BAIT
ITGA5
Cd49e, Fnra, VLA5
integrin alpha 5 (fibronectin receptor alpha)
GO Process (14)
GO Function (4)
GO Component (12)
Gene Ontology Biological Process
- cell adhesion [ISO]
- cell-cell adhesion mediated by integrin [IMP]
- cell-substrate adhesion [ISO]
- cell-substrate junction assembly [IDA]
- endodermal cell differentiation [ISO]
- heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [IMP]
- heterotypic cell-cell adhesion [ISO]
- integrin-mediated signaling pathway [ISO]
- leukocyte cell-cell adhesion [IMP]
- memory [IMP]
- negative regulation of anoikis [ISO]
- positive regulation of cell migration [ISO]
- positive regulation of cell-substrate adhesion [ISO]
- positive regulation of peptidyl-tyrosine phosphorylation [ISO]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Mus musculus
PREY
SHARPIN
0610041B22Rik, AW121341, RBCKL1, SIPL1, cpdm
SHANK-associated RH domain interacting protein
GO Process (10)
GO Function (4)
GO Component (7)
Gene Ontology Biological Process
- apoptotic nuclear changes [IMP]
- epidermis development [IMP]
- keratinization [IMP]
- mitochondrion organization [IMP]
- negative regulation of inflammatory response [IMP]
- positive regulation of I-kappaB kinase/NF-kappaB signaling [IMP, ISO]
- protein homooligomerization [ISO]
- protein linear polyubiquitination [ISO]
- regulation of CD40 signaling pathway [ISO]
- regulation of tumor necrosis factor-mediated signaling pathway [IMP, ISO]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Mus musculus
FRET
An interaction is inferred when close proximity of interaction partners is detected by fluorescence resonance energy transfer between pairs of fluorophore-labeled molecules, such as occurs between CFP (donor) and YFP (acceptor) fusion proteins.
Publication
SHARPIN is an endogenous inhibitor of β1-integrin activation.
Regulated activation of integrins is critical for cell adhesion, motility and tissue homeostasis. Talin and kindlins activate β1-integrins, but the counteracting inhibiting mechanisms are poorly defined. We identified SHARPIN as an important inactivator of β1-integrins in an RNAi screen. SHARPIN inhibited β1-integrin functions in human cancer cells and primary leukocytes. Fibroblasts, leukocytes and keratinocytes from SHARPIN-deficient mice exhibited increased β1-integrin ... [more]
Nat. Cell Biol. Nov. 01, 2011; 13(11);1315-24 [Pubmed: 21947080]
Throughput
- Low Throughput
Curated By
- BioGRID