Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P28652 (KCC2B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Synonyms:Camk2d
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length542 AA.
Sequence statusComplete.
Protein existenceEvidence 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 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. Ref.8

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 By similarity.

Subcellular location

Cytoplasmcytoskeleton. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Sarcoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side By similarity.

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.

Disruption phenotype

Impaired long-term potentiation (LTP) and hippocampus-dependent learning. Ref.8

Sequence similarities

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processDifferentiation
Neurogenesis
   Cellular componentCytoplasm
Cytoskeleton
Membrane
Sarcoplasmic reticulum
   LigandATP-binding
Calmodulin-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG1/S transition of mitotic cell cycle

Inferred from mutant phenotype PubMed 12660151. Source: MGI

activation of meiosis involved in egg activation

Inferred from mutant phenotype PubMed 9882483. Source: MGI

calcium ion transport

Inferred from mutant phenotype PubMed 12660151. Source: MGI

inhibitory G-protein coupled receptor phosphorylation

Inferred from direct assay PubMed 19332541. Source: MGI

neuromuscular process controlling balance

Inferred from mutant phenotype PubMed 19503086. Source: MGI

peptidyl-serine phosphorylation

Inferred from direct assay PubMed 19332541. Source: MGI

positive regulation of apoptotic signaling pathway

Inferred from direct assay PubMed 17367784. Source: MGI

positive regulation of dendritic spine morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of neuron projection development

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of synapse maturation

Inferred from sequence or structural similarity. Source: UniProtKB

protein autophosphorylation

Inferred from mutant phenotype PubMed 12660151. Source: MGI

regulation of long-term neuronal synaptic plasticity

Inferred from mutant phenotype PubMed 19503086. Source: MGI

regulation of synaptic transmission, cholinergic

Inferred from mutant phenotype PubMed 19332541. Source: MGI

response to cadmium ion

Inferred from direct assay PubMed 17367784. Source: MGI

   Cellular_componentcalcium- and calmodulin-dependent protein kinase complex

Traceable author statement PubMed 11264466. Source: UniProtKB

cytosol

Inferred from direct assay PubMed 9882483. Source: MGI

microtubule organizing center

Inferred from electronic annotation. Source: UniProtKB-SubCell

sarcoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

spindle midzone

Inferred from direct assay PubMed 9882483. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

calmodulin-dependent protein kinase activity

Inferred from direct assay PubMed 9882483. Source: MGI

protein serine/threonine kinase activity

Inferred from direct assay PubMed 19332541. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ArcQ9WV312EBI-397029,EBI-397779
RYR1P117164EBI-397029,EBI-6477441From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 542542Calcium/calmodulin-dependent protein kinase type II subunit beta
PRO_0000086097

Regions

Domain14 – 272259Protein kinase
Nucleotide binding20 – 289ATP By similarity
Region283 – 29210Autoinhibitory domain By similarity
Region291 – 30111Calmodulin-binding

Sites

Active site1361Proton acceptor By similarity
Binding site431ATP By similarity

Amino acid modifications

Modified residue171Phosphotyrosine Ref.7
Modified residue2871Phosphothreonine; by autocatalysis Ref.5
Modified residue3061Phosphothreonine; by autocatalysis By similarity
Modified residue3071Phosphothreonine; by autocatalysis By similarity

Experimental info

Mutagenesis3031A → R: Blocks calcium/calmodulin binding. Ref.8
Sequence conflict191D → E in CAA45160. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P28652 [UniParc].

Last modified May 2, 2006. Version 2.
Checksum: 8A7962A6495FD0D0

FASTA54260,461
        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 RRDGKWQNVH FHCSGAPVAP 


LQ 

« Hide

References

« Hide 'large scale' references
[1]"Structure, expression, and chromosome location of the gene for the beta subunit of brain-specific Ca2+/calmodulin-dependent protein kinase II identified by transgene integration in an embryonic lethal mouse mutant."
Karls U., Mueller U., Gilbert D.J., Copeland N.G., Jenkins N.A., Harbers K.
Mol. Cell. Biol. 12:3644-3652(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Brain.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Cerebellum.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 136-147, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[5]"Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-287, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[6]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain cortex.
[7]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-17, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[8]"{beta}CaMKII plays a nonenzymatic role in hippocampal synaptic plasticity and learning by targeting {alpha}CaMKII to synapses."
Borgesius N.Z., van Woerden G.M., Buitendijk G.H., Keijzer N., Jaarsma D., Hoogenraad C.C., Elgersma Y.
J. Neurosci. 31:10141-10148(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF ALA-303.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X63615 mRNA. Translation: CAA45160.1.
AK163698 mRNA. Translation: BAE37464.1.
AL611926, AL645469 Genomic DNA. Translation: CAI24948.1.
AL645469, AL611926 Genomic DNA. Translation: CAI25258.1.
PIRA45025.
RefSeqNP_031621.3. NM_007595.5.
UniGeneMm.439733.

3D structure databases

ProteinModelPortalP28652.
SMRP28652. Positions 8-538.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198462. 5 interactions.
DIPDIP-31582N.
IntActP28652. 13 interactions.
MINTMINT-136473.

Chemistry

BindingDBP28652.

PTM databases

PhosphoSiteP28652.

Proteomic databases

PaxDbP28652.
PRIDEP28652.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000109813; ENSMUSP00000105438; ENSMUSG00000057897.
ENSMUST00000109815; ENSMUSP00000105440; ENSMUSG00000057897.
GeneID12323.
KEGGmmu:12323.
UCSCuc007hxr.2. mouse.

Organism-specific databases

CTD816.
MGIMGI:88257. Camk2b.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00720000108643.
HOGENOMHOG000233016.
HOVERGENHBG108055.
KOK04515.
OrthoDBEOG7ZD1VM.
TreeFamTF315229.

Enzyme and pathway databases

BRENDA2.7.11.17. 3474.

Gene expression databases

ArrayExpressP28652.
BgeeP28652.
GenevestigatorP28652.

Family and domain databases

InterProIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR013543. Ca/CaM-dep_prot_kinase-assoc.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERPTHR24347. PTHR24347. 1 hit.
PfamPF08332. CaMKII_AD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCAMK2B. mouse.
NextBio280904.
PROP28652.
SOURCESearch...

Entry information

Entry nameKCC2B_MOUSE
AccessionPrimary (citable) accession number: P28652
Secondary accession number(s): Q5SVH9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: May 2, 2006
Last modified: April 16, 2014
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot