background:
Docking protein 1 is constitutively tyrosine phosphorylated in hematopoietic progenitors isolated from chronic myelogenous leukemia (CML) patients in the chronic phase. It may be a critical substrate for p210(bcr/abl), a chimeric protein whose presence is associated with CML. Docking protein 1 contains a putative pleckstrin homology domain at the amino terminus and ten PXXP SH3 recognition motifs. Docking protein 2 binds p120 (RasGAP) from CML cells. It has been postulated to play a role in mitogenic signaling.
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.
Subunit:
Interacts with ABL1. Interacts with RasGAP and INPP5D/SHIP1. Interacts directly with phosphorylated ITGB3.
Subcellular Location:
Isoform 1: Cytoplasm. Isoform 3: Cytoplasm, perinuclear region.
Tissue Specificity:
Expressed in pancreas, heart, leukocyte and spleen. Expressed in both resting and activated peripheral blood T-cells.
Post-translational modifications:
Constitutively tyrosine-phosphorylated. Phosphorylated by TEC (By similarity). Phosphorylated by LYN.
Phosphorylated on tyrosine residues by the insulin receptor kinase. Results in the negative regulation of the insulin signaling pathway.
Isoform 3 contains a N-acetylmethionine at position 1.
Similarity:
Belongs to the DOK family. Type A subfamily.
Contains 1 IRS-type PTB domain.
Contains 1 PH domain.
Database links:
UniProtKB/Swiss-Prot: Q99704.1
Important Note:
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
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