Search Results
Overview
| Uniprot ID | Q13554 |
|---|---|
| Protein Name | Calcium/calmodulin-dependent protein kinase type II subunit beta |
| Gene Name | CAMK2B |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 147 | ENLLLASKCKGAAVK |
| 292 | QETVECLKKFNARRK |
| 43 | TGHEYAAKIINTKKL |
Function
Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca(2+)/calmodulin-binding and autophosphorylation, and is involved in dendritic spine and synapse formation, neuronal plasticity and regulation of sarcoplasmic reticulum Ca(2+) transport in skeletal muscle (PubMed:16690701). 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. Also regulates the migration of developing neurons (PubMed:29100089). Participates in the modulation of skeletal muscle function in response to exercise (PubMed:16690701). In slow-twitch muscles, is involved in regulation of sarcoplasmic reticulum (SR) Ca(2+) transport and in fast-twitch muscle participates in the control of Ca(2+) release from the SR through phosphorylation of triadin, a ryanodine receptor-coupling factor, and phospholamban (PLN/PLB), an endogenous inhibitor of SERCA2A/ATP2A2. In response to interferon-gamma (IFN-gamma) stimulation, catalyzes phosphorylation of STAT1, stimulating the JAK-STAT signaling pathway (By similarity). Phosphorylates reticulophagy regulator RETREG1 at 'Ser-151' under endoplasmic reticulum stress conditions which enhances RETREG1 oligomerization and its membrane scission and reticulophagy activity (PubMed:31930741)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005954 | calcium- and calmodulin-dependent protein kinase complex |
| Cellular Component | GO:0005813 | centrosome |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0030666 | endocytic vesicle membrane |
| Cellular Component | GO:0043005 | neuron projection |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0014069 | postsynaptic density |
| Cellular Component | GO:0033017 | sarcoplasmic reticulum membrane |
| Molecular Function | GO:0003779 | actin binding |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0004683 | calcium/calmodulin-dependent protein kinase activity |
| Molecular Function | GO:0005516 | calmodulin binding |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0042803 | protein homodimerization activity |
| Molecular Function | GO:0106310 | protein serine kinase activity |
| Biological Process | GO:0030154 | cell differentiation |
| Biological Process | GO:0060291 | long-term synaptic potentiation |
| Biological Process | GO:0007399 | nervous system development |
| Biological Process | GO:0061003 | positive regulation of dendritic spine morphogenesis |
| Biological Process | GO:0010976 | positive regulation of neuron projection development |
| Biological Process | GO:0090129 | positive regulation of synapse maturation |
| Biological Process | GO:0046777 | protein autophosphorylation |
| Biological Process | GO:0006468 | protein phosphorylation |
| Biological Process | GO:0051924 | regulation of calcium ion transport |
| Biological Process | GO:0060998 | regulation of dendritic spine development |
| Biological Process | GO:0048169 | regulation of long-term neuronal synaptic plasticity |
| Biological Process | GO:2001222 | regulation of neuron migration |
| Biological Process | GO:0048168 | regulation of neuronal synaptic plasticity |
| Biological Process | GO:1903076 | regulation of protein localization to plasma membrane |
| Biological Process | GO:0014733 | regulation of skeletal muscle adaptation |
| Biological Process | GO:0051823 | regulation of synapse structural plasticity |
| Biological Process | GO:0007165 | signal transduction |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[2] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.