Q9JKV2 · CILK1_MOUSE
- ProteinSerine/threonine-protein kinase ICK
- GeneCilk1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids629 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Has an essential role in ciliogenesis, particularly in neuronal and retinal progenitor cells (PubMed:24797473).
Phosphorylates KIF3A (PubMed:24797473).
Involved in the control of ciliary length (PubMed:24853502).
Regulates the ciliary localization of SHH pathway components as well as the localization of IFT components at ciliary tips (PubMed:24797473, PubMed:24853502).
May play a role in cardiac development (By similarity).
Regulates intraflagellar transport (IFT) speed and negatively regulates cilium length in a cAMP and mTORC1 signaling -dependent manner and this regulation requires its kinase activity (PubMed:25243405).
Phosphorylates KIF3A (PubMed:24797473).
Involved in the control of ciliary length (PubMed:24853502).
Regulates the ciliary localization of SHH pathway components as well as the localization of IFT components at ciliary tips (PubMed:24797473, PubMed:24853502).
May play a role in cardiac development (By similarity).
Regulates intraflagellar transport (IFT) speed and negatively regulates cilium length in a cAMP and mTORC1 signaling -dependent manner and this regulation requires its kinase activity (PubMed:25243405).
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Cofactor
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | ciliary basal body | |
Cellular Component | ciliary base | |
Cellular Component | ciliary tip | |
Cellular Component | cilium | |
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | fibrillar center | |
Cellular Component | nucleus | |
Molecular Function | ATP binding | |
Molecular Function | magnesium ion binding | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity | |
Biological Process | cilium assembly | |
Biological Process | intracellular signal transduction | |
Biological Process | intraciliary anterograde transport | |
Biological Process | intraciliary retrograde transport | |
Biological Process | intraciliary transport | |
Biological Process | protein phosphorylation | |
Biological Process | signal transduction |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerine/threonine-protein kinase ICK
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9JKV2
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Knockout mice manifest hydrocephalus, polydactyly, and delayed skeletal development. At cellular levels, ICK knockout results in abnormally elongated cilia and compromised SHH signaling.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 33 | No effect on cilium length. | ||||
Sequence: K → M | ||||||
Mutagenesis | 33 | Loss of kinase activity; no effect on nuclear subcellular location. | ||||
Sequence: K → R | ||||||
Mutagenesis | 157 | Loss of kinase activity; loss of phosphorylation by CDK7; no effect on autophosphorylation. | ||||
Sequence: T → A | ||||||
Mutagenesis | 157-159 | Loss of kinase activity and of autophosphorylation; loss of phosphorylation by CDK7; no effect on nuclear subcellular location. | ||||
Sequence: TDY → ADF | ||||||
Mutagenesis | 159 | Loss of kinase activity and of autophosphorylation; no effect on phosphorylation by CDK7. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 169 | Complete loss of kinase activity and of nuclear localization. | ||||
Sequence: E → A | ||||||
Mutagenesis | 184 | Complete loss of kinase activity and of nuclear localization. | ||||
Sequence: W → A | ||||||
Mutagenesis | 270 | Partial loss of autocatalytic kinase activity. Complete loss of kinase activity and of nuclear localization; when associated with A-271 and A-272. | ||||
Sequence: K → A | ||||||
Mutagenesis | 271 | Partial loss of kinase activity. Complete loss of kinase activity and of nuclear localization; when associated with A-270 and A-272. | ||||
Sequence: K → A | ||||||
Mutagenesis | 272 | Complete loss of kinase activity and of nuclear localization. Complete loss of kinase activity and of nuclear localization; when associated with A-270 and A-272. | ||||
Sequence: R → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 49 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000086008 | 1-629 | Serine/threonine-protein kinase ICK | |||
Sequence: MNRYTTIKQLGDGTYGSVLLGRSIESGELIAIKKMKRKFYSWEECMNLREVKSLKKLNHANIVKLKEVIRENDHLYFIFEYMKENLYQLIKERNKLFPESAIRNIMYQILQGLAFIHKHGFFHRDLKPENLLCMGPELVKIADFGLAREIRSRPPYTDYVSTRWYRAPEVLLRSTNYSSPIDIWAVGCIMAEVYTLRPLFPGASEIDTIFKICQVLGTPKKTDWPEGYQLSSAMNFLWPQCIPNNLKTLIPNASSEAIQLLRDLLQWDPKKRPTASQALRYPYFQIGHPLGIISKDSGKPQREVQDKTGPPPYIKPAPPAQAPAKAYTLISSRPSQASQPPQHSVHPYKGDVSRTEQLSHVQEGKPSPPFFPSLHNKNLQPKILASLEQKNGEIKPKSRRRWGLISRSTKGSDDWADLDDLDFSPSLTRIDVKNKKRQSDDTLCRFESVLDLKPSESVGTGTTVSTQASSQRRDTPTLQSSAKQHYLKHSRYLPGINIRNGVLPNPGKDFLPSNSWSSSGLSGKSSGTVSVVSKITSVGSGSASSSGLTGSYIPSFLKKEIGSVMQRVQLAPLAAPPPGYSSLKAVRPHPGRPFFHTQPRSTPGLIPRPPAAQPVHGRIDWSSKYPSRR | ||||||
Modified residue | 157 | Phosphothreonine; by CDK7 | ||||
Sequence: T | ||||||
Modified residue | 159 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 161 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Autophosphorylated on serine and threonine residues. Phosphorylation at Thr-157 by CDK7/Cak1p increases kinase activity.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly expressed in colon and lung, lower levels present in heart, esophagus, stomach, small intestine and ovary. Localizes to the crypt region of large and small intestine.
Developmental stage
At 14.5 dpc, expressed in the brain cortex, including the cortical plate, intermediate zone, and ventricular and subventricular zones.
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-284 | Protein kinase | ||||
Sequence: YTTIKQLGDGTYGSVLLGRSIESGELIAIKKMKRKFYSWEECMNLREVKSLKKLNHANIVKLKEVIRENDHLYFIFEYMKENLYQLIKERNKLFPESAIRNIMYQILQGLAFIHKHGFFHRDLKPENLLCMGPELVKIADFGLAREIRSRPPYTDYVSTRWYRAPEVLLRSTNYSSPIDIWAVGCIMAEVYTLRPLFPGASEIDTIFKICQVLGTPKKTDWPEGYQLSSAMNFLWPQCIPNNLKTLIPNASSEAIQLLRDLLQWDPKKRPTASQALRYPYF | ||||||
Region | 292-376 | Disordered | ||||
Sequence: IISKDSGKPQREVQDKTGPPPYIKPAPPAQAPAKAYTLISSRPSQASQPPQHSVHPYKGDVSRTEQLSHVQEGKPSPPFFPSLHN | ||||||
Compositional bias | 328-343 | Polar residues | ||||
Sequence: TLISSRPSQASQPPQH | ||||||
Region | 455-483 | Disordered | ||||
Sequence: SESVGTGTTVSTQASSQRRDTPTLQSSAK | ||||||
Region | 581-629 | Disordered | ||||
Sequence: SSLKAVRPHPGRPFFHTQPRSTPGLIPRPPAAQPVHGRIDWSSKYPSRR |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length629
- Mass (Da)70,592
- Last updated2004-06-07 v2
- Checksum43E863847C5FD9C5
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 328-343 | Polar residues | ||||
Sequence: TLISSRPSQASQPPQH | ||||||
Sequence conflict | 533 | in Ref. 1; AAF37277 | ||||
Sequence: S → R | ||||||
Sequence conflict | 616 | in Ref. 1; AAF37277 | ||||
Sequence: H → L |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF225918 EMBL· GenBank· DDBJ | AAF37277.1 EMBL· GenBank· DDBJ | mRNA | ||
BC028863 EMBL· GenBank· DDBJ | AAH28863.1 EMBL· GenBank· DDBJ | mRNA |