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Proline-serine-threonine phosphatase-interacting protein 1 (PEST phosphatase-interacting protein 1) (CD2-binding protein 1) (H-PIP)

 PPIP1_HUMAN             Reviewed;         416 AA.
O43586; B5BU74; B5BUK4; O43585; O95657;
13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
30-AUG-2017, entry version 155.
RecName: Full=Proline-serine-threonine phosphatase-interacting protein 1;
Short=PEST phosphatase-interacting protein 1;
AltName: Full=CD2-binding protein 1;
AltName: Full=H-PIP;
Name=PSTPIP1; Synonyms=CD2BP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION
WITH CD2 AND PTPN12, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=9857189; DOI=10.1093/emboj/17.24.7320;
Li J., Nishizawa K., An W., Hussey R.E., Lialios F.E., Salgia R.,
Sunder-Plassmann R., Reinherz E.L.;
"A cdc15-like adaptor protein (CD2BP1) interacts with the CD2
cytoplasmic domain and regulates CD2-triggered adhesion.";
EMBO J. 17:7320-7336(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS HIS-48; LYS-106;
HIS-146; LEU-149; SER-151; ASP-155 AND HIS-156.
Wilson L.A., Fields D., Cruz L., Lasky L., Friesen J.,
Siminovitch K.A.;
"The human homologue of mouse PTP-PIP interactor protein.";
Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=19054851; DOI=10.1038/nmeth.1273;
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.;
"Human protein factory for converting the transcriptome into an in
vitro-expressed proteome.";
Nat. Methods 5:1011-1017(2008).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
INTERACTION WITH MEFV, TISSUE SPECIFICITY, CHARACTERIZATION OF
VARIANTS PAPAS THR-230 AND GLN-250, AND MUTAGENESIS OF TRP-232 AND
TYR-345.
PubMed=14595024; DOI=10.1073/pnas.2135380100;
Shoham N.G., Centola M., Mansfield E., Hull K.M., Wood G., Wise C.A.,
Kastner D.L.;
"Pyrin binds the PSTPIP1/CD2BP1 protein, defining familial
Mediterranean fever and PAPA syndrome as disorders in the same
pathway.";
Proc. Natl. Acad. Sci. U.S.A. 100:13501-13506(2003).
[7]
FUNCTION, SUBUNIT, INTERACTION WITH MEFV, AND CHARACTERIZATION OF
VARIANTS THR-230 AND GLN-250.
PubMed=17964261; DOI=10.1016/j.molcel.2007.08.029;
Yu J.W., Fernandes-Alnemri T., Datta P., Wu J., Juliana C.,
Solorzano L., McCormick M., Zhang Z., Alnemri E.S.;
"Pyrin activates the ASC pyroptosome in response to engagement by
autoinflammatory PSTPIP1 mutants.";
Mol. Cell 28:214-227(2007).
[8]
FUNCTION, INTERACTION WITH DNM2, AND SUBCELLULAR LOCATION.
PubMed=18480402; DOI=10.1091/mbc.E08-02-0225;
Cooper K.M., Bennin D.A., Huttenlocher A.;
"The PCH family member proline-serine-threonine phosphatase-
interacting protein 1 targets to the leukocyte uropod and regulates
directed cell migration.";
Mol. Biol. Cell 19:3180-3191(2008).
[9]
INTERACTION WITH FASLG.
PubMed=19807924; DOI=10.1186/1471-2172-10-53;
Voss M., Lettau M., Janssen O.;
"Identification of SH3 domain interaction partners of human FasL
(CD178) by phage display screening.";
BMC Immunol. 10:53-53(2009).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MEFV.
PubMed=19109554; DOI=10.3181/0806-RM-184;
Waite A.L., Schaner P., Hu C., Richards N., Balci-Peynircioglu B.,
Hong A., Fox M., Gumucio D.L.;
"Pyrin and ASC co-localize to cellular sites that are rich in
polymerizing actin.";
Exp. Biol. Med. (Maywood) 234:40-52(2009).
[11]
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS
THR-230 AND GLN-250, AND MUTAGENESIS OF TRP-232 AND ASP-266.
PubMed=19584923; DOI=10.1371/journal.pone.0006147;
Waite A.L., Schaner P., Richards N., Balci-Peynircioglu B.,
Masters S.L., Brydges S.D., Fox M., Hong A., Yilmaz E., Kastner D.L.,
Reinherz E.L., Gumucio D.L.;
"Pyrin Modulates the Intracellular Distribution of PSTPIP1.";
PLoS ONE 4:E6147-E6147(2009).
[12]
STRUCTURE BY NMR OF 358-416.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the SH3 domain of the human proline-serine-
threonine phosphatase-interacting protein 1.";
Submitted (FEB-2007) to the PDB data bank.
[13]
VARIANTS PAPAS THR-230 AND GLN-250, AND CHARACTERIZATION OF VARIANTS
PAPAS THR-230 AND GLN-250.
PubMed=11971877; DOI=10.1093/hmg/11.8.961;
Wise C.A., Gillum J.D., Seidman C.E., Lindor N.M., Veile R.,
Bashiardes S., Lovett M.;
"Mutations in CD2BP1 disrupt binding to PTP PEST and are responsible
for PAPA syndrome, an autoinflammatory disorder.";
Hum. Mol. Genet. 11:961-969(2002).
[14]
VARIANTS PAPAS THR-230; GLN-250 AND LYS-250.
PubMed=22161697; DOI=10.1002/art.34332;
Demidowich A.P., Freeman A.F., Kuhns D.B., Aksentijevich I.,
Gallin J.I., Turner M.L., Kastner D.L., Holland S.M.;
"Brief report: genotype, phenotype, and clinical course in five
patients with PAPA syndrome (pyogenic sterile arthritis, pyoderma
gangrenosum, and acne).";
Arthritis Rheum. 64:2022-2027(2012).
-!- 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}.
-!- SUBUNIT: 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. {ECO:0000269|PubMed:14595024,
ECO:0000269|PubMed:17964261, ECO:0000269|PubMed:18480402,
ECO:0000269|PubMed:19109554, ECO:0000269|PubMed:19584923,
ECO:0000269|PubMed:19807924, ECO:0000269|PubMed:9857189}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-1050964, EBI-1050964;
O43684:BUB3; NbExp=3; IntAct=EBI-1050964, EBI-1050987;
Q86YD7:FAM90A1; NbExp=5; IntAct=EBI-1050964, EBI-6658203;
P48023:FASLG; NbExp=5; IntAct=EBI-1050964, EBI-495538;
Q96D16:FBXL18; NbExp=3; IntAct=EBI-1050964, EBI-744419;
Q9Y4Z0:LSM4; NbExp=7; IntAct=EBI-1050964, EBI-372521;
O15553:MEFV; NbExp=4; IntAct=EBI-1050964, EBI-7644532;
Q9Y5E9:PCDHB14; NbExp=5; IntAct=EBI-1050964, EBI-10329013;
Q8WWY3:PRPF31; NbExp=8; IntAct=EBI-1050964, EBI-1567797;
Q05209:PTPN12; NbExp=4; IntAct=EBI-1050964, EBI-2266035;
Q99952:PTPN18; NbExp=4; IntAct=EBI-1050964, EBI-1384210;
Q9Y2R2:PTPN22; NbExp=6; IntAct=EBI-1050964, EBI-1211241;
Q14D33:RTP5; NbExp=5; IntAct=EBI-1050964, EBI-10217913;
O00560:SDCBP; NbExp=3; IntAct=EBI-1050964, EBI-727004;
Q9H788:SH2D4A; NbExp=3; IntAct=EBI-1050964, EBI-747035;
Q96GM5:SMARCD1; NbExp=4; IntAct=EBI-1050964, EBI-358489;
Q9UQ90:SPG7; NbExp=3; IntAct=EBI-1050964, EBI-717201;
Q9Y228:TRAF3IP3; NbExp=3; IntAct=EBI-1050964, EBI-765817;
O75386:TULP3; NbExp=5; IntAct=EBI-1050964, EBI-5357290;
Q96B02:UBE2W; NbExp=4; IntAct=EBI-1050964, EBI-716589;
Q9Y473:ZNF175; NbExp=3; IntAct=EBI-1050964, EBI-3438881;
-!- 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}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=CD2BP1L;
IsoId=O43586-1; Sequence=Displayed;
Name=2; Synonyms=CD2BP1S;
IsoId=O43586-2; Sequence=VSP_015627;
-!- TISSUE SPECIFICITY: 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.
{ECO:0000269|PubMed:14595024, ECO:0000269|PubMed:9857189}.
-!- DOMAIN: The F-BAR domain is important for filament formation. The
SH3 domain is not required for filament formation or localization
to the uropod.
-!- 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}.
-!- DISEASE: 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. {ECO:0000269|PubMed:11971877,
ECO:0000269|PubMed:14595024, ECO:0000269|PubMed:22161697}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- WEB RESOURCE: Name=INFEVERS; Note=Repertory of FMF and hereditary
autoinflammatory disorders mutations;
URL="http://fmf.igh.cnrs.fr/ISSAID/infevers/search.php?n=5";
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EMBL; AF038602; AAD11958.1; -; mRNA.
EMBL; AF038603; AAD11959.1; -; mRNA.
EMBL; U94778; AAD00762.1; -; mRNA.
EMBL; AB451310; BAG70124.1; -; mRNA.
EMBL; AB451440; BAG70254.1; -; mRNA.
EMBL; CH471136; EAW99213.1; -; Genomic_DNA.
EMBL; BC008602; AAH08602.1; -; mRNA.
CCDS; CCDS45312.1; -. [O43586-1]
CCDS; CCDS81910.1; -. [O43586-2]
RefSeq; NP_001308064.1; NM_001321135.1. [O43586-2]
RefSeq; NP_001308066.1; NM_001321137.1.
RefSeq; NP_003969.2; NM_003978.4. [O43586-1]
UniGene; Hs.129758; -.
PDB; 2DIL; NMR; -; A=361-416.
PDBsum; 2DIL; -.
ProteinModelPortal; O43586; -.
SMR; O43586; -.
BioGrid; 114513; 52.
IntAct; O43586; 45.
MINT; MINT-1130527; -.
STRING; 9606.ENSP00000452746; -.
iPTMnet; O43586; -.
PhosphoSitePlus; O43586; -.
SwissPalm; O43586; -.
BioMuta; PSTPIP1; -.
EPD; O43586; -.
MaxQB; O43586; -.
PaxDb; O43586; -.
PeptideAtlas; O43586; -.
PRIDE; O43586; -.
DNASU; 9051; -.
Ensembl; ENST00000558012; ENSP00000452746; ENSG00000140368. [O43586-1]
Ensembl; ENST00000559295; ENSP00000452743; ENSG00000140368. [O43586-2]
GeneID; 9051; -.
KEGG; hsa:9051; -.
UCSC; uc002bcf.3; human. [O43586-1]
CTD; 9051; -.
DisGeNET; 9051; -.
GeneCards; PSTPIP1; -.
HGNC; HGNC:9580; PSTPIP1.
HPA; HPA010600; -.
MalaCards; PSTPIP1; -.
MIM; 604416; phenotype.
MIM; 606347; gene.
neXtProt; NX_O43586; -.
OpenTargets; ENSG00000140368; -.
Orphanet; 69126; Pyogenic arthritis - pyoderma gangrenosum - acne.
PharmGKB; PA33931; -.
eggNOG; ENOG410IU8N; Eukaryota.
eggNOG; ENOG410XR8X; LUCA.
GeneTree; ENSGT00860000133756; -.
HOGENOM; HOG000294218; -.
HOVERGEN; HBG052960; -.
InParanoid; O43586; -.
KO; K12804; -.
OMA; YYDREVT; -.
OrthoDB; EOG091G09F9; -.
PhylomeDB; O43586; -.
TreeFam; TF313677; -.
Reactome; R-HSA-844456; The NLRP3 inflammasome.
SignaLink; O43586; -.
SIGNOR; O43586; -.
EvolutionaryTrace; O43586; -.
GeneWiki; PSTPIP1; -.
GenomeRNAi; 9051; -.
PRO; PR:O43586; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000140368; -.
CleanEx; HS_PSTPIP1; -.
ExpressionAtlas; O43586; baseline and differential.
Genevisible; O43586; HS.
GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0001931; C:uropod; IEA:UniProtKB-SubCell.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
CDD; cd11824; SH3_PSTPIP1; 1.
InterPro; IPR027267; AH/BAR-dom.
InterPro; IPR031160; F_BAR.
InterPro; IPR001060; FCH_dom.
InterPro; IPR030777; PSTPIP1_SH3.
InterPro; IPR001452; SH3_domain.
Pfam; PF00611; FCH; 1.
Pfam; PF14604; SH3_9; 1.
PRINTS; PR00452; SH3DOMAIN.
SMART; SM00055; FCH; 1.
SMART; SM00326; SH3; 1.
SUPFAM; SSF103657; SSF103657; 1.
SUPFAM; SSF50044; SSF50044; 1.
PROSITE; PS51741; F_BAR; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
Cell projection; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Disease mutation; Endocytosis; Immunity;
Inflammatory response; Innate immunity; Membrane; Phosphoprotein;
Polymorphism; Reference proteome; SH3 domain.
CHAIN 1 416 Proline-serine-threonine phosphatase-
interacting protein 1.
/FTId=PRO_0000058539.
DOMAIN 5 264 F-BAR. {ECO:0000255|PROSITE-
ProRule:PRU01077}.
DOMAIN 359 416 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
COILED 166 212 {ECO:0000255}.
MOD_RES 318 318 Phosphoserine.
{ECO:0000250|UniProtKB:P97814}.
VAR_SEQ 280 309 APVPYQNYYDREVTPLTSSPGIQPSCGMIK -> GEVRLAD
SAAS (in isoform 2).
{ECO:0000303|PubMed:9857189}.
/FTId=VSP_015627.
VARIANT 48 48 Q -> H (in dbSNP:rs1141038).
{ECO:0000269|Ref.2}.
/FTId=VAR_023515.
VARIANT 106 106 E -> K (in dbSNP:rs1141039).
{ECO:0000269|Ref.2}.
/FTId=VAR_023516.
VARIANT 146 146 Q -> H (in dbSNP:rs1141041).
{ECO:0000269|Ref.2}.
/FTId=VAR_023517.
VARIANT 149 149 R -> L (in dbSNP:rs1141042).
{ECO:0000269|Ref.2}.
/FTId=VAR_023518.
VARIANT 151 151 A -> S (in dbSNP:rs1141043).
{ECO:0000269|Ref.2}.
/FTId=VAR_023519.
VARIANT 155 155 E -> D (in dbSNP:rs1141044).
{ECO:0000269|Ref.2}.
/FTId=VAR_023520.
VARIANT 156 156 Q -> H (in dbSNP:rs1141045).
{ECO:0000269|Ref.2}.
/FTId=VAR_023521.
VARIANT 230 230 A -> 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;
dbSNP:rs28939381).
{ECO:0000269|PubMed:11971877,
ECO:0000269|PubMed:14595024,
ECO:0000269|PubMed:17964261,
ECO:0000269|PubMed:19584923,
ECO:0000269|PubMed:22161697}.
/FTId=VAR_023522.
VARIANT 250 250 E -> K (in PAPAS; dbSNP:rs28939089).
{ECO:0000269|PubMed:22161697}.
/FTId=VAR_070635.
VARIANT 250 250 E -> 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;
dbSNP:rs28939089).
{ECO:0000269|PubMed:11971877,
ECO:0000269|PubMed:14595024,
ECO:0000269|PubMed:17964261,
ECO:0000269|PubMed:19584923,
ECO:0000269|PubMed:22161697}.
/FTId=VAR_023523.
MUTAGEN 232 232 W->A: Abolishes binding to MEFV.
Cytoplasmic filaments are finer with
fewer branches.
{ECO:0000269|PubMed:14595024,
ECO:0000269|PubMed:19584923}.
MUTAGEN 266 266 D->N: No effect on filament formation.
{ECO:0000269|PubMed:19584923}.
MUTAGEN 345 345 Y->F: Decreases binding to MEFV.
{ECO:0000269|PubMed:14595024}.
CONFLICT 367 367 L -> F (in Ref. 2; AAD00762).
{ECO:0000305}.
STRAND 363 365 {ECO:0000244|PDB:2DIL}.
STRAND 373 377 {ECO:0000244|PDB:2DIL}.
STRAND 385 390 {ECO:0000244|PDB:2DIL}.
STRAND 393 401 {ECO:0000244|PDB:2DIL}.
STRAND 404 409 {ECO:0000244|PDB:2DIL}.
HELIX 410 412 {ECO:0000244|PDB:2DIL}.
SEQUENCE 416 AA; 47591 MW; 97818150B3D5D600 CRC64;
MMPQLQFKDA FWCRDFTAHT GYEVLLQRLL DGRKMCKDME ELLRQRAQAE ERYGKELVQI
ARKAGGQTEI NSLRASFDSL KQQMENVGSS HIQLALTLRE ELRSLEEFRE RQKEQRKKYE
AVMDRVQKSK LSLYKKAMES KKTYEQKCRD ADDAEQAFER ISANGHQKQV EKSQNKARQC
KDSATEAERV YRQSIAQLEK VRAEWEQEHR TTCEAFQLQE FDRLTILRNA LWVHSNQLSM
QCVKDDELYE EVRLTLEGCS IDADIDSFIQ AKSTGTEPPA PVPYQNYYDR EVTPLTSSPG
IQPSCGMIKR FSGLLHGSPK TTSLAASAAS TETLTPTPER NEGVYTAIAV QEIQGNPASP
AQEYRALYDY TAQNPDELDL SAGDILEVIL EGEDGWWTVE RNGQRGFVPG SYLEKL


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