| UniProt ID | TRY2_HUMAN | |
|---|---|---|
| UniProt AC | P07478 | |
| Protein Name | Trypsin-2 | |
| Gene Name | PRSS2 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 247 | |
| Subcellular Localization | Secreted, extracellular space. | |
| Protein Description | In the ileum, may be involved in defensin processing, including DEFA5.. | |
| Protein Sequence | MNLLLILTFVAAAVAAPFDDDDKIVGGYICEENSVPYQVSLNSGYHFCGGSLISEQWVVSAGHCYKSRIQVRLGEHNIEVLEGNEQFINAAKIIRHPKYNSRTLDNDILLIKLSSPAVINSRVSAISLPTAPPAAGTESLISGWGNTLSSGADYPDELQCLDAPVLSQAECEASYPGKITNNMFCVGFLEGGKDSCQGDSGGPVVSNGELQGIVSWGYGCAQKNRPGVYTKVYNYVDWIKDTIAANS | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 8 | Phosphorylation | MNLLLILTFVAAAVA CCHHHHHHHHHHHHH | 14.74 | 18187866 | |
| 92 | Ubiquitination | EQFINAAKIIRHPKY HHHHHHHHHHHCCCC | 35.93 | - | |
| 154 | Sulfation | TLSSGADYPDELQCL CCCCCCCCCCCCEEC | 16.43 | - | |
| 154 | Sulfation | TLSSGADYPDELQCL CCCCCCCCCCCCEEC | 16.43 | 17087724 | |
| 180 | Phosphorylation | ASYPGKITNNMFCVG HCCCCCCCCCEEEEE | 24.83 | - | |
| 195 | Phosphorylation | FLEGGKDSCQGDSGG EEECCCCCCCCCCCC | 16.30 | - | |
| 200 | Phosphorylation | KDSCQGDSGGPVVSN CCCCCCCCCCCEEEC | 53.10 | - | |
| 206 | Phosphorylation | DSGGPVVSNGELQGI CCCCCEEECCEEEEE | 39.07 | - | |
| 218 | Phosphorylation | QGIVSWGYGCAQKNR EEEEEECCCCCCCCC | 11.63 | 25884760 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of TRY2_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TRY2_HUMAN !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of TRY2_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| CASA1_HUMAN | CSN1S1 | physical | 20304780 | |
| TBB1_HUMAN | TUBB1 | physical | 28514442 | |
| ITA4_HUMAN | ITGA4 | physical | 28514442 | |
| GDF11_HUMAN | GDF11 | physical | 28514442 | |
| GRP78_HUMAN | HSPA5 | physical | 28514442 | |
| FINC_HUMAN | FN1 | physical | 28514442 | |
| TBB3_HUMAN | TUBB3 | physical | 28514442 |
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-8, AND MASSSPECTROMETRY. | |
