PPIRE11202
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 | Cbf1pS155 |
|---|---|
| Peptide_Sequence | SLEGMTpSSPMES |
| Peptide_Length | 13 |
| Peptide_SMILES | CSCC[C@H](NC(=O)CNC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)CO)C(=O)N[C@H](C(=O)N1CCC[C@H]1C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCC(=O)O)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 | |
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Peptide Physicochemical
| Molecular_Weight | 1352.49 |
|---|---|
| Aliphatic_Index | 30.00000 |
| Aromaticity | 0.00000 |
| Average_Rotatable_Bonds | 3.23077 |
| Charge_at_pH_7 | -1.99847 |
| Isoelectric_Point | 3.61369 |
|---|---|
| Number_of_Hydrogen_Bond_Acceptors | 23 |
| Number_of_Hydrogen_Bond_Donors | 19 |
| Topological_Polar_Surface_Area | 570.69000 |
| X_logP_energy | -8.50840 |
Interaction Information
| Affinity | KD=172.43 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 |