| UniProt ID | PPIP1_HUMAN | |
|---|---|---|
| UniProt AC | O43586 | |
| Protein Name | Proline-serine-threonine phosphatase-interacting protein 1 | |
| Gene Name | PSTPIP1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 416 | |
| Subcellular Localization |
Cytoplasm . Cell membrane Peripheral membrane protein . Cell projection, uropodium . Cytoplasm, cytoskeleton . Cytoplasm, perinuclear region . Cell projection, lamellipodium . Cleavage furrow . Mainly cytoplasmic in T-cells (PubMed:9857189). Coloca |
|
| Protein Description | Involved in regulation of the actin cytoskeleton. May regulate WAS actin-bundling activity. Bridges the interaction between ABL1 and PTPN18 leading to ABL1 dephosphorylation. May play a role as a scaffold protein between PTPN12 and WAS and allow PTPN12 to dephosphorylate WAS. Has the potential to physically couple CD2 and CD2AP to WAS. Acts downstream of CD2 and CD2AP to recruit WAS to the T-cell:APC contact site so as to promote the actin polymerization required for synapse induction during T-cell activation (By similarity). Down-regulates CD2-stimulated adhesion through the coupling of PTPN12 to CD2. Also has a role in innate immunity and the inflammatory response. Recruited to inflammasomes by MEFV. Induces formation of pyroptosomes, large supramolecular structures composed of oligomerized PYCARD dimers which form prior to inflammatory apoptosis. Binding to MEFV allows MEFV to bind to PYCARD and facilitates pyroptosome formation. Regulates endocytosis and cell migration in neutrophils.. | |
| Protein Sequence | MMPQLQFKDAFWCRDFTAHTGYEVLLQRLLDGRKMCKDMEELLRQRAQAEERYGKELVQIARKAGGQTEINSLRASFDSLKQQMENVGSSHIQLALTLREELRSLEEFRERQKEQRKKYEAVMDRVQKSKLSLYKKAMESKKTYEQKCRDADDAEQAFERISANGHQKQVEKSQNKARQCKDSATEAERVYRQSIAQLEKVRAEWEQEHRTTCEAFQLQEFDRLTILRNALWVHSNQLSMQCVKDDELYEEVRLTLEGCSIDADIDSFIQAKSTGTEPPAPVPYQNYYDREVTPLTSSPGIQPSCGMIKRFSGLLHGSPKTTSLAASAASTETLTPTPERNEGVYTAIAVQEIQGNPASPAQEYRALYDYTAQNPDELDLSAGDILEVILEGEDGWWTVERNGQRGFVPGSYLEKL | |
| 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 |
|---|---|---|---|---|---|
| 63 | Ubiquitination | ELVQIARKAGGQTEI HHHHHHHHCCCCHHH | 42.22 | - | |
| 72 | Phosphorylation | GGQTEINSLRASFDS CCCHHHHHHHHHHHH | 25.54 | 24825855 | |
| 119 | Phosphorylation | QKEQRKKYEAVMDRV HHHHHHHHHHHHHHH | 16.50 | 18083107 | |
| 128 | Acetylation | AVMDRVQKSKLSLYK HHHHHHHHHHHHHHH | 46.85 | 19666605 | |
| 135 | Acetylation | KSKLSLYKKAMESKK HHHHHHHHHHHHCHH | 39.07 | 19666613 | |
| 140 | Phosphorylation | LYKKAMESKKTYEQK HHHHHHHCHHHHHHH | 26.77 | - | |
| 173 | Phosphorylation | HQKQVEKSQNKARQC CHHHHHHHHHHHHHC | 26.02 | - | |
| 211 | Phosphorylation | EWEQEHRTTCEAFQL HHHHHHHHHHHHHHC | 37.39 | 25627689 | |
| 212 | Phosphorylation | WEQEHRTTCEAFQLQ HHHHHHHHHHHHHCC | 14.33 | 25627689 | |
| 260 | Phosphorylation | RLTLEGCSIDADIDS HHHHCCCCCCCCHHH | 34.07 | 27251275 | |
| 287 (in isoform 2) | Phosphorylation | - | 7.39 | 20873877 | |
| 290 (in isoform 2) | Phosphorylation | - | 24.94 | 20873877 | |
| 293 (in isoform 2) | Phosphorylation | - | 14.08 | 20873877 | |
| 293 | Phosphorylation | NYYDREVTPLTSSPG CCCCCCCCCCCCCCC | 14.08 | 27080861 | |
| 296 | Phosphorylation | DREVTPLTSSPGIQP CCCCCCCCCCCCCCC | 28.50 | 23401153 | |
| 297 | Phosphorylation | REVTPLTSSPGIQPS CCCCCCCCCCCCCCC | 42.07 | 29978859 | |
| 298 | Phosphorylation | EVTPLTSSPGIQPSC CCCCCCCCCCCCCCC | 23.16 | 29978859 | |
| 299 (in isoform 2) | Phosphorylation | - | 43.61 | 20873877 | |
| 304 | Phosphorylation | SSPGIQPSCGMIKRF CCCCCCCCCCHHHHH | 13.61 | 27080861 | |
| 312 | Phosphorylation | CGMIKRFSGLLHGSP CCHHHHHHCCCCCCC | 32.34 | 23401153 | |
| 318 | Phosphorylation | FSGLLHGSPKTTSLA HHCCCCCCCCHHHHH | 16.69 | 23401153 | |
| 327 | Phosphorylation | KTTSLAASAASTETL CHHHHHHHHHCCCCC | 20.82 | 27080861 | |
| 330 | Phosphorylation | SLAASAASTETLTPT HHHHHHHCCCCCCCC | 26.88 | 27080861 | |
| 331 | Phosphorylation | LAASAASTETLTPTP HHHHHHCCCCCCCCC | 28.41 | 27080861 | |
| 333 | Phosphorylation | ASAASTETLTPTPER HHHHCCCCCCCCCCC | 35.70 | 28857561 | |
| 335 | Phosphorylation | AASTETLTPTPERNE HHCCCCCCCCCCCCC | 32.32 | 27080861 | |
| 345 | Phosphorylation | PERNEGVYTAIAVQE CCCCCCEEEEEEEEE | 11.00 | 11163214 | |
| 345 | Dephosphorylation | PERNEGVYTAIAVQE CCCCCCEEEEEEEEE | 11.00 | 11711533 | |
| 359 | Phosphorylation | EIQGNPASPAQEYRA EECCCCCCHHHHHHH | 23.25 | 27080861 | |
| 364 | Phosphorylation | PASPAQEYRALYDYT CCCHHHHHHHHHHHH | 6.79 | 27080861 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 345 | Y | Phosphorylation | Kinase | ABL1 | P00519 | PhosphoELM |
| 345 | Y | Phosphorylation | Kinase | ABL-FAMILY | - | GPS |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PPIP1_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 PPIP1_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| 604416 | PAPA syndrome (PAPAS) | |||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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