Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Calcium/calmodulin-dependent protein kinase type II subunit beta

Gene

Camk2b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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 sarcoplasmic 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 in the modulation of skeletal muscle function in response to exercise. In slow-twitch muscles, is involved in regulation of sarcoplasmic reticulum (SR) Ca2+ transport and in fast-twitch muscle participates in 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/ATP2A2.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Activated by Ca2+/calmodulin. Binding of calmodulin results in conformational change that relieves intrasteric autoinhibition and allows autophosphorylation of Thr-287 which turns the kinase in a constitutively active form and confers to the kinase a Ca2+-independent activity.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei43ATPPROSITE-ProRule annotation1
Active sitei136Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi20 – 28ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

  • activation of meiosis involved in egg activation Source: MGI
  • calcium ion transport Source: MGI
  • cell differentiation Source: GO_Central
  • G1/S transition of mitotic cell cycle Source: MGI
  • inhibitory G-protein coupled receptor phosphorylation Source: MGI
  • intracellular signal transduction Source: GO_Central
  • long-term synaptic potentiation Source: MGI
  • nervous system development Source: GO_Central
  • neuromuscular process controlling balance Source: MGI
  • peptidyl-serine phosphorylation Source: MGI
  • peptidyl-threonine phosphorylation Source: GO_Central
  • positive regulation of apoptotic signaling pathway Source: MGI
  • positive regulation of dendritic spine morphogenesis Source: UniProtKB
  • positive regulation of neuron projection development Source: UniProtKB
  • positive regulation of synapse maturation Source: UniProtKB
  • protein autophosphorylation Source: MGI
  • regulation of long-term neuronal synaptic plasticity Source: MGI
  • regulation of synaptic transmission, cholinergic Source: MGI
  • response to cadmium ion Source: MGI

Keywordsi

Molecular functionCalmodulin-binding, Kinase, Serine/threonine-protein kinase, Transferase
Biological processDifferentiation, Neurogenesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.17 3474
ReactomeiR-MMU-3371571 HSF1-dependent transactivation
R-MMU-399719 Trafficking of AMPA receptors
R-MMU-438066 Unblocking of NMDA receptor, glutamate binding and activation
R-MMU-442729 CREB phosphorylation through the activation of CaMKII
R-MMU-442742 CREB phosphorylation through the activation of Ras
R-MMU-442982 Ras activation upon Ca2+ influx through NMDA receptor
R-MMU-5673001 RAF/MAP kinase cascade
R-MMU-877300 Interferon gamma signaling

Names & Taxonomyi

Protein namesi
Recommended name:
Calcium/calmodulin-dependent protein kinase type II subunit beta (EC:2.7.11.17)
Short name:
CaM kinase II subunit beta
Short name:
CaMK-II subunit beta
Gene namesi
Name:Camk2b
Synonyms:Camk2d
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:88257 Camk2b

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton, Membrane, Sarcoplasmic reticulum, Synapse

Pathology & Biotechi

Disruption phenotypei

Impaired long-term potentiation (LTP) and hippocampus-dependent learning.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi303A → R: Blocks calcium/calmodulin binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000860971 – 542Calcium/calmodulin-dependent protein kinase type II subunit betaAdd BLAST542

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei17PhosphotyrosineCombined sources1
Modified residuei287Phosphothreonine; by autocatalysisCombined sources1
Modified residuei306Phosphothreonine; by autocatalysisBy similarity1
Modified residuei307Phosphothreonine; by autocatalysisBy similarity1
Modified residuei367PhosphoserineBy similarity1
Modified residuei371PhosphoserineCombined sources1
Modified residuei394PhosphoserineCombined sources1
Modified residuei397PhosphoserineBy similarity1
Modified residuei400PhosphothreonineCombined sources1
Modified residuei401PhosphothreonineCombined sources1

Post-translational modificationi

Autophosphorylation of Thr-287 following activation by Ca2+/calmodulin. Phosphorylation of Thr-287 locks the kinase into an activated state.

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP28652
MaxQBiP28652
PeptideAtlasiP28652
PRIDEiP28652

PTM databases

iPTMnetiP28652
PhosphoSitePlusiP28652
SwissPalmiP28652

Expressioni

Gene expression databases

BgeeiENSMUSG00000057897
ExpressionAtlasiP28652 baseline and differential
GenevisibleiP28652 MM

Interactioni

Subunit structurei

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. Interacts with SYNGAP1, CAMK2N2 and MPDZ (By similarity). Interacts with FOXO3 (PubMed:23805378). Interacts (when in a kinase inactive state not associated with calmodulin) with ARC; leading to target ARC to inactive synapses (By similarity).By similarity1 Publication

Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198462, 23 interactors
DIPiDIP-31582N
IntActiP28652, 29 interactors
MINTiP28652

Structurei

3D structure databases

ProteinModelPortaliP28652
SMRiP28652
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini14 – 272Protein kinasePROSITE-ProRule annotationAdd BLAST259

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni283 – 292Autoinhibitory domainBy similarity10
Regioni291 – 301Calmodulin-bindingAdd BLAST11

Domaini

The CAMK2 protein kinases contain a unique C-terminal subunit association domain responsible for oligomerization.

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00760000118944
HOGENOMiHOG000233016
HOVERGENiHBG108055
InParanoidiP28652
KOiK04515
TreeFamiTF315229

Family and domain databases

InterProiView protein in InterPro
IPR013543 Ca/CaM-dep_prot_kinase-assoc
IPR011009 Kinase-like_dom_sf
IPR032710 NTF2-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF08332 CaMKII_AD, 1 hit
PF00069 Pkinase, 1 hit
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SUPFAMiSSF54427 SSF54427, 1 hit
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

Sequencei

Sequence statusi: Complete.

P28652-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATTVTCTRF TDEYQLYEDI GKGAFSVVRR CVKLCTGHEY AAKIINTKKL
60 70 80 90 100
SARDHQKLER EARICRLLKH SNIVRLHDSI SEEGFHYLVF DLVTGGELFE
110 120 130 140 150
DIVAREYYSE ADASHCIQQI LEAVLHCHQM GVVHRDLKPE NLLLASKCKG
160 170 180 190 200
AAVKLADFGL AIEVQGDQQA WFGFAGTPGY LSPEVLRKEA YGKPVDIWAC
210 220 230 240 250
GVILYILLVG YPPFWDEDQH KLYQQIKAGA YDFPSPEWDT VTPEAKNLIN
260 270 280 290 300
QMLTINPAKR ITAHEALKHP WVCQRSTVAS MMHRQETVEC LKKFNARRKL
310 320 330 340 350
KGAILTTMLA TRNFSVGRQT TAPATMSTAA SGTTMGLVEQ AKSLLNKKAD
360 370 380 390 400
GVKPQTNSTK NSSAITSPKG SLPPAALEPQ TTVIHNPVDG IKESSDSTNT
410 420 430 440 450
TIEDEDAKAR KQEIIKTTEQ LIEAVNNGDF EAYAKICDPG LTSFEPEALG
460 470 480 490 500
NLVEGMDFHR FYFENLLAKN SKPIHTTILN PHVHVIGEDA ACIAYIRLTQ
510 520 530 540
YIDGQGRPRT SQSEETRVWH RRDGKWQNVH FHCSGAPVAP LQ
Length:542
Mass (Da):60,461
Last modified:May 2, 2006 - v2
Checksum:i8A7962A6495FD0D0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti19D → E in CAA45160 (PubMed:1321343).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63615 mRNA Translation: CAA45160.1
AK163698 mRNA Translation: BAE37464.1
AL611926, AL645469 Genomic DNA Translation: CAI24948.1
AL645469, AL611926 Genomic DNA Translation: CAI25258.1
CCDSiCCDS24411.1
PIRiA45025
RefSeqiNP_031621.3, NM_007595.5
UniGeneiMm.439733

Genome annotation databases

EnsembliENSMUST00000109813; ENSMUSP00000105438; ENSMUSG00000057897
ENSMUST00000109815; ENSMUSP00000105440; ENSMUSG00000057897
GeneIDi12323
KEGGimmu:12323
UCSCiuc007hxr.2 mouse

Similar proteinsi

Entry informationi

Entry nameiKCC2B_MOUSE
AccessioniPrimary (citable) accession number: P28652
Secondary accession number(s): Q5SVH9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: May 2, 2006
Last modified: May 23, 2018
This is version 183 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health