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P28652

- KCC2B_MOUSE

UniProt

P28652 - KCC2B_MOUSE

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Protein

Calcium/calmodulin-dependent protein kinase type II subunit beta

Gene
Camk2b, Camk2d
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei43 – 431ATP By similarity
Active sitei136 – 1361Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi20 – 289ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. calmodulin-dependent protein kinase activity Source: MGI
  3. protein binding Source: IntAct
  4. protein serine/threonine kinase activity Source: MGI

GO - Biological processi

  1. activation of meiosis involved in egg activation Source: MGI
  2. calcium ion transport Source: MGI
  3. G1/S transition of mitotic cell cycle Source: MGI
  4. inhibitory G-protein coupled receptor phosphorylation Source: MGI
  5. neuromuscular process controlling balance Source: MGI
  6. peptidyl-serine phosphorylation Source: MGI
  7. positive regulation of apoptotic signaling pathway Source: MGI
  8. positive regulation of dendritic spine morphogenesis Source: UniProtKB
  9. positive regulation of neuron projection development Source: UniProtKB
  10. positive regulation of synapse maturation Source: UniProtKB
  11. protein autophosphorylation Source: MGI
  12. regulation of long-term neuronal synaptic plasticity Source: MGI
  13. regulation of synaptic transmission, cholinergic Source: MGI
  14. response to cadmium ion Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Differentiation, Neurogenesis

Keywords - Ligandi

ATP-binding, Calmodulin-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.17. 3474.
ReactomeiREACT_198244. Ras activation uopn Ca2+ infux through NMDA receptor.
REACT_198246. CREB phosphorylation through the activation of Ras.
REACT_198248. CREB phosphorylation through the activation of CaMKII.
REACT_198660. Interferon gamma signaling.
REACT_213550. HSF1-dependent transactivation.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:88257. Camk2b.

Subcellular locationi

GO - Cellular componenti

  1. calcium- and calmodulin-dependent protein kinase complex Source: UniProtKB
  2. cytosol Source: MGI
  3. microtubule organizing center Source: UniProtKB-SubCell
  4. sarcoplasmic reticulum membrane Source: UniProtKB-SubCell
  5. spindle midzone Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane, Sarcoplasmic reticulum

Pathology & Biotechi

Disruption phenotypei

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

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi303 – 3031A → R: Blocks calcium/calmodulin binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 542542Calcium/calmodulin-dependent protein kinase type II subunit betaPRO_0000086097Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei17 – 171Phosphotyrosine1 Publication
Modified residuei287 – 2871Phosphothreonine; by autocatalysis1 Publication
Modified residuei306 – 3061Phosphothreonine; by autocatalysis By similarity
Modified residuei307 – 3071Phosphothreonine; by autocatalysis By similarity

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

MaxQBiP28652.
PaxDbiP28652.
PRIDEiP28652.

PTM databases

PhosphoSiteiP28652.

Expressioni

Gene expression databases

ArrayExpressiP28652.
BgeeiP28652.
GenevestigatoriP28652.

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
ArcQ9WV312EBI-397029,EBI-397779
RYR1P117164EBI-397029,EBI-6477441From a different organism.

Protein-protein interaction databases

BioGridi198462. 5 interactions.
DIPiDIP-31582N.
IntActiP28652. 13 interactions.
MINTiMINT-136473.

Structurei

3D structure databases

ProteinModelPortaliP28652.
SMRiP28652. Positions 10-536.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 272259Protein kinaseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni283 – 29210Autoinhibitory domain By similarity
Regioni291 – 30111Calmodulin-bindingAdd
BLAST

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00720000108643.
HOGENOMiHOG000233016.
HOVERGENiHBG108055.
KOiK04515.
OrthoDBiEOG7ZD1VM.
TreeFamiTF315229.

Family and domain databases

InterProiIPR020636. 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]
PANTHERiPTHR24347. PTHR24347. 1 hit.
PfamiPF08332. CaMKII_AD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P28652-1 [UniParc]FASTAAdd to Basket

« Hide

MATTVTCTRF TDEYQLYEDI GKGAFSVVRR CVKLCTGHEY AAKIINTKKL    50
SARDHQKLER EARICRLLKH SNIVRLHDSI SEEGFHYLVF DLVTGGELFE 100
DIVAREYYSE ADASHCIQQI LEAVLHCHQM GVVHRDLKPE NLLLASKCKG 150
AAVKLADFGL AIEVQGDQQA WFGFAGTPGY LSPEVLRKEA YGKPVDIWAC 200
GVILYILLVG YPPFWDEDQH KLYQQIKAGA YDFPSPEWDT VTPEAKNLIN 250
QMLTINPAKR ITAHEALKHP WVCQRSTVAS MMHRQETVEC LKKFNARRKL 300
KGAILTTMLA TRNFSVGRQT TAPATMSTAA SGTTMGLVEQ AKSLLNKKAD 350
GVKPQTNSTK NSSAITSPKG SLPPAALEPQ TTVIHNPVDG IKESSDSTNT 400
TIEDEDAKAR KQEIIKTTEQ LIEAVNNGDF EAYAKICDPG LTSFEPEALG 450
NLVEGMDFHR FYFENLLAKN SKPIHTTILN PHVHVIGEDA ACIAYIRLTQ 500
YIDGQGRPRT SQSEETRVWH RRDGKWQNVH FHCSGAPVAP LQ 542
Length:542
Mass (Da):60,461
Last modified:May 2, 2006 - v2
Checksum:i8A7962A6495FD0D0
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 191D → E in CAA45160. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS24411.1.
PIRi A45025.
RefSeqi NP_031621.3. NM_007595.5.
UniGenei Mm.439733.

3D structure databases

ProteinModelPortali P28652.
SMRi P28652. Positions 10-536.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198462. 5 interactions.
DIPi DIP-31582N.
IntActi P28652. 13 interactions.
MINTi MINT-136473.

Chemistry

BindingDBi P28652.

PTM databases

PhosphoSitei P28652.

Proteomic databases

MaxQBi P28652.
PaxDbi P28652.
PRIDEi P28652.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000109813 ; ENSMUSP00000105438 ; ENSMUSG00000057897 .
ENSMUST00000109815 ; ENSMUSP00000105440 ; ENSMUSG00000057897 .
GeneIDi 12323.
KEGGi mmu:12323.
UCSCi uc007hxr.2. mouse.

Organism-specific databases

CTDi 816.
MGIi MGI:88257. Camk2b.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00720000108643.
HOGENOMi HOG000233016.
HOVERGENi HBG108055.
KOi K04515.
OrthoDBi EOG7ZD1VM.
TreeFami TF315229.

Enzyme and pathway databases

BRENDAi 2.7.11.17. 3474.
Reactomei REACT_198244. Ras activation uopn Ca2+ infux through NMDA receptor.
REACT_198246. CREB phosphorylation through the activation of Ras.
REACT_198248. CREB phosphorylation through the activation of CaMKII.
REACT_198660. Interferon gamma signaling.
REACT_213550. HSF1-dependent transactivation.

Miscellaneous databases

ChiTaRSi CAMK2B. mouse.
NextBioi 280904.
PROi P28652.
SOURCEi Search...

Gene expression databases

ArrayExpressi P28652.
Bgeei P28652.
Genevestigatori P28652.

Family and domain databases

InterProi IPR020636. 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 ]
PANTHERi PTHR24347. PTHR24347. 1 hit.
Pfami PF08332. CaMKII_AD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiKCC2B_MOUSE
AccessioniPrimary (citable) accession number: P28652
Secondary accession number(s): Q5SVH9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: May 2, 2006
Last modified: September 3, 2014
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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