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Entry version 188 (16 Oct 2019)
Sequence version 2 (18 May 2010)
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Protein

Calcium/calmodulin-dependent protein kinase type II subunit alpha

Gene

CAMK2A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca2+/calmodulin-binding and autophosphorylation, and is involved in synaptic plasticity, neurotransmitter release and long-term potentiation. Member of the NMDAR signaling complex in excitatory synapses, it regulates NMDAR-dependent potentiation of the AMPAR and therefore excitatory synaptic transmission (By similarity). Regulates dendritic spine development (PubMed:28130356). Also regulates the migration of developing neurons (PubMed:29100089). Phosphorylates the transcription factor FOXO3 to activate its transcriptional activity (PubMed:23805378).By similarity3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Activated by Ca2+/calmodulin. Binding of calmodulin results in conformational change that relieves intrasteric autoinhibition and allows autophosphorylation of Thr-286 which turns the kinase in a constitutively active form and confers to the kinase a Ca2+-independent activity.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei42ATPPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei135Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi19 – 27ATPPROSITE-ProRule annotation9

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionCalmodulin-binding, Kinase, Serine/threonine-protein kinase, Transferase
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.11.17 2681

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-111932 CaMK IV-mediated phosphorylation of CREB
R-HSA-3371571 HSF1-dependent transactivation
R-HSA-399719 Trafficking of AMPA receptors
R-HSA-4086398 Ca2+ pathway
R-HSA-438066 Unblocking of NMDA receptors, glutamate binding and activation
R-HSA-442982 Ras activation upon Ca2+ influx through NMDA receptor
R-HSA-5576892 Phase 0 - rapid depolarisation
R-HSA-5578775 Ion homeostasis
R-HSA-5673000 RAF activation
R-HSA-5673001 RAF/MAP kinase cascade
R-HSA-6802946 Signaling by moderate kinase activity BRAF mutants
R-HSA-6802949 Signaling by RAS mutants
R-HSA-6802952 Signaling by BRAF and RAF fusions
R-HSA-6802955 Paradoxical activation of RAF signaling by kinase inactive BRAF
R-HSA-877300 Interferon gamma signaling
R-HSA-9022692 Regulation of MECP2 expression and activity
R-HSA-936837 Ion transport by P-type ATPases
R-HSA-9609736 Assembly and cell surface presentation of NMDA receptors
R-HSA-9617324 Negative regulation of NMDA receptor-mediated neuronal transmission
R-HSA-9620244 Long-term potentiation

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...
SignaLinki
Q9UQM7

SIGNOR Signaling Network Open Resource

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SIGNORi
Q9UQM7

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Calcium/calmodulin-dependent protein kinase type II subunit alpha (EC:2.7.11.171 Publication)
Short name:
CaM kinase II subunit alpha
Short name:
CaMK-II subunit alpha
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CAMK2A
Synonyms:CAMKA, KIAA0968
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 5

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:1460 CAMK2A

Online Mendelian Inheritance in Man (OMIM)

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MIMi
114078 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q9UQM7

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Membrane, Postsynaptic cell membrane, Synapse

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Mental retardation, autosomal dominant 53 (MRD53)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of mental retardation, a disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_08057998F → S in MRD53; no effect on protein abundance; decreased autophosphorylation; decreased neuronal migration. 1 PublicationCorresponds to variant dbSNP:rs1554122526EnsemblClinVar.1
Natural variantiVAR_080580109E → D in MRD53; no effect on protein abundance; increased autophosphorylation; decreased neuronal migration. 1 Publication1
Natural variantiVAR_080581112A → V in MRD53; unknown pathological significance. 1 Publication1
Natural variantiVAR_080582138P → A in MRD53; unknown pathological significance; no effect on protein abundance; no effect on autophosphorylation; no effect on neuronal migration. 2 Publications1
Natural variantiVAR_080583183E → V in MRD53; increased ubiquitin-mediated proteasomal degradation with a dominant negative effect on wild-type protein; decreased localization to dendritic spines; no effect on holoenzyme assembly; loss of interaction with SHANK3; loss of interaction with GRIN2B; loss of interaction with CACNB2; loss of interaction with LRRC7; loss of interaction with GRM5; decreased protein serine/threonine kinase activity with a dominant negative effect on wild-type protein; decreased autophosphorylation; changed dendritic spine development; decreased neuronal migration. 2 PublicationsCorresponds to variant dbSNP:rs1554122129EnsemblClinVar.1
Natural variantiVAR_080584212P → L in MRD53; unknown pathological significance; no effect on protein abundance; no effect on autophosphorylation; no effect on neuronal migration. 1 PublicationCorresponds to variant dbSNP:rs926027867EnsemblClinVar.1
Natural variantiVAR_081160212P → Q in MRD53; increased basal autophosphorylation. 1 Publication1
Natural variantiVAR_080585235P → L in MRD53; unknown pathological significance; no effect on protein abundance; no effect on autophosphorylation; no effect on neuronal migration. 2 PublicationsCorresponds to variant dbSNP:rs864309606EnsemblClinVar.1
Natural variantiVAR_080586282H → R in MRD53; decreased protein abundance; increased autophosphorylation; decreased neuronal migration. 1 PublicationCorresponds to variant dbSNP:rs1554121875EnsemblClinVar.1
Natural variantiVAR_080587286T → P in MRD53; no effect on protein abundance; loss of autophosphorylation; loss of neuronal migration. 1 PublicationCorresponds to variant dbSNP:rs1554121872EnsemblClinVar.1
Mental retardation, autosomal recessive 63 (MRT63)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of mental retardation, a disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRT63 patients manifest global developmental delay, severe intellectual disability, and seizures.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_081161466H → Y in MRT63; decreased oligomerization. 1 PublicationCorresponds to variant dbSNP:rs1554119274Ensembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi42K → R: No effect on protein stability or degradation. No effect on neuronal migration; when associated with P-286. 1 Publication1
Mutagenesisi286T → A: No effect on neuronal migration. 1 Publication1
Mutagenesisi286T → D: Loss of neuronal migration. 1 Publication1
Mutagenesisi286T → P: No effect on neuronal migration; when associated with R-42. 1 Publication1
Mutagenesisi466 – 478Missing : Loss of oligomerization. 1 PublicationAdd BLAST13

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

DisGeNET

More...
DisGeNETi
815

MalaCards human disease database

More...
MalaCardsi
CAMK2A
MIMi617798 phenotype
618095 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000070808

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
178469 Autosomal dominant non-syndromic intellectual disability

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA90

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
Q9UQM7

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4147

Drug and drug target database

More...
DrugBanki
DB07766 (2Z,3E)-2,3'-BIINDOLE-2',3(1H,1'H)-DIONE 3-{O-[(3R)-3,4-DIHYDROXYBUTYL]OXIME}
DB04447 1,4-Dithiothreitol
DB12010 Fostamatinib
DB04119 Hexatantalum Dodecabromide

DrugCentral

More...
DrugCentrali
Q9UQM7

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
CAMK2A

Domain mapping of disease mutations (DMDM)

More...
DMDMi
296434552

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000860911 – 478Calcium/calmodulin-dependent protein kinase type II subunit alphaAdd BLAST478

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei13PhosphotyrosineBy similarity1
Modified residuei257PhosphoserineBy similarity1
Modified residuei286Phosphothreonine; by autocatalysisBy similarity1
Modified residuei330PhosphoserineBy similarity1
Modified residuei331PhosphoserineBy similarity1
Modified residuei333PhosphoserineBy similarity1
Modified residuei336PhosphothreonineBy similarity1
Modified residuei337PhosphothreonineBy similarity1
Modified residuei404PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Autophosphorylation of Thr-286 following activation by Ca2+/calmodulin. Phosphorylation of Thr-286 locks the kinase into an activated state.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q9UQM7

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
Q9UQM7

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q9UQM7

PeptideAtlas

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PeptideAtlasi
Q9UQM7

PRoteomics IDEntifications database

More...
PRIDEi
Q9UQM7

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
85559 [Q9UQM7-1]
85560 [Q9UQM7-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9UQM7

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q9UQM7

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000070808 Expressed in 130 organ(s), highest expression level in right frontal lobe

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q9UQM7 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q9UQM7 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB004330
HPA051783
HPA051785
HPA053973

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

There are 4 genes encoding calcium/calmodulin-dependent protein kinase type II chains: CAMK2A, CAMK2B, CAMK2G and CAMK2D. The corresponding proteins assemble into homo- or heteromultimeric holoenzymes composed of 12 subunits with two hexameric rings stacked one on top of the other (PubMed:14722083, PubMed:29784083).

Interacts with BAALC.

Interacts with MPDZ.

Interacts with SYN1.

Interacts with CAMK2N2.

Interacts with SYNGAP1.

Interacts with SYNPO2 (By similarity).

Interacts with SHANK3 (PubMed:28130356).

Interacts with GRIN2B (PubMed:28130356).

Interacts with CACNB2 (PubMed:28130356).

Interacts with LRRC7 (PubMed:28130356).

Interacts with GRM5 (PubMed:28130356).

By similarity3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
107265, 65 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
Q9UQM7

Database of interacting proteins

More...
DIPi
DIP-39705N

Protein interaction database and analysis system

More...
IntActi
Q9UQM7, 68 interactors

Molecular INTeraction database

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MINTi
Q9UQM7

STRING: functional protein association networks

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STRINGi
9606.ENSP00000381412

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
Q9UQM7

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1478
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q9UQM7

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q9UQM7

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini13 – 271Protein kinasePROSITE-ProRule annotationAdd BLAST259

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni290 – 300Calmodulin-bindingAdd BLAST11
Regioni310 – 320Interaction with BAALCBy similarityAdd BLAST11

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0033 Eukaryota
ENOG410XNRX LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000155150

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000233016

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9UQM7

KEGG Orthology (KO)

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KOi
K04515

Identification of Orthologs from Complete Genome Data

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OMAi
YIDNNGM

Database of Orthologous Groups

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OrthoDBi
330091at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9UQM7

TreeFam database of animal gene trees

More...
TreeFami
TF315229

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View 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

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF08332 CaMKII_AD, 1 hit
PF00069 Pkinase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00220 S_TKc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF54427 SSF54427, 1 hit
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

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

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
D6RFJ0D6RFJ0_HUMAN
Calcium/calmodulin-dependent protei...
CAMK2A
90Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
D6RHX9D6RHX9_HUMAN
Calcium/calmodulin-dependent protei...
CAMK2A
24Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence BAA76812 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti365D → G in AAD30558 (Ref. 1) Curated1
Sequence conflicti365D → G in AAD30559 (Ref. 1) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_08057998F → S in MRD53; no effect on protein abundance; decreased autophosphorylation; decreased neuronal migration. 1 PublicationCorresponds to variant dbSNP:rs1554122526EnsemblClinVar.1
Natural variantiVAR_080580109E → D in MRD53; no effect on protein abundance; increased autophosphorylation; decreased neuronal migration. 1 Publication1
Natural variantiVAR_080581112A → V in MRD53; unknown pathological significance. 1 Publication1
Natural variantiVAR_080582138P → A in MRD53; unknown pathological significance; no effect on protein abundance; no effect on autophosphorylation; no effect on neuronal migration. 2 Publications1
Natural variantiVAR_080583183E → V in MRD53; increased ubiquitin-mediated proteasomal degradation with a dominant negative effect on wild-type protein; decreased localization to dendritic spines; no effect on holoenzyme assembly; loss of interaction with SHANK3; loss of interaction with GRIN2B; loss of interaction with CACNB2; loss of interaction with LRRC7; loss of interaction with GRM5; decreased protein serine/threonine kinase activity with a dominant negative effect on wild-type protein; decreased autophosphorylation; changed dendritic spine development; decreased neuronal migration. 2 PublicationsCorresponds to variant dbSNP:rs1554122129EnsemblClinVar.1
Natural variantiVAR_080584212P → L in MRD53; unknown pathological significance; no effect on protein abundance; no effect on autophosphorylation; no effect on neuronal migration. 1 PublicationCorresponds to variant dbSNP:rs926027867EnsemblClinVar.1
Natural variantiVAR_081160212P → Q in MRD53; increased basal autophosphorylation. 1 Publication1
Natural variantiVAR_080585235P → L in MRD53; unknown pathological significance; no effect on protein abundance; no effect on autophosphorylation; no effect on neuronal migration. 2 PublicationsCorresponds to variant dbSNP:rs864309606EnsemblClinVar.1
Natural variantiVAR_080586282H → R in MRD53; decreased protein abundance; increased autophosphorylation; decreased neuronal migration. 1 PublicationCorresponds to variant dbSNP:rs1554121875EnsemblClinVar.1
Natural variantiVAR_080587286T → P in MRD53; no effect on protein abundance; loss of autophosphorylation; loss of neuronal migration. 1 PublicationCorresponds to variant dbSNP:rs1554121872EnsemblClinVar.1
Natural variantiVAR_081161466H → Y in MRT63; decreased oligomerization. 1 PublicationCorresponds to variant dbSNP:rs1554119274Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_004766328K → KKRKSSSSVQLM in isoform B. 1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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.

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS43386.1 [Q9UQM7-1]
CCDS43387.1 [Q9UQM7-2]

NCBI Reference Sequences

More...
RefSeqi
NP_741960.1, NM_171825.2 [Q9UQM7-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000348628; ENSP00000261793; ENSG00000070808 [Q9UQM7-1]
ENST00000398376; ENSP00000381412; ENSG00000070808 [Q9UQM7-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
815

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:815

UCSC genome browser

More...
UCSCi
uc003lrt.3 human [Q9UQM7-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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.
CCDSiCCDS43386.1 [Q9UQM7-1]
CCDS43387.1 [Q9UQM7-2]
RefSeqiNP_741960.1, NM_171825.2 [Q9UQM7-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2VZ6X-ray2.30A/B13-302[»]
3SOAX-ray3.55A1-474[»]
5IG3X-ray2.75A/B/C/D/E/F345-475[»]
6OF8X-ray2.10A/B/C/D/E/F/G345-475[»]
SMRiQ9UQM7
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi107265, 65 interactors
CORUMiQ9UQM7
DIPiDIP-39705N
IntActiQ9UQM7, 68 interactors
MINTiQ9UQM7
STRINGi9606.ENSP00000381412

Chemistry databases

BindingDBiQ9UQM7
ChEMBLiCHEMBL4147
DrugBankiDB07766 (2Z,3E)-2,3'-BIINDOLE-2',3(1H,1'H)-DIONE 3-{O-[(3R)-3,4-DIHYDROXYBUTYL]OXIME}
DB04447 1,4-Dithiothreitol
DB12010 Fostamatinib
DB04119 Hexatantalum Dodecabromide
DrugCentraliQ9UQM7

PTM databases

iPTMnetiQ9UQM7
PhosphoSitePlusiQ9UQM7

Polymorphism and mutation databases

BioMutaiCAMK2A
DMDMi296434552

Proteomic databases

jPOSTiQ9UQM7
MassIVEiQ9UQM7
PaxDbiQ9UQM7
PeptideAtlasiQ9UQM7
PRIDEiQ9UQM7
ProteomicsDBi85559 [Q9UQM7-1]
85560 [Q9UQM7-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
815

Genome annotation databases

EnsembliENST00000348628; ENSP00000261793; ENSG00000070808 [Q9UQM7-1]
ENST00000398376; ENSP00000381412; ENSG00000070808 [Q9UQM7-2]
GeneIDi815
KEGGihsa:815
UCSCiuc003lrt.3 human [Q9UQM7-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
815
DisGeNETi815

GeneCards: human genes, protein and diseases

More...
GeneCardsi
CAMK2A
HGNCiHGNC:1460 CAMK2A
HPAiCAB004330
HPA051783
HPA051785
HPA053973
MalaCardsiCAMK2A
MIMi114078 gene
617798 phenotype
618095 phenotype
neXtProtiNX_Q9UQM7
OpenTargetsiENSG00000070808
Orphaneti178469 Autosomal dominant non-syndromic intellectual disability
PharmGKBiPA90

Human Unidentified Gene-Encoded large proteins database

More...
HUGEi
Search...

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0033 Eukaryota
ENOG410XNRX LUCA
GeneTreeiENSGT00940000155150
HOGENOMiHOG000233016
InParanoidiQ9UQM7
KOiK04515
OMAiYIDNNGM
OrthoDBi330091at2759
PhylomeDBiQ9UQM7
TreeFamiTF315229

Enzyme and pathway databases

BRENDAi2.7.11.17 2681
ReactomeiR-HSA-111932 CaMK IV-mediated phosphorylation of CREB
R-HSA-3371571 HSF1-dependent transactivation
R-HSA-399719 Trafficking of AMPA receptors
R-HSA-4086398 Ca2+ pathway
R-HSA-438066 Unblocking of NMDA receptors, glutamate binding and activation
R-HSA-442982 Ras activation upon Ca2+ influx through NMDA receptor
R-HSA-5576892 Phase 0 - rapid depolarisation
R-HSA-5578775 Ion homeostasis
R-HSA-5673000 RAF activation
R-HSA-5673001 RAF/MAP kinase cascade
R-HSA-6802946 Signaling by moderate kinase activity BRAF mutants
R-HSA-6802949 Signaling by RAS mutants
R-HSA-6802952 Signaling by BRAF and RAF fusions
R-HSA-6802955 Paradoxical activation of RAF signaling by kinase inactive BRAF
R-HSA-877300 Interferon gamma signaling
R-HSA-9022692 Regulation of MECP2 expression and activity
R-HSA-936837 Ion transport by P-type ATPases
R-HSA-9609736 Assembly and cell surface presentation of NMDA receptors
R-HSA-9617324 Negative regulation of NMDA receptor-mediated neuronal transmission
R-HSA-9620244 Long-term potentiation
SignaLinkiQ9UQM7
SIGNORiQ9UQM7

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
CAMK2A human
EvolutionaryTraceiQ9UQM7

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
CAMK2A

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
815
PharosiQ9UQM7

Protein Ontology

More...
PROi
PR:Q9UQM7

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000070808 Expressed in 130 organ(s), highest expression level in right frontal lobe
ExpressionAtlasiQ9UQM7 baseline and differential
GenevisibleiQ9UQM7 HS

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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiKCC2A_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9UQM7
Secondary accession number(s): Q9UL21, Q9Y2H4, Q9Y352
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: May 18, 2010
Last modified: October 16, 2019
This is version 188 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  7. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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