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P11275

- KCC2A_RAT

UniProt

P11275 - KCC2A_RAT

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Protein

Calcium/calmodulin-dependent protein kinase type II subunit alpha

Gene

Camk2a

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Autophosphorylation of Thr-286 allows the kinase to switch from a calmodulin-dependent to a calmodulin-independent state.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei42 – 421ATPPROSITE-ProRule annotation
Active sitei135 – 1351Proton acceptor

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi19 – 279ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. calmodulin-dependent protein kinase activity Source: BHF-UCL
  3. GTPase activating protein binding Source: RGD

GO - Biological processi

  1. ionotropic glutamate receptor signaling pathway Source: UniProtKB
  2. peptidyl-serine phosphorylation Source: RGD
  3. protein autophosphorylation Source: RGD
  4. protein phosphorylation Source: BHF-UCL
  5. regulation of neurotransmitter secretion Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Calmodulin-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.17. 5301.

Names & Taxonomyi

Protein namesi
Recommended name:
Calcium/calmodulin-dependent protein kinase type II subunit alpha (EC:2.7.11.17)
Short name:
CaM kinase II subunit alpha
Short name:
CaMK-II subunit alpha
Gene namesi
Name:Camk2a
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi2261. Camk2a.

Subcellular locationi

Cell junctionsynapsepresynaptic cell membrane 1 Publication. Cell junctionsynapse 1 Publication
Note: Postsynaptic lipid rafts.

GO - Cellular componenti

  1. calcium- and calmodulin-dependent protein kinase complex Source: UniProtKB
  2. cell junction Source: UniProtKB-KW
  3. dendrite Source: UniProtKB
  4. dendrite cytoplasm Source: BHF-UCL
  5. plasma membrane Source: UniProtKB-KW
  6. synapse Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Synapse

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi432 – 4354IRIT → MGTA: Loss of interaction with MPDZ. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 478478Calcium/calmodulin-dependent protein kinase type II subunit alphaPRO_0000086094Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei13 – 131PhosphotyrosineBy similarity
Modified residuei286 – 2861Phosphothreonine; by autocatalysis1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP11275.
PRIDEiP11275.

PTM databases

PhosphoSiteiP11275.

Miscellaneous databases

PMAP-CutDBP11275.

Expressioni

Gene expression databases

GenevestigatoriP11275.

Interactioni

Subunit structurei

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 SYNGAP1.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Chrm3P084832EBI-2640645,EBI-7946407
Chrm4P0848510EBI-2640645,EBI-7946147
Grin2bQ009602EBI-2640645,EBI-396905
Lrrc7P705872EBI-2640645,EBI-7798464
PSMC5P621954EBI-2640645,EBI-357745From a different organism.

Protein-protein interaction databases

BioGridi247435. 13 interactions.
DIPiDIP-29639N.
IntActiP11275. 15 interactions.
MINTiMINT-153011.
STRINGi10116.ENSRNOP00000025283.

Structurei

Secondary structure

1
478
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi295 – 30915

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CDMX-ray2.00B290-314[»]
1CM1X-ray2.00B290-314[»]
1CM4X-ray2.00B290-314[»]
ProteinModelPortaliP11275.
SMRiP11275. Positions 7-474.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11275.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 271259Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni290 – 30011Calmodulin-bindingAdd
BLAST
Regioni310 – 32011Interaction with BAALCAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
HOVERGENiHBG108055.
InParanoidiP11275.
KOiK04515.
PhylomeDBiP11275.

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.
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]

Sequencei

Sequence statusi: Complete.

P11275-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATITCTRFT EEYQLFEELG KGAFSVVRRC VKVLAGQEYA AKIINTKKLS
60 70 80 90 100
ARDHQKLERE ARICRLLKHP NIVRLHDSIS EEGHHYLIFD LVTGGELFED
110 120 130 140 150
IVAREYYSEA DASHCIQQIL EAVLHCHQMG VVHRDLKPEN LLLASKLKGA
160 170 180 190 200
AVKLADFGLA IEVEGEQQAW FGFAGTPGYL SPEVLRKDPY GKPVDLWACG
210 220 230 240 250
VILYILLVGY PPFWDEDQHR LYQQIKAGAY DFPSPEWDTV TPEAKDLINK
260 270 280 290 300
MLTINPSKRI TAAEALKHPW ISHRSTVASC MHRQETVDCL KKFNARRKLK
310 320 330 340 350
GAILTTMLAT RNFSGGKSGG NKKNDGVKES SESTNTTIED EDTKVRKQEI
360 370 380 390 400
IKVTEQLIEA ISNGDFESYT KMCDPGMTAF EPEALGNLVE GLDFHRFYFE
410 420 430 440 450
NLWSRNSKPV HTTILNPHIH LMGDESACIA YIRITQYLDA GGIPRTAQSE
460 470
ETRVWHRRDG KWQIVHFHRS GAPSVLPH
Length:478
Mass (Da):54,115
Last modified:July 1, 1989 - v1
Checksum:i306F416CCE9B5F62
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti301 – 3011G → A in AAA41855. (PubMed:3037704)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02942 mRNA. Translation: AAA41870.1.
M16960 mRNA. Translation: AAA41855.1.
M29699 Genomic DNA. Translation: AAA40841.1.
PIRiA30355.
RefSeqiNP_037052.1. NM_012920.1.
UniGeneiRn.107499.

Genome annotation databases

GeneIDi25400.
KEGGirno:25400.
UCSCiRGD:2261. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02942 mRNA. Translation: AAA41870.1 .
M16960 mRNA. Translation: AAA41855.1 .
M29699 Genomic DNA. Translation: AAA40841.1 .
PIRi A30355.
RefSeqi NP_037052.1. NM_012920.1.
UniGenei Rn.107499.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CDM X-ray 2.00 B 290-314 [» ]
1CM1 X-ray 2.00 B 290-314 [» ]
1CM4 X-ray 2.00 B 290-314 [» ]
ProteinModelPortali P11275.
SMRi P11275. Positions 7-474.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 247435. 13 interactions.
DIPi DIP-29639N.
IntActi P11275. 15 interactions.
MINTi MINT-153011.
STRINGi 10116.ENSRNOP00000025283.

Chemistry

BindingDBi P11275.
ChEMBLi CHEMBL2359.

PTM databases

PhosphoSitei P11275.

Proteomic databases

PaxDbi P11275.
PRIDEi P11275.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 25400.
KEGGi rno:25400.
UCSCi RGD:2261. rat.

Organism-specific databases

CTDi 815.
RGDi 2261. Camk2a.

Phylogenomic databases

eggNOGi COG0515.
HOVERGENi HBG108055.
InParanoidi P11275.
KOi K04515.
PhylomeDBi P11275.

Enzyme and pathway databases

BRENDAi 2.7.11.17. 5301.

Miscellaneous databases

EvolutionaryTracei P11275.
NextBioi 606489.
PMAP-CutDB P11275.

Gene expression databases

Genevestigatori P11275.

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.
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. "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, ENZYME REGULATION, 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.

Entry informationi

Entry nameiKCC2A_RAT
AccessioniPrimary (citable) accession number: P11275
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: October 29, 2014
This is version 139 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3