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O43586

- PPIP1_HUMAN

UniProt

O43586 - PPIP1_HUMAN

Protein

Proline-serine-threonine phosphatase-interacting protein 1

Gene

PSTPIP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      Previous versions | rss
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    Functioni

    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.By similarity5 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. cell adhesion Source: ProtInc
    2. endocytosis Source: UniProtKB-KW
    3. inflammatory response Source: UniProtKB-KW
    4. innate immune response Source: Reactome
    5. nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway Source: Reactome
    6. signal transduction Source: ProtInc

    Keywords - Biological processi

    Cell adhesion, Endocytosis, Immunity, Inflammatory response, Innate immunity

    Enzyme and pathway databases

    ReactomeiREACT_75808. The NLRP3 inflammasome.
    SignaLinkiO43586.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proline-serine-threonine phosphatase-interacting protein 1
    Short name:
    PEST phosphatase-interacting protein 1
    Alternative name(s):
    CD2-binding protein 1
    H-PIP
    Gene namesi
    Name:PSTPIP1
    Synonyms:CD2BP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:9580. PSTPIP1.

    Subcellular locationi

    Cytoplasm. Cytoplasmcytoskeleton. Cell projectionlamellipodium By similarity. Cell projectionuropodium. Cytoplasmperinuclear region By similarity. Cleavage furrow By similarity
    Note: 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 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 By similarity. In monocytes, forms a branched filamentous network in the cytoplasm. In migrating neutrophils, localizes most strongly to the trailing edge of the uropod where it colocalizes with PIP5K1C. In transfected cells, forms relatively straight filaments radiating out from the nucleus. Colocalizes with MEFV, particularly at the branch point of filaments. Filament formation requires an intact tubulin cytoskeleton.By similarity

    GO - Cellular componenti

    1. actomyosin contractile ring Source: Ensembl
    2. cleavage furrow Source: UniProtKB-SubCell
    3. cytosol Source: Reactome
    4. lamellipodium Source: UniProtKB-SubCell
    5. membrane Source: UniProtKB
    6. perinuclear region of cytoplasm Source: UniProtKB-SubCell
    7. stress fiber Source: Ensembl
    8. uropod Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell projection, Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Involvement in diseasei

    PAPA syndrome (PAPAS) [MIM:604416]: Characterized by autosomal dominant inheritance of early-onset, primarily affecting skin and joint tissues. Recurring inflammatory episodes lead to accumulation of sterile, pyogenic, neutrophil-rich material within the affected joints, ultimately resulting in significant destruction.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti230 – 2301A → T in PAPAS; severely reduced binding with PTPN12; markedly increased binding to MEFV; accentuates IL1B secretion; no effect on filament formation; increased induction of MEFV in response to retroviral infection. 2 Publications
    Corresponds to variant rs28939381 [ dbSNP | Ensembl ].
    VAR_023522
    Natural varianti250 – 2501E → K in PAPAS; no effect on filament formation. 1 Publication
    VAR_070635
    Natural varianti250 – 2501E → Q in PAPAS; severely reduced binding with PTPN12; markedly increased binding to MEFV; accentuates IL1B secretion; increased induction of MEFV in response to retroviral infection. 2 Publications
    Corresponds to variant rs28939089 [ dbSNP | Ensembl ].
    VAR_023523

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi232 – 2321W → A: Abolishes binding to MEFV. Cytoplasmic filaments are finer with fewer branches. 2 Publications
    Mutagenesisi266 – 2661D → N: No effect on filament formation. 1 Publication
    Mutagenesisi345 – 3451Y → F: Decreases binding to MEFV. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi604416. phenotype.
    Orphaneti69126. Pyogenic arthritis - pyoderma gangrenosum - acne.
    PharmGKBiPA33931.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 416416Proline-serine-threonine phosphatase-interacting protein 1PRO_0000058539Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei345 – 3451PhosphotyrosineBy similarity

    Post-translational modificationi

    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.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO43586.
    PaxDbiO43586.
    PRIDEiO43586.

    PTM databases

    PhosphoSiteiO43586.

    Expressioni

    Tissue specificityi

    Highly expressed in the peripheral blood leukocytes, granulocytes and monocytes, namely in T-cells and natural killer cells, and in spleen. Weakly expressed in the thymus, small intestine, lung and placenta.2 Publications

    Gene expression databases

    ArrayExpressiO43586.
    BgeeiO43586.
    CleanExiHS_PSTPIP1.
    GenevestigatoriO43586.

    Organism-specific databases

    HPAiHPA010600.

    Interactioni

    Subunit structurei

    Homodimer (PubMed:19584923). Homotrimer (PubMed:17964261). Interacts (via coiled-coil domain) with CD2AP, PTPN12 and PTPN18. Interacts (via SH3 domain) with ABL1 and WAS. Interacts (via SH3 and coiled-coil domains) with MEFV (via B-box zinc finger); the interaction allows binding of MEFV to PYCARD and facilitates formation of PYCARD pyroptosomes. Interacts with CD2, DNM2 and FASLG.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FASLGP480235EBI-1050964,EBI-495538
    PTPN18Q999524EBI-1050964,EBI-1384210

    Protein-protein interaction databases

    BioGridi114513. 35 interactions.
    IntActiO43586. 5 interactions.
    MINTiMINT-1130527.
    STRINGi9606.ENSP00000368914.

    Structurei

    Secondary structure

    1
    416
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi363 – 3653
    Beta strandi373 – 3775
    Beta strandi385 – 3906
    Beta strandi393 – 4019
    Beta strandi404 – 4096
    Helixi410 – 4123

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DILNMR-A361-416[»]
    ProteinModelPortaliO43586.
    SMRiO43586. Positions 9-265, 328-416.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO43586.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 8278FCHPROSITE-ProRule annotationAdd
    BLAST
    Domaini359 – 41658SH3PROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili166 – 21247Sequence AnalysisAdd
    BLAST

    Domaini

    The FCH domain is important for filament formation. The SH3 domain is not required for filament formation or localization to the uropod.

    Sequence similaritiesi

    Contains 1 FCH domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, SH3 domain

    Phylogenomic databases

    eggNOGiNOG303711.
    HOGENOMiHOG000294218.
    HOVERGENiHBG052960.
    InParanoidiO43586.
    KOiK12804.
    OMAiNYYDREV.
    PhylomeDBiO43586.
    TreeFamiTF313677.

    Family and domain databases

    InterProiIPR001060. FCH_dom.
    IPR001452. SH3_domain.
    IPR013315. Spectrin_alpha_SH3.
    [Graphical view]
    PfamiPF00611. FCH. 1 hit.
    PF14604. SH3_9. 1 hit.
    [Graphical view]
    PRINTSiPR00452. SH3DOMAIN.
    PR01887. SPECTRNALPHA.
    SMARTiSM00055. FCH. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    PROSITEiPS50133. FCH. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O43586-1) [UniParc]FASTAAdd to Basket

    Also known as: CD2BP1L

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MMPQLQFKDA FWCRDFTAHT GYEVLLQRLL DGRKMCKDME ELLRQRAQAE    50
    ERYGKELVQI ARKAGGQTEI NSLRASFDSL KQQMENVGSS HIQLALTLRE 100
    ELRSLEEFRE RQKEQRKKYE AVMDRVQKSK LSLYKKAMES KKTYEQKCRD 150
    ADDAEQAFER ISANGHQKQV EKSQNKARQC KDSATEAERV YRQSIAQLEK 200
    VRAEWEQEHR TTCEAFQLQE FDRLTILRNA LWVHSNQLSM QCVKDDELYE 250
    EVRLTLEGCS IDADIDSFIQ AKSTGTEPPA PVPYQNYYDR EVTPLTSSPG 300
    IQPSCGMIKR FSGLLHGSPK TTSLAASAAS TETLTPTPER NEGVYTAIAV 350
    QEIQGNPASP AQEYRALYDY TAQNPDELDL SAGDILEVIL EGEDGWWTVE 400
    RNGQRGFVPG SYLEKL 416
    Length:416
    Mass (Da):47,591
    Last modified:June 1, 1998 - v1
    Checksum:i97818150B3D5D600
    GO
    Isoform 2 (identifier: O43586-2) [UniParc]FASTAAdd to Basket

    Also known as: CD2BP1S

    The sequence of this isoform differs from the canonical sequence as follows:
         280-309: APVPYQNYYDREVTPLTSSPGIQPSCGMIK → GEVRLADSAAS

    Show »
    Length:397
    Mass (Da):45,354
    Checksum:i54D64A3AAE16A2FC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti367 – 3671L → F in AAD00762. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti48 – 481Q → H.1 Publication
    Corresponds to variant rs1141038 [ dbSNP | Ensembl ].
    VAR_023515
    Natural varianti106 – 1061E → K.1 Publication
    Corresponds to variant rs1141039 [ dbSNP | Ensembl ].
    VAR_023516
    Natural varianti146 – 1461Q → H.1 Publication
    Corresponds to variant rs1141041 [ dbSNP | Ensembl ].
    VAR_023517
    Natural varianti149 – 1491R → L.1 Publication
    Corresponds to variant rs1141042 [ dbSNP | Ensembl ].
    VAR_023518
    Natural varianti151 – 1511A → S.1 Publication
    Corresponds to variant rs1141043 [ dbSNP | Ensembl ].
    VAR_023519
    Natural varianti155 – 1551E → D.1 Publication
    Corresponds to variant rs1141044 [ dbSNP | Ensembl ].
    VAR_023520
    Natural varianti156 – 1561Q → H.1 Publication
    Corresponds to variant rs1141045 [ dbSNP | Ensembl ].
    VAR_023521
    Natural varianti230 – 2301A → T in PAPAS; severely reduced binding with PTPN12; markedly increased binding to MEFV; accentuates IL1B secretion; no effect on filament formation; increased induction of MEFV in response to retroviral infection. 2 Publications
    Corresponds to variant rs28939381 [ dbSNP | Ensembl ].
    VAR_023522
    Natural varianti250 – 2501E → K in PAPAS; no effect on filament formation. 1 Publication
    VAR_070635
    Natural varianti250 – 2501E → Q in PAPAS; severely reduced binding with PTPN12; markedly increased binding to MEFV; accentuates IL1B secretion; increased induction of MEFV in response to retroviral infection. 2 Publications
    Corresponds to variant rs28939089 [ dbSNP | Ensembl ].
    VAR_023523

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei280 – 30930APVPY…CGMIK → GEVRLADSAAS in isoform 2. 1 PublicationVSP_015627Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF038602 mRNA. Translation: AAD11958.1.
    AF038603 mRNA. Translation: AAD11959.1.
    U94778 mRNA. Translation: AAD00762.1.
    AB451310 mRNA. Translation: BAG70124.1.
    AB451440 mRNA. Translation: BAG70254.1.
    CH471136 Genomic DNA. Translation: EAW99213.1.
    BC008602 mRNA. Translation: AAH08602.1.
    CCDSiCCDS45312.1. [O43586-1]
    RefSeqiNP_003969.2. NM_003978.3. [O43586-1]
    UniGeneiHs.129758.

    Genome annotation databases

    EnsembliENST00000558012; ENSP00000452746; ENSG00000140368. [O43586-1]
    ENST00000559295; ENSP00000452743; ENSG00000140368. [O43586-2]
    GeneIDi9051.
    KEGGihsa:9051.
    UCSCiuc002bcf.2. human. [O43586-1]
    uc010bkw.1. human. [O43586-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    INFEVERS

    Repertory of FMF and hereditary autoinflammatory disorders mutations

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF038602 mRNA. Translation: AAD11958.1 .
    AF038603 mRNA. Translation: AAD11959.1 .
    U94778 mRNA. Translation: AAD00762.1 .
    AB451310 mRNA. Translation: BAG70124.1 .
    AB451440 mRNA. Translation: BAG70254.1 .
    CH471136 Genomic DNA. Translation: EAW99213.1 .
    BC008602 mRNA. Translation: AAH08602.1 .
    CCDSi CCDS45312.1. [O43586-1 ]
    RefSeqi NP_003969.2. NM_003978.3. [O43586-1 ]
    UniGenei Hs.129758.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DIL NMR - A 361-416 [» ]
    ProteinModelPortali O43586.
    SMRi O43586. Positions 9-265, 328-416.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114513. 35 interactions.
    IntActi O43586. 5 interactions.
    MINTi MINT-1130527.
    STRINGi 9606.ENSP00000368914.

    PTM databases

    PhosphoSitei O43586.

    Proteomic databases

    MaxQBi O43586.
    PaxDbi O43586.
    PRIDEi O43586.

    Protocols and materials databases

    DNASUi 9051.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000558012 ; ENSP00000452746 ; ENSG00000140368 . [O43586-1 ]
    ENST00000559295 ; ENSP00000452743 ; ENSG00000140368 . [O43586-2 ]
    GeneIDi 9051.
    KEGGi hsa:9051.
    UCSCi uc002bcf.2. human. [O43586-1 ]
    uc010bkw.1. human. [O43586-2 ]

    Organism-specific databases

    CTDi 9051.
    GeneCardsi GC15P077287.
    HGNCi HGNC:9580. PSTPIP1.
    HPAi HPA010600.
    MIMi 604416. phenotype.
    606347. gene.
    neXtProti NX_O43586.
    Orphaneti 69126. Pyogenic arthritis - pyoderma gangrenosum - acne.
    PharmGKBi PA33931.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG303711.
    HOGENOMi HOG000294218.
    HOVERGENi HBG052960.
    InParanoidi O43586.
    KOi K12804.
    OMAi NYYDREV.
    PhylomeDBi O43586.
    TreeFami TF313677.

    Enzyme and pathway databases

    Reactomei REACT_75808. The NLRP3 inflammasome.
    SignaLinki O43586.

    Miscellaneous databases

    EvolutionaryTracei O43586.
    GeneWikii PSTPIP1.
    GenomeRNAii 9051.
    NextBioi 33911.
    PROi O43586.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O43586.
    Bgeei O43586.
    CleanExi HS_PSTPIP1.
    Genevestigatori O43586.

    Family and domain databases

    InterProi IPR001060. FCH_dom.
    IPR001452. SH3_domain.
    IPR013315. Spectrin_alpha_SH3.
    [Graphical view ]
    Pfami PF00611. FCH. 1 hit.
    PF14604. SH3_9. 1 hit.
    [Graphical view ]
    PRINTSi PR00452. SH3DOMAIN.
    PR01887. SPECTRNALPHA.
    SMARTi SM00055. FCH. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    PROSITEi PS50133. FCH. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A cdc15-like adaptor protein (CD2BP1) interacts with the CD2 cytoplasmic domain and regulates CD2-triggered adhesion."
      Li J., Nishizawa K., An W., Hussey R.E., Lialios F.E., Salgia R., Sunder-Plassmann R., Reinherz E.L.
      EMBO J. 17:7320-7336(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION WITH CD2 AND PTPN12, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    2. "The human homologue of mouse PTP-PIP interactor protein."
      Wilson L.A., Fields D., Cruz L., Lasky L., Friesen J., Siminovitch K.A.
      Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS HIS-48; LYS-106; HIS-146; LEU-149; SER-151; ASP-155 AND HIS-156.
    3. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
      Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
      , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
      Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 1).
      Tissue: Brain.
    6. "Pyrin binds the PSTPIP1/CD2BP1 protein, defining familial Mediterranean fever and PAPA syndrome as disorders in the same pathway."
      Shoham N.G., Centola M., Mansfield E., Hull K.M., Wood G., Wise C.A., Kastner D.L.
      Proc. Natl. Acad. Sci. U.S.A. 100:13501-13506(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MEFV, TISSUE SPECIFICITY, CHARACTERIZATION OF VARIANTS PAPAS THR-230 AND GLN-250, MUTAGENESIS OF TRP-232 AND TYR-345.
    7. "Pyrin activates the ASC pyroptosome in response to engagement by autoinflammatory PSTPIP1 mutants."
      Yu J.W., Fernandes-Alnemri T., Datta P., Wu J., Juliana C., Solorzano L., McCormick M., Zhang Z., Alnemri E.S.
      Mol. Cell 28:214-227(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, INTERACTION WITH MEFV, CHARACTERIZATION OF VARIANTS THR-230 AND GLN-250.
    8. "The PCH family member proline-serine-threonine phosphatase-interacting protein 1 targets to the leukocyte uropod and regulates directed cell migration."
      Cooper K.M., Bennin D.A., Huttenlocher A.
      Mol. Biol. Cell 19:3180-3191(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DNM2, SUBCELLULAR LOCATION.
    9. "Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
      Voss M., Lettau M., Janssen O.
      BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FASLG.
    10. "Pyrin and ASC co-localize to cellular sites that are rich in polymerizing actin."
      Waite A.L., Schaner P., Hu C., Richards N., Balci-Peynircioglu B., Hong A., Fox M., Gumucio D.L.
      Exp. Biol. Med. (Maywood) 234:40-52(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MEFV.
    11. Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS THR-230 AND LYS-250, MUTAGENESIS OF TRP-232 AND ASP-266.
    12. "Solution structure of the SH3 domain of the human proline-serine-threonine phosphatase-interacting protein 1."
      RIKEN structural genomics initiative (RSGI)
      Submitted (FEB-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 358-416.
    13. "Mutations in CD2BP1 disrupt binding to PTP PEST and are responsible for PAPA syndrome, an autoinflammatory disorder."
      Wise C.A., Gillum J.D., Seidman C.E., Lindor N.M., Veile R., Bashiardes S., Lovett M.
      Hum. Mol. Genet. 11:961-969(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PAPAS THR-230 AND GLN-250, CHARACTERIZATION OF VARIANTS PAPAS THR-230 AND GLN-250.
    14. "Brief report: genotype, phenotype, and clinical course in five patients with PAPA syndrome (pyogenic sterile arthritis, pyoderma gangrenosum, and acne)."
      Demidowich A.P., Freeman A.F., Kuhns D.B., Aksentijevich I., Gallin J.I., Turner M.L., Kastner D.L., Holland S.M.
      Arthritis Rheum. 64:2022-2027(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PAPAS THR-230; GLN-250 AND LYS-250.

    Entry informationi

    Entry nameiPPIP1_HUMAN
    AccessioniPrimary (citable) accession number: O43586
    Secondary accession number(s): B5BU74
    , B5BUK4, O43585, O95657
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 13, 2005
    Last sequence update: June 1, 1998
    Last modified: October 1, 2014
    This is version 125 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3