| Dual-specificity kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.12.1 | ||||||||
| CAS no. | 134549-83-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
In biochemistry, a dual-specificity kinase (EC 2.7.12.1) is a kinase that can act as both tyrosine kinase and serine/threonine kinase.
MEKs, involved in MAP pathways, are principal examples of dual-specificity kinases. Other common examples include:
- ADK1 (Arabidopsis dual specificity kinase 1)
- CLK1, CLK2, CLK3, CLK4
- DSTYK
- DYRK1A, DYRK1B, DYRK2, DYRK3, DYRK4
- Mps1p
- TESK1, TESK2
- TTK
The systematic name of this enzyme class is ATP:protein phosphotransferase (Ser/Thr- and Tyr-phosphorylating).
References[edit]
- Dhanasekaran N, Premkumar Reddy E (1998). "Signaling by dual specificity kinases". Oncogene. 17 (11 Reviews): 1447–1455. doi:10.1038/sj.onc.1202251. PMID 9779990.
- Ali N, Halfter U, Chua NH (1994). "Cloning and biochemical characterization of a plant protein kinase that phosphorylates serine, threonine, and tyrosine". J. Biol. Chem. 269 (50): 31626–9. PMID 7527390.
- Lauze E, Stoelcker B, Luca FC, Weiss E, Schutz AR, Winey M (1995). "Yeast spindle pole body duplication gene MPS1 encodes an essential dual specificity protein kinase". EMBO J. 14 (8): 1655–63. PMC 398258. PMID 7737118.
- Menegay HJ, Myers MP, Moeslein FM, Landreth GE. "Biochemical characterization and localization of the dual specificity kinase CLK1". J. Cell Sci. 113: 3241–53. PMID 10954422.
- Cleghon V; Sibbet, G; Kinstrie, R; Cleghon, T; Rylatt, M; Morrison, DK; Cleghon, V (2003). "dDYRK2: a novel dual-specificity tyrosine-phosphorylation-regulated kinase in Drosophila". Biochem. J. 374 (Pt 2): 381–91. doi:10.1042/BJ20030500. PMC 1223608. PMID 12786602.
