INTERNAL ADAN INFORMATION

• Record: 3176
• Number: 294
• Inclusion date: 20-IV-2008

WHOLE PROTEIN INFORMATION

• Domains within protein: PPIP1_HUMAN by SMART
• Basic UniProtKB Entry: PPIP1_HUMAN
• InterPro link: PPIP1_HUMAN
• Swiss-Prot ENTRY: PPIP1_HUMAN
• Swiss-Prot AC number: O43586
• Sequence: O43586
• Pfam database: PPIP1_HUMAN

ALIGNMENT

• BLAST against Swiss-Prot: O43586
• BLAST for whole protein: O43586
• SAS for whole protein: O43586
• BLAST for modular domain: 2DIL
• SAS for domain: 2DIL

PREDICTED INTERACTIONS AND EXPERIMENTAL DATA

• FoldX Results: no ligand 
• iPfam: SH3
• PsiBase: 2DIL
• MINT: whole protein: O43586 or domain: 2DIL
• DOMINO database: O43586
• APID: O43586

• Title: Solution Structure Of The Sh3 Domain Of The Human Proline- Serine-Threonine Phosphatase-Interacting Protein 1
• Experimental Technique: nmr
• Resolution Å: n/a
• Protein Source: Homo sapiens
• Reference:
• Sequence domain: SeqA_2DIL2.txt
• Peptide sequence of ligand:
• Biochemical affinity data for: 2DIL
• Drugs:
• Phosphorylated residue type: Dephosphorylated on Tyr-345 by PTPN18, this event negatively regulates the association of PSTPIP1 with SH2 domain-containing proteins as tyrosine kinase. Phosphorylation of Tyr-345 is probably required for subsequent phosphorylation at other tyrosine residues. Phosphorylation is induced by activation of the EGFR and PDGFR in a ABL1 dependent manner. The phosphorylation regulates the interaction with WAS and with MEFV (By similarity)
• Pfam family: SH3
• Pfam structure: 2DIL
• RCSB_PDB_ID: 2DIL
• SMART: SH3
• PDBsum (domain): 2DIL
• PDBsum (Ligand): 2DIL
• MSD (summary): 2DIL
• MSD (ligands): 2DIL
• Molecular Surface: 2DIL

PDB1: Original Protein Data Bank file.

PDB2: Simplified coordinate files.