| UniProt ID | SPIT1_HUMAN | |
|---|---|---|
| UniProt AC | O43278 | |
| Protein Name | Kunitz-type protease inhibitor 1 | |
| Gene Name | SPINT1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 529 | |
| Subcellular Localization | Secreted. | |
| Protein Description | Inhibitor of HGF activator. Also acts as an inhibitor of matriptase (ST14).. | |
| Protein Sequence | MAPARTMARARLAPAGIPAVALWLLCTLGLQGTQAGPPPAPPGLPAGADCLNSFTAGVPGFVLDTNASVSNGATFLESPTVRRGWDCVRACCTTQNCNLALVELQPDRGEDAIAACFLINCLYEQNFVCKFAPREGFINYLTREVYRSYRQLRTQGFGGSGIPKAWAGIDLKVQPQEPLVLKDVENTDWRLLRGDTDVRVERKDPNQVELWGLKEGTYLFQLTVTSSDHPEDTANVTVTVLSTKQTEDYCLASNKVGRCRGSFPRWYYDPTEQICKSFVYGGCLGNKNNYLREEECILACRGVQGGPLRGSSGAQATFPQGPSMERRHPVCSGTCQPTQFRCSNGCCIDSFLECDDTPNCPDASDEAACEKYTSGFDELQRIHFPSDKGHCVDLPDTGLCKESIPRWYYNPFSEHCARFTYGGCYGNKNNFEEEQQCLESCRGISKKDVFGLRREIPIPSTGSVEMAVAVFLVICIVVVVAILGYCFFKNQRKDFHGHHHHPPPTPASSTVSTTEDTEHLVYNHTTRPL | |
| 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 |
|---|---|---|---|---|---|
| 66 | N-linked_Glycosylation | PGFVLDTNASVSNGA CCEEEECCCCCCCCC | 29.86 | UniProtKB CARBOHYD | |
| 154 | Phosphorylation | RSYRQLRTQGFGGSG HHHHHHHHCCCCCCC | 41.45 | 22210691 | |
| 160 | Phosphorylation | RTQGFGGSGIPKAWA HHCCCCCCCCCCCCC | 33.65 | 24719451 | |
| 172 (in isoform 2) | Ubiquitination | - | 34.77 | 21906983 | |
| 172 (in isoform 1) | Ubiquitination | - | 34.77 | 21906983 | |
| 172 | Ubiquitination | AWAGIDLKVQPQEPL CCCCCCCEECCCCCE | 34.77 | 22817900 | |
| 235 | N-linked_Glycosylation | DHPEDTANVTVTVLS CCCCCCCEEEEEEEE | 31.89 | UniProtKB CARBOHYD | |
| 277 | Phosphorylation | PTEQICKSFVYGGCL CHHHHHHHHHHHCCC | 18.61 | 18669648 | |
| 311 | Phosphorylation | QGGPLRGSSGAQATF CCCCCCCCCCCCCCC | 21.11 | 22210691 | |
| 312 | Phosphorylation | GGPLRGSSGAQATFP CCCCCCCCCCCCCCC | 40.76 | 22210691 | |
| 317 | O-linked_Glycosylation | GSSGAQATFPQGPSM CCCCCCCCCCCCCCC | 24.62 | OGP | |
| 334 | O-linked_Glycosylation | RHPVCSGTCQPTQFR CCCCCCCCCCCCEEE | 7.53 | OGP | |
| 373 | O-linked_Glycosylation | EAACEKYTSGFDELQ HHHHHHHHCCCHHHH | 33.18 | OGP | |
| 403 | Phosphorylation | DTGLCKESIPRWYYN CCCCCCCCCCHHHCC | 24.32 | 24719451 | |
| 505 | Phosphorylation | HHHHPPPTPASSTVS CCCCCCCCCCCCCCC | 36.94 | - | |
| 508 | Phosphorylation | HPPPTPASSTVSTTE CCCCCCCCCCCCCCC | 27.96 | - | |
| 510 | Phosphorylation | PPTPASSTVSTTEDT CCCCCCCCCCCCCCC | 18.91 | - | |
| 512 | Phosphorylation | TPASSTVSTTEDTEH CCCCCCCCCCCCCCE | 29.69 | - | |
| 514 | Phosphorylation | ASSTVSTTEDTEHLV CCCCCCCCCCCCEEE | 25.10 | - | |
| 522 | Phosphorylation | EDTEHLVYNHTTRPL CCCCEEEECCCCCCC | 13.95 | 27259358 | |
| 523 | N-linked_Glycosylation | DTEHLVYNHTTRPL- CCCEEEECCCCCCC- | 20.67 | UniProtKB CARBOHYD | |
| 526 | Phosphorylation | HLVYNHTTRPL---- EEEECCCCCCC---- | 23.80 | - |
| 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 SPIT1_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SPIT1_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 SPIT1_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of SPIT1_HUMAN !! | ||||
| 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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