BAIT
PMAIP1
APR, NOXA
phorbol-12-myristate-13-acetate-induced protein 1
GO Process (21)
GO Function (1)
GO Component (4)
Gene Ontology Biological Process
- T cell homeostasis [ISS]
- apoptotic process [IMP, TAS]
- cellular response to glucose starvation [IMP]
- cellular response to hypoxia [IEP]
- defense response to virus [IDA]
- intrinsic apoptotic signaling pathway [IDA, TAS]
- intrinsic apoptotic signaling pathway by p53 class mediator [IMP]
- negative regulation of mitochondrial membrane potential [ISS]
- positive regulation of DNA damage response, signal transduction by p53 class mediator [IMP]
- positive regulation of apoptotic process [IDA, IMP]
- positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [IDA]
- positive regulation of extrinsic apoptotic signaling pathway via death domain receptors [IDA]
- positive regulation of glucose metabolic process [IDA]
- positive regulation of intrinsic apoptotic signaling pathway [IDA, TAS]
- positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway [TAS]
- positive regulation of protein oligomerization [IDA]
- positive regulation of release of cytochrome c from mitochondria [IDA, IMP]
- proteasomal protein catabolic process [IDA]
- reactive oxygen species metabolic process [IDA]
- regulation of mitochondrial membrane permeability [IDA]
- response to dsRNA [IDA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
PREY
ESYT1
FAM62A, MBC2
extended synaptotagmin-like protein 1
GO Process (0)
GO Function (2)
GO Component (3)
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
CHIP ubiquitylates NOXA and induces its lysosomal degradation in response to DNA damage.
The BH3-only protein NOXA is a regulator of mitochondrial apoptosis by specifically antagonizing the anti-apoptotic protein MCL-1. Here we show that the E3 ubiquitin ligase CHIP controls NOXA stability after DNA damage. Our findings reveal that CHIP and MCL-1 are binding partners of NOXA and differentially define the fate of NOXA. Whereas NOXA is initially targeted to mitochondria upon MCL-1-binding, ... [more]
Cell Death Dis Dec. 10, 2019; 11(9);740 [Pubmed: 32913203]
Throughput
- High Throughput
Curated By
- BioGRID