Variant position: 230 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 416 The length of the canonical sequence.
Location on the sequence:
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human RTTCEAFQLQEFDRLTILRN ALWVHSNQLSMQCVKDDELYE
Mouse RTTCEAFQLQEFDRLTILRN ALWVHCNQLSMQCVKDDELYE
Sequence annotation in neighborhood: The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
Type: the type of sequence feature. Positions: endpoints of the sequence feature. Description: contains additional information about the feature.
Type Positions Description
1 – 416 Proline-serine-threonine phosphatase-interacting protein 1
5 – 264 F-BAR
232 – 232 W -> A. Abolishes binding to MEFV. Cytoplasmic filaments are finer with fewer branches.
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)
Cited for: INTERACTION WITH MEFV; TISSUE SPECIFICITY; CHARACTERIZATION OF VARIANTS PAPAS THR-230 AND GLN-250; MUTAGENESIS OF TRP-232 AND TYR-345;
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)
Cited for: FUNCTION; SUBUNIT; INTERACTION WITH MEFV; CHARACTERIZATION OF VARIANTS THR-230 AND GLN-250;
Pyrin Modulates the Intracellular Distribution of PSTPIP1.
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.;
PLoS ONE 4:E6147-E6147(2009)
Cited for: FUNCTION; SUBUNIT; SUBCELLULAR LOCATION; CHARACTERIZATION OF VARIANTS THR-230 AND GLN-250; MUTAGENESIS OF TRP-232 AND ASP-266;
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)
Cited for: VARIANTS PAPAS THR-230 AND GLN-250; CHARACTERIZATION OF VARIANTS PAPAS THR-230 AND GLN-250;
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)
Cited for: VARIANTS PAPAS THR-230; GLN-250 AND LYS-250;
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