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Q923T9 (KCC2G_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Calcium/calmodulin-dependent protein kinase type II subunit gamma
Short name=CaM kinase II subunit gamma
Short name=CaMK-II subunit gamma
EC=2.7.11.17
Gene names
Name:Camk2g
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length529 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

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.

Subunit structure

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.

Subcellular location

Sarcoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side Probable.

Domain

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

Post-translational modification

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

Sequence similarities

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily.

Contains 1 protein kinase domain.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: Q923T9-1)

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.
Isoform 2 (identifier: Q923T9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     331-341: Missing.
Isoform 3 (identifier: Q923T9-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 529529Calcium/calmodulin-dependent protein kinase type II subunit gamma
PRO_0000086102

Regions

Domain14 – 272259Protein kinase
Nucleotide binding20 – 289ATP By similarity
Region283 – 29210Autoinhibitory domain By similarity
Region291 – 30111Calmodulin-binding By similarity

Sites

Active site1361Proton acceptor By similarity
Binding site431ATP By similarity

Amino acid modifications

Modified residue2351Phosphoserine Ref.5
Modified residue2871Phosphothreonine; by autocatalysis Probable
Modified residue3061Phosphothreonine; by autocatalysis By similarity
Modified residue3071Phosphothreonine; by autocatalysis By similarity
Modified residue3111Phosphoserine By similarity
Modified residue3491Phosphoserine By similarity
Modified residue3521Phosphoserine By similarity

Natural variations

Alternative sequence331 – 36434Missing in isoform 3.
VSP_004780
Alternative sequence331 – 34111Missing in isoform 2.
VSP_004779

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: EE1D127BBA178544

FASTA52959,607
        10         20         30         40         50         60 
MATTATCTRF TDDYQLFEEL GKGAFSVVRR CVKKTSTQEY AAKIINTKKL SARDHQKLER 

        70         80         90        100        110        120 
EARICRLLKH PNIVRLHDSI SEEGFHYLVF DLVTGGELFE DIVAREYYSE ADASHCIHQI 

       130        140        150        160        170        180 
LESVNHIHQH DIVHRDLKPE NLLLASKCKG AAVKLADFGL AIEVQGEQQA WFGFAGTPGY 

       190        200        210        220        230        240 
LSPEVLRKDP YGKPVDIWAC GVILYILLVG YPPFWDEDQH KLYQQIKAGA YDFPSPEWDT 

       250        260        270        280        290        300 
VTPEAKNLIN QMLTINPAKR ITADQALKHP WVCQRSTVAS MMHRQETVEC LRKFNARRKL 

       310        320        330        340        350        360 
KGAILTTMLV SRNFSAAKSL LNKKSDGGVK KRKSSSSVHL MPQSNNKNSL VSPAQEPAPL 

       370        380        390        400        410        420 
QTAMEPQTTV VHNATDGIKG STESCNTTTE DEDLKVRKQE IIKITEQLIE AINNGDFEAY 

       430        440        450        460        470        480 
TKICDPGLTS FEPEALGNLV EGMDFHKFYF ENLLSKNSKP IHTTILNPHV HVIGEDAACI 

       490        500        510        520 
AYIRLTQYID GQGRPRTSQS EETRVWHRRD GKWLNVHYHC SGAPAAPLQ

« Hide

Isoform 2 [UniParc].

Checksum: 127250AF541196BF
Show »

FASTA51858,365
Isoform 3 [UniParc].

Checksum: 168EA409723DF4C4
Show »

FASTA49555,961

References

« Hide 'large scale' references
[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. expand/collapse author list , 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, MASS SPECTROMETRY.
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235 AND THR-287, MASS SPECTROMETRY.
Tissue: Brain cortex.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF395884 mRNA. Translation: AAK84142.1.
AK154764 mRNA. Translation: BAE32813.1.
BC019162 mRNA. Translation: AAH19162.1.
BC025597 mRNA. Translation: AAH25597.1.
IPIIPI00124695.
IPI00228044.
IPI00228045.
RefSeqNP_001034227.1. NM_001039138.1.
NP_001034228.1. NM_001039139.1.
NP_848712.2. NM_178597.4.
UniGeneMm.235182.

3D structure databases

ProteinModelPortalQ923T9.
SMRQ923T9. Positions 3-302, 317-525.
ModBaseSearch...

Protein-protein interaction databases

IntActQ923T9. 2 interactions.
MINTMINT-4099582.
STRING10090.ENSMUSP00000071720.

PTM databases

PhosphoSiteQ923T9.

Proteomic databases

PRIDEQ923T9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000071816; ENSMUSP00000071720; ENSMUSG00000021820.
ENSMUST00000080440; ENSMUSP00000079298; ENSMUSG00000021820.
ENSMUST00000100837; ENSMUSP00000098398; ENSMUSG00000021820.
GeneID12325.
KEGGmmu:12325.
UCSCuc007skt.1. mouse.
uc007sku.1. mouse.

Organism-specific databases

CTD818.
MGIMGI:88259. Camk2g.

Phylogenomic databases

GeneTreeENSGT00680000099653.
HOGENOMHOG000233016.
HOVERGENHBG108055.
InParanoidQ923T9.
KOK04515.
OMACIPSVGR.
OrthoDBEOG42JNR7.

Enzyme and pathway databases

BRENDA2.7.11.17. 3474.

Gene expression databases

ArrayExpressQ923T9.
BgeeQ923T9.
GenevestigatorQ923T9.
GermOnlineENSMUSG00000021820. Mus musculus.

Family and domain databases

InterProIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR013543. Ca/CaM-dep_prot_kinase-assoc.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERPTHR24347. PTHR24347. 1 hit.
PfamPF08332. CaMKII_AD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. Kinase_like. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBQ923T9.
ChEMBLCHEMBL4456.
ChiTaRSCAMK2G. mouse.
NextBio280908.
SOURCESearch...

Entry information

Entry nameKCC2G_MOUSE
AccessionPrimary (citable) accession number: Q923T9
Secondary accession number(s): Q3U3H3, Q8VED3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: December 1, 2001
Last modified: May 29, 2013
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents