ADRB2
Gene Ontology Biological Process
- activation of adenylate cyclase activity [IDA]
- activation of transmembrane receptor protein tyrosine kinase activity [TAS]
- adenylate cyclase-modulating G-protein coupled receptor signaling pathway [TAS]
- adrenergic receptor signaling pathway [IDA]
- cell surface receptor signaling pathway [TAS]
- desensitization of G-protein coupled receptor protein signaling pathway by arrestin [IDA]
- endosome to lysosome transport [TAS]
- positive regulation of MAPK cascade [IDA]
- positive regulation of protein ubiquitination [IMP]
- receptor-mediated endocytosis [IDA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
HDAC6
Gene Ontology Biological Process
- Hsp90 deacetylation [IMP]
- aggresome assembly [IMP]
- cellular response to hydrogen peroxide [IMP]
- cellular response to topologically incorrect protein [IMP]
- histone deacetylation [IDA, ISS]
- intracellular protein transport [IMP]
- lysosome localization [IMP]
- macroautophagy [IMP]
- misfolded or incompletely synthesized protein catabolic process [IMP]
- negative regulation of hydrogen peroxide metabolic process [IC]
- negative regulation of oxidoreductase activity [IC]
- negative regulation of protein complex disassembly [IMP]
- negative regulation of proteolysis [IMP]
- negative regulation of transcription, DNA-templated [ISS]
- peptidyl-lysine deacetylation [IMP]
- polyubiquitinated misfolded protein transport [IMP]
- positive regulation of chaperone-mediated protein complex assembly [IMP]
- positive regulation of epithelial cell migration [IMP]
- positive regulation of hydrogen peroxide-mediated programmed cell death [IDA]
- positive regulation of receptor biosynthetic process [IMP]
- positive regulation of signal transduction [IMP]
- protein deacetylation [IMP]
- regulation of androgen receptor signaling pathway [TAS]
- regulation of gene expression, epigenetic [IMP]
- regulation of microtubule-based movement [IC]
- regulation of receptor activity [IMP]
- response to growth factor [IMP]
- response to misfolded protein [IMP]
- response to organic substance [IMP]
- response to toxic substance [IMP]
- tubulin deacetylation [IDA, ISS]
Gene Ontology Molecular Function- Hsp90 protein binding [IDA]
- alpha-tubulin binding [IDA]
- beta-catenin binding [IPI]
- core promoter binding [IDA]
- dynein complex binding [IDA]
- enzyme binding [ISS]
- histone deacetylase activity [IDA]
- histone deacetylase binding [IPI]
- microtubule binding [IDA, ISS]
- polyubiquitin binding [IDA]
- protein binding [IPI]
- tau protein binding [IDA]
- tubulin deacetylase activity [IDA, ISS]
- ubiquitin protein ligase binding [IPI]
- Hsp90 protein binding [IDA]
- alpha-tubulin binding [IDA]
- beta-catenin binding [IPI]
- core promoter binding [IDA]
- dynein complex binding [IDA]
- enzyme binding [ISS]
- histone deacetylase activity [IDA]
- histone deacetylase binding [IPI]
- microtubule binding [IDA, ISS]
- polyubiquitin binding [IDA]
- protein binding [IPI]
- tau protein binding [IDA]
- tubulin deacetylase activity [IDA, ISS]
- ubiquitin protein ligase binding [IPI]
Gene Ontology Cellular Component
- aggresome [IDA]
- axon [ISS]
- caveola [IDA]
- cell leading edge [IDA]
- cytoplasm [ISS]
- cytosol [ISS]
- dendrite [ISS]
- dynein complex [IDA]
- histone deacetylase complex [IDA]
- inclusion body [IDA]
- microtubule [IDA]
- microtubule associated complex [IDA]
- nucleoplasm [IDA]
- nucleus [ISS]
- perikaryon [ISS]
- perinuclear region of cytoplasm [IDA]
PCA
A Protein-Fragment Complementation Assay (PCA) is a protein-protein interaction assay in which a bait protein is expressed as fusion to one of the either N- or C- terminal peptide fragments of a reporter protein and prey protein is expressed as fusion to the complementary N- or C- terminal fragment of the same reporter protein. Interaction of bait and prey proteins bring together complementary fragments, which can then fold into an active reporter, e.g. the split-ubiquitin assay.
Publication
CHIP-MYTH: A novel interactive proteomics method for the assessment of agonist-dependent interactions of the human β2-adrenergic receptor.
G-protein coupled receptors (GPCRs) are involved in a variety of disease processes and comprise major drug targets. However, the complexity of integral membrane proteins such as GPCRs makes the identification of their interacting partners and subsequent drug development challenging. A comprehensive understanding of GPCR protein interaction networks is needed to design effective therapeutic strategies to inhibit these drug targets. Here, ... [more]
Throughput
- High Throughput
Additional Notes
- MYTH split-ubiquitin system
Curated By
- BioGRID