Protein kinase Spk1

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.

Disease

Relevance

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.

3D structures of protein kinase Spk1

Updated on 20-August-2014

Rad53 FHA1 domain

1k3j – yRad53 FHA1 domain – yeast - NMR
1g3g, 1j4o – yRad53 FHA1 domain (mutant) - NMR
1j4p, 1j4q, 1k3n, 1k3q – yRad53 FHA1 domain + Rad9 peptide - NMR
1g6g, 2a0t, 2jqi – yRad53 FHA1 domain + phosphothreonine peptide

Rad53 FHA2 domain

1qu5, 1dmz, 1fhq – yRad53 FHA2 domain – yeast - NMR
1fhr, 1j4k, 1j4l, 1k2m, 1k2n – yRad53 FHA2 domain + Rad9 peptide - NMR

Rad53 kinase and SCD2 domains

4pdp – yRad53 kinase and SCD2 domain (mutant)
4pds – yRad53 kinase and SCD2 domain (mutant) + AMPPNP

References