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Q9UQM7

- KCC2A_HUMAN

UniProt

Q9UQM7 - KCC2A_HUMAN

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Protein

Calcium/calmodulin-dependent protein kinase type II subunit alpha

Gene

CAMK2A

Organism
Homo sapiens (Human)
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 (By similarity).By similarity

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.By similarity

Sites

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

Regions

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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. calmodulin binding Source: BHF-UCL
  3. calmodulin-dependent protein kinase activity Source: UniProtKB-EC
  4. kinase activity Source: UniProtKB
  5. protein homodimerization activity Source: BHF-UCL

GO - Biological processi

  1. calcium ion transport Source: Ensembl
  2. cytokine-mediated signaling pathway Source: Reactome
  3. G1/S transition of mitotic cell cycle Source: Ensembl
  4. interferon-gamma-mediated signaling pathway Source: Reactome
  5. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  6. protein autophosphorylation Source: Ensembl
  7. protein phosphorylation Source: UniProtKB
  8. regulation of neuronal synaptic plasticity Source: Ensembl
  9. regulation of neurotransmitter secretion Source: ParkinsonsUK-UCL
  10. synaptic transmission Source: Reactome
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. 2681.
ReactomeiREACT_172761. Ca2+ pathway.
REACT_18307. Trafficking of AMPA receptors.
REACT_200775. HSF1-dependent transactivation.
REACT_20546. Ras activation uopn Ca2+ infux through NMDA receptor.
REACT_20568. CREB phosphorylation through the activation of Ras.
REACT_20594. Unblocking of NMDA receptor, glutamate binding and activation.
REACT_20642. CREB phosphorylation through the activation of CaMKII.
REACT_25078. Interferon gamma signaling.
SignaLinkiQ9UQM7.

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
Synonyms:CAMKA, KIAA0968
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:1460. CAMK2A.

Subcellular locationi

Cell junctionsynapsepresynaptic cell membrane By similarity. Cell junctionsynapse By similarity
Note: Postsynaptic lipid rafts.By similarity

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. cytosol Source: Reactome
  3. endocytic vesicle membrane Source: Reactome
  4. nucleoplasm Source: Reactome
  5. nucleus Source: UniProt
  6. plasma membrane Source: Reactome
  7. synapse Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Synapse

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA90.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 478478Calcium/calmodulin-dependent protein kinase type II subunit alphaPRO_0000086091Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UQM7.
PaxDbiQ9UQM7.
PRIDEiQ9UQM7.

PTM databases

PhosphoSiteiQ9UQM7.

Expressioni

Gene expression databases

BgeeiQ9UQM7.
CleanExiHS_CAMK2A.
ExpressionAtlasiQ9UQM7. baseline and differential.
GenevestigatoriQ9UQM7.

Organism-specific databases

HPAiCAB004330.

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 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
GRIN2BQ132243EBI-1383687,EBI-2256942

Protein-protein interaction databases

BioGridi107265. 44 interactions.
DIPiDIP-39705N.
IntActiQ9UQM7. 9 interactions.
MINTiMINT-95446.
STRINGi9606.ENSP00000381412.

Structurei

Secondary structure

1
478
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi13 – 208Combined sources
Beta strandi26 – 327Combined sources
Helixi33 – 353Combined sources
Beta strandi37 – 459Combined sources
Helixi46 – 483Combined sources
Helixi51 – 6616Combined sources
Beta strandi75 – 806Combined sources
Beta strandi82 – 909Combined sources
Helixi97 – 1026Combined sources
Helixi109 – 12820Combined sources
Helixi138 – 1403Combined sources
Beta strandi141 – 1444Combined sources
Beta strandi152 – 1543Combined sources
Helixi177 – 1793Combined sources
Helixi182 – 1854Combined sources
Helixi193 – 20816Combined sources
Helixi218 – 22710Combined sources
Helixi236 – 2394Combined sources
Helixi242 – 25110Combined sources
Turni256 – 2583Combined sources
Helixi262 – 2654Combined sources
Helixi269 – 2724Combined sources
Helixi274 – 2774Combined sources
Helixi284 – 29815Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VZ6X-ray2.30A/B13-302[»]
3SOAX-ray3.55A1-474[»]
ProteinModelPortaliQ9UQM7.
SMRiQ9UQM7. Positions 7-474.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UQM7.

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 BAALCBy similarityAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118944.
HOGENOMiHOG000233016.
HOVERGENiHBG108055.
InParanoidiQ9UQM7.
KOiK04515.
OMAiITCTRFS.
OrthoDBiEOG7ZD1VM.
PhylomeDBiQ9UQM7.
TreeFamiTF315229.

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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform A (identifier: Q9UQM7-1) [UniParc]FASTAAdd to Basket

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.

« 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 NKKSDGVKES 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):54,088
Last modified:May 18, 2010 - v2
Checksum:i208143A311BA9262
GO
Isoform B (identifier: Q9UQM7-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     328-328: K → KKRKSSSSVQLM

Show »
Length:489
Mass (Da):55,320
Checksum:i41E67A1E15EB142B
GO

Sequence cautioni

The sequence BAA76812.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti365 – 3651D → G in AAD30558. 1 PublicationCurated
Sequence conflicti365 – 3651D → G in AAD30559. 1 PublicationCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei328 – 3281K → KKRKSSSSVQLM in isoform B. 1 PublicationVSP_004766

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF145710 mRNA. Translation: AAD30558.1.
AF145711 mRNA. Translation: AAD30559.1.
AB023185 mRNA. Translation: BAA76812.1. Different initiation.
AC011372 Genomic DNA. No translation available.
CCDSiCCDS43386.1. [Q9UQM7-1]
CCDS43387.1. [Q9UQM7-2]
RefSeqiNP_741960.1. NM_171825.2. [Q9UQM7-1]
UniGeneiHs.743976.

Genome annotation databases

EnsembliENST00000348628; ENSP00000261793; ENSG00000070808. [Q9UQM7-1]
ENST00000398376; ENSP00000381412; ENSG00000070808. [Q9UQM7-2]
GeneIDi815.
KEGGihsa:815.
UCSCiuc003lru.2. human. [Q9UQM7-1]

Polymorphism databases

DMDMi296434552.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF145710 mRNA. Translation: AAD30558.1 .
AF145711 mRNA. Translation: AAD30559.1 .
AB023185 mRNA. Translation: BAA76812.1 . Different initiation.
AC011372 Genomic DNA. No translation available.
CCDSi CCDS43386.1. [Q9UQM7-1 ]
CCDS43387.1. [Q9UQM7-2 ]
RefSeqi NP_741960.1. NM_171825.2. [Q9UQM7-1 ]
UniGenei Hs.743976.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2VZ6 X-ray 2.30 A/B 13-302 [» ]
3SOA X-ray 3.55 A 1-474 [» ]
ProteinModelPortali Q9UQM7.
SMRi Q9UQM7. Positions 7-474.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107265. 44 interactions.
DIPi DIP-39705N.
IntActi Q9UQM7. 9 interactions.
MINTi MINT-95446.
STRINGi 9606.ENSP00000381412.

Chemistry

BindingDBi Q9UQM7.
ChEMBLi CHEMBL2097164.
GuidetoPHARMACOLOGYi 1555.

PTM databases

PhosphoSitei Q9UQM7.

Polymorphism databases

DMDMi 296434552.

Proteomic databases

MaxQBi Q9UQM7.
PaxDbi Q9UQM7.
PRIDEi Q9UQM7.

Protocols and materials databases

DNASUi 815.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000348628 ; ENSP00000261793 ; ENSG00000070808 . [Q9UQM7-1 ]
ENST00000398376 ; ENSP00000381412 ; ENSG00000070808 . [Q9UQM7-2 ]
GeneIDi 815.
KEGGi hsa:815.
UCSCi uc003lru.2. human. [Q9UQM7-1 ]

Organism-specific databases

CTDi 815.
GeneCardsi GC05M149579.
HGNCi HGNC:1460. CAMK2A.
HPAi CAB004330.
MIMi 114078. gene.
neXtProti NX_Q9UQM7.
PharmGKBi PA90.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118944.
HOGENOMi HOG000233016.
HOVERGENi HBG108055.
InParanoidi Q9UQM7.
KOi K04515.
OMAi ITCTRFS.
OrthoDBi EOG7ZD1VM.
PhylomeDBi Q9UQM7.
TreeFami TF315229.

Enzyme and pathway databases

BRENDAi 2.7.11.17. 2681.
Reactomei REACT_172761. Ca2+ pathway.
REACT_18307. Trafficking of AMPA receptors.
REACT_200775. HSF1-dependent transactivation.
REACT_20546. Ras activation uopn Ca2+ infux through NMDA receptor.
REACT_20568. CREB phosphorylation through the activation of Ras.
REACT_20594. Unblocking of NMDA receptor, glutamate binding and activation.
REACT_20642. CREB phosphorylation through the activation of CaMKII.
REACT_25078. Interferon gamma signaling.
SignaLinki Q9UQM7.

Miscellaneous databases

ChiTaRSi CAMK2A. human.
EvolutionaryTracei Q9UQM7.
GeneWikii CAMK2A.
GenomeRNAii 815.
NextBioi 3304.
PROi Q9UQM7.
SOURCEi Search...

Gene expression databases

Bgeei Q9UQM7.
CleanExi HS_CAMK2A.
ExpressionAtlasi Q9UQM7. baseline and differential.
Genevestigatori Q9UQM7.

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

« Hide 'large scale' publications
  1. "Human calcium/calmodulin-dependent protein kinase II: cDNA cloning and gene analysis."
    Li G.Y., Cooper N.G.F.
    Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
    Tissue: Brain.
  2. "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  3. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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 MPDZ.

Entry informationi

Entry nameiKCC2A_HUMAN
AccessioniPrimary (citable) accession number: Q9UQM7
Secondary accession number(s): Q9UL21, Q9Y2H4, Q9Y352
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: May 18, 2010
Last modified: October 29, 2014
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3