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P28652

- KCC2B_MOUSE

UniProt

P28652 - KCC2B_MOUSE

Protein

Calcium/calmodulin-dependent protein kinase type II subunit beta

Gene

Camk2b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 2 (02 May 2006)
      Previous versions | rss
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    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 – 431ATPPROSITE-ProRule annotation
    Active sitei136 – 1361Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi20 – 289ATPPROSITE-ProRule annotation

    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

    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

    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 autocatalysisBy similarity
    Modified residuei307 – 3071Phosphothreonine; by autocatalysisBy similarity

    Post-translational modificationi

    Autophosphorylation of Thr-287 following activation by Ca2+/calmodulin. Phosphorylation of Thr-287 locks the kinase into an activated state.2 Publications

    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.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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini14 – 272259Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

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

    Domaini

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

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti19 – 191D → E in CAA45160. (PubMed:1321343)Curated

    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

    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: October 1, 2014
    This is version 149 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