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Q923T9

- KCC2G_MOUSE

UniProt

Q923T9 - KCC2G_MOUSE

Protein

Calcium/calmodulin-dependent protein kinase type II subunit gamma

Gene

Camk2g

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      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 sarcoplasmic reticulum Ca2+ transport in skeletal muscle and may function in dendritic spine and synapse formation and neuronal plasticity. 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 the ryanodine receptor-coupling factor triadin. In neurons, may participate in the promotion of dendritic spine and synapse formation and maintenance of synaptic plasticity which enables long-term potentiation (LTP) and hippocampus-dependent learning By similarity.By similarity

    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: UniProtKB-EC
    3. protein serine/threonine kinase activity Source: MGI

    GO - Biological processi

    1. calcium ion transport Source: MGI
    2. cell differentiation Source: UniProtKB-KW
    3. G1/S transition of mitotic cell cycle Source: MGI
    4. nervous system development Source: UniProtKB-KW
    5. protein autophosphorylation Source: MGI
    6. regulation of relaxation of cardiac muscle Source: BHF-UCL

    Keywords - Molecular functioni

    Developmental protein, 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 gamma (EC:2.7.11.17)
    Short name:
    CaM kinase II subunit gamma
    Short name:
    CaMK-II subunit gamma
    Gene namesi
    Name:Camk2g
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 14

    Organism-specific databases

    MGIiMGI:88259. Camk2g.

    Subcellular locationi

    GO - Cellular componenti

    1. sarcoplasmic reticulum membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Membrane, Sarcoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 529529Calcium/calmodulin-dependent protein kinase type II subunit gammaPRO_0000086102Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei287 – 2871Phosphothreonine; alternate1 Publication
    Modified residuei287 – 2871Phosphothreonine; by autocatalysis; alternate1 Publication
    Modified residuei306 – 3061Phosphothreonine; by autocatalysisBy similarity
    Modified residuei307 – 3071Phosphothreonine; by autocatalysisBy similarity
    Modified residuei311 – 3111PhosphoserineBy similarity
    Modified residuei349 – 3491PhosphoserineBy similarity
    Modified residuei352 – 3521PhosphoserineBy similarity

    Post-translational modificationi

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

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ923T9.
    PRIDEiQ923T9.

    PTM databases

    PhosphoSiteiQ923T9.

    Expressioni

    Gene expression databases

    ArrayExpressiQ923T9.
    BgeeiQ923T9.
    GenevestigatoriQ923T9.

    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 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi198463. 1 interaction.
    IntActiQ923T9. 3 interactions.
    MINTiMINT-4099582.
    STRINGi10090.ENSMUSP00000071720.

    Structurei

    3D structure databases

    ProteinModelPortaliQ923T9.
    SMRiQ923T9. Positions 3-302, 317-525.
    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-bindingBy similarityAdd
    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

    GeneTreeiENSGT00720000108643.
    HOGENOMiHOG000233016.
    HOVERGENiHBG108055.
    InParanoidiQ923T9.
    KOiK04515.
    OMAiRDCIPSV.
    OrthoDBiEOG7ZD1VM.
    PhylomeDBiQ923T9.
    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 (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: Q923T9-1) [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

    MATTATCTRF TDDYQLFEEL GKGAFSVVRR CVKKTSTQEY AAKIINTKKL    50
    SARDHQKLER EARICRLLKH PNIVRLHDSI SEEGFHYLVF DLVTGGELFE 100
    DIVAREYYSE ADASHCIHQI LESVNHIHQH DIVHRDLKPE NLLLASKCKG 150
    AAVKLADFGL AIEVQGEQQA WFGFAGTPGY LSPEVLRKDP YGKPVDIWAC 200
    GVILYILLVG YPPFWDEDQH KLYQQIKAGA YDFPSPEWDT VTPEAKNLIN 250
    QMLTINPAKR ITADQALKHP WVCQRSTVAS MMHRQETVEC LRKFNARRKL 300
    KGAILTTMLV SRNFSAAKSL LNKKSDGGVK KRKSSSSVHL MPQSNNKNSL 350
    VSPAQEPAPL QTAMEPQTTV VHNATDGIKG STESCNTTTE DEDLKVRKQE 400
    IIKITEQLIE AINNGDFEAY TKICDPGLTS FEPEALGNLV EGMDFHKFYF 450
    ENLLSKNSKP IHTTILNPHV HVIGEDAACI AYIRLTQYID GQGRPRTSQS 500
    EETRVWHRRD GKWLNVHYHC SGAPAAPLQ 529
    Length:529
    Mass (Da):59,607
    Last modified:December 1, 2001 - v1
    Checksum:iEE1D127BBA178544
    GO
    Isoform 2 (identifier: Q923T9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         331-341: Missing.

    Show »
    Length:518
    Mass (Da):58,365
    Checksum:i127250AF541196BF
    GO
    Isoform 3 (identifier: Q923T9-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         331-364: Missing.

    Show »
    Length:495
    Mass (Da):55,961
    Checksum:i168EA409723DF4C4
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei331 – 36434Missing in isoform 3. 1 PublicationVSP_004780Add
    BLAST
    Alternative sequencei331 – 34111Missing in isoform 2. 2 PublicationsVSP_004779Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF395884 mRNA. Translation: AAK84142.1.
    AK154764 mRNA. Translation: BAE32813.1.
    BC019162 mRNA. Translation: AAH19162.1.
    BC025597 mRNA. Translation: AAH25597.1.
    CCDSiCCDS26855.1. [Q923T9-2]
    CCDS26856.1. [Q923T9-3]
    CCDS26857.1. [Q923T9-1]
    RefSeqiNP_001034227.1. NM_001039138.2. [Q923T9-2]
    NP_001034228.1. NM_001039139.2. [Q923T9-3]
    NP_848712.2. NM_178597.5. [Q923T9-1]
    UniGeneiMm.235182.

    Genome annotation databases

    EnsembliENSMUST00000071816; ENSMUSP00000071720; ENSMUSG00000021820. [Q923T9-1]
    ENSMUST00000080440; ENSMUSP00000079298; ENSMUSG00000021820. [Q923T9-2]
    ENSMUST00000100837; ENSMUSP00000098398; ENSMUSG00000021820. [Q923T9-3]
    GeneIDi12325.
    KEGGimmu:12325.
    UCSCiuc007skt.1. mouse. [Q923T9-1]
    uc007sku.1. mouse. [Q923T9-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF395884 mRNA. Translation: AAK84142.1 .
    AK154764 mRNA. Translation: BAE32813.1 .
    BC019162 mRNA. Translation: AAH19162.1 .
    BC025597 mRNA. Translation: AAH25597.1 .
    CCDSi CCDS26855.1. [Q923T9-2 ]
    CCDS26856.1. [Q923T9-3 ]
    CCDS26857.1. [Q923T9-1 ]
    RefSeqi NP_001034227.1. NM_001039138.2. [Q923T9-2 ]
    NP_001034228.1. NM_001039139.2. [Q923T9-3 ]
    NP_848712.2. NM_178597.5. [Q923T9-1 ]
    UniGenei Mm.235182.

    3D structure databases

    ProteinModelPortali Q923T9.
    SMRi Q923T9. Positions 3-302, 317-525.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198463. 1 interaction.
    IntActi Q923T9. 3 interactions.
    MINTi MINT-4099582.
    STRINGi 10090.ENSMUSP00000071720.

    Chemistry

    BindingDBi Q923T9.

    PTM databases

    PhosphoSitei Q923T9.

    Proteomic databases

    MaxQBi Q923T9.
    PRIDEi Q923T9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000071816 ; ENSMUSP00000071720 ; ENSMUSG00000021820 . [Q923T9-1 ]
    ENSMUST00000080440 ; ENSMUSP00000079298 ; ENSMUSG00000021820 . [Q923T9-2 ]
    ENSMUST00000100837 ; ENSMUSP00000098398 ; ENSMUSG00000021820 . [Q923T9-3 ]
    GeneIDi 12325.
    KEGGi mmu:12325.
    UCSCi uc007skt.1. mouse. [Q923T9-1 ]
    uc007sku.1. mouse. [Q923T9-2 ]

    Organism-specific databases

    CTDi 818.
    MGIi MGI:88259. Camk2g.

    Phylogenomic databases

    GeneTreei ENSGT00720000108643.
    HOGENOMi HOG000233016.
    HOVERGENi HBG108055.
    InParanoidi Q923T9.
    KOi K04515.
    OMAi RDCIPSV.
    OrthoDBi EOG7ZD1VM.
    PhylomeDBi Q923T9.
    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 CAMK2G. mouse.
    NextBioi 280908.
    PROi Q923T9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q923T9.
    Bgeei Q923T9.
    Genevestigatori Q923T9.

    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 a mouse Ca2+/calmodulin-dependent protein kinase II."
      Szendro P.I., Cadenas C., Eichele G.
      Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: C57BL/6.
    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] (ISOFORM 2).
      Strain: NOD.
      Tissue: Dendritic cell.
    3. "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] (ISOFORMS 2 AND 3).
    4. "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.
    5. "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.

    Entry informationi

    Entry nameiKCC2G_MOUSE
    AccessioniPrimary (citable) accession number: Q923T9
    Secondary accession number(s): Q3U3H3, Q8VED3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 16, 2002
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 133 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, 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