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Q923T9

- KCC2G_MOUSE

UniProt

Q923T9 - KCC2G_MOUSE

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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

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.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Activated by Ca2+/calmodulin. Binding of calmodulin results in conformational change that relieves intrasteric autoinhibition and allows autophosphorylation of Thr-287 which turns the kinase in a constitutively active form and confers to the kinase a Ca2+-independent activity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei43 – 431ATP By similarity
Active sitei136 – 1361Proton acceptor By similarity

Regions

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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. calmodulin-dependent protein kinase activity Source: 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
Complete GO annotation...

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
Complete GO annotation...

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; alternate Inferred
Modified residuei306 – 3061Phosphothreonine; by autocatalysis By similarity
Modified residuei307 – 3071Phosphothreonine; by autocatalysis By similarity
Modified residuei311 – 3111Phosphoserine By similarity
Modified residuei349 – 3491Phosphoserine By similarity
Modified residuei352 – 3521Phosphoserine By similarity

Post-translational modificationi

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

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.

Family & Domainsi

Domains and Repeats

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

Region

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

Domaini

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

Sequence similaritiesi

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. VSP_004780Add
BLAST
Alternative sequencei331 – 34111Missing in isoform 2. VSP_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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 132 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

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