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Protein

Calcium/calmodulin-dependent protein kinase type II subunit alpha

Gene

Camk2a

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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 (PubMed:15312654). Phosphorylates transcription factor FOXO3 on 'Ser-298'. Activates FOXO3 transcriptional activity (By similarity).By similarity1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.By similarity

Cofactori

Mg2+By similarity

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)DescriptionActionsGraphical viewLength
Binding sitei42ATPPROSITE-ProRule annotation1
Active sitei135Proton acceptor1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi19 – 27ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionCalmodulin-binding, Kinase, Serine/threonine-protein kinase, Transferase
LigandATP-binding, Magnesium, Metal-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:2.7.11.17By similarity)
Short name:
CaM kinase II subunit alpha
Short name:
CaMK-II subunit alpha
Gene namesi
Name:Camk2a
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2261. Camk2a.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Synapse

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi432 – 435IRIT → MGTA: Loss of interaction with MPDZ. 1 Publication4

Chemistry databases

ChEMBLiCHEMBL2359.
GuidetoPHARMACOLOGYi1555.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000860941 – 478Calcium/calmodulin-dependent protein kinase type II subunit alphaAdd BLAST478

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei13PhosphotyrosineBy similarity1
Modified residuei257PhosphoserineCombined sources1
Modified residuei286Phosphothreonine; by autocatalysis1 Publication1
Modified residuei330PhosphoserineBy similarity1
Modified residuei331PhosphoserineBy similarity1
Modified residuei333PhosphoserineBy similarity1
Modified residuei336PhosphothreonineBy similarity1
Modified residuei337PhosphothreonineBy similarity1
Modified residuei404PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP11275.

PTM databases

iPTMnetiP11275.
PhosphoSitePlusiP11275.
SwissPalmiP11275.

Miscellaneous databases

PMAP-CutDBiP11275.

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. Interacts with SYNPO2.5 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

BioGridi247435. 13 interactors.
CORUMiP11275.
DIPiDIP-29639N.
IntActiP11275. 19 interactors.
MINTiMINT-153011.

Chemistry databases

BindingDBiP11275.

Structurei

Secondary structure

1478
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi295 – 309Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CDMX-ray2.00B290-314[»]
1CM1X-ray2.00B290-314[»]
1CM4X-ray2.00B290-314[»]
5U6Yelectron microscopy20.00A/B/C/D/E/F/G/H/I/J/K/L13-472[»]
ProteinModelPortaliP11275.
SMRiP11275.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11275.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini13 – 271Protein kinasePROSITE-ProRule annotationAdd BLAST259

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni290 – 300Calmodulin-bindingAdd BLAST11
Regioni310 – 320Interaction with BAALC1 PublicationAdd BLAST11

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG108055.
InParanoidiP11275.
KOiK04515.
PhylomeDBiP11275.

Family and domain databases

InterProiView protein in InterPro
IPR013543. Ca/CaM-dep_prot_kinase-assoc.
IPR011009. Kinase-like_dom_sf.
IPR032710. NTF2-like_dom_sf.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
PfamiView protein in Pfam
PF08332. CaMKII_AD. 1 hit.
PF00069. Pkinase. 1 hit.
SMARTiView protein in SMART
SM00220. S_TKc. 1 hit.
SUPFAMiSSF54427. SSF54427. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiView protein in PROSITE
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.

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)DescriptionActionsGraphical viewLength
Sequence conflicti301G → A in AAA41855 (PubMed:3037704).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

Similar proteinsi

Entry informationi

Entry nameiKCC2A_RAT
AccessioniPrimary (citable) accession number: P11275
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 22, 2017
This is version 165 of the entry and version 1 of the sequence. See 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