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- B343575cc0c4fc7dd3a9729822be1e92f NCIT_P378 "NCI" @default.
- B343575cc0c4fc7dd3a9729822be1e92f type Axiom @default.
- B343575cc0c4fc7dd3a9729822be1e92f annotatedProperty IAO_0000115 @default.
- B343575cc0c4fc7dd3a9729822be1e92f annotatedSource NCIT_C14106 @default.
- B343575cc0c4fc7dd3a9729822be1e92f annotatedTarget "Proline-Rich Domains may be involved in heterotypic protein-protein interactions in signal transduction or other pathways. Found in signaling and structural proteins, WW domains are composed of approximately 40 amino acids folded as a stable, triple stranded beta-sheet that recognize proline-rich sequences. Some WW domains show a remarkable similarity to SH3 domains, which also appear to recognize some proline-rich sequences. Ena/VASP (Drosophila Enabled/Vasodilator-Stimulated Phosphoprotein) Family members regulate actin filament assembly, often through association with binding partners that display a proline-rich FPPPP motif. Ena/VASP proteins interact with these partners via the highly conserved Ena/VASP homology 1 (EVH1) domain. (NCI)" @default.