PPIRE16757

Target Protein Information
Protein_Name Disabled homolog 1
Protein_Sequence MSTETELQVAVKTSAKKDSRKKGQDRSEATLIKRFKGEGVRYKAKLIGIDEVSAARGDKLCQDSMMKLKGVVAGARSKGEHKQKIFLTISFGGIKIFDEKTGALQHHHAVHEISYIAKDITDHRAFGYVCGKEGNHRFVAIKTAQAAEPVILDLRDLFQLIYELKQREELEKKAQKDKQCEQAVYQTILEEDVEDPVYQYIVFEAGHEPIRDPETEENIYQVPTSQKKEGVYDVPKSQPNSQPLEDFESRFAAATPNRNLSMDFDELLEATKVSAVTQLELFGDMSTPPDITSPPTPATPGDAFLPSSSQTLPGSADVFGSMSFGTAAVPSGYVAMGAVLPSFWGQQPLVQQQIAMGAQPPVAQVIPGAQPIAWGQPGLFPATQQAWPTVAGQFPPAAFMPTQTVMPLAAAMFQGPLTPLATVPGTNDSARSSPQSDKPRQKMGKESFKDFQMVQPPPVPSRKPDQPSLTCTSEAFSSYFNKVGVAQDTDDCDDFDISQLNLTPVTSTTPSTNSPPTPAPRQSSPSKSSASHVSDPTADDIFEEGFESPSKSEEQEAPDGSQASSTSDPFGEPSGEPSGDNISPQDGS
Organism_Source Mus musculus
Functional_Classification phosphotyrosine binding domains
Cellular_Localization Cytoplasm
Gene_Names Dab1
UniProt_ID P97318
Protein-Protein Interaction Networks
Peptide Basic Information
Peptide_Name ApoER2 peptide
Peptide_Sequence TKSMNFDNPVYRKT
Peptide_Length 14
Peptide_SMILES CSCC[C@H](NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](N)[C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(N)=O)C(=O)N1CCC[C@H]1C(=O)N[C@H](C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(=O)O)[C@@H](C)O)C(C)C
Chemical_Modification None
Cyclization_Method None
Linear/Cyclic Linear
N-terminal_Modification Acetyl
C-terminal_Modification Amide
Amino_Acid_Distribution
Peptide Physicochemical
Molecular_Weight 1700.93
Aliphatic_Index 20.71429
Aromaticity 0.14286
Average_Rotatable_Bonds 3.92857
Charge_at_pH_7 1.99699
Isoelectric_Point 10.24366
Hydrogen_Bond_Acceptors 26
Hydrogen_Bond_Donors 26
Topological_Polar_Surface_Area 751.17000
X_logP_energy -8.69233
Interaction Information
Affinity KD=3 uM
Affinity_Assay Isothermal Titration Calorimetry
PDB_ID 1NU2
Type Affinity ligand
Structure
Reference Information
Document_Type Research Articles
Title The Dual-Function Disabled-1 PTB Domain Exhibits Site Independence in Binding Phosphoinositide and Peptide Ligands
Release_Year 2004
PMID 15323557
DOI 10.1021/bi049092l