Pstpip1
entrez
19200
canonical
uniprot
P97814
canonical
ensembl
ENSMUSG00000032322
resolver
ensp
ENSMUSP00000055823
resolver
ensp
ENSMUSP00000226378
resolver
enst
ENSMUST00000059206
resolver
genesymbol
Pstpip1
resolver
uniprot
A0A0R4J0P5
resolver
uniprot
Q4V9R4
resolver
uniprot_entry
A0A0R4J0P5_MOUSE
resolver
uniprot_entry
PPIP1_MOUSE
resolver
uniprot_sec
Q4V9R4
resolver
amino_acid_sequence
MMAQLQFRDAFWCRDFTAHTGYEVLLQRLLDGRKMCKDVEELLRQRAQAEERYGKELVQIARKAGGQTEMNSLRTSFDSLKQQTENVGSAHIQLALALREELRSLEEFRERQKEQRKKYEAIMDRVQKSKLSLYKKTMESKKAYDQKCRDADDAEQAFERVSANGHQKQVEKSQNKAKQCKESATEAERVYRQNIEQLERARTEWEQEHRTTCEAFQLQEFDRLTILRNALWVHCNQLSMQCVKDDELYEEVRLTLEGCDVEGDINGFIQSKSTGREPPAPVPYQNYYDREVTPLIGSPSIQPSCGVIKRFSGLLHGSPKTTPSAPAASTETLTPTPERNELVYASIEVQATQGNLNSSAQDYRALYDYTAQNSDELDISAGDILAVILEGEDGWWTVERNGQRGFVPGSYLEKL
uniprot
proteins
function
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}.
uniprot
proteins
mass_dalton
47590
uniprot
proteins
mutagenesis
MUTAGEN 344; /note="Y->F: Complete loss of protein phosphorylation."; /evidence="ECO:0000269|PubMed:11163214, ECO:0000269|PubMed:11711533, ECO:0000269|PubMed:9488710"; MUTAGEN 367; /note="Y->F: No effect on phosphorylation."; /evidence="ECO:0000269|PubMed:11163214, ECO:0000269|PubMed:11711533, ECO:0000269|PubMed:9488710
uniprot
proteins
post_translational_modification
PTM: Dephosphorylated on Tyr-344 by PTPN18, this event negatively regulates the association of PSTPIP1 with SH2 domain-containing proteins as tyrosine kinase. Phosphorylation of Tyr-344 is probably required for subsequent phosphorylation at other tyrosine residues. Phosphorylation is induced by activation of the EGFR and PDGFR in a ABL1 dependent manner. The phosphorylation regulates the interaction with WAS and with MEFV. {ECO:0000269|PubMed:11163214, ECO:0000269|PubMed:11711533, ECO:0000269|PubMed:9265651, ECO:0000269|PubMed:9488710}.
uniprot
proteins
pubmed
11163214
uniprot
proteins
pubmed
11711533
uniprot
proteins
pubmed
12530983
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
9265651
uniprot
proteins
pubmed
9488710
uniprot
proteins
sequence_length
415
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: 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}.
uniprot
proteins