| Accepted Name |
|---|
| CRIK-subfamily protein kinase
|
| Alternative Name(s) |
|---|
| Citron Rho-Interacting Kinase |
| CRIK |
| Sticky/Citron Kinase |
| Reaction catalysed |
|---|
- L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+)
- L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H(+)
|
| Comment(s) |
|---|
- Requires Mg(2+).
- Peptide array data show a preference for phosphorylation of Thr over
Ser and a preference for basic residues in the -5 to -1 positions.
- CRIK is an animal-specific protein kinase that phosphorylates myosin
light chain (cf. EC 2.7.11.18) and is involved in cytokinesis in both
mammals and Drosophila.
- Human CRIK phosphorylates myosin light chain, MYL9/MRLC1 on T19/S20
and GLI2 on S14.
- Drosophila CRIK (sticky) interacts with the kinesins Nebbish and
Pavarotti, and human CRIK interacts with their orthologs, KIF14 and
KIF23/MKLP1 to promote midbody formation during cytokinesis.
- In Drosophila, CRIK/Sticky catalytic activity was required for this
function.
- Human CRIK is mostly highly expressed in brain, and mutations that
alter splicing or kinase activity lead to microcephaly, as do
knockouts in mouse and rat, and mutations in its interacting partner,
the kinesin KIF14.
|
| Cross-references |
|---|
| BRENDA | 2.7.11.35 |
| EC2PDB | 2.7.11.35 |
| ExplorEnz | 2.7.11.35 |
| KEGG Ligand Database for Enzyme Nomenclature | 2.7.11.35 |
| IUBMB Enzyme Nomenclature | 2.7.11.35 |
| MEDLINE | Find literature relating to 2.7.11.35 |
| MetaCyc | 2.7.11.35 |
| Rhea expert-curated reactions | 2.7.11.35 |
View entry in original ENZYME format
View entry in raw text format (no links)
All
ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 2.7.11.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.7.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.-.-.-
