IDA]
- negative regulation of transcription from RNA polymerase II promoter [IDA]
- negative regulation of transcription, DNA-templated [IDA]
- negative regulation of translation [ISS, TAS]
- peptide antigen assembly with MHC class I protein complex [ISS]
- positive regulation of DNA replication [IGI]
- positive regulation of cell cycle [IGI]
- positive regulation of cell proliferation [IGI]
- positive regulation of dendritic cell chemotaxis [IMP]
- positive regulation of phagocytosis [ISS]
- positive regulation of substrate adhesion-dependent cell spreading [IMP]
- post-translational protein modification [TAS]
- protein N-linked glycosylation via asparagine [TAS]
- protein export from nucleus [IDA]
- protein folding [TAS]
- protein localization to nucleus [IDA]
- protein maturation by protein folding [TAS]
- protein stabilization [ISS, TAS]
- regulation of apoptotic process [TAS]
- regulation of transcription, DNA-templated [TAS]
- sequestering of calcium ion [TAS]
Gene Ontology Molecular Function- DNA binding [NAS]
- androgen receptor binding [IDA]
- calcium ion binding [ISS, TAS]
- carbohydrate binding [TAS]
- chaperone binding [TAS]
- complement component C1q binding [TAS]
- glycoprotein binding [IPI]
- integrin binding [IPI]
- mRNA binding [IDA]
- poly(A) RNA binding [IDA]
- protein binding [IPI]
- protein binding involved in protein folding [TAS]
- ubiquitin protein ligase binding [IPI]
- unfolded protein binding [TAS]
- zinc ion binding [TAS]
- DNA binding [NAS]
- androgen receptor binding [IDA]
- calcium ion binding [ISS, TAS]
- carbohydrate binding [TAS]
- chaperone binding [TAS]
- complement component C1q binding [TAS]
- glycoprotein binding [IPI]
- integrin binding [IPI]
- mRNA binding [IDA]
- poly(A) RNA binding [IDA]
- protein binding [IPI]
- protein binding involved in protein folding [TAS]
- ubiquitin protein ligase binding [IPI]
- unfolded protein binding [TAS]
- zinc ion binding [TAS]
Gene Ontology Cellular Component
- MHC class I peptide loading complex [ISS]
- cell surface [TAS]
- cytoplasm [IDA]
- cytosol [IDA]
- endocytic vesicle lumen [TAS]
- endoplasmic reticulum [IDA, TAS]
- endoplasmic reticulum lumen [IDA, TAS]
- extracellular region [TAS]
- extracellular space [IDA]
- extracellular vesicular exosome [IDA]
- focal adhesion [IDA]
- integral component of lumenal side of endoplasmic reticulum membrane [TAS]
- intracellular [TAS]
- membrane [IDA]
- nucleus [IDA]
- perinuclear region of cytoplasm [IDA]
- polysome [ISS]
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]
Throughput
- High Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| UBE2M CALR | Cross-Linking-MS (XL-MS) Cross-Linking-MS (XL-MS) An interaction is detected between two proteins using chemically reactive or photo-activatable cross-linking reagents that covalently link amino acids in close proximity, followed by mass spectrometry analysis to identify the linked peptides (reviewed in PMID 37406423, 37104977). Experiments may be carried with live cells or cell lysates in which all proteins are expressed at endogenous levels (e.g. PMID 34349018, 35235311) or with recombinant proteins (e.g., PMID 28537071). | High | - | BioGRID | 3745546 |
Curated By
- BioGRID