BAIT
PML
MYL, PP8675, RNF71, TRIM19
promyelocytic leukemia
GO Process (39)
GO Function (8)
GO Component (9)
Gene Ontology Biological Process
- DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [ISS]
- PML body organization [IDA, IMP]
- apoptotic process [IDA]
- cell cycle arrest [IDA]
- cellular senescence [IDA]
- circadian regulation of gene expression [ISS]
- cytokine-mediated signaling pathway [TAS]
- endoplasmic reticulum calcium ion homeostasis [ISS]
- entrainment of circadian clock by photoperiod [ISS]
- innate immune response [IDA]
- interferon-gamma-mediated signaling pathway [TAS]
- intrinsic apoptotic signaling pathway in response to DNA damage [IDA]
- intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [ISS]
- maintenance of protein location in nucleus [IDA]
- negative regulation of angiogenesis [IMP]
- negative regulation of cell growth [IDA]
- negative regulation of cell proliferation [IMP]
- negative regulation of mitotic cell cycle [IDA]
- negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process [IMP]
- negative regulation of telomerase activity [IMP]
- negative regulation of telomere maintenance via telomerase [IMP]
- negative regulation of transcription, DNA-templated [IDA]
- negative regulation of translation in response to oxidative stress [IDA]
- negative regulation of viral release from host cell [IDA]
- positive regulation of apoptotic process involved in mammary gland involution [IDA]
- positive regulation of defense response to virus by host [IMP]
- positive regulation of extrinsic apoptotic signaling pathway [IMP]
- positive regulation of histone deacetylation [IDA]
- proteasome-mediated ubiquitin-dependent protein catabolic process [IDA]
- protein complex assembly [IDA]
- protein stabilization [IDA]
- protein targeting [IDA, IMP]
- regulation of calcium ion transport into cytosol [ISS]
- regulation of circadian rhythm [ISS]
- regulation of double-strand break repair [IMP]
- regulation of protein phosphorylation [ISS]
- regulation of transcription, DNA-templated [IMP]
- response to cytokine [IDA]
- response to hypoxia [IDA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
PREY
HSPA5
BIP, GRP78, HEL-S-89n, MIF2
heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa)
GO Process (14)
GO Function (10)
GO Component (12)
Gene Ontology Biological Process
- ATP catabolic process [ISS]
- ER-associated ubiquitin-dependent protein catabolic process [TAS]
- activation of signaling protein activity involved in unfolded protein response [TAS]
- blood coagulation [TAS]
- cellular protein metabolic process [TAS]
- cellular response to glucose starvation [IDA]
- endoplasmic reticulum unfolded protein response [TAS]
- maintenance of protein localization in endoplasmic reticulum [IMP]
- negative regulation of apoptotic process [IMP, TAS]
- platelet activation [TAS]
- platelet degranulation [TAS]
- positive regulation of cell migration [IMP]
- regulation of protein folding in endoplasmic reticulum [TAS]
- substantia nigra development [IEP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- COP9 signalosome [IDA]
- endoplasmic reticulum [IDA, IMP, TAS]
- endoplasmic reticulum chaperone complex [IDA]
- endoplasmic reticulum lumen [TAS]
- endoplasmic reticulum membrane [TAS]
- endoplasmic reticulum-Golgi intermediate compartment [IDA]
- extracellular vesicular exosome [IDA]
- focal adhesion [IDA]
- integral component of endoplasmic reticulum membrane [IDA]
- membrane [IDA]
- midbody [IDA]
- nucleus [IDA, IMP]
Homo sapiens
Proximity Label-MS
An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods.
Publication
Identification of proximal SUMO-dependent interactors using SUMO-ID.
The fast dynamics and reversibility of posttranslational modifications by the ubiquitin family pose significant challenges for research. Here we present SUMO-ID, a technology that merges proximity biotinylation by TurboID and protein-fragment complementation to find SUMO-dependent interactors of proteins of interest. We develop an optimized split-TurboID version and show SUMO interaction-dependent labelling of proteins proximal to PML and RANGAP1. SUMO-dependent interactors ... [more]
Nat Commun Dec. 18, 2020; 12(1);6671 [Pubmed: 34795231]
Throughput
- High Throughput
Additional Notes
- Sumo-dependent interaction
Curated By
- BioGRID