PPIRE12630

Target Protein Information
Protein_Name DDK kinase regulatory subunit DBF4
Protein_Sequence MVSPTKMIIRSPLKETDTNLKHNNGIAASTTAAGHLNVFSNDNNCNNNNTTESFPKKRSLERLELQQQQHLHEKKRARIERARSIEGAVQVSKGTGLKNVEPRVTPKELLEWQTNWKKIMKRDSRIYFDITDDVEMNTYNKSKMDKRRDLLKRGFLTLGAQITQFFDTTVTIVITRRSVENIYLLKDTDILSRAKKNYMKVWSYEKAARFLKNLDVDLDHLSKTKSASLAAPTLSNLLHNEKLYGPTDRDPRTKRDDIHYFKYPHVYLYDLWQTWAPIITLEWKPQELTNLDELPYPILKIGSFGRCPFIGDRNYDESSYKRVVKRYSRDKANKKYALQLRALFQYHADTLLNTSSVNDQTKNLIFIPHTCNDSTKSFKKWMQEKAKNFEKTELKKTDDSAVQDVRNEHADQTDEKNSILLNETETKEPPLKEEKENKQSIAEESNKYPQRKELAATPKLNHPVLATFARQETEEVPDDLCTLKTKSRQAFEIKASGAHQSNDVATSFGNGLGPTRASVMSKNMKSLSRLMVDRKLGVKQTNGNNKNYTATIATTAETSKENRHRLDFNALKKDEAPSKETGKDSAVHLETNRKPQNFPKVATKSVSADSKVHNDIKITTTESPTASKKSTSTNVTLHFNAQTAQTAQPVKKETVKNSGYCENCRVKYESLEQHIVSEKHLSFAENDLNFEAIDSLIENLRFQI
Organism_Source Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Functional_Classification kinase regulatory subunit
Cellular_Localization Nucleus
Gene_Names DBF4
UniProt_ID P32325
Protein-Protein Interaction Networks
Peptide Basic Information
Peptide_Name Esc1pS1450
Peptide_Sequence IPSTDLPpSDPPSDKEE
Peptide_Length 17
Peptide_SMILES CC[C@H](C)[C@H](N)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CO)C(=O)N[C@H](C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(C)C)C(=O)N1CCC[C@H]1C(=O)N1CCC[C@H]1C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(=O)O)C(=O)N1CCC[C@H]1C(=O)N1CCC[C@H]1C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCC(=O)O)C(=O)O)[C@@H](C)O
Chemical_Modification None
Cyclization_Method None
Linear/Cyclic Linear
N-terminal_Modification Free
C-terminal_Modification Free
Amino_Acid_Distribution
Peptide Physicochemical
Molecular_Weight 1823.93
Aliphatic_Index 45.88235
Aromaticity 0.00000
Average_Rotatable_Bonds 3.05882
Charge_at_pH_7 -3.99742
Isoelectric_Point 3.60605
Number_of_Hydrogen_Bond_Acceptors 28
Number_of_Hydrogen_Bond_Donors 23
Topological_Polar_Surface_Area 778.41000
X_logP_energy -9.58130
Interaction Information
Affinity KD=0.9 uM
Affinity_Assay MicroScale Thermophoresis
PDB_ID None
Type Affinity ligand
Structure
Reference Information
Document_Type Research Articles
Title The Sir4 H-BRCT domain interacts with phospho-proteins to sequester and repress yeast heterochromatin.
Release_Year 2019
PMID 31515872
DOI 10.15252/embj.2019101744