ID:DOK1_MOUSE DESCRIPTION: RecName: Full=Docking protein 1; AltName: Full=Downstream of tyrosine kinase 1; AltName: Full=p62(dok); FUNCTION: DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK1 appears to be a negative regulator of the insulin signaling pathway. Modulates integrin activation by competing with talin for the same binding site on ITGB3 (By similarity). SUBUNIT: Interacts with RasGAP, INPP5D/SHIP1 and ABL1. Interacts directly with phosphorylated ITGB3 (By similarity). INTERACTION: P00520:Abl1; NbExp=4; IntAct=EBI-914917, EBI-914519; Q99M51:Nck1; NbExp=5; IntAct=EBI-914917, EBI-642202; SUBCELLULAR LOCATION: Cytoplasm (By similarity). TISSUE SPECIFICITY: Expressed in lung, spleen, skeletal muscle and kidney. DOMAIN: PTB domain mediates receptor interaction. PTM: Constitutively tyrosine-phosphorylated. Phosphorylated by TEC. PTM: Phosphorylated on tyrosine residues by the insulin receptor kinase. Results in the negative regulation of the insulin signaling pathway (By similarity). Phosphorylated by LYN. DISRUPTION PHENOTYPE: No visible phenotype. Mice appear healthy and are fertile. SIMILARITY: Belongs to the DOK family. Type A subfamily. SIMILARITY: Contains 1 IRS-type PTB domain. SIMILARITY: Contains 1 PH domain.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on P97465
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.