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P11798 (KCC2A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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 alpha

Short name=CaM kinase II subunit alpha
Short name=CaMK-II subunit alpha
EC=2.7.11.17
Gene names
Name:Camk2a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length478 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

CaM-kinase II (CAMK2) is a prominent kinase in the central nervous system that may function in long-term potentiation and neurotransmitter release. Member of the NMDAR signaling complex in excitatory synapses it may regulate NMDAR-dependent potentiation of the AMPAR and synaptic plasticity By similarity.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Autophosphorylation of Thr-286 allows the kinase to switch from a calmodulin-dependent to a calmodulin-independent state By similarity.

Subunit structure

CAMK2 is composed of four different chains: alpha, beta, gamma, and delta. The different isoforms assemble into homo- or heteromultimeric holoenzymes composed of 8 to 12 subunits. Interacts with BAALC, MPDZ, SYN1, CAMK2N2 and SYNGAP1 By similarity.

Subcellular location

Isoform Alpha KAP: Cytoplasm Probable. Cell junctionsynapsepresynaptic cell membrane By similarity. Cell junctionsynapse By similarity. Note: Postsynaptic lipid rafts By similarity.

Tissue specificity

Isoform AlphaCaMKII is expressed in brain while isoform AlphaKAP is expressed in skeletal muscle.

Sequence similarities

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

Contains 1 protein kinase domain.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Cytoplasm
Membrane
Synapse
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Calmodulin-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG1/S transition of mitotic cell cycle

Inferred from mutant phenotype PubMed 12660151. Source: MGI

calcium ion transport

Inferred from mutant phenotype PubMed 12660151. Source: MGI

positive regulation of NF-kappaB transcription factor activity

Inferred from electronic annotation. Source: Ensembl

protein autophosphorylation

Inferred from mutant phenotype PubMed 12660151. Source: MGI

regulation of neuronal synaptic plasticity

Inferred from mutant phenotype PubMed 17610578. Source: MGI

regulation of neurotransmitter secretion

Inferred from mutant phenotype PubMed 12629219. Source: MGI

   Cellular_componentcalcium- and calmodulin-dependent protein kinase complex

Traceable author statement PubMed 11264466. Source: UniProtKB

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

presynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

calmodulin-dependent protein kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

glutamate receptor binding

Inferred from physical interaction PubMed 16710293. Source: MGI

protein serine/threonine kinase activity

Inferred from direct assay PubMed 18480293. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Actn2Q9JI913EBI-400384,EBI-299169
Bag6Q9Z1R23EBI-400402,EBI-644645
Dlg4Q621083EBI-400384,EBI-300895
Grin2bQ009603EBI-400384,EBI-396905From a different organism.
Grin2bQ010976EBI-400384,EBI-400125
Lrrc7P705872EBI-400384,EBI-7798464From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Alpha CaMKII (identifier: P11798-1)

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 Alpha KAP (identifier: P11798-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-289: Missing.
     290-314: LKKFNARRKLKGAILTTMLATRNFS → MLLFLTLWALVPCLVLLTLYFLSST
     328-328: K → KKRKSSSSVQLM
Note: Has no kinase activity.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 478478Calcium/calmodulin-dependent protein kinase type II subunit alpha
PRO_0000086092

Regions

Domain13 – 271259Protein kinase
Nucleotide binding19 – 279ATP By similarity
Region290 – 30011Calmodulin-binding
Region310 – 32011Interaction with BAALC By similarity

Sites

Active site1351Proton acceptor
Binding site421ATP By similarity

Amino acid modifications

Modified residue131Phosphotyrosine Ref.7
Modified residue2861Phosphothreonine; by autocatalysis

Natural variations

Alternative sequence1 – 289289Missing in isoform Alpha KAP.
VSP_004767
Alternative sequence290 – 31425LKKFN…TRNFS → MLLFLTLWALVPCLVLLTLY FLSST in isoform Alpha KAP.
VSP_004768
Alternative sequence3281K → KKRKSSSSVQLM in isoform Alpha KAP.
VSP_004769

Experimental info

Sequence conflict401A → P in CAA32946. Ref.1
Sequence conflict1691A → R in CAA32946. Ref.1
Sequence conflict2281G → R in CAA32946. Ref.1

Secondary structure

...................... 478
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Alpha CaMKII [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 306F416CCE9B5F62

FASTA47854,115
        10         20         30         40         50         60 
MATITCTRFT EEYQLFEELG KGAFSVVRRC VKVLAGQEYA AKIINTKKLS ARDHQKLERE 

        70         80         90        100        110        120 
ARICRLLKHP NIVRLHDSIS EEGHHYLIFD LVTGGELFED IVAREYYSEA DASHCIQQIL 

       130        140        150        160        170        180 
EAVLHCHQMG VVHRDLKPEN LLLASKLKGA AVKLADFGLA IEVEGEQQAW FGFAGTPGYL 

       190        200        210        220        230        240 
SPEVLRKDPY GKPVDLWACG VILYILLVGY PPFWDEDQHR LYQQIKAGAY DFPSPEWDTV 

       250        260        270        280        290        300 
TPEAKDLINK MLTINPSKRI TAAEALKHPW ISHRSTVASC MHRQETVDCL KKFNARRKLK 

       310        320        330        340        350        360 
GAILTTMLAT RNFSGGKSGG NKKNDGVKES SESTNTTIED EDTKVRKQEI IKVTEQLIEA 

       370        380        390        400        410        420 
ISNGDFESYT KMCDPGMTAF EPEALGNLVE GLDFHRFYFE NLWSRNSKPV HTTILNPHIH 

       430        440        450        460        470 
LMGDESACIA YIRITQYLDA GGIPRTAQSE ETRVWHRRDG KWQIVHFHRS GAPSVLPH 

« Hide

Isoform Alpha KAP [UniParc].

Checksum: 3FB8D6A5C891CBD4
Show »

FASTA20022,584

References

« Hide 'large scale' references
[1]"Sequence of the cDNA for the alpha subunit of calmodulin kinase II from mouse brain."
Hanley R.M., Payne M.E., Cruzalegui F., Christenson M.A., Means A.R.
Nucleic Acids Res. 17:3992-3992(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ICR.
Tissue: Brain.
[2]"An alternative, nonkinase product of the brain-specifically expressed Ca2+/calmodulin-dependent kinase II alpha isoform gene in skeletal muscle."
Bayer K.-U., Loehler J., Harbers K.
Mol. Cell. Biol. 16:29-36(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA KAP).
Strain: BALB/c.
Tissue: Skeletal muscle.
[3]"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].
Strain: C57BL/6J.
Tissue: Hippocampus.
[4]"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].
Tissue: Eye.
[5]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 9-21; 33-42; 135-146; 260-267; 301-311; 329-344; 353-371; 397-405; 434-445 AND 470-478, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[6]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[7]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-13, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X14836 mRNA. Translation: CAA32946.1.
X87142 mRNA. Translation: CAA60620.1.
AK083245 mRNA. Translation: BAC38829.1.
BC031745 mRNA. Translation: AAH31745.1.
PIRJC6083.
S04365.
RefSeqNP_001273738.1. NM_001286809.1.
NP_033922.1. NM_009792.3.
NP_803126.1. NM_177407.4.
UniGeneMm.131530.
Mm.446530.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HKXX-ray2.65A/B/C/D/E/F/G/H/I/J/K/L/M/N336-478[»]
ProteinModelPortalP11798.
SMRP11798. Positions 7-474.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198461. 6 interactions.
DIPDIP-31593N.
IntActP11798. 26 interactions.
MINTMINT-136541.

Chemistry

BindingDBP11798.

PTM databases

PhosphoSiteP11798.

Proteomic databases

PaxDbP11798.
PRIDEP11798.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000102888; ENSMUSP00000099952; ENSMUSG00000024617. [P11798-1]
ENSMUST00000115295; ENSMUSP00000110950; ENSMUSG00000024617. [P11798-2]
GeneID12322.
KEGGmmu:12322.
UCSCuc008fbg.2. mouse. [P11798-1]
uc008fbh.2. mouse. [P11798-2]

Organism-specific databases

CTD815.
MGIMGI:88256. Camk2a.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00720000108643.
HOGENOMHOG000233016.
HOVERGENHBG108055.
KOK04515.
OrthoDBEOG7ZD1VM.
TreeFamTF315229.

Enzyme and pathway databases

BRENDA2.7.11.17. 3474.

Gene expression databases

ArrayExpressP11798.
BgeeP11798.
GenevestigatorP11798.

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_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. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCAMK2A. mouse.
EvolutionaryTraceP11798.
NextBio280898.
PROP11798.
SOURCESearch...

Entry information

Entry nameKCC2A_MOUSE
AccessionPrimary (citable) accession number: P11798
Secondary accession number(s): Q61284, Q6ZWN4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 154 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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