| Unique identifier for interactor A | uniprotkb:P01034 |
| Unique identifier for interactor B | uniprotkb:P01034 |
| Alternative identifier for interactor A | intact:EBI-948622 uniprotkb:Q6FGW9 uniprotkb:B2R5J9 ensembl:ENSP00000366124.3 ensembl:ENSP00000381446.1 ensembl:ENSP00000381448.1 uniprotkb:D3DW42 |
| Alternative identifier for interactor B | intact:EBI-948622 uniprotkb:Q6FGW9 uniprotkb:B2R5J9 ensembl:ENSP00000366124.3 ensembl:ENSP00000381446.1 ensembl:ENSP00000381448.1 uniprotkb:D3DW42 |
| Aliases for A | psi-mi:cytc_human(display_long) uniprotkb:Cystatin-3(gene name synonym) uniprotkb:Neuroendocrine basic polypeptide(gene name synonym) uniprotkb:Gamma-trace(gene name synonym) uniprotkb:Post-gamma-globulin(gene name synonym) uniprotkb:CST3(gene name) psi-mi:CST3(display_short) |
| Aliases for B | psi-mi:cytc_human(display_long) uniprotkb:Cystatin-3(gene name synonym) uniprotkb:Neuroendocrine basic polypeptide(gene name synonym) uniprotkb:Gamma-trace(gene name synonym) uniprotkb:Post-gamma-globulin(gene name synonym) uniprotkb:CST3(gene name) psi-mi:CST3(display_short) |
| Interaction detection methods | psi-mi:"MI:0964"(infrared spectroscopy) |
| First author | Sant'Anna et al. (2016) |
| Identifier of the publication | pubmed:26865059 imex:IM-25095 |
| NCBI Taxonomy identifier for interactor A | taxid:9606(human) taxid:9606(Homo sapiens) |
| NCBI Taxonomy identifier for interactor B | taxid:9606(human) taxid:9606(Homo sapiens) |
| Interaction types | psi-mi:"MI:0407"(direct interaction) |
| Source databases and identifiers | psi-mi:"MI:0471"(MINT) |
| Interaction identifier(s) in the corresponding source database | intact:EBI-11686076 imex:IM-25095-5 |
| Confidence score | intact-miscore:0.77 |
| Complex expansion | - |
| Biological role A | Unspecified role |
| Biological role B | Unspecified role |
| Experimental role A | Neutral component |
| Experimental role B | Neutral component |
| Interactor type A | Protein |
| Interactor type B | Protein |
| Annotations for the interaction | comment:"\"In order to get insights into the secondary structural changes that take place with the signal peptide upon aggregation, we took advantage of ATR-FTIR (Fig. 3 B). Left panel shows the FTIR spectra of the peptide dried from a stock solution with 100% DMSO (continuous line) and those collected during the first hour of aggregation. As seen, in DMSO the peptide presented a unique and broad peak centered at 1660 cm−1, which corresponds to disordered, random-coiled structures, which is a strong evidence that the peptide is monomeric in DMSO [48-50]. At the initial times of aggregation (up to 1 h), the spectra changed and a new peak at 1628 cm−1 appeared which was assigned to β-sheet structures. At the same time, the peak related to random-coil structures (1660 cm−1) decreased but was still present. The presence of β-sheet structures in these initial aggregates explains why these species bind Th-T (as shown in Fig. 2), but they are not fully organized, as seen by TEM (Fig. 3A, left). As aggregation proceeded for longer times (16, 24 and 72 h), the peak of β-sheet (1627 cm−1) increased even further, with a concomitant decrease of the peak of random coil at 1660 cm−1. Table 1 summarizes the secondary structural changes that take place upon aggregation of the signal peptide of cystatin C.\"" figure legend:f3b t1 curation depth:imex curation full coverage:Only protein-protein interactions |
| NCBI Taxonomy identifier for the host organism | taxid:-1(in vitro) taxid:-1(In vitro) |
| Parameters of the interaction | - |
| Creation date | 2016/04/08 |
| Update date | 2024/11/14 |
| negative Boolean value | false |
| Feature(s) for interactor A | - |
| Feature(s) for interactor B | - |
| Stoichiometry for interactor A | - |
| Stoichiometry for interactor B | - |
| Participant identification method for interactor A | Predetermined participant |
| Participant identification method for interactor B | Predetermined participant |