Q00168 · KCC2A_DROME
- ProteinCalcium/calmodulin-dependent protein kinase type II alpha chain
- GeneCaMKII
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids530 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
A key regulator of plasticity in synaptic physiology and behavior, alterations in its activity produce pleiotrophic effects that involve synaptic transmission and development as well as various aspects of behavior. Directly modulates eag potassium channels.
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Activity regulation
CASK plays a role in regulation of CaMKII autophosphorylation. When complexed with CASK and in the presence Ca[2+]/CaM, autophosphorylation of Thr-287 causes constitutive activation of the kinase. In the absence of Ca[2+]/CaM, autophosphorylation of Thr-306 causes inactivation of the kinase.
Features
Showing features for binding site, active site.
GO annotations
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCalcium/calmodulin-dependent protein kinase type II alpha chain
- EC number
- Short namesCaM-kinase II alpha chain
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionQ00168
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 306 | Fails to interact with CASK, catalytically active but fails to autophosphorylate, when associated with A-307. | ||||
Sequence: T → A | ||||||
Mutagenesis | 306 | Fails to interact with CASK, kinase inactive, when associated with D-307. | ||||
Sequence: T → D | ||||||
Mutagenesis | 306 | Fails to interact with CASK, catalytically active and can autophosphorylate, when associated with S-307. | ||||
Sequence: T → S | ||||||
Mutagenesis | 307 | Fails to interact with CASK, catalytically active but fails to autophosphorylate, when associated with A-306. | ||||
Sequence: T → A | ||||||
Mutagenesis | 307 | Fails to interact with CASK, kinase inactive, when associated with D-306. | ||||
Sequence: T → D | ||||||
Mutagenesis | 307 | Fails to interact with CASK, catalytically active and can autophosphorylate, when associated with S-306. | ||||
Sequence: T → S |
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000086095 | 1-530 | Calcium/calmodulin-dependent protein kinase type II alpha chain | |||
Sequence: MAAPAACTRFSDNYDIKEELGKGAFSIVKRCVQKSTGFEFAAKIINTKKLTARDFQKLEREARICRKLHHPNIVRLHDSIQEENYHYLVFDLVTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGVVHRDLKPENLLLASKAKGAAVKLADFGLAIEVQGDHQAWFGFAGTPGYLSPEVLKKEPYGKSVDIWACGVILYILLVGYPPFWDEDQHRLYSQIKAGAYDYPSPEWDTVTPEAKNLINQMLTVNPNKRITAAEALKHPWICQRERVASVVHRQETVDCLKKFNARRKLKGAILTTMLATRNFSSRSMITKKGEGSQVKESTDSSSTTLEDDDIKEDKKGTVDRSTTVVSKEPEDIRILCPAKTYQQNIGNSQCSSARRQEIIKITEQLIEAINSGDFDGYTKICDPHLTAFEPEALGNLVEGIDFHKFYFENVLGKNCKAINTTILNPHVHLLGEEAACIAYVRLTQYIDKQGHAHTHQSEETRVWHKRDNKWQNVHFHRSASAKISGATTFDFIPQK | ||||||
Modified residue | 287 | Phosphothreonine; by autocatalysis | ||||
Sequence: T | ||||||
Modified residue | 306 | Phosphothreonine; by autocatalysis | ||||
Sequence: T | ||||||
Modified residue | 307 | Phosphothreonine; by autocatalysis | ||||
Sequence: T | ||||||
Modified residue | 327 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Autophosphorylation at Thr-287 is independent of autophosphorylation at Thr-306 and Thr-307.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed at a high level in the central nervous system during the late embryonic stage. In adults, expression is more abundant in the head than in the body.
Gene expression databases
Interaction
Subunit
Interacts with CASK.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q00168 | CASK Q24210 | 5 | EBI-124595, EBI-214423 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 12-272 | Protein kinase | ||||
Sequence: DNYDIKEELGKGAFSIVKRCVQKSTGFEFAAKIINTKKLTARDFQKLEREARICRKLHHPNIVRLHDSIQEENYHYLVFDLVTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGVVHRDLKPENLLLASKAKGAAVKLADFGLAIEVQGDHQAWFGFAGTPGYLSPEVLKKEPYGKSVDIWACGVILYILLVGYPPFWDEDQHRLYSQIKAGAYDYPSPEWDTVTPEAKNLINQMLTVNPNKRITAAEALKHPWI | ||||||
Region | 291-301 | Calmodulin-binding | ||||
Sequence: LKKFNARRKLK | ||||||
Compositional bias | 320-335 | Polar residues | ||||
Sequence: ITKKGEGSQVKESTDS | ||||||
Region | 320-358 | Disordered | ||||
Sequence: ITKKGEGSQVKESTDSSSTTLEDDDIKEDKKGTVDRSTT | ||||||
Compositional bias | 336-358 | Basic and acidic residues | ||||
Sequence: SSTTLEDDDIKEDKKGTVDRSTT |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
Q00168-1
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.
- Name1
- Synonyms530aa, D
- Length530
- Mass (Da)59,920
- Last updated1996-11-01 v1
- Checksum4F3D83582ABDFCFD
Q00168-2
- Name2
- Synonyms516aa, G
- Differences from canonical
- 366-387: DIRILCPAKTYQQNIGNSQCSS → VNLFTNKA
Q00168-3
- Name3
- Synonyms509aa, B, E
- Differences from canonical
- 366-387: DIRILCPAKTYQQNIGNSQCSS → A
Q00168-4
- Name4
- Synonyms490aa, A, C
Computationally mapped potential isoform sequences
There are 7 potential isoforms mapped to this entry
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 320-335 | Polar residues | ||||
Sequence: ITKKGEGSQVKESTDS | ||||||
Compositional bias | 336-358 | Basic and acidic residues | ||||
Sequence: SSTTLEDDDIKEDKKGTVDRSTT | ||||||
Alternative sequence | VSP_050261 | 347-386 | in isoform 4 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_050262 | 366-387 | in isoform 2 | |||
Sequence: DIRILCPAKTYQQNIGNSQCSS → VNLFTNKA | ||||||
Alternative sequence | VSP_050263 | 366-387 | in isoform 3 | |||
Sequence: DIRILCPAKTYQQNIGNSQCSS → A | ||||||
Alternative sequence | VSP_050264 | 387 | in isoform 4 | |||
Sequence: S → A | ||||||
Sequence conflict | 388 | in Ref. 2; AAB28246/AAB28248 | ||||
Sequence: A → S |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D13330 EMBL· GenBank· DDBJ | BAA02593.1 EMBL· GenBank· DDBJ | mRNA | ||
D13331 EMBL· GenBank· DDBJ | BAA02594.1 EMBL· GenBank· DDBJ | mRNA | ||
D13332 EMBL· GenBank· DDBJ | BAA02595.1 EMBL· GenBank· DDBJ | mRNA | ||
D13333 EMBL· GenBank· DDBJ | BAA02596.1 EMBL· GenBank· DDBJ | mRNA | ||
M74583 EMBL· GenBank· DDBJ | AAA51459.1 EMBL· GenBank· DDBJ | mRNA | ||
AE014135 EMBL· GenBank· DDBJ | AAF59388.3 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014135 EMBL· GenBank· DDBJ | AAF59390.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014135 EMBL· GenBank· DDBJ | AAN06568.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014135 EMBL· GenBank· DDBJ | AAX53595.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
S65712 EMBL· GenBank· DDBJ | AAB28244.1 EMBL· GenBank· DDBJ | mRNA | ||
S65716 EMBL· GenBank· DDBJ | AAB28245.1 EMBL· GenBank· DDBJ | mRNA | ||
S65717 EMBL· GenBank· DDBJ | AAB28246.2 EMBL· GenBank· DDBJ | mRNA | ||
S65719 EMBL· GenBank· DDBJ | AAB28247.1 EMBL· GenBank· DDBJ | mRNA | ||
S65724 EMBL· GenBank· DDBJ | AAB28248.2 EMBL· GenBank· DDBJ | mRNA |