Protein kinase Spk1
From Proteopedia
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== Function == | == Function == | ||
| - | '''Protein kinase Spk1 (Rad53)''' is a serine/threonine protein kinase which phosphorylates proteins. Rad53 controls S-phase checkpoint and G1 and G2 DNA damage checkpoints. Rad53 phosphorylates proteins at serine, threonine and tyrosine residues. | + | '''Protein kinase Spk1 (Rad53)''' is a yeast serine/threonine protein kinase which phosphorylates proteins on serene, threonine and tyrosine<ref>PMID:1899289</ref>. Rad53 controls S-phase checkpoint and G1 and G2 DNA damage checkpoints. Rad53 phosphorylates proteins at serine, threonine and tyrosine residues. |
== Structural highlights == | == Structural highlights == | ||
| - | Rad53 contains phosphothreonine recognition domains: '''FHA1''' at the N-terminal (residues 1-164) which selects for Asp at position +3 relative to phosphothreonine and '''FHA2''' at the C-terminal (residues 573-730) which selects for Ile at position +3 relative to phosphothreonine. Two '''SCD''' - SQ/TQ-rich cluster domains – are flanking the '''kinase''' domain. | + | Rad53 contains phosphothreonine recognition domains: '''FHA1''' at the N-terminal (residues 1-164) which selects for Asp at position +3 relative to phosphothreonine and '''FHA2''' at the C-terminal (residues 573-730) which selects for Ile at position +3 relative to phosphothreonine. Two '''SCD''' - SQ/TQ-rich cluster domains – are flanking the '''kinase''' domain. SCD domain is associated with DNA-damage-response proteins. The yeast FHA1 domain interacts with peptide containing phosphothreonine<ref>PMID:11106755</ref>. |
</StructureSection> | </StructureSection> | ||
Revision as of 08:33, 18 July 2016
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3D structures of protein kinase Spk1
Updated on 18-July-2016
References
- ↑ Stern DF, Zheng P, Beidler DR, Zerillo C. Spk1, a new kinase from Saccharomyces cerevisiae, phosphorylates proteins on serine, threonine, and tyrosine. Mol Cell Biol. 1991 Feb;11(2):987-1001. PMID:1899289
- ↑ Durocher D, Taylor IA, Sarbassova D, Haire LF, Westcott SL, Jackson SP, Smerdon SJ, Yaffe MB. The molecular basis of FHA domain:phosphopeptide binding specificity and implications for phospho-dependent signaling mechanisms. Mol Cell. 2000 Nov;6(5):1169-82. PMID:11106755
