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Q13555

- KCC2G_HUMAN

UniProt

Q13555 - KCC2G_HUMAN

Protein

Calcium/calmodulin-dependent protein kinase type II subunit gamma

Gene

CAMK2G

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 3 (12 Apr 2005)
      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 sarcoplsamic 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.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. calcium-dependent protein serine/threonine phosphatase activity Source: UniProtKB
    3. calmodulin binding Source: UniProtKB
    4. calmodulin-dependent protein kinase activity Source: UniProtKB-EC
    5. protein binding Source: IntAct

    GO - Biological processi

    1. calcium ion transport Source: Ensembl
    2. cell differentiation Source: UniProtKB-KW
    3. cytokine-mediated signaling pathway Source: Reactome
    4. dephosphorylation Source: GOC
    5. G1/S transition of mitotic cell cycle Source: Ensembl
    6. insulin secretion Source: UniProtKB
    7. interferon-gamma-mediated signaling pathway Source: Reactome
    8. nervous system development Source: UniProtKB-KW
    9. protein autophosphorylation Source: Ensembl
    10. regulation of calcium ion transport Source: UniProtKB
    11. regulation of relaxation of cardiac muscle Source: Ensembl
    12. regulation of skeletal muscle adaptation Source: UniProtKB
    13. synaptic transmission Source: Reactome

    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

    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.
    SignaLinkiQ13555.

    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
    Synonyms:CAMK, CAMK-II, CAMKG
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:1463. CAMK2G.

    Subcellular locationi

    GO - Cellular componenti

    1. calcium- and calmodulin-dependent protein kinase complex Source: UniProtKB
    2. cytosol Source: Reactome
    3. endocytic vesicle membrane Source: Reactome
    4. membrane Source: UniProtKB
    5. nucleoplasm Source: Reactome
    6. plasma membrane Source: Reactome
    7. sarcoplasmic reticulum membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Membrane, Sarcoplasmic reticulum

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA93.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 558558Calcium/calmodulin-dependent protein kinase type II subunit gammaPRO_0000086101Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei287 – 2871Phosphothreonine; by autocatalysis2 Publications
    Modified residuei306 – 3061Phosphothreonine; by autocatalysisBy similarity
    Modified residuei307 – 3071Phosphothreonine; by autocatalysisCurated
    Modified residuei311 – 3111Phosphoserine3 Publications
    Modified residuei349 – 3491Phosphoserine1 Publication
    Modified residuei352 – 3521Phosphoserine2 Publications
    Modified residuei419 – 4191Phosphoserine2 Publications

    Post-translational modificationi

    Autophosphorylation of Thr-287 following activation by Ca2+/calmodulin. Phosphorylation of Thr-287 locks the kinase into an activated state.4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ13555.
    PaxDbiQ13555.
    PRIDEiQ13555.

    PTM databases

    PhosphoSiteiQ13555.

    Expressioni

    Tissue specificityi

    Expressed in skeletal muscle.1 Publication

    Inductioni

    Activity is induced in skeletal muscle during exercise.1 Publication

    Gene expression databases

    ArrayExpressiQ13555.
    BgeeiQ13555.
    GenevestigatoriQ13555.

    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.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HSP90AB1P082382EBI-1383465,EBI-352572

    Protein-protein interaction databases

    BioGridi107268. 20 interactions.
    DIPiDIP-51315N.
    IntActiQ13555. 7 interactions.

    Structurei

    Secondary structure

    1
    558
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 135
    Beta strandi14 – 229
    Beta strandi26 – 338
    Turni34 – 374
    Beta strandi38 – 469
    Helixi52 – 6716
    Beta strandi76 – 816
    Beta strandi83 – 919
    Helixi98 – 1036
    Helixi110 – 12920
    Helixi139 – 1413
    Beta strandi142 – 1454
    Beta strandi153 – 1553
    Helixi178 – 1803
    Helixi183 – 1875
    Helixi194 – 20916
    Helixi219 – 2279
    Helixi237 – 2404
    Helixi243 – 25210
    Turni257 – 2593
    Helixi263 – 2664
    Helixi270 – 2734
    Helixi275 – 2784
    Helixi285 – 30117
    Helixi390 – 3978
    Helixi427 – 44317
    Helixi446 – 4527
    Beta strandi453 – 4608
    Helixi462 – 4643
    Beta strandi468 – 4703
    Helixi471 – 48111
    Turni482 – 4854
    Beta strandi490 – 50112
    Beta strandi506 – 51813
    Beta strandi524 – 53815
    Beta strandi541 – 55010

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2UX0X-ray2.46A/B/C/D/E/F389-556[»]
    2V7OX-ray2.25A5-315[»]
    ProteinModelPortaliQ13555.
    SMRiQ13555. Positions 3-302, 387-552.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13555.

    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 domain
    Regioni291 – 30111Calmodulin-bindingBy similarityAdd
    BLAST
    Regioni294 – 31623Calmodulin-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.
    InParanoidiQ13555.
    KOiK04515.
    OMAiERIRESC.
    OrthoDBiEOG7ZD1VM.
    PhylomeDBiQ13555.
    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 (10)i

    Sequence statusi: Complete.

    This entry describes 10 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q13555-1) [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 DEDLKARSPE 400
    GRSSRDRTAP SAGMQPQPSL CSSAMRKQEI IKITEQLIEA INNGDFEAYT 450
    KICDPGLTSF EPEALGNLVE GMDFHKFYFE NLLSKNSKPI HTTILNPHVH 500
    VIGEDAACIA YIRLTQYIDG QGRPRTSQSE ETRVWHRRDG KWLNVHYHCS 550
    GAPAAPLQ 558
    Length:558
    Mass (Da):62,609
    Last modified:April 12, 2005 - v3
    Checksum:i38D4112C2FDBD44C
    GO
    Isoform 2 (identifier: Q13555-2) [UniParc]FASTAAdd to Basket

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

    Note: Contains a phosphoserine at position 325.

    Show »
    Length:547
    Mass (Da):61,368
    Checksum:i1A1B6D508CF3D210
    GO
    Isoform 3 (identifier: Q13555-3) [UniParc]FASTAAdd to Basket

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

    Note: Contains a phosphoserine at position 325.

    Show »
    Length:524
    Mass (Da):58,963
    Checksum:i75E1E7B03A01C061
    GO
    Isoform 4 (identifier: Q13555-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         396-425: ARSPEGRSSRDRTAPSAGMQPQPSLCSSAM → V

    Show »
    Length:529
    Mass (Da):59,607
    Checksum:iEE1D127BBA178544
    GO
    Isoform 5 (identifier: Q13555-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         315-315: S → SVGRQSSAPASPAASAAGLAGQ
         341-363: Missing.
         396-425: ARSPEGRSSRDRTAPSAGMQPQPSLCSSAM → V

    Note: Contains a phosphoserine at position 325.

    Show »
    Length:527
    Mass (Da):59,038
    Checksum:i58DBF1B72F64FA31
    GO
    Isoform 6 (identifier: Q13555-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         315-315: S → SVGRQSSAPASPAASAAGLAGQ
         397-398: RS → APLRTGNGSSV

    Note: Contains a phosphoserine at position 325.

    Show »
    Length:588
    Mass (Da):65,242
    Checksum:i2B608F45E8FD3F86
    GO
    Isoform 7 (identifier: Q13555-7) [UniParc]FASTAAdd to Basket

    Also known as: gamma F

    The sequence of this isoform differs from the canonical sequence as follows:
         331-364: Missing.
         397-398: RS → APLRTGNGSSV

    Note: Contains a phosphoserine at position 325.

    Show »
    Length:533
    Mass (Da):59,760
    Checksum:i864E8CCF92872FB3
    GO
    Isoform 8 (identifier: Q13555-8) [UniParc]FASTAAdd to Basket

    Also known as: gamma E

    The sequence of this isoform differs from the canonical sequence as follows:
         331-341: Missing.
         397-398: RS → APLRTGNGSSV

    Note: Contains a phosphoserine at position 325.

    Show »
    Length:556
    Mass (Da):62,165
    Checksum:iB0E88BF9F07715CB
    GO
    Isoform 9 (identifier: Q13555-9) [UniParc]FASTAAdd to Basket

    Also known as: gamma D

    The sequence of this isoform differs from the canonical sequence as follows:
         331-341: Missing.
         351-364: Missing.
         397-398: RS → APLRTGNGSSV

    Note: Contains a phosphoserine at position 325. Contains a phosphoserine at position 338.

    Show »
    Length:542
    Mass (Da):60,743
    Checksum:i99F906D2A0BBCA36
    GO
    Isoform 10 (identifier: Q13555-10) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         331-364: Missing.
         396-425: ARSPEGRSSRDRTAPSAGMQPQPSLCSSAM → V

    Note: Contains a phosphoserine at position 325.

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

    Sequence cautioni

    The sequence AAB61379.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti230 – 2301A → T in AAB61379. (PubMed:8449910)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti36 – 361S → P.2 Publications
    Corresponds to variant rs17853266 [ dbSNP | Ensembl ].
    VAR_042430
    Natural varianti292 – 2921R → P Found in a patient with severe mental retardation, myopia, strabismus, low ATP production and decreased oxidation velocities. 1 Publication
    VAR_069390

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei315 – 3151S → SVGRQSSAPASPAASAAGLA GQ in isoform 5 and isoform 6. 1 PublicationVSP_032699
    Alternative sequencei331 – 36434Missing in isoform 3, isoform 7 and isoform 10. 2 PublicationsVSP_013350Add
    BLAST
    Alternative sequencei331 – 34111Missing in isoform 2, isoform 8 and isoform 9. 2 PublicationsVSP_013349Add
    BLAST
    Alternative sequencei341 – 36323Missing in isoform 5. 1 PublicationVSP_032700Add
    BLAST
    Alternative sequencei351 – 36414Missing in isoform 9. 1 PublicationVSP_036027Add
    BLAST
    Alternative sequencei396 – 42530ARSPE…CSSAM → V in isoform 4, isoform 5 and isoform 10. 3 PublicationsVSP_004778Add
    BLAST
    Alternative sequencei397 – 3982RS → APLRTGNGSSV in isoform 6, isoform 7, isoform 8 and isoform 9. 1 PublicationVSP_035456

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL713896, AC022400, AL596247 Genomic DNA. Translation: CAI13789.1.
    AL713896, AC022400, AL596247 Genomic DNA. Translation: CAI13790.1.
    AL713896, AC022400, AL596247 Genomic DNA. Translation: CAI13791.1.
    AL596247, AC022400, AL713896 Genomic DNA. Translation: CAI13965.1.
    AL596247, AC022400, AL713896 Genomic DNA. Translation: CAI13966.1.
    AL596247, AC022400, AL713896 Genomic DNA. Translation: CAI13968.1.
    CH471083 Genomic DNA. Translation: EAW54532.1.
    CH471083 Genomic DNA. Translation: EAW54536.1.
    BC034044 mRNA. Translation: AAH34044.1.
    U66064 mRNA. Translation: AAB80848.1.
    AH011636 Genomic DNA. Translation: AAM33514.1.
    L07043 mRNA. Translation: AAB61379.1. Different initiation.
    U50359 mRNA. Translation: AAB16864.1.
    U50360 mRNA. Translation: AAB16865.1.
    U32472 mRNA. Translation: AAA75201.1.
    U32473 mRNA. Translation: AAA75202.1.
    U32509 mRNA. Translation: AAA75203.1.
    CCDSiCCDS7336.1. [Q13555-10]
    CCDS7337.1. [Q13555-5]
    CCDS7338.1. [Q13555-8]
    PIRiG01975.
    G01978.
    RefSeqiNP_001213.2. NM_001222.3. [Q13555-10]
    NP_751909.1. NM_172169.2. [Q13555-5]
    NP_751913.1. NM_172173.2.
    XP_005270258.1. XM_005270201.1. [Q13555-9]
    XP_005270259.1. XM_005270202.1. [Q13555-7]
    XP_005270260.1. XM_005270203.1. [Q13555-4]
    XP_006718056.1. XM_006717993.1. [Q13555-6]
    UniGeneiHs.523045.

    Genome annotation databases

    EnsembliENST00000305762; ENSP00000307082; ENSG00000148660. [Q13555-4]
    ENST00000322635; ENSP00000315599; ENSG00000148660. [Q13555-5]
    ENST00000322680; ENSP00000319060; ENSG00000148660. [Q13555-8]
    ENST00000351293; ENSP00000277853; ENSG00000148660. [Q13555-10]
    ENST00000394762; ENSP00000378243; ENSG00000148660. [Q13555-7]
    ENST00000423381; ENSP00000410298; ENSG00000148660. [Q13555-6]
    GeneIDi818.
    KEGGihsa:818.
    UCSCiuc001jvm.2. human. [Q13555-8]
    uc001jvo.2. human. [Q13555-5]
    uc001jvq.2. human. [Q13555-10]

    Polymorphism databases

    DMDMi62512173.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL713896 , AC022400 , AL596247 Genomic DNA. Translation: CAI13789.1 .
    AL713896 , AC022400 , AL596247 Genomic DNA. Translation: CAI13790.1 .
    AL713896 , AC022400 , AL596247 Genomic DNA. Translation: CAI13791.1 .
    AL596247 , AC022400 , AL713896 Genomic DNA. Translation: CAI13965.1 .
    AL596247 , AC022400 , AL713896 Genomic DNA. Translation: CAI13966.1 .
    AL596247 , AC022400 , AL713896 Genomic DNA. Translation: CAI13968.1 .
    CH471083 Genomic DNA. Translation: EAW54532.1 .
    CH471083 Genomic DNA. Translation: EAW54536.1 .
    BC034044 mRNA. Translation: AAH34044.1 .
    U66064 mRNA. Translation: AAB80848.1 .
    AH011636 Genomic DNA. Translation: AAM33514.1 .
    L07043 mRNA. Translation: AAB61379.1 . Different initiation.
    U50359 mRNA. Translation: AAB16864.1 .
    U50360 mRNA. Translation: AAB16865.1 .
    U32472 mRNA. Translation: AAA75201.1 .
    U32473 mRNA. Translation: AAA75202.1 .
    U32509 mRNA. Translation: AAA75203.1 .
    CCDSi CCDS7336.1. [Q13555-10 ]
    CCDS7337.1. [Q13555-5 ]
    CCDS7338.1. [Q13555-8 ]
    PIRi G01975.
    G01978.
    RefSeqi NP_001213.2. NM_001222.3. [Q13555-10 ]
    NP_751909.1. NM_172169.2. [Q13555-5 ]
    NP_751913.1. NM_172173.2.
    XP_005270258.1. XM_005270201.1. [Q13555-9 ]
    XP_005270259.1. XM_005270202.1. [Q13555-7 ]
    XP_005270260.1. XM_005270203.1. [Q13555-4 ]
    XP_006718056.1. XM_006717993.1. [Q13555-6 ]
    UniGenei Hs.523045.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2UX0 X-ray 2.46 A/B/C/D/E/F 389-556 [» ]
    2V7O X-ray 2.25 A 5-315 [» ]
    ProteinModelPortali Q13555.
    SMRi Q13555. Positions 3-302, 387-552.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107268. 20 interactions.
    DIPi DIP-51315N.
    IntActi Q13555. 7 interactions.

    Chemistry

    BindingDBi Q13555.
    ChEMBLi CHEMBL2097164.
    GuidetoPHARMACOLOGYi 1557.

    PTM databases

    PhosphoSitei Q13555.

    Polymorphism databases

    DMDMi 62512173.

    Proteomic databases

    MaxQBi Q13555.
    PaxDbi Q13555.
    PRIDEi Q13555.

    Protocols and materials databases

    DNASUi 818.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000305762 ; ENSP00000307082 ; ENSG00000148660 . [Q13555-4 ]
    ENST00000322635 ; ENSP00000315599 ; ENSG00000148660 . [Q13555-5 ]
    ENST00000322680 ; ENSP00000319060 ; ENSG00000148660 . [Q13555-8 ]
    ENST00000351293 ; ENSP00000277853 ; ENSG00000148660 . [Q13555-10 ]
    ENST00000394762 ; ENSP00000378243 ; ENSG00000148660 . [Q13555-7 ]
    ENST00000423381 ; ENSP00000410298 ; ENSG00000148660 . [Q13555-6 ]
    GeneIDi 818.
    KEGGi hsa:818.
    UCSCi uc001jvm.2. human. [Q13555-8 ]
    uc001jvo.2. human. [Q13555-5 ]
    uc001jvq.2. human. [Q13555-10 ]

    Organism-specific databases

    CTDi 818.
    GeneCardsi GC10M075572.
    HGNCi HGNC:1463. CAMK2G.
    MIMi 602123. gene.
    neXtProti NX_Q13555.
    PharmGKBi PA93.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG108055.
    InParanoidi Q13555.
    KOi K04515.
    OMAi ERIRESC.
    OrthoDBi EOG7ZD1VM.
    PhylomeDBi Q13555.
    TreeFami TF315229.

    Enzyme and pathway databases

    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 Q13555.

    Miscellaneous databases

    ChiTaRSi CAMK2G. human.
    EvolutionaryTracei Q13555.
    GeneWikii CAMK2G.
    GenomeRNAii 818.
    NextBioi 3340.
    PROi Q13555.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13555.
    Bgeei Q13555.
    Genevestigatori Q13555.

    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. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PRO-36.
    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] (ISOFORM 5), VARIANT PRO-36.
      Tissue: Brain.
    4. "Human islets of Langerhans express multiple isoforms of calcium/calmodulin-dependent protein kinase II."
      Breen M.A., Ashcroft S.J.
      Biochem. Biophys. Res. Commun. 236:473-478(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-315.
    5. "Human calcium/calmodulin-dependent protein kinase II gamma: cloning, genomic structure and detection of variants in subjects with type II diabetes."
      Gloyn A.L., Desai M., Clark A., Levy J.C., Holman R.R., Frayling T.M., Hattersley A.T., Ashcroft S.J.
      Diabetologia 45:580-583(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-558, ALTERNATIVE SPLICING (ISOFORM 6).
    6. "Cloning and analysis of two new isoforms of multifunctional Ca2+/calmodulin-dependent protein kinase. Expression in multiple human tissues."
      Nghiem P., Saati S.M., Martens C.L., Gardner P., Schulman H.
      J. Biol. Chem. 268:5471-5479(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 66-436 (ISOFORM 10).
    7. "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 302-497 (ISOFORMS 2 AND 4).
    8. "Human biliary epithelial cell line Mz-ChA-1 expresses new isoforms of calmodulin-dependent protein kinase II."
      Kwiatkowski A.P., McGill J.M.
      Gastroenterology 109:1316-1323(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 326-432 (ISOFORMS 7; 8 AND 9).
    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. "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.
    11. "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.
    12. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311; SER-349; SER-352 AND SER-419, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325 (ISOFORMS 10; 2; 3; 5; 6; 7; 8 AND 9), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338 (ISOFORM 9), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-287; SER-311; SER-352 AND SER-419, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325 (ISOFORMS 10; 2; 3; 7; 8 AND 9), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation."
      Rellos P., Pike A.C., Niesen F.H., Salah E., Lee W.H., von Delft F., Knapp S.
      PLoS Biol. 8:E1000426-E1000426(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 5-315 AND 426-556 IN COMPLEX WITH INHIBITOR.
    18. Cited for: VARIANT PRO-292.

    Entry informationi

    Entry nameiKCC2G_HUMAN
    AccessioniPrimary (citable) accession number: Q13555
    Secondary accession number(s): O00561
    , O15378, Q13279, Q13282, Q13556, Q5SQZ3, Q5SQZ4, Q5SWX4, Q7KYX5, Q8N4I3, Q8NIA4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: April 12, 2005
    Last modified: October 1, 2014
    This is version 148 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 10
      Human chromosome 10: 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