PPIRE11120

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 Ubp10pT123
Peptide_Sequence LSTELSpTEPPSS
Peptide_Length 13
Peptide_SMILES CC(C)C[C@H](NC(=O)[C@H](CCC(=O)O)NC(=O)[C@@H](NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC(C)C)[C@@H](C)O)C(=O)N[C@@H](CO)C(=O)N1CCC[C@H]1C(=O)N[C@H](C(=O)N[C@@H](CCC(=O)O)C(=O)N1CCC[C@H]1C(=O)N1CCC[C@H]1C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)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 1344.44
Aliphatic_Index 60.00000
Aromaticity 0.00000
Average_Rotatable_Bonds 2.92308
Charge_at_pH_7 -1.99847
Isoelectric_Point 3.61369
Number_of_Hydrogen_Bond_Acceptors 22
Number_of_Hydrogen_Bond_Donors 19
Topological_Polar_Surface_Area 582.13000
X_logP_energy -8.71290
Interaction Information
Affinity KD=0.63 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