BAIT
ZBTB18
C2H2-171, MRD22, RP58, TAZ-1, ZNF238
zinc finger and BTB domain containing 18
GO Process (3)
GO Function (3)
GO Component (5)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
PREY
KPNB1
IMB1, IPO1, IPOB, Impnb, NTF97
karyopherin (importin) beta 1
GO Process (12)
GO Function (6)
GO Component (9)
Gene Ontology Biological Process
- NLS-bearing protein import into nucleus [TAS]
- apoptotic DNA fragmentation [TAS]
- apoptotic process [TAS]
- cellular component disassembly involved in execution phase of apoptosis [TAS]
- cytokine-mediated signaling pathway [TAS]
- intracellular transport of virus [TAS]
- protein import into nucleus [IDA]
- protein import into nucleus, translocation [TAS]
- ribosomal protein import into nucleus [IDA]
- small molecule metabolic process [TAS]
- viral life cycle [TAS]
- viral process [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
Calpain-mediated cleavage generates a ZBTB18 N-terminal product that regulates HIF1A signaling and glioblastoma metabolism.
Proteolytic cleavage is an important post-translational mechanism to increase protein variability and functionality. In cancer, this process can be deregulated to shut off tumor-suppressive functions. Here, we report that in glioblastoma (GBM), the tumor suppressor ZBTB18 is targeted for protein cleavage by the intracellular protease calpain. The N-terminal (Nte) ZBTB18 cleaved fragment localizes to the cytoplasm and thus, is unable ... [more]
iScience Jul. 15, 2022; 25(7);104625 [Pubmed: 35800763]
Throughput
- High Throughput
Curated By
- BioGRID