Calcium/calmodulin-dependent protein kinase type II subunit alpha

Contribute

Send feedback

Read comments (?) or add your own

P11275 (KCC2A_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 128. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	478 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.8
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.
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. Ref.5 Ref.7 Ref.8 Ref.9
Subcellular location	Cell junction › synapse › presynaptic cell membrane. Cell junction › synapse. Note: Postsynaptic lipid rafts. Ref.9
Sequence similarities	Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Cell junction Cell membrane Membrane Synapse
Ligand	ATP-binding Calmodulin-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ionotropic glutamate receptor signaling pathway Inferred from direct assay PubMed 12223541. Source: UniProtKB peptidyl-serine phosphorylation Inferred from direct assay PubMed 12951199. Source: RGD protein autophosphorylation Inferred from direct assay PubMed 16095822. Source: RGD
Cellular_component	calcium- and calmodulin-dependent protein kinase complex Traceable author statement PubMed 11264466. Source: UniProtKB cell junction Inferred from electronic annotation. Source: UniProtKB-KW dendrite cytoplasm Inferred from direct assay PubMed 1419001. Source: BHF-UCL plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW presynaptic membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calmodulin-dependent protein kinase activity Inferred from direct assay PubMed 12401560 PubMed 12951199 PubMed 16095822. Source: RGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PSMC5	P62195	4	EBI-2640645,EBI-357745	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 478

478

Calcium/calmodulin-dependent protein kinase type II subunit alpha

PRO_0000086094

Regions

Domain

13 – 271

259

Protein kinase

Nucleotide binding

19 – 27

ATP By similarity

Region

290 – 300

Calmodulin-binding

Region

310 – 320

Interaction with BAALC

Sites

Active site

135

Proton acceptor

Binding site

ATP By similarity

Amino acid modifications

Modified residue

Phosphotyrosine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

275

Phosphoserine By similarity

Modified residue

286

Phosphothreonine; by autocatalysis Ref.6

Modified residue

333

Phosphoserine By similarity

Modified residue

334

Phosphothreonine By similarity

Modified residue

337

Phosphothreonine By similarity

Experimental info

Mutagenesis

432 – 435

IRIT → MGTA: Loss of interaction with MPDZ. Ref.8

Sequence conflict

301

G → A in AAA41855. Ref.3

Secondary structure

478

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P11275 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 306F416CCE9B5F62
Show »

FASTA

478

54,115

        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

References

[1]	"Molecular cloning of a brain-specific calcium/calmodulin-dependent protein kinase." Lin C.R., Kapiloff M.S., Durgerian S., Tatemoto K., Russo A.F., Hanson P., Schulman H., Rosenfeld M.G. Proc. Natl. Acad. Sci. U.S.A. 84:5962-5966(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Conserved and variable regions in the subunits of brain type II Ca2+/calmodulin-dependent protein kinase." Bulleit R.F., Bennett M.K., Molloy S.S., Hurley J.B., Kennedy M.B. Neuron 1:63-72(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Functional analysis of a complementary DNA for the 50-kilodalton subunit of calmodulin kinase II." Hanley R.M., Means A.R., Ono T., Kemp B.E., Burgin K.E., Waxham N., Kelly P.T. Science 237:293-297(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 132-327.
[4]	"Sequence analysis and DNA-protein interactions within the 5' flanking region of the Ca2+/calmodulin-dependent protein kinase II alpha-subunit gene." Sunyer T., Sahyoun N. Proc. Natl. Acad. Sci. U.S.A. 87:278-282(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
[5]	"Synaptic vesicle-associated Ca2+/calmodulin-dependent protein kinase II is a binding protein for synapsin I." Benfenati F., Valtorta F., Rubenstein J.L., Gorelick F.S., Greengard P., Czernik A.J. Nature 359:417-420(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 231-236; 238-246 AND 461-476, INTERACTION WITH SYN1.
[6]	"Ca2+/calmodulin-dependent protein kinase II: identification of threonine-286 as the autophosphorylation site in the alpha subunit associated with the generation of Ca2+-independent activity." Thiel G., Czernik A.J., Gorelick F., Nairn A.C., Greengard P. Proc. Natl. Acad. Sci. U.S.A. 85:6337-6341(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 282-299, PHOSPHORYLATION AT THR-286.
[7]	"Characterization of a calmodulin kinase II inhibitor protein in brain." Chang B.H., Mukherji S., Soderling T.R. Proc. Natl. Acad. Sci. U.S.A. 95:10890-10895(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CAMK2N2.
[8]	"SynGAP-MUPP1-CaMKII synaptic complexes regulate p38 MAP kinase activity and NMDA receptor-dependent synaptic AMPA receptor potentiation." Krapivinsky G., Medina I., Krapivinsky L., Gapon S., Clapham D.E. Neuron 43:563-574(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SYNGAP1 AND MPDZ, MUTAGENESIS OF 432-ILE--THR-435, FUNCTION.
[9]	"BAALC 1-6-8 protein is targeted to postsynaptic lipid rafts by its N-terminal miristoylation and palmitoylation, and interacts with a, but not b, subunit of Ca2+/calmodulin-dependent protein kinase II." Wang X., Tian Q.-B., Okano A., Sakagami H., Moon I.S., Kondo H., Endo S., Suzuki T. J. Neurochem. 92:647-659(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BAALC, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J02942 mRNA. Translation: AAA41870.1.
M16960 mRNA. Translation: AAA41855.1.
M29699 Genomic DNA. Translation: AAA40841.1.

IPI

IPI00192337.

PIR

A30355.

RefSeq

NP_037052.1. NM_012920.1.

UniGene

Rn.107499.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CM1	X-ray	2.00	B	290-314	[»]
1CM4	X-ray	2.00	B	290-314	[»]

ProteinModelPortal

P11275.

SMR

P11275. Positions 7-474.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29639N.

IntAct

P11275. 7 interactions.

MINT

MINT-153011.

STRING

10116.ENSRNOP00000025283.

PTM databases

PhosphoSite

P11275.

Proteomic databases

PaxDb

P11275.

PRIDE

P11275.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

25400.

KEGG

rno:25400.

UCSC

RGD:2261. rat.

Organism-specific databases

CTD

815.

RGD

2261. Camk2a.

Phylogenomic databases

eggNOG

COG0515.

HOVERGEN

HBG108055.

K04515.

Enzyme and pathway databases

BRENDA

2.7.11.17. 5301.

Gene expression databases

Genevestigator

P11275.

Family and domain databases

InterPro

IPR020636. 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]

PANTHER

PTHR24347. PTHR24347. 1 hit.

Pfam

PF08332. CaMKII_AD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]

SMART

SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P11275.

ChEMBL

CHEMBL2359.

EvolutionaryTrace

P11275.

NextBio

606489.

PMAP-CutDB

P11275.

Entry information

Entry name

KCC2A_RAT

Accession

Primary (citable) accession number: P11275

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	May 1, 2013
This is version 128 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents