Kinase suppressor of Ras 1 - Q8IVT5 (KSR1_HUMAN)


Protein Feature View of PDB entries mapped to a UniProtKB sequence  

  • Number of PDB entries for Q8IVT5: 1
Part of a multiprotein signaling complex which promotes phosphorylation of Raf family members and activation of downstream MAP kinases (By similarity). Independently of its kinase activity, acts as MAP2K1/MEK1 and MAP2K2/MEK2-dependent allosteric activator of BRAF; upon binding to MAP2K1/MEK1 or MAP2K2/MEK2, dimerizes with BRAF and promotes BRAF-mediated phosphorylation of MAP2K1/MEK1 and/or MAP2K2/MEK2 (PubMed:29433126). Promotes activation of MAPK1 and/or MAPK3, both in response to EGF and to cAMP (By similarity). Its kinase activity is unsure (By similarity). Some protein kinase activity has been detected in vitro, however the physiological relevance of this activity is unknown (By similarity). UniProt
Catalytic Activity
ATP + L-threonyl-[protein] = ADP + H+ + O-phospho-L-threonyl-[protein] UniProt
Pathway Maps
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Subunit Structure
Homodimer (PubMed:29433126). Heterodimerizes (via N-terminus) with BRAF (via N-terminus) in a MAP2K1/MEK1 or MAP2K2/MEK2-dependent manner (PubMed:29433126). Interacts with MAP2K1/MEK1 and MAP2K2/MEK2 (PubMed:10409742, PubMed:29433126). Binding to MAP2K1/MEK1 releases the intramolecular inhibitory interaction between KSR1 N-terminus and kinase domains which is required for the subsequent RSK1 dimerization with BRAF (PubMed:29433126). Identified in a complex with AKAP13, MAP2K1 and BRAF (By similarity). Interacts with AKAP13 and BRAF (PubMed:21102438). Interacts with RAF and MAPK/ERK, in a Ras-dependent manner (By similarity). Interacts with 14-3-3 proteins including YWHAB (By similarity). Interacts with HSP90AA1/HSP90, YWHAE/14-3-3 and CDC37 (PubMed:10409742, PubMed:29433126). The binding of 14-3-3 proteins to phosphorylated KSR1 prevents the membrane localization (By similarity). Interacts with MARK3 (By similarity). Interacts with PPP2R1A and PPP2CA (By similarity). Interacts with isoform 1 of VRK2 (PubMed:20679487). UniProt
The N-terminal region mediates interaction with BRAF (PubMed:29433126). Also mediates membrane localization (By similarity). UniProt
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