BAIT
TNK2
ACK, ACK-1, ACK1, p21cdc42Hs
tyrosine kinase, non-receptor, 2
GO Process (12)
GO Function (8)
GO Component (9)
Gene Ontology Biological Process
- cell differentiation [IBA]
- cell migration [IBA]
- cell surface receptor signaling pathway [TAS]
- innate immune response [IBA]
- negative regulation of catalytic activity [TAS]
- peptidyl-tyrosine autophosphorylation [IBA]
- phosphorylation [IDA]
- positive regulation of peptidyl-tyrosine phosphorylation [IDA]
- regulation of cell proliferation [IBA]
- regulation of clathrin-mediated endocytosis [IDA]
- small GTPase mediated signal transduction [TAS]
- transmembrane receptor protein tyrosine kinase signaling pathway [IBA]
Gene Ontology Molecular Function- GTPase inhibitor activity [TAS]
- WW domain binding [ISS]
- epidermal growth factor receptor binding [IDA]
- hormone receptor binding [IBA]
- non-membrane spanning protein tyrosine kinase activity [IBA]
- protein binding [IPI]
- protein serine/threonine/tyrosine kinase activity [IDA]
- protein tyrosine kinase activity [IDA]
- GTPase inhibitor activity [TAS]
- WW domain binding [ISS]
- epidermal growth factor receptor binding [IDA]
- hormone receptor binding [IBA]
- non-membrane spanning protein tyrosine kinase activity [IBA]
- protein binding [IPI]
- protein serine/threonine/tyrosine kinase activity [IDA]
- protein tyrosine kinase activity [IDA]
Gene Ontology Cellular Component
Homo sapiens
PREY
HSPA1A
HEL-S-103, HSP70-1, HSP70-1A, HSP70I, HSP72, HSPA1, DAQB-147D11.1
heat shock 70kDa protein 1A
GO Process (20)
GO Function (13)
GO Component (17)
Gene Ontology Biological Process
- ATP catabolic process [IDA]
- RNA metabolic process [TAS]
- cellular heat acclimation [IMP]
- cellular response to heat [IDA]
- cellular response to oxidative stress [TAS]
- gene expression [TAS]
- mRNA catabolic process [IDA]
- mRNA metabolic process [TAS]
- negative regulation of apoptotic process [IMP, TAS]
- negative regulation of cell death [IDA, IMP]
- negative regulation of cell growth [IMP]
- negative regulation of cell proliferation [IMP]
- negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [IMP]
- negative regulation of inclusion body assembly [IDA]
- negative regulation of protein ubiquitination [IDA]
- positive regulation of erythrocyte differentiation [IMP]
- protein refolding [IDA]
- protein stabilization [TAS]
- regulation of cell death [IMP]
- response to unfolded protein [IDA]
Gene Ontology Molecular Function- ATP binding [IDA]
- ATPase activity [IDA]
- ATPase activity, coupled [IDA]
- G-protein coupled receptor binding [IPI]
- double-stranded RNA binding [IDA]
- enzyme binding [IPI]
- heat shock protein binding [IPI]
- poly(A) RNA binding [IDA]
- protein N-terminus binding [IPI]
- protein binding [IPI]
- protein binding involved in protein folding [IDA]
- ubiquitin protein ligase binding [IPI]
- unfolded protein binding [IDA, NAS, TAS]
- ATP binding [IDA]
- ATPase activity [IDA]
- ATPase activity, coupled [IDA]
- G-protein coupled receptor binding [IPI]
- double-stranded RNA binding [IDA]
- enzyme binding [IPI]
- heat shock protein binding [IPI]
- poly(A) RNA binding [IDA]
- protein N-terminus binding [IPI]
- protein binding [IPI]
- protein binding involved in protein folding [IDA]
- ubiquitin protein ligase binding [IPI]
- unfolded protein binding [IDA, NAS, TAS]
Gene Ontology Cellular Component
- COP9 signalosome [IDA]
- aggresome [IDA]
- blood microparticle [IDA]
- centriole [IDA]
- cytoplasm [IDA, TAS]
- cytosol [IDA, TAS]
- endoplasmic reticulum [TAS]
- extracellular vesicular exosome [IDA]
- focal adhesion [IDA]
- inclusion body [IDA]
- mitochondrion [TAS]
- nuclear speck [IDA]
- nucleus [IDA]
- perinuclear region of cytoplasm [IDA]
- ribonucleoprotein complex [IDA]
- ubiquitin ligase complex [IDA]
- vesicle [IDA]
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
Extensive rewiring of the EGFR network in colorectal cancer cells expressing transforming levels of KRASG13D.
Protein-protein-interaction networks (PPINs) organize fundamental biological processes, but how oncogenic mutations impact these interactions and their functions at a network-level scale is poorly understood. Here, we analyze how a common oncogenic KRAS mutation (KRASG13D) affects PPIN structure and function of the Epidermal Growth Factor Receptor (EGFR) network in colorectal cancer (CRC) cells. Mapping >6000 PPIs shows that this network is ... [more]
Nat Commun Dec. 24, 2019; 11(1);499 [Pubmed: 31980649]
Throughput
- High Throughput
Curated By
- BioGRID