BAIT
EYA4
CMD1J, DFNA10, RP11-704J17.4
EYA transcriptional coactivator and phosphatase 4
GO Process (2)
GO Function (1)
GO Component (0)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Homo sapiens
PREY
HSPB1
CMT2F, HEL-S-102, HMN2B, HS.76067, HSP27, HSP28, Hsp25, SRP27
heat shock 27kDa protein 1
GO Process (21)
GO Function (7)
GO Component (8)
Gene Ontology Biological Process
- RNA metabolic process [TAS]
- cellular component movement [TAS]
- cellular response to vascular endothelial growth factor stimulus [IMP]
- gene expression [TAS]
- intracellular signal transduction [IMP]
- mRNA metabolic process [TAS]
- negative regulation of apoptotic process [TAS]
- negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway [ISS]
- negative regulation of protein kinase activity [ISS]
- platelet aggregation [IMP]
- positive regulation of angiogenesis [IMP]
- positive regulation of blood vessel endothelial cell migration [IMP]
- positive regulation of endothelial cell chemotaxis [IMP]
- positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway [IMP]
- positive regulation of interleukin-1 beta production [ISS]
- positive regulation of tumor necrosis factor biosynthetic process [ISS]
- regulation of I-kappaB kinase/NF-kappaB signaling [ISS]
- regulation of translational initiation [TAS]
- response to unfolded protein [NAS]
- response to virus [IEP]
- retina homeostasis [IEP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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
The Eyes Absent family members EYA4 and EYA1 promote PLK1 activation and successful mitosis through tyrosine dephosphorylation.
The Eyes Absent proteins (EYA1-4) are a biochemically unique group of tyrosine phosphatases known to be tumour-promoting across a range of cancer types. To date, the targets of EYA phosphatase activity remain largely uncharacterised. Here, we identify Polo-like kinase 1 (PLK1) as an interactor and phosphatase substrate of EYA4 and EYA1, with pY445 on PLK1 being the primary target site. ... [more]
Nat Commun Feb. 15, 2024; 15(1);1385 [Pubmed: 38360978]
Throughput
- High Throughput
Additional Notes
- BioID
Curated By
- BioGRID