Cancer Protein Description
This report provides a detailed description of a selected cancer protein with information collected from various sources, including UniProt, the Wellcome Trust Sanger Institute’s Catalogue of Somatic Mutations in Cancer (COSMIC), and the Atlas of Genetics and Cytogenetics in Oncology and Haematology.
| Protein Name: | CAMK2B |
| Gene Name: | CAMK2B |
| Protein Full Name: | Calcium/calmodulin-dependent protein kinase type I |
| Alias: | Calcium/calmodulin-dependent protein kinase II beta; Calcium/calmodulin-dependent protein kinase type II beta chain; CaM kinase II beta subunit; CAM2; CAMK2; CAMK2B; CAMKB; CaMK-II beta; CaMK-II beta subunit; CaM-kinase II beta chain; EC 2.7.1.123; EC 2.7.11.17; KCC2B; Kinase CaMK2-beta; Proline rich calmodulin-dependent protein kinase |
| Mass (Da): | 72727 |
| Number AA: | 664 |
| UniProt ID: | Q13554 |
| Locus ID: | 816 |
| COSMIC ID: | CAMK2B |
| Gene location on chromosome: | 22q12; 7p14.3-p14.1 |
| Cancer protein type: | OP |
| Effect of cancer mutation on protein: | GAIN |
| Effect of active protein on cancer: | PROMOTES |
| Number of cancer specimens: | 19948 |
| Percent of cancer specimens with mutations: | 0.69 |
| Normal role description: | CAMK2B is a protein-serine/threonine kinase. Its activation by intracellular calcium can lead to indirect activation of the Ras/Erk pathway, which is pro-growth/anti-apoptotic; therefore hightened activity due to a certain mutation could cause it to be an oncoprotein. |
| Commentary on involvement of protein in cancer: | Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca2+/calmodulin-binding and autophosphorylation, and is involved in dendritic spine and synapse formation, neuronal plasticity and regulation of sarcoplamic reticulum Ca2+ transport in skeletal muscle. In neurons, plays an essential structural role in the reorganization of the actin cytoskeleton during plasticity by binding and bundling actin filaments in a kinase-independent manner. This structural function is required for correct targeting of CaMK2A, which acts downstream of NMDAR to promote dendritic spine and synapse formation and maintain synaptic plasticity which enables long-term potentiation (LTP) and hippocampus-dependent learning. In developing hippocampal neurons, promotes arborization of the dendritic tree and in mature neurons, promotes dendritic remodeling. Participates to the modulation of skeletal muscle function in response to exercise. In slow-twitch muscles, is involved in regulation of sarcoplamic reticulum (SR) Ca2+ transport and in fast-twitch muscle participates to the control of Ca2+ release from the SR through phosphorylation of triadin, a ryanodine receptor-coupling factor, and phospholamban (PLN/PLB), an endogenous inhibitor of SERCA2A/ATP2A2 |