PPIRE10573

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 Tom1pS2376
Peptide_Sequence HSREIDpSFLEA
Peptide_Length 12
Peptide_SMILES CC[C@H](C)[C@H](NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CO)NC(=O)[C@@H](N)Cc1c[nH]cn1)C(=O)N[C@@H](CC(=O)O)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CO)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](C)C(=O)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 1400.51
Aliphatic_Index 73.33333
Aromaticity 0.08333
Average_Rotatable_Bonds 3.66667
Charge_at_pH_7 -1.90711
Isoelectric_Point 4.42146
Number_of_Hydrogen_Bond_Acceptors 20
Number_of_Hydrogen_Bond_Donors 21
Topological_Polar_Surface_Area 617.57000
X_logP_energy -5.98993
Interaction Information
Affinity KD=75.46 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