PPIP1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PPIP1_MOUSE
• UniProt AC: P97814
• Protein Name: Proline-serine-threonine phosphatase-interacting protein 1
• Gene Name: Pstpip1
• Organism: Mus musculus (Mouse).
• Sequence Length: 415
• Subcellular Localization: Cytoplasm . Cytoplasm, perinuclear region . Cell projection, lamellipodium . Cleavage furrow . Cytoplasm, cytoskeleton . Cell membrane ; Peripheral membrane protein . Cell projection, uropodium . Colocalized with PTPN12 in the cytoplasm and the perin
• 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. 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: MMAQLQFRDAFWCRDFTAHTGYEVLLQRLLDGRKMCKDVEELLRQRAQAEERYGKELVQIARKAGGQTEMNSLRTSFDSLKQQTENVGSAHIQLALALREELRSLEEFRERQKEQRKKYEAIMDRVQKSKLSLYKKTMESKKAYDQKCRDADDAEQAFERVSANGHQKQVEKSQNKAKQCKESATEAERVYRQNIEQLERARTEWEQEHRTTCEAFQLQEFDRLTILRNALWVHCNQLSMQCVKDDELYEEVRLTLEGCDVEGDINGFIQSKSTGREPPAPVPYQNYYDREVTPLIGSPSIQPSCGVIKRFSGLLHGSPKTTPSAPAASTETLTPTPERNELVYASIEVQATQGNLNSSAQDYRALYDYTAQNSDELDISAGDILAVILEGEDGWWTVERNGQRGFVPGSYLEKL

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
298	Phosphorylation	EVTPLIGSPSIQPSC CCCCCCCCCCCCCCC	14.42	25266776
300	Phosphorylation	TPLIGSPSIQPSCGV CCCCCCCCCCCCCCH	35.24	28066266
312	Phosphorylation	CGVIKRFSGLLHGSP CCHHHHHCCCCCCCC	32.34	25266776
318	Phosphorylation	FSGLLHGSPKTTPSA HCCCCCCCCCCCCCC	16.69	26824392
322	Phosphorylation	LHGSPKTTPSAPAAS CCCCCCCCCCCCCCC	22.75	28285833
329	Phosphorylation	TPSAPAASTETLTPT CCCCCCCCCCCCCCC	28.96	27566939
330	Phosphorylation	PSAPAASTETLTPTP CCCCCCCCCCCCCCC	28.41	22942356
332	Phosphorylation	APAASTETLTPTPER CCCCCCCCCCCCCCC	35.70	30635358
334	Phosphorylation	AASTETLTPTPERNE CCCCCCCCCCCCCCC	32.32	27566939
336	Phosphorylation	STETLTPTPERNELV CCCCCCCCCCCCCEE	32.33	30635358
344	Phosphorylation	PERNELVYASIEVQA CCCCCEEEEEEEEEE	13.78	9488710

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
344	Y	Phosphorylation	Kinase	ABL1	P00520	Uniprot
344	Y	Phosphorylation	Kinase	ABL-FAMILY	-	GPS

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PPIP1_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of PPIP1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
WASP_HUMAN	WAS	physical	9488710

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.