thumb|Biological assembly of SHOC2 protein as shown by crystal structure to a resolution of 2.4 Angstrom. Sulfate molecules are labeled purple. Structure from 10.2210/pdb7TVG/pdb.thumb|SHOC2 protein leucine rich domain. Leucine amino acids shown as bright orange sticks.Leucine-rich repeat (LRR) protein SHOC-2 is a protein that in humans is encoded by the SHOC2 gene. The best-studied role of SHOC2 is in modulating signals of the extracellular signal-regulated kinase 1 and 2 (ERK1/2) pathway by forming a holophosphatase complex that activates RAF proteins. This protein was initially identified i
thumb|Biological assembly of SHOC2 protein as shown by crystal structure to a resolution of 2.4 Angstrom. Sulfate molecules are labeled purple. Structure from 10.2210/pdb7TVG/pdb.thumb|SHOC2 protein leucine rich domain. Leucine amino acids shown as bright orange sticks.Leucine-rich repeat (LRR) protein SHOC-2 is a protein that in humans is encoded by the SHOC2 gene. The best-studied role of SHOC2 is in modulating signals of the extracellular signal-regulated kinase 1 and 2 (ERK1/2) pathway by forming a holophosphatase complex that activates RAF proteins. This protein was initially identified in Caenorhabditis elegans as SUR-8/SOC2 and was found to be a critical positive regulator of the ERK1/2 signaling pathway that integrates the Ras and RAF components of the ERK1/2 pathway into a multiprotein complex. Specifically, SHOC2 tethers RAS and PP1C proteins and in close proximity to RAF to dephosphorylate “S259” to enable MAPK signaling. It has been shown that activity that results in lipidation (specifically Myristoylation) of SHOC2 can cause Noonan syndrome.
== Interactions ==
Discovered by embedding cosine similarity (sentence-transformers MiniLM, 384-dim).