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O43586

- PPIP1_HUMAN

UniProt

O43586 - PPIP1_HUMAN

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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

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 - 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
Complete GO annotation...

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. cell projection Source: UniProtKB-KW
  3. cleavage furrow Source: Ensembl
  4. cytosol Source: Reactome
  5. membrane Source: UniProtKB
  6. stress fiber Source: Ensembl
Complete GO annotation...

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

BgeeiO43586.
CleanExiHS_PSTPIP1.
ExpressionAtlasiO43586. baseline and differential.
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
PTPN22Q9Y2R26EBI-1050964,EBI-1211241

Protein-protein interaction databases

BioGridi114513. 36 interactions.
IntActiO43586. 6 interactions.
MINTiMINT-1130527.
STRINGi9606.ENSP00000368914.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00730000110901.
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

        10         20         30         40         50
MMPQLQFKDA FWCRDFTAHT GYEVLLQRLL DGRKMCKDME ELLRQRAQAE
60 70 80 90 100
ERYGKELVQI ARKAGGQTEI NSLRASFDSL KQQMENVGSS HIQLALTLRE
110 120 130 140 150
ELRSLEEFRE RQKEQRKKYE AVMDRVQKSK LSLYKKAMES KKTYEQKCRD
160 170 180 190 200
ADDAEQAFER ISANGHQKQV EKSQNKARQC KDSATEAERV YRQSIAQLEK
210 220 230 240 250
VRAEWEQEHR TTCEAFQLQE FDRLTILRNA LWVHSNQLSM QCVKDDELYE
260 270 280 290 300
EVRLTLEGCS IDADIDSFIQ AKSTGTEPPA PVPYQNYYDR EVTPLTSSPG
310 320 330 340 350
IQPSCGMIKR FSGLLHGSPK TTSLAASAAS TETLTPTPER NEGVYTAIAV
360 370 380 390 400
QEIQGNPASP AQEYRALYDY TAQNPDELDL SAGDILEVIL EGEDGWWTVE
410
RNGQRGFVPG SYLEKL
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 36 interactions.
IntActi O43586. 6 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.
GeneTreei ENSGT00730000110901.
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

Bgeei O43586.
CleanExi HS_PSTPIP1.
ExpressionAtlasi O43586. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 127 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