产品概述
产品性能
免疫原
产品应用
研究背景
domain:PTB domain mediates receptor interaction.,function:DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK3 is a negative regulator of JNK signaling in B-cells through interaction with INPP5D/SHIP1. May modulate ABL function.,PTM:Constitutively tyrosine-phosphorylated.,PTM:On IL2 stimulation, phosphorylated on C-terminal tyrosine residues possibly by Src kinases. Can also be phosphorylated by ABL kinase.,similarity:Belongs to the DOK family. Type A subfamily.,similarity:Contains 1 IRS-type PTB domain.,similarity:Contains 1 PH domain.,subunit:On tyrosine phosphorylation, interacts with CSK and INPP5D/SHIP1 via their SH2 domains. Both Tyr-381 and Tyr-398 are required for interaction with INPP5D. Only Tyr-381 is required for interaction with CSK. Binds ABL through the PTB domain and in a kinase-dependent manner. Does not interact with RasGAP.,tissue specificity:Expressed in spleen.,domain:PTB domain mediates receptor interaction.,function:DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK3 is a negative regulator of JNK signaling in B-cells through interaction with INPP5D/SHIP1. May modulate ABL function.,PTM:Constitutively tyrosine-phosphorylated.,PTM:On IL2 stimulation, phosphorylated on C-terminal tyrosine residues possibly by Src kinases. Can also be phosphorylated by ABL kinase.,similarity:Belongs to the DOK family. Type A subfamily.,similarity:Contains 1 IRS-type PTB domain.,similarity:Contains 1 PH domain.,subunit:On tyrosine phosphorylation, interacts with CSK and INPP5D/SHIP1 via their SH2 domains. Both Tyr-381 and Tyr-398 are required for interaction with INPP5D. Only Tyr-381 is required for interaction with CSK. Binds ABL through the PTB domain and in a kinase-dependent manner. Does not interact with RasGAP.,tissue specificity:Expressed in spleen.,
研究领域
B_Cell_Antigen
