Calcium/calmodulin-dependent protein kinase type II subunit beta

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P08413 (KCC2B_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 110. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Calcium/calmodulin-dependent protein kinase type II subunit beta
Short name=CaM kinase II subunit beta
Short name=CaMK-II subunit beta
EC=2.7.11.17

Gene names

Name:

Camk2b

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	542 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 in 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 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. Ref.4 Ref.5 Ref.7
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	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.
Subunit structure	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. Ref.3 Ref.5
Subcellular location	Sarcoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cytoplasm › cytoskeleton. Cytoplasm › cytoskeleton › centrosome. Note: Colocalizes with the cortical actin cytoskeleton by binding to F-actin in hippocampal cells. Ref.2 Ref.4
Induction	By cocaine in cardiomyocytes. Ref.6 Ref.7
Domain	The CAMK2 protein kinases contain a unique C-terminal subunit association domain responsible for oligomerization.
Post-translational modification	Autophosphorylation of Thr-287 following activation by Ca²⁺/calmodulin. Phosphorylation of Thr-287 locks the kinase into an activated state.
Sequence similarities	Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Differentiation Neurogenesis
Cellular component	Cytoplasm Cytoskeleton Membrane Sarcoplasmic reticulum
Ligand	ATP-binding Calmodulin-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	long-term synaptic potentiation Inferred from mutant phenotype. Source: MGI positive regulation of dendritic spine morphogenesis Inferred from mutant phenotype Ref.4. Source: UniProtKB positive regulation of neuron projection development Inferred from mutant phenotype Ref.4. Source: UniProtKB positive regulation of synapse maturation Inferred from mutant phenotype Ref.4. Source: UniProtKB protein autophosphorylation Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	calcium- and calmodulin-dependent protein kinase complex Traceable author statement. Source: UniProtKB microtubule organizing center Inferred from electronic annotation. Source: UniProtKB-SubCell sarcoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calmodulin binding Inferred from electronic annotation. Source: UniProtKB-KW calmodulin-dependent protein kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PSMC5	P62195	3	EBI-916155,EBI-357745	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 542

542

Calcium/calmodulin-dependent protein kinase type II subunit beta

PRO_0000086098

Regions

Domain

14 – 272

259

Protein kinase

Nucleotide binding

20 – 28

ATP By similarity

Region

283 – 292

Autoinhibitory domain By similarity

Region

291 – 301

Calmodulin-binding

Sites

Active site

136

Proton acceptor By similarity

Binding site

ATP By similarity

Amino acid modifications

Modified residue

Phosphotyrosine By similarity

Modified residue

287

Phosphothreonine; by autocatalysis Ref.7

Modified residue

306

Phosphothreonine; by autocatalysis By similarity

Modified residue

307

Phosphothreonine; by autocatalysis By similarity

Modified residue

315

Phosphoserine By similarity

Modified residue

358

Phosphoserine By similarity

Modified residue

367

Phosphoserine By similarity

Modified residue

397

Phosphoserine By similarity

Experimental info

Mutagenesis

K → R: Catalytically inactive form. Ref.4

Mutagenesis

287

T → D: Constitutively active form. Ref.4

Mutagenesis

303

A → R: Blocks calcium/calmodulin binding. Ref.4

Sequences

Sequence

Length

Mass (Da)

Tools

P08413 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: 8A7962A64AE930D0
Show »

FASTA

542

60,402

        10         20         30         40         50         60 
MATTVTCTRF TDEYQLYEDI GKGAFSVVRR CVKLCTGHEY AAKIINTKKL SARDHQKLER 

        70         80         90        100        110        120 
EARICRLLKH SNIVRLHDSI SEEGFHYLVF DLVTGGELFE DIVAREYYSE ADASHCIQQI 

       130        140        150        160        170        180 
LEAVLHCHQM GVVHRDLKPE NLLLASKCKG AAVKLADFGL AIEVQGDQQA WFGFAGTPGY 

       190        200        210        220        230        240 
LSPEVLRKEA YGKPVDIWAC GVILYILLVG YPPFWDEDQH KLYQQIKAGA YDFPSPEWDT 

       250        260        270        280        290        300 
VTPEAKNLIN QMLTINPAKR ITAHEALKHP WVCQRSTVAS MMHRQETVEC LKKFNARRKL 

       310        320        330        340        350        360 
KGAILTTMLA TRNFSVGRQT TAPATMSTAA SGTTMGLVEQ AKSLLNKKAD GVKPQTNSTK 

       370        380        390        400        410        420 
NSSAITSPKG SLPPAALEPQ TTVIHNPVDG IKESSDSTNT TIEDEDAKAR KQEIIKTTEQ 

       430        440        450        460        470        480 
LIEAVNNGDF EAYAKICDPG LTSFEPEALG NLVEGMDFHR FYFENLLAKN SKPIHTTILN 

       490        500        510        520        530        540 
PHVHVIGEDA ACIAYIRLTQ YIDGQGRPRT SQSEETRVWH RPDGKWQNVH FHCSGAPVAP 


LQ

« Hide

References

[1]	"Deduced primary structure of the beta subunit of brain type II Ca2+/calmodulin-dependent protein kinase determined by molecular cloning." Bennett M.K., Kennedy M.B. Proc. Natl. Acad. Sci. U.S.A. 84:1794-1798(1987) [PubMed: 3470758] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"CaMKIIbeta functions as an F-actin targeting module that localizes CaMKIIalpha/beta heterooligomers to dendritic spines." Shen K., Teruel M.N., Subramanian K., Meyer T. Neuron 21:593-606(1998) [PubMed: 9768845] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[3]	"Characterization of a calmodulin kinase II inhibitor protein in brain." Chang B.H., Mukherji S., Soderling T.R. Proc. Natl. Acad. Sci. U.S.A. 95:10890-10895(1998) [PubMed: 9724800] [Abstract] Cited for: INTERACTION WITH CAMK2N2.
[4]	"Selective regulation of neurite extension and synapse formation by the beta but not the alpha isoform of CaMKII." Fink C.C., Bayer K.U., Myers J.W., Ferrell J.E. Jr., Schulman H., Meyer T. Neuron 39:283-297(2003) [PubMed: 12873385] [Abstract] Cited for: FUNCTION IN SYNAPSE FORMATION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-43; THR-287 AND ALA-303.
[5]	"SynGAP-MUPP1-CaMKII synaptic complexes regulate p38 MAP kinase activity and NMDA receptor-dependent synaptic AMPA receptor potentiation." Krapivinsky G., Medina I., Krapivinsky L., Gapon S., Clapham D.E. Neuron 43:563-574(2004) [PubMed: 15312654] [Abstract] Cited for: INTERACTION WITH SYNGAP1 AND MPDZ, FUNCTION.
[6]	"Cocaine activates calcium/calmodulin kinase II and causes cardiomyocyte hypertrophy." Henning R.J., Cuevas J. J. Cardiovasc. Pharmacol. 48:802-813(2006) [PubMed: 16891908] [Abstract] Cited for: INDUCTION BY COCAINE.
[7]	"Regulation and function of Ca2+-calmodulin-dependent protein kinase II of fast-twitch rat skeletal muscle." Rose A.J., Alsted T.J., Kobberoe J.B., Richter E.A. J. Physiol. (Lond.) 580:993-1005(2007) [PubMed: 17272343] [Abstract] Cited for: FUNCTION, INDUCTION, PHOSPHORYLATION AT THR-287.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M16112 mRNA. Translation: AAA41866.1.
IPI	IPI00211185.
PIR	A26464.
RefSeq	NP_001035815.1. NM_001042356.1. NP_068507.2. NM_021739.2.
UniGene	Rn.9743.
3D structure databases
ProteinModelPortal	P08413.
SMR	P08413. Positions 11-301, 403-536.
ModBase	Search...
Protein-protein interaction databases
IntAct	P08413. 3 interactions.
STRING	P08413.
PTM databases
PhosphoSite	P08413.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	24245.
KEGG	rno:24245.
UCSC	NM_021739. rat.
Organism-specific databases
CTD	816.
RGD	2262. Camk2b.
Phylogenomic databases
eggNOG	maNOG17752.
HOVERGEN	HBG108055.
PhylomeDB	P08413.
Enzyme and pathway databases
BRENDA	2.7.11.17. 5301.
Gene expression databases
ArrayExpress	P08413.
Genevestigator	P08413.
GermOnline	ENSRNOG00000004005. Rattus norvegicus.
Family and domain databases
InterPro	IPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase. IPR013543. Ca/CaM-dep_prot_kinase-assoc. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_kinase-like_dom. IPR008271. Ser/Thr_kinase_AS. IPR002290. Ser/Thr_kinase_dom. [Graphical view]
KO	K04515.
PANTHER	PTHR24347. PTHR24347. 1 hit.
Pfam	PF08332. CaMKII_AD. 1 hit. PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	602737.

Entry information

Entry name

KCC2B_RAT

Accession

Primary (citable) accession number: P08413

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1988
Last modified:	January 25, 2012
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents