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- Bc1de0f0310397198498778dc525a88c0 NCIT_P378 "NCI" @default.
- Bc1de0f0310397198498778dc525a88c0 NCIT_P381 "Pawson Lab, SLRI, Mount Sinai Hospital, 2003" @default.
- Bc1de0f0310397198498778dc525a88c0 type Axiom @default.
- Bc1de0f0310397198498778dc525a88c0 annotatedProperty IAO_0000115 @default.
- Bc1de0f0310397198498778dc525a88c0 annotatedSource NCIT_C26118 @default.
- Bc1de0f0310397198498778dc525a88c0 annotatedTarget "Phosphotyrosine binding (PTB) domains are 100-150 residue modules that commonly bind Asn-Pro-X-Tyr motifs. The PTB domains of the docking proteins Shc and IRS-1 require ligand phosphorylation on the tyrosine residue (NPXpY) for binding. More N-terminal sequences are also required for high affinity binding and conferring specificity. The peptide binds as a b-strand to an anti-parallel b-sheet, while the NPXpY motif makes a turn, positioning the pY for recognition by basic residues. The PTB domains of proteins such as X11, Dab, Fe65 and Numb apparently recognize NPXY or related peptide motifs, but are not dependent on ligand phosphorylation. In addition, the Numb PTB domain can bind an unrelated peptide that forms a helical turn." @default.