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Q13554

- KCC2B_HUMAN

UniProt

Q13554 - KCC2B_HUMAN

Protein

Calcium/calmodulin-dependent protein kinase type II subunit beta

Gene

CAMK2B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 3 (31 May 2011)
      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.1 Publication

    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: UniProtKB-EC

    GO - Biological processi

    1. activation of meiosis involved in egg activation Source: Ensembl
    2. calcium ion transport Source: Ensembl
    3. cytokine-mediated signaling pathway Source: Reactome
    4. G1/S transition of mitotic cell cycle Source: Ensembl
    5. inhibitory G-protein coupled receptor phosphorylation Source: Ensembl
    6. interferon-gamma-mediated signaling pathway Source: Reactome
    7. neuromuscular process controlling balance Source: Ensembl
    8. peptidyl-serine phosphorylation Source: Ensembl
    9. positive regulation of apoptotic signaling pathway Source: Ensembl
    10. positive regulation of dendritic spine morphogenesis Source: UniProtKB
    11. positive regulation of neuron projection development Source: UniProtKB
    12. positive regulation of synapse maturation Source: UniProtKB
    13. protein autophosphorylation Source: UniProtKB
    14. protein phosphorylation Source: ProtInc
    15. regulation of calcium ion transport Source: UniProtKB
    16. regulation of dendritic spine development Source: UniProtKB
    17. regulation of long-term neuronal synaptic plasticity Source: UniProtKB
    18. regulation of skeletal muscle adaptation Source: UniProtKB
    19. regulation of synapse structural plasticity Source: UniProtKB
    20. regulation of synaptic transmission, cholinergic Source: Ensembl
    21. response to cadmium ion Source: Ensembl
    22. signal transduction Source: ProtInc
    23. synaptic transmission Source: Reactome

    Keywords - Molecular functioni

    Developmental protein, Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Differentiation, Neurogenesis

    Keywords - Ligandi

    Actin-binding, ATP-binding, Calmodulin-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.17. 2681.
    ReactomeiREACT_18307. Trafficking of AMPA receptors.
    REACT_200775. HSF1-dependent transactivation.
    REACT_20546. Ras activation uopn Ca2+ infux through NMDA receptor.
    REACT_20568. CREB phosphorylation through the activation of Ras.
    REACT_20594. Unblocking of NMDA receptor, glutamate binding and activation.
    REACT_20642. CREB phosphorylation through the activation of CaMKII.
    REACT_25078. Interferon gamma signaling.
    SignaLinkiQ13554.

    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:CAM2, CAMK2, CAMKB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:1461. CAMK2B.

    Subcellular locationi

    Cytoplasmcytoskeleton 1 Publication. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Sarcoplasmic reticulum membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication
    Note: In slow-twitch muscle, evenly distributed between longitudinal SR and junctional SR.

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. endocytic vesicle membrane Source: Reactome
    3. microtubule organizing center Source: UniProtKB-SubCell
    4. nucleoplasm Source: Reactome
    5. plasma membrane Source: Reactome
    6. sarcoplasmic reticulum membrane Source: UniProtKB-SubCell
    7. spindle midzone Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Membrane, Sarcoplasmic reticulum

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA91.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 666666Calcium/calmodulin-dependent protein kinase type II subunit betaPRO_0000086096Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei17 – 171PhosphotyrosineBy similarity
    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.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ13554.
    PaxDbiQ13554.
    PRIDEiQ13554.

    PTM databases

    PhosphoSiteiQ13554.

    Expressioni

    Tissue specificityi

    Widely expressed. Expressed in adult and fetal brain. Expression is slightly lower in fetal brain. Expressed in skeletal muscle.1 Publication

    Inductioni

    Activity is induced in skeletal muscle during exercise.1 Publication

    Gene expression databases

    ArrayExpressiQ13554.
    BgeeiQ13554.
    GenevestigatoriQ13554.

    Organism-specific databases

    HPAiCAB006849.
    HPA026307.
    HPA051783.
    HPA051785.
    HPA053973.

    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 and CAMK2N2 By similarity. Interacts with MPDZ.By similarity3 Publications

    Protein-protein interaction databases

    BioGridi107266. 11 interactions.
    DIPiDIP-39770N.
    IntActiQ13554. 4 interactions.

    Structurei

    Secondary structure

    1
    666
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi14 – 196
    Beta strandi27 – 337
    Turni34 – 363
    Beta strandi39 – 468
    Helixi52 – 6716
    Beta strandi76 – 816
    Beta strandi83 – 919
    Beta strandi95 – 973
    Helixi98 – 1025
    Helixi110 – 12920
    Helixi139 – 1413
    Beta strandi142 – 1454
    Beta strandi153 – 1553
    Helixi178 – 1803
    Helixi183 – 1864
    Helixi194 – 20916
    Helixi219 – 22810
    Turni235 – 2384
    Beta strandi239 – 2413
    Helixi243 – 25210
    Turni257 – 2593
    Helixi263 – 2664
    Helixi270 – 2734
    Helixi275 – 2784
    Helixi285 – 29814

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3BHHX-ray2.40A/B/C/D11-303[»]
    ProteinModelPortaliQ13554.
    SMRiQ13554. Positions 10-396, 534-660.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13554.

    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.
    HOVERGENiHBG108055.
    InParanoidiQ13554.
    KOiK04515.
    OMAiQGPPPCL.
    OrthoDBiEOG7ZD1VM.
    PhylomeDBiQ13554.
    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]

    Sequences (8)i

    Sequence statusi: Complete.

    This entry describes 8 isoformsi produced by alternative splicing. Align

    Note: The variable region of the CAMK2B protein is encoded by at least 7 exons (V1 to V7). Alternative splicing within this region gives rise to CAMK2B isoforms.

    Isoform 4 (identifier: Q13554-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « 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 NSAAATSPKG TLPPAALEPQ TTVIHNPVDG IKESSDSANT 400
    TIEDEDAKAP RVPDILSSVR RGSGAPEAEG PLPCPSPAPF SPLPAPSPRI 450
    SDILNSVRRG SGTPEAEGPL SAGPPPCLSP ALLGPLSSPS PRISDILNSV 500
    RRGSGTPEAE GPSPVGPPPC PSPTIPGPLP TPSRKQEIIK TTEQLIEAVN 550
    NGDFEAYAKI CDPGLTSFEP EALGNLVEGM DFHRFYFENL LAKNSKPIHT 600
    TILNPHVHVI GEDAACIAYI RLTQYIDGQG RPRTSQSEET RVWHRRDGKW 650
    QNVHFHCSGA PVAPLQ 666
    Length:666
    Mass (Da):72,678
    Last modified:May 31, 2011 - v3
    Checksum:i8CACFC3E392C3857
    GO
    Isoform 1 (identifier: Q13554-2) [UniParc]FASTAAdd to Basket

    Also known as: Beta

    The sequence of this isoform differs from the canonical sequence as follows:
         410-533: Missing.

    Show »
    Length:542
    Mass (Da):60,387
    Checksum:i1F7AF874A78C9D26
    GO
    Isoform 2 (identifier: Q13554-3) [UniParc]FASTAAdd to Basket

    Also known as: Beta1, Beta'E

    The sequence of this isoform differs from the canonical sequence as follows:
         316-316: V → A
         317-340: Missing.
         379-393: Missing.
         410-533: Missing.

    Show »
    Length:503
    Mass (Da):56,379
    Checksum:i4389A566D66A9FE1
    GO
    Isoform 3 (identifier: Q13554-4) [UniParc]FASTAAdd to Basket

    Also known as: Beta2

    The sequence of this isoform differs from the canonical sequence as follows:
         316-316: V → A
         317-340: Missing.
         354-392: Missing.
         410-533: Missing.

    Show »
    Length:479
    Mass (Da):54,074
    Checksum:iE8A4B57BD6AA98AC
    GO
    Isoform 5 (identifier: Q13554-5) [UniParc]FASTAAdd to Basket

    Also known as: Beta4, BetaE

    The sequence of this isoform differs from the canonical sequence as follows:
         316-316: V → A
         317-340: Missing.
         410-533: Missing.

    Show »
    Length:518
    Mass (Da):58,009
    Checksum:i5853A731579E86D8
    GO
    Isoform 6 (identifier: Q13554-6) [UniParc]FASTAAdd to Basket

    Also known as: Beta6

    The sequence of this isoform differs from the canonical sequence as follows:
         354-377: Missing.
         410-533: Missing.
         559-584: Missing.

    Show »
    Length:492
    Mass (Da):55,223
    Checksum:i1102B7F9B979E307
    GO
    Isoform 7 (identifier: Q13554-7) [UniParc]FASTAAdd to Basket

    Also known as: Beta7

    The sequence of this isoform differs from the canonical sequence as follows:
         316-316: V → A
         317-533: Missing.

    Show »
    Length:449
    Mass (Da):50,955
    Checksum:i6EB6617646B54829
    GO
    Isoform 8 (identifier: Q13554-8) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         316-340: Missing.
         410-533: Missing.

    Show »
    Length:517
    Mass (Da):57,938
    Checksum:i1F4A8797FB7458A4
    GO

    Sequence cautioni

    The sequence AAC99802.1 differs from that shown. Reason: Frameshift at positions 426, 433, 511 and 516.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti68 – 681L → V in AAD03744. 1 PublicationCurated
    Sequence conflicti68 – 681L → V in AAD03743. 1 PublicationCurated
    Sequence conflicti535 – 5351K → N in AAB16863. (PubMed:9060999)Curated
    Isoform 2 (identifier: Q13554-3)
    Sequence conflicti316 – 3161A → V in AAD42036. (PubMed:10858498)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti489 – 4891P → L in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_045581
    Natural varianti510 – 5101E → K.1 Publication
    Corresponds to variant rs35452727 [ dbSNP | Ensembl ].
    VAR_045582

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei316 – 34025Missing in isoform 8. CuratedVSP_041219Add
    BLAST
    Alternative sequencei316 – 3161V → A in isoform 2, isoform 3, isoform 5 and isoform 7. 6 PublicationsVSP_004770
    Alternative sequencei317 – 533217Missing in isoform 7. 1 PublicationVSP_004772Add
    BLAST
    Alternative sequencei317 – 34024Missing in isoform 2, isoform 3 and isoform 5. 6 PublicationsVSP_004771Add
    BLAST
    Alternative sequencei354 – 39239Missing in isoform 3. 1 PublicationVSP_004774Add
    BLAST
    Alternative sequencei354 – 37724Missing in isoform 6. 1 PublicationVSP_004773Add
    BLAST
    Alternative sequencei379 – 39315Missing in isoform 2. 5 PublicationsVSP_004775Add
    BLAST
    Alternative sequencei410 – 533124Missing in isoform 1, isoform 2, isoform 3, isoform 5, isoform 6 and isoform 8. 6 PublicationsVSP_004776Add
    BLAST
    Alternative sequencei559 – 58426Missing in isoform 6. 1 PublicationVSP_004777Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF078803 mRNA. Translation: AAD42035.1.
    AF081572 mRNA. Translation: AAD42036.1.
    AF081924 mRNA. Translation: AAD42037.1.
    AF083419 mRNA. Translation: AAD42038.1.
    AF140350 mRNA. Translation: AAD42070.1.
    U23460 mRNA. Translation: AAC99802.1. Frameshift.
    AF112472 mRNA. Translation: AAD03744.1.
    AF112471 mRNA. Translation: AAD03743.1.
    AJ252236 mRNA. Translation: CAB65120.1.
    AJ252237 mRNA. Translation: CAB65121.1.
    AJ252238 mRNA. Translation: CAB65122.1.
    AK290148 mRNA. Translation: BAF82837.1.
    AK315663 mRNA. Translation: BAG38029.1.
    CH236960 Genomic DNA. Translation: EAL23756.1.
    CH236960 Genomic DNA. Translation: EAL23757.1.
    CH236960 Genomic DNA. Translation: EAL23758.1.
    CH236960 Genomic DNA. Translation: EAL23759.1.
    CH236960 Genomic DNA. Translation: EAL23760.1.
    CH236960 Genomic DNA. Translation: EAL23761.1.
    CH236960 Genomic DNA. Translation: EAL23762.1.
    BC019070 mRNA. Translation: AAH19070.1.
    U50358 mRNA. Translation: AAB16863.1.
    CCDSiCCDS43573.1. [Q13554-8]
    CCDS5483.1. [Q13554-1]
    CCDS5484.1. [Q13554-2]
    CCDS5485.1. [Q13554-5]
    CCDS5486.1. [Q13554-3]
    CCDS5487.1. [Q13554-6]
    CCDS5488.1. [Q13554-4]
    CCDS5489.1. [Q13554-7]
    RefSeqiNP_001211.3. NM_001220.4. [Q13554-1]
    NP_742075.1. NM_172078.2. [Q13554-2]
    NP_742076.1. NM_172079.2. [Q13554-5]
    NP_742077.1. NM_172080.2. [Q13554-8]
    NP_742078.1. NM_172081.2. [Q13554-3]
    NP_742079.1. NM_172082.2. [Q13554-6]
    NP_742080.1. NM_172083.2. [Q13554-4]
    NP_742081.1. NM_172084.2. [Q13554-7]
    XP_006715839.1. XM_006715776.1. [Q13554-1]
    UniGeneiHs.351887.

    Genome annotation databases

    EnsembliENST00000258682; ENSP00000258682; ENSG00000058404. [Q13554-8]
    ENST00000346990; ENSP00000326518; ENSG00000058404. [Q13554-7]
    ENST00000347193; ENSP00000326544; ENSG00000058404. [Q13554-6]
    ENST00000350811; ENSP00000326375; ENSG00000058404. [Q13554-2]
    ENST00000353625; ENSP00000326427; ENSG00000058404. [Q13554-4]
    ENST00000358707; ENSP00000351542; ENSG00000058404. [Q13554-3]
    ENST00000395747; ENSP00000379096; ENSG00000058404. [Q13554-5]
    ENST00000395749; ENSP00000379098; ENSG00000058404. [Q13554-1]
    ENST00000440254; ENSP00000397937; ENSG00000058404. [Q13554-2]
    ENST00000457475; ENSP00000390292; ENSG00000058404. [Q13554-5]
    GeneIDi816.
    KEGGihsa:816.
    UCSCiuc003tkp.2. human. [Q13554-2]
    uc003tkq.2. human. [Q13554-1]
    uc003tkr.2. human. [Q13554-5]
    uc003tks.2. human. [Q13554-8]
    uc003tkt.2. human. [Q13554-6]
    uc003tku.2. human. [Q13554-3]
    uc003tkv.2. human. [Q13554-4]
    uc003tkw.2. human. [Q13554-7]

    Polymorphism databases

    DMDMi334302890.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF078803 mRNA. Translation: AAD42035.1 .
    AF081572 mRNA. Translation: AAD42036.1 .
    AF081924 mRNA. Translation: AAD42037.1 .
    AF083419 mRNA. Translation: AAD42038.1 .
    AF140350 mRNA. Translation: AAD42070.1 .
    U23460 mRNA. Translation: AAC99802.1 . Frameshift.
    AF112472 mRNA. Translation: AAD03744.1 .
    AF112471 mRNA. Translation: AAD03743.1 .
    AJ252236 mRNA. Translation: CAB65120.1 .
    AJ252237 mRNA. Translation: CAB65121.1 .
    AJ252238 mRNA. Translation: CAB65122.1 .
    AK290148 mRNA. Translation: BAF82837.1 .
    AK315663 mRNA. Translation: BAG38029.1 .
    CH236960 Genomic DNA. Translation: EAL23756.1 .
    CH236960 Genomic DNA. Translation: EAL23757.1 .
    CH236960 Genomic DNA. Translation: EAL23758.1 .
    CH236960 Genomic DNA. Translation: EAL23759.1 .
    CH236960 Genomic DNA. Translation: EAL23760.1 .
    CH236960 Genomic DNA. Translation: EAL23761.1 .
    CH236960 Genomic DNA. Translation: EAL23762.1 .
    BC019070 mRNA. Translation: AAH19070.1 .
    U50358 mRNA. Translation: AAB16863.1 .
    CCDSi CCDS43573.1. [Q13554-8 ]
    CCDS5483.1. [Q13554-1 ]
    CCDS5484.1. [Q13554-2 ]
    CCDS5485.1. [Q13554-5 ]
    CCDS5486.1. [Q13554-3 ]
    CCDS5487.1. [Q13554-6 ]
    CCDS5488.1. [Q13554-4 ]
    CCDS5489.1. [Q13554-7 ]
    RefSeqi NP_001211.3. NM_001220.4. [Q13554-1 ]
    NP_742075.1. NM_172078.2. [Q13554-2 ]
    NP_742076.1. NM_172079.2. [Q13554-5 ]
    NP_742077.1. NM_172080.2. [Q13554-8 ]
    NP_742078.1. NM_172081.2. [Q13554-3 ]
    NP_742079.1. NM_172082.2. [Q13554-6 ]
    NP_742080.1. NM_172083.2. [Q13554-4 ]
    NP_742081.1. NM_172084.2. [Q13554-7 ]
    XP_006715839.1. XM_006715776.1. [Q13554-1 ]
    UniGenei Hs.351887.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3BHH X-ray 2.40 A/B/C/D 11-303 [» ]
    ProteinModelPortali Q13554.
    SMRi Q13554. Positions 10-396, 534-660.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107266. 11 interactions.
    DIPi DIP-39770N.
    IntActi Q13554. 4 interactions.

    Chemistry

    BindingDBi Q13554.
    ChEMBLi CHEMBL4121.
    GuidetoPHARMACOLOGYi 1556.

    PTM databases

    PhosphoSitei Q13554.

    Polymorphism databases

    DMDMi 334302890.

    Proteomic databases

    MaxQBi Q13554.
    PaxDbi Q13554.
    PRIDEi Q13554.

    Protocols and materials databases

    DNASUi 816.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000258682 ; ENSP00000258682 ; ENSG00000058404 . [Q13554-8 ]
    ENST00000346990 ; ENSP00000326518 ; ENSG00000058404 . [Q13554-7 ]
    ENST00000347193 ; ENSP00000326544 ; ENSG00000058404 . [Q13554-6 ]
    ENST00000350811 ; ENSP00000326375 ; ENSG00000058404 . [Q13554-2 ]
    ENST00000353625 ; ENSP00000326427 ; ENSG00000058404 . [Q13554-4 ]
    ENST00000358707 ; ENSP00000351542 ; ENSG00000058404 . [Q13554-3 ]
    ENST00000395747 ; ENSP00000379096 ; ENSG00000058404 . [Q13554-5 ]
    ENST00000395749 ; ENSP00000379098 ; ENSG00000058404 . [Q13554-1 ]
    ENST00000440254 ; ENSP00000397937 ; ENSG00000058404 . [Q13554-2 ]
    ENST00000457475 ; ENSP00000390292 ; ENSG00000058404 . [Q13554-5 ]
    GeneIDi 816.
    KEGGi hsa:816.
    UCSCi uc003tkp.2. human. [Q13554-2 ]
    uc003tkq.2. human. [Q13554-1 ]
    uc003tkr.2. human. [Q13554-5 ]
    uc003tks.2. human. [Q13554-8 ]
    uc003tkt.2. human. [Q13554-6 ]
    uc003tku.2. human. [Q13554-3 ]
    uc003tkv.2. human. [Q13554-4 ]
    uc003tkw.2. human. [Q13554-7 ]

    Organism-specific databases

    CTDi 816.
    GeneCardsi GC07M044225.
    HGNCi HGNC:1461. CAMK2B.
    HPAi CAB006849.
    HPA026307.
    HPA051783.
    HPA051785.
    HPA053973.
    MIMi 607707. gene.
    neXtProti NX_Q13554.
    PharmGKBi PA91.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG108055.
    InParanoidi Q13554.
    KOi K04515.
    OMAi QGPPPCL.
    OrthoDBi EOG7ZD1VM.
    PhylomeDBi Q13554.
    TreeFami TF315229.

    Enzyme and pathway databases

    BRENDAi 2.7.11.17. 2681.
    Reactomei REACT_18307. Trafficking of AMPA receptors.
    REACT_200775. HSF1-dependent transactivation.
    REACT_20546. Ras activation uopn Ca2+ infux through NMDA receptor.
    REACT_20568. CREB phosphorylation through the activation of Ras.
    REACT_20594. Unblocking of NMDA receptor, glutamate binding and activation.
    REACT_20642. CREB phosphorylation through the activation of CaMKII.
    REACT_25078. Interferon gamma signaling.
    SignaLinki Q13554.

    Miscellaneous databases

    EvolutionaryTracei Q13554.
    GeneWikii CAMK2B.
    GenomeRNAii 816.
    NextBioi 3310.
    PROi Q13554.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13554.
    Bgeei Q13554.
    Genevestigatori Q13554.

    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. "Identification of alternative splicing variants of the beta subunit of human Ca(2+)/calmodulin-dependent protein kinase II with different activities."
      Wang P., Wu Y., Zhou T.H., Sun Y., Pei G.
      FEBS Lett. 475:107-110(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 5; 6 AND 7).
      Tissue: Brain.
    2. Leddy J.J., Salih M., Tuana B.S.
      Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
      Tissue: Skeletal muscle.
    3. "Molecular cloning and sequencing of human calcium/calmodulin dependent protein kinase II beta subunit."
      Li G.Y., Cooper N.G.F.
      Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 5).
      Tissue: Brain.
    4. "Cloning and quantitative determination of the human Ca2+/calmodulin-dependent protein kinase II (CaMK II) isoforms in human beta cells."
      Rochlitz H., Voigt A., Lankat-Buttgereit B., Goeke B., Heimberg H., Nauck M.A., Schiemann U., Schatz H., Pfeiffer A.F.
      Diabetologia 43:465-473(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 5).
      Tissue: Insulinoma.
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Testis and Thalamus.
    6. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Lung.
    8. "Identification of novel human tumor cell-specific CaMK-II variants."
      Tombes R.M., Krystal G.W.
      Biochim. Biophys. Acta 1355:281-292(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 302-605 (ISOFORM 2).
    9. "Comparative analyses of the three-dimensional structures and enzymatic properties of alpha, beta, gamma and delta isoforms of Ca2+-calmodulin-dependent protein kinase II."
      Gaertner T.R., Kolodziej S.J., Wang D., Kobayashi R., Koomen J.M., Stoops J.K., Waxham M.N.
      J. Biol. Chem. 279:12484-12494(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, SUBUNIT, AUTOPHOSPHORYLATION.
    10. "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] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MPDZ.
    11. "Ca2+-calmodulin-dependent protein kinase expression and signalling in skeletal muscle during exercise."
      Rose A.J., Kiens B., Richter E.A.
      J. Physiol. (Lond.) 574:889-903(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN SKELETAL MUSCLE, PHOSPHORYLATION AT THR-287, FUNCTION IN PHOSPHORYLATION OF PLN, TISSUE SPECIFICITY, INDUCTION.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: SUBCELLULAR LOCATION.
    14. "The role of calcium and calcium/calmodulin-dependent kinases in skeletal muscle plasticity and mitochondrial biogenesis."
      Chin E.R.
      Proc. Nutrit. Soc. 63:279-286(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION IN SKELETAL MUSCLE.
    15. "The Ca2+-calmodulin dependent protein kinase II system of skeletal muscle sarcoplasmic reticulum."
      Sacchetto R., Bovo E., Damiani E.
      Basic Appl. Myol. 15:5-17(2005)
      Cited for: REVIEW ON FUNCTION IN SKELETAL MUSCLE.
    16. "Calmodulin-kinases: modulators of neuronal development and plasticity."
      Wayman G.A., Lee Y.S., Tokumitsu H., Silva A.J., Silva A., Soderling T.R.
      Neuron 59:914-931(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION IN NEURONAL PLASTICITY.
    17. "The roles of CaMKII and F-actin in the structural plasticity of dendritic spines: a potential molecular identity of a synaptic tag?"
      Okamoto K., Bosch M., Hayashi Y.
      Physiology (Bethesda) 24:357-366(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION IN NEURONAL PLASTICITY.
    18. "Crystal structure of human calcium/calmodulin-dependent protein kinase IIb isoform 1 (CAMK2B)."
      Structural genomics consortium (SGC)
      Submitted (DEC-2007) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 11-303 IN COMPLEX WITH INHIBITOR.
    19. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-489 AND LYS-510.

    Entry informationi

    Entry nameiKCC2B_HUMAN
    AccessioniPrimary (citable) accession number: Q13554
    Secondary accession number(s): A4D2K0
    , A4D2K1, A4D2K2, A4D2K3, A4D2K4, A4D2K5, A4D2K6, O95437, O95438, O95599, Q9UGH7, Q9UGH8, Q9UGH9, Q9UNX0, Q9UNX7, Q9UP00, Q9Y5N4, Q9Y6F4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: May 31, 2011
    Last modified: October 1, 2014
    This is version 152 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3