ID  P97814;
PN  Proline-serine-threonine phosphatase-interacting protein 1;
GN  Pstpip1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:11711533, ECO:0000269|PubMed:12530983}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11711533}. Cell projection, lamellipodium {ECO:0000269|PubMed:9265651}. Cleavage furrow {ECO:0000269|PubMed:9265651}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9265651, ECO:0000269|PubMed:9488710}. Cell membrane {ECO:0000250|UniProtKB:O43586}; Peripheral membrane protein {ECO:0000250|UniProtKB:O43586}. Cell projection, uropodium {ECO:0000250|UniProtKB:O43586}. Note=Colocalized with PTPN12 in the cytoplasm and the perinuclear region (PubMed:11711533). During interphase, colocalizes with F-actin in the cortical cytoskeleton, lamellipodia, and stress fibers (PubMed:9265651). In dividing cells, colocalizes with the F-actin rich cytokinetic cleavage furrow (PubMed:9265651). Colocalized with CD2AP and WAS in the actin cytoskeleton within the cytoplasm (PubMed:12530983, PubMed:9488710). Colocalized with CD2, CD2AP and WAS at the site of T-cell:APC contact (PubMed:12530983). Mainly cytoplasmic in T cells. Colocalizes in cluster with CD2 near the cell surface membrane in activated T-cells. In monocytes, forms a branched filamentous network in the cytoplasm. In transfected cells, forms relatively straight filaments radiating out from the nucleus. Filament formation requires an intact tubulin cytoskeleton. In migrating neutrophils, colocalizes with PIP5K1C and DNM2 to the trailing edge of the uropod in a actin-dependent manner (By similarity). {ECO:0000250|UniProtKB:O43586, ECO:0000269|PubMed:11711533, ECO:0000269|PubMed:12530983, ECO:0000269|PubMed:9265651, ECO:0000269|PubMed:9488710}.
DR  UNIPROT: P97814;
DR  UNIPROT: Q4V9R4;
DR  Pfam: PF00611;
DR  Pfam: PF14604;
DR  PROSITE: PS51741;
DR  PROSITE: PS50002;
DE  Function: 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. 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. {ECO:0000269|PubMed:11163214, ECO:0000269|PubMed:11711533, ECO:0000269|PubMed:12530983, ECO:0000269|PubMed:9265651, ECO:0000269|PubMed:9488710}.
DE  Reference Proteome: Yes;
DE  Interaction: P70315; IntAct: EBI-8678726; Score: 0.60
DE  Interaction: P41047; IntAct: EBI-7833774; Score: 0.63
DE  Interaction: Q53ZZ1; IntAct: EBI-7833845; Score: 0.60
DE  Interaction: P35831; IntAct: EBI-7834118; Score: 0.78
DE  Interaction: P00520; IntAct: EBI-7484569; Score: 0.66
DE  Interaction: P70602; IntAct: EBI-7484657; Score: 0.40
DE  Interaction: Q61152; IntAct: EBI-8654066; Score: 0.44
DE  Interaction: P29352; IntAct: EBI-8654312; Score: 0.44
GO  GO:0005884;
GO  GO:0005826;
GO  GO:0032154;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030027;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0001725;
GO  GO:0001931;
GO  GO:0003779;
GO  GO:0051015;
GO  GO:0042802;
GO  GO:0019903;
GO  GO:0030041;
GO  GO:0007155;
GO  GO:0006897;
GO  GO:0006954;
GO  GO:0045087;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:O43586};
SQ  MMAQLQFRDAFWCRDFTAHTGYEVLLQRLLDGRKMCKDVEELLRQRAQAEERYGKELVQIARKAGGQTEMNSLRTSFDSL
SQ  KQQTENVGSAHIQLALALREELRSLEEFRERQKEQRKKYEAIMDRVQKSKLSLYKKTMESKKAYDQKCRDADDAEQAFER
SQ  VSANGHQKQVEKSQNKAKQCKESATEAERVYRQNIEQLERARTEWEQEHRTTCEAFQLQEFDRLTILRNALWVHCNQLSM
SQ  QCVKDDELYEEVRLTLEGCDVEGDINGFIQSKSTGREPPAPVPYQNYYDREVTPLIGSPSIQPSCGVIKRFSGLLHGSPK
SQ  TTPSAPAASTETLTPTPERNELVYASIEVQATQGNLNSSAQDYRALYDYTAQNSDELDISAGDILAVILEGEDGWWTVER
SQ  NGQRGFVPGSYLEKL
//