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DOK proteins are enzymatically inert adaptor or scaffolding proteins. Additionally we are shipping DOK3 Antibodies (95) and many more products for this protein.
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Mutations in DOK3 gene is associated with prostate cancer
DOK2 and DOK3 expression was significantly reduced in HTLV-1-infected T cells.
The Dok-3/Grb2 (show GRB2 Proteins) protein signal module attenuates Lyn (show LYN Proteins) kinase-dependent activation of Syk (show SYK Proteins) kinase in B cell antigen receptor microclusters
absence of DOK3 increases LPS (show IRF6 Proteins) signaling, contributing to LPS (show IRF6 Proteins)-induced tolerance. Thus, DOK3 plays a role in TLR signaling during both naive and endotoxin-induced tolerant conditions
The novel platelet adapter Dok-3 is tyrosine phosphorylated in an Src kinase (show CSK Proteins)-independent manner downstream of alphaIIbbeta3 in human platelets, leading to an interaction with Grb2 (show GRB2 Proteins) and SHIP-1 (show INPP5D Proteins).
findings indicate that Dok-3 sequesters Grb2 (show GRB2 Proteins) from Shc (show SHC1 Proteins) and inhibits the Ras-Erk (show EPHB2 Proteins) pathway downstream of PTKs
we demonstrate that CpG treatment leads to ubiquitin-mediated degradation of DOK3 via interaction with an E3 ligase TNFR (show TNFRSF1A Proteins)-associated factor 6 (TRAF6 (show TRAF6 Proteins)).
This study reveals DOK3 as a nonredundant regulator of plasma cell differentiation by up-regulating PD-1 (show PDCD1 Proteins) ligand expression through the attenuation of calcium signaling.
Data show that docking protein 3 (DOK3) plays a role in TLR3 (show TLR3 Proteins) signaling by enabling TNFR (show TNFRSF1A Proteins)-associated factor (TRAF) 3 (show TRAF3 Proteins)/TANK-binding kinase (TBK) 1 (show TBK1 Proteins) binding and facilitating TBK1 (show TBK1 Proteins) and IFN regulatory factor 3 activation and the induction of IFN-beta (show IFNB1 Proteins) production.
DOK3 physically associated with the ITAM of DAP12 (show TYROBP Proteins) through its phosphotyrosine-binding domain. In response to LPS (show TLR4 Proteins), DOK3 was phosphorylated in a DAP12 (show TYROBP Proteins)- and Src (show SRC Proteins)-dependent manner, which led to translocation of phosphorylated DOK3 to the plasma membrane.
Triple Dok1 (show DOK1 Proteins) Doc2 (show DOC2A Proteins) Doc3 knockout leads to spontaneous pulmonary inflammation with hallmarks of asthma.
absence of DOK3 increases LPS (show TLR4 Proteins) signaling, contributing to LPS (show TLR4 Proteins)-induced tolerance. Thus, DOK3 plays a role in TLR signaling during both naive and endotoxin-induced tolerant conditions
identify a surprising but pivotal role for dynein and the microtubule network alongside Grb2 (show GRB2 Proteins), Dok-3, and Cbl (show CBL Proteins) in antigen gathering during B cell activation (show BLNK Proteins)
Subcellular localization of Grb2 (show GRB2 Proteins) by the adaptor protein Dok-3 restricts the intensity of Ca2 (show CA2 Proteins)+ signaling in B cells.
In the absence of Dok-3, the localization of the inhibitory phosphatase SHIP-1 (show INPP5D Proteins) to the plasma membrane is intact while its phosphorylation is compromised, suggesting that Dok-3 could function to facilitate or sustain the activation of SHIP-1 (show INPP5D Proteins).
DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. Plays a role as negative regulator of the mobilization of calcium ions and of calcium signaling.
docking protein 3
, Dok-like protein
, downstream of tyrosine kinase 3
, p62(dok)-like protein
, p62Dok-like protein
, Downstream of tyrosine kinase 3