Molecular Target Synopsis
Overview
Domains and Structures
Drugs and Clinical Candidates
Druggability
Chemistry
Ligand Efficiency Plot
Pathways
Family Cladogram
Interaction Network
Gene Expression
Gene Copy Number Variation
RNAi
Mutations
Germline Genetics

CAMK2B (Q13554) - Overview - Molecular Target Synopsis

Protein


CAMK2B, Calcium/calmodulin-dependent protein kinase type II subunit beta
Enzyme Classification 2.7.11.17
UniProt Q13554

Also Known as KCC2B_HUMAN, CAMK2B, CAM2, CAMK2, CAMKB

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. 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. 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. CAMK2 is composed of 4 different chains: alpha (CAMK2A), beta (CAMK2B), gamma (CAMK2G), and delta (CAMK2D). The different isoforms assemble into homo- or heteromultimeric holoenzymes composed of 12 subunits with two hexameric rings stacked one on top of the other (PubMed:14722083, Ref.19). Interacts with SYNGAP1 and CAMK2N2 (By similarity). Interacts with MPDZ (PubMed:15312654). Interacts with FOXO3 (By similarity). Interacts (when in a kinase inactive state not associated with calmodulin) with ARC; leading to target ARC to inactive synapses.

3BHH
CRYSTAL STRUCTURE OF HUMAN CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE IIB ISOFORM 1 (CAMK2B)
RCSB/PDB
Inspect Structure
See all 3D Structures for CAMK2B

Isoforms / Transcripts (Protein Coding)


Sub-cellular localization


UniProt: CAMK2B is active in the following subcellular-locations: cell junction, centrosome, cytoplasm, cytoskeleton, microtubule organizing center, sarcoplasmic reticulum membrane, synapse.
GO terms: CAMK2B is active in the following subcellular-locations: cell junction, cytoplasm, cytosol, endocytic vesicle membrane, microtubule organizing center, neuron projection, nucleoplasm, plasma membrane, sarcoplasmic reticulum membrane, synapse.



UniProt
GO terms

Gene Copy Number Variation


In COSMIC - Cell Lines Project CAMK2B has gain in 6 cell-lines, loss in 1 cell-lines and no signal in 998 cell-lines. (see details)

Gene Expression


In NCI60, the highest expressing cell lines are: PC_3, OVCAR_5, EKVX

In Array Express (RNA-seq of 675 commonly used human cancer cell lines), the highest expressing cell lines are: DMS 53, SCLC-21H, DMS 79

In Array Express (RNA-seq of long poly adenylated RNA and long non poly adenylated RNA from ENCODE cell lines), the highest expressing cell lines are: SK-N-SH, NHLF, HSMM

(see details)

RNA Interference


CAMK2B was reported in the following RNAI studies:

Cell - Large Scale Profiling of Kinase Dependencies in Cancer Cell Lines, the highest RNAi cell lines are: SKGT4, KPD. (see details)

3D Structures


For CAMK2B there are:
1 structures (4 chains) solved
1 are solved in complex with at least one small molecule ligand



(see details)
Molecular Target 3D Synopsis

Screening and Chemistry


CAMK2B has been screened with 570 compounds (891 bioactivities), 28 compounds have bioactivities that show binding affinity of <= 500nM (38 bioactivities). (see details)