Proline-serine-threonine phosphatase-interacting protein 1

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P97814 (PPIP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 93. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Proline-serine-threonine phosphatase-interacting protein 1
Short name=PEST phosphatase-interacting protein 1

Gene names

Name:

Pstpip1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	415 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in regulation of the actin cytoskeleton. May regulate the WAS actin-bundling activity. Bridges the interaction between ABL1 and PTPN18 leading to the ABL1 dephosphorylation. May play a role as a scaffold protein between PTPN12 and WAS, and allows 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 coupling PTPN12 to CD2. Ref.1 Ref.3 Ref.4 Ref.5 Ref.6
Subunit structure	Interacts with MEFV/pyrin By similarity. Interacts with PTPN18/PTP HSCF, ABL1, PTPN12, CD2, CD2AP and WAS. Interacts with FASLG By similarity. Ref.1 Ref.3 Ref.4 Ref.5 Ref.6
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton. Cell projection › lamellipodium. Cytoplasm › perinuclear region. Cleavage furrow. Note: Colocalized with the cortical actin cytoskeleton during interphase, lamellipodia and actin-rich cytokinetic cleavage furrow. Colocalized with WAS to filamentous structures within the cytoplasm. Colocalized with PTPN12 in the cytoplasm and the perinuclear region. Colocalized with CD2AP and WAS in the actin cytoskeleton. Colocalized with CD2, CD2AP and WAS at the site of T-cell:APC contact. Ref.1 Ref.3 Ref.5 Ref.6
Tissue specificity	Highly expressed in adult lung and spleen, and weakly expressed in testis, muscle, kidney, brain and heart. Highly expressed in spleen and thymus, moderately in lung, brain and muscle, and weakly expressed in heart and liver (at protein level). Ref.1 Ref.5
Developmental stage	Highly expressed in the day 7 embryo (E7). Ref.1
Domain	The SH3 and coiled-coil domains are necessary for the interaction with MEFV By similarity. The coiled domain mediates interaction with PTPN18, PTPN12 and CD2AP. The SH3 domain mediates interaction with WAS and ABL1.
Post-translational modification	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. Ref.1 Ref.3 Ref.4 Ref.5
Sequence similarities	Contains 1 FCH domain. Contains 1 SH3 domain.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cell projection Cytoplasm Cytoskeleton
Domain	Coiled coil SH3 domain
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW cytokinesis Inferred by curator Ref.1. Source: MGI
Cellular_component	actomyosin contractile ring Inferred from direct assay Ref.1. Source: MGI cleavage furrow Inferred from direct assay Ref.1. Source: MGI lamellipodium Inferred from electronic annotation. Source: UniProtKB-SubCell perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell stress fiber Inferred from direct assay Ref.1. Source: MGI
Molecular_function	actin binding Inferred from direct assay Ref.1. Source: MGI oxidoreductase activity Inferred from electronic annotation. Source: InterPro protein phosphatase binding Inferred from direct assay Ref.1. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 415

415

Proline-serine-threonine phosphatase-interacting protein 1

PRO_0000058540

Regions

Domain

5 – 82

FCH

Domain

358 – 415

SH3

Coiled coil

94 – 133

Potential

Coiled coil

162 – 215

Potential

Amino acid modifications

Modified residue

344

Phosphotyrosine; by ABL1

Experimental info

Mutagenesis

344

Y → F: Complete loss of protein phosphorylation. Ref.3 Ref.4 Ref.5

Mutagenesis

367

Y → F: No effect on phosphorylation. Ref.3 Ref.4 Ref.5

Sequence conflict

301

I → V in AAH96761. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P97814 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 16C0329284D2739C
Show »

FASTA

415

47,590

        10         20         30         40         50         60 
MMAQLQFRDA FWCRDFTAHT GYEVLLQRLL DGRKMCKDVE ELLRQRAQAE ERYGKELVQI 

        70         80         90        100        110        120 
ARKAGGQTEM NSLRTSFDSL KQQTENVGSA HIQLALALRE ELRSLEEFRE RQKEQRKKYE 

       130        140        150        160        170        180 
AIMDRVQKSK LSLYKKTMES KKAYDQKCRD ADDAEQAFER VSANGHQKQV EKSQNKAKQC 

       190        200        210        220        230        240 
KESATEAERV YRQNIEQLER ARTEWEQEHR TTCEAFQLQE FDRLTILRNA LWVHCNQLSM 

       250        260        270        280        290        300 
QCVKDDELYE EVRLTLEGCD VEGDINGFIQ SKSTGREPPA PVPYQNYYDR EVTPLIGSPS 

       310        320        330        340        350        360 
IQPSCGVIKR FSGLLHGSPK TTPSAPAAST ETLTPTPERN ELVYASIEVQ ATQGNLNSSA 

       370        380        390        400        410 
QDYRALYDYT AQNSDELDIS AGDILAVILE GEDGWWTVER NGQRGFVPGS YLEKL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"PSTPIP: a tyrosine phosphorylated cleavage furrow-associated protein that is a substrate for a PEST tyrosine phosphatase." Spencer S., Dowbenko D., Cheng J., Li W., Brush J., Utzig S., Simanis V., Lasky L.A. J. Cell Biol. 138:845-860(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH PTPN18, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, PHOSPHORYLATION.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6NCr. Tissue: Hematopoietic stem cell.
[3]	"Tyrosine phosphorylation regulates the SH3-mediated binding of the Wiskott-Aldrich syndrome protein to PSTPIP, a cytoskeletal-associated protein." Wu Y., Spencer S.D., Lasky L.A. J. Biol. Chem. 273:5765-5770(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH WAS, SUBCELLULAR LOCATION, PHOSPHORYLATION, MUTAGENESIS OF TYR-344 AND TYR-367.
[4]	"Cytoskeletal protein PSTPIP1 directs the PEST-type protein tyrosine phosphatase to the c-Abl kinase to mediate Abl dephosphorylation." Cong F., Spencer S., Cote J.F., Wu Y., Tremblay M.L., Lasky L.A., Goff S.P. Mol. Cell 6:1413-1423(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ABL1, PHOSPHORYLATION, MUTAGENESIS OF TYR-344 AND TYR-367.
[5]	"PSTPIP is a substrate of PTP-PEST and serves as a scaffold guiding PTP-PEST toward a specific dephosphorylation of WASP." Cote J.-F., Chung P.L., Theberge J.-F., Halle M., Spencer S., Lasky L.A., Tremblay M.L. J. Biol. Chem. 277:2973-2986(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PTPN12, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION, MUTAGENESIS OF TYR-344 AND TYR-367.
[6]	"The Wiskott-Aldrich syndrome protein acts downstream of CD2 and the CD2AP and PSTPIP1 adaptors to promote formation of the immunological synapse." Badour K., Zhang J., Shi F., McGavin M.K.H., Rampersad V., Hardy L.A., Field D., Siminovitch K.A. Immunity 18:141-154(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH CD2; CD2AP AND WAS, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U87814 mRNA. Translation: AAB48483.1. BC096761 mRNA. Translation: AAH96761.1.
IPI	IPI00314743.
RefSeq	NP_035323.2. NM_011193.2.
UniGene	Mm.2534.
3D structure databases
ProteinModelPortal	P97814.
SMR	P97814. Positions 7-285, 326-415.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-444743.
STRING	10090.ENSMUSP00000055823.
PTM databases
PhosphoSite	P97814.
Proteomic databases
PaxDb	P97814.
PRIDE	P97814.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000059206; ENSMUSP00000055823; ENSMUSG00000032322.
GeneID	19200.
KEGG	mmu:19200.
UCSC	uc009psv.2. mouse.
Organism-specific databases
CTD	9051.
MGI	MGI:1321396. Pstpip1.
Phylogenomic databases
eggNOG	NOG303711.
GeneTree	ENSGT00530000063207.
HOGENOM	HOG000294218.
HOVERGEN	HBG052960.
InParanoid	P97814.
KO	K12804.
OrthoDB	EOG4PZJ6T.
Gene expression databases
Bgee	P97814.
Genevestigator	P97814.
GermOnline	ENSMUSG00000032322. Mus musculus.
Family and domain databases
InterPro	IPR001060. FCH_dom. IPR011254. Prismane-like. IPR001452. SH3_domain. IPR013315. Spectrin_alpha_SH3. [Graphical view]
Pfam	PF00611. FCH. 1 hit. PF00018. SH3_1. 1 hit. [Graphical view]
PRINTS	PR00452. SH3DOMAIN. PR01887. SPECTRNALPHA.
SMART	SM00055. FCH. 1 hit. SM00326. SH3. 1 hit. [Graphical view]
SUPFAM	SSF56821. Prismane_like. 1 hit. SSF50044. SH3. 1 hit.
PROSITE	PS50133. FCH. 1 hit. PS50002. SH3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	295916.
SOURCE	Search...

Entry information

Entry name

PPIP1_MOUSE

Accession

Primary (citable) accession number: P97814
Secondary accession number(s): Q4V9R4

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2005
Last sequence update:	May 1, 1997
Last modified:	May 1, 2013
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents