Protein kinase Spk1
From Proteopedia
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'''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 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. | ||
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| - | == Disease == | ||
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| - | == Relevance == | ||
== 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. The yeast FHA1 domain interacts with peptide containing phosphothreonine<ref>PMID:11106755</ref>. |
</StructureSection> | </StructureSection> | ||
Revision as of 10:30, 14 July 2016
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3D structures of protein kinase Spk1
Updated on 14-July-2016
References
- ↑ 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
