PSTPIP1
entrez
9051
canonical
uniprot
O43586
canonical
ensembl
ENSG00000140368
resolver
ensp
ENSP00000368914
resolver
ensp
ENSP00000452743
resolver
ensp
ENSP00000452746
resolver
ensp
ENSP00000452986
resolver
enst
ENST00000379595
resolver
genesymbol
PSTPIP1
resolver
genesymbol_syn
CD2BP1
resolver
hgnc
HGNC:9580
resolver
uniprot
A0A0S2Z5P3
resolver
uniprot
B5BU74
resolver
uniprot
B5BUK4
resolver
uniprot
J3KPG6
resolver
uniprot
O43585
resolver
uniprot
O95657
resolver
uniprot_entry
A0A0S2Z5P3_HUMAN
resolver
uniprot_entry
J3KPG6_HUMAN
resolver
uniprot_entry
PPIP1_HUMAN
resolver
uniprot_sec
B5BU74
resolver
uniprot_sec
B5BUK4
resolver
uniprot_sec
O43585
resolver
uniprot_sec
O95657
resolver
amino_acid_sequence
MMPQLQFKDAFWCRDFTAHTGYEVLLQRLLDGRKMCKDMEELLRQRAQAEERYGKELVQIARKAGGQTEINSLRASFDSLKQQMENVGSSHIQLALTLREELRSLEEFRERQKEQRKKYEAVMDRVQKSKLSLYKKAMESKKTYEQKCRDADDAEQAFERISANGHQKQVEKSQNKARQCKDSATEAERVYRQSIAQLEKVRAEWEQEHRTTCEAFQLQEFDRLTILRNALWVHSNQLSMQCVKDDELYEEVRLTLEGCSIDADIDSFIQAKSTGTEPPAPVPYQNYYDREVTPLTSSPGIQPSCGMIKRFSGLLHGSPKTTSLAASAASTETLTPTPERNEGVYTAIAVQEIQGNPASPAQEYRALYDYTAQNPDELDLSAGDILEVILEGEDGWWTVERNGQRGFVPGSYLEKL
uniprot
proteins
disease_involvement
DISEASE: Pyogenic sterile arthritis, pyoderma gangrenosum, and acne (PAPA) [MIM:604416]: A rare autosomal dominant autoinflammatory disease that typically presents with recurrent sterile, erosive arthritis in childhood, occurring spontaneously or after minor trauma, occasionally resulting in significant joint destruction. By puberty, joint symptoms tend to subside and cutaneous symptoms increase. Cutaneous manifestations include pathergy, frequently with abscesses at the sites of injections, severe cystic acne, and recurrent nonhealing sterile ulcers, often diagnosed as pyoderma gangrenosum. {ECO:0000269|PubMed:11971877, ECO:0000269|PubMed:14595024, ECO:0000269|PubMed:22161697, ECO:0000269|PubMed:28251506, ECO:0000269|PubMed:34938582}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Autoinflammatory syndrome with cytopenia, hyperzincemia, and hypercalprotectinemia (AICZC) [MIM:601979]: An autosomal dominant, autoinflammatory disorder characterized by severe systemic and cutaneous inflammation, hepatosplenomegaly, arthritis, pancytopenia, failure to thrive, and marked elevation of zinc and calprotectin blood levels. AICZC shows intrafamilial variable expressivity and incomplete penetrance. {ECO:0000269|PubMed:22161697, ECO:0000269|PubMed:26025129, ECO:0000269|PubMed:28628471, ECO:0000269|PubMed:29150835, ECO:0000269|PubMed:30198636, ECO:0000269|PubMed:34047005, ECO:0000269|PubMed:36203570}. Note=The disease is caused by variants affecting the gene represented in this entry.
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 (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. {ECO:0000250, ECO:0000269|PubMed:17964261, ECO:0000269|PubMed:18480402, ECO:0000269|PubMed:19109554, ECO:0000269|PubMed:19584923, ECO:0000269|PubMed:9857189}.
uniprot
proteins
mass_dalton
47591
uniprot
proteins
mutagenesis
MUTAGEN 232; /note="W->A: Abolishes binding to MEFV. Cytoplasmic filaments are finer with fewer branches."; /evidence="ECO:0000269|PubMed:14595024, ECO:0000269|PubMed:19584923"; MUTAGEN 266; /note="D->N: No effect on filament formation."; /evidence="ECO:0000269|PubMed:19584923"; MUTAGEN 345; /note="Y->F: Decreases binding to MEFV."; /evidence="ECO:0000269|PubMed:14595024
uniprot
proteins
post_translational_modification
PTM: Dephosphorylated on Tyr-345 by PTPN18, this event negatively regulates the association of PSTPIP1 with SH2 domain-containing proteins as tyrosine kinase. Phosphorylation of Tyr-345 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 (By similarity). {ECO:0000250}.
uniprot
proteins
pubmed
11971877
uniprot
proteins
pubmed
14595024
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17964261
uniprot
proteins
pubmed
18480402
uniprot
proteins
pubmed
19054851
uniprot
proteins
pubmed
19109554
uniprot
proteins
pubmed
19584923
uniprot
proteins
pubmed
19807924
uniprot
proteins
pubmed
22161697
uniprot
proteins
pubmed
26025129
uniprot
proteins
pubmed
28251506
uniprot
proteins
pubmed
28628471
uniprot
proteins
pubmed
29150835
uniprot
proteins
pubmed
30198636
uniprot
proteins
pubmed
34047005
uniprot
proteins
pubmed
34938582
uniprot
proteins
pubmed
36203570
uniprot
proteins
pubmed
9857189
uniprot
proteins
sequence_length
416
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9857189}. Cell membrane {ECO:0000269|PubMed:18480402, ECO:0000269|PubMed:9857189}; Peripheral membrane protein {ECO:0000269|PubMed:9857189}. Cell projection, uropodium {ECO:0000269|PubMed:18480402}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19109554, ECO:0000269|PubMed:19584923}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P97814}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:P97814}. Cleavage furrow {ECO:0000250|UniProtKB:P97814}. Note=Mainly cytoplasmic in T-cells (PubMed:9857189). Colocalizes in cluster with CD2 near the cell surface membrane in activated T-cells (PubMed:9857189). In monocytes, forms a branched filamentous network in the cytoplasm (PubMed:19584923). In transfected cells, forms relatively straight filaments radiating out from the nucleus (PubMed:19584923). Filament formation requires an intact tubulin cytoskeleton (PubMed:19584923). In migrating neutrophils, colocalizes with PIP5K1C and DNM2 to the trailing edge of the uropod in a actin-dependent manner (PubMed:18480402). Colocalized with PTPN12 in the cytoplasm and the perinuclear region. During interphase, colocalizes with F-actin in the cortical cytoskeleton, lamellipodia, and stress fibers. In dividing cells, colocalizes with the F-actin rich cytokinetic cleavage furrow. Colocalized with CD2AP and WAS in the actin cytoskeleton within the cytoplasm. Colocalized with CD2, CD2AP and WAS at the site of T-cell:APC contact (By similarity). {ECO:0000250|UniProtKB:P97814, ECO:0000269|PubMed:18480402, ECO:0000269|PubMed:19584923, ECO:0000269|PubMed:9857189}.
uniprot
proteins