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Apoptosis-associated speck-like protein containing a CARD (hASC) (Caspase recruitment domain-containing protein 5) (PYD and CARD domain-containing protein) (Target of methylation-induced silencing 1)

 ASC_HUMAN               Reviewed;         195 AA.
Q9ULZ3; Q96D12; Q9BSZ5; Q9HBD0; Q9NXJ8;
18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 2.
22-NOV-2017, entry version 172.
RecName: Full=Apoptosis-associated speck-like protein containing a CARD;
Short=hASC;
AltName: Full=Caspase recruitment domain-containing protein 5;
AltName: Full=PYD and CARD domain-containing protein;
AltName: Full=Target of methylation-induced silencing 1;
Name=PYCARD; Synonyms=ASC, CARD5, TMS1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Leukemia;
PubMed=10567338; DOI=10.1074/jbc.274.48.33835;
Masumoto J., Taniguchi S., Ayukawa K., Sarvotham H., Kishino T.,
Niikawa N., Hidaka E., Katsuyama T., Higuchi T., Sagara J.;
"ASC, a novel 22-kDa protein, aggregates during apoptosis of human
promyelocytic leukemia HL-60 cells.";
J. Biol. Chem. 274:33835-33838(1999).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
TISSUE=Fibroblast;
PubMed=11103776;
Conway K.E., McConnell B.B., Bowring C.E., Donald C.D., Warren S.T.,
Vertino P.M.;
"TMS1, a novel proapoptotic caspase recruitment domain protein, is a
target of methylation-induced gene silencing in human breast
cancers.";
Cancer Res. 60:6236-6242(2000).
[3]
NUCLEOTIDE SEQUENCE (ISOFORM 2), FUNCTION (ISOFORM 2), AND MASS
SPECTROMETRY (ISOFORM 2).
PubMed=19759850; DOI=10.1155/2009/287387;
Matsushita K., Takeoka M., Sagara J., Itano N., Kurose Y.,
Nakamura A., Taniguchi S.;
"A splice variant of ASC regulates IL-1beta release and aggregates
differently from intact ASC.";
Mediators Inflamm. 2009:287387-287387(2009).
[4]
NUCLEOTIDE SEQUENCE (ISOFORM 1).
Martinon F., Hofmann K., Tschopp J.;
"Pycard a PYD and CARD containing molecule.";
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE (ISOFORM 1).
Bertin J.;
"CARD5 protein is a CARD/PYRIN family member that is involved in
apoptosis signal transduction.";
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Colon mucosa;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 4-195 (ISOFORM 1).
TISSUE=Lymph, and Pancreas;
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).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11103777;
McConnell B.B., Vertino P.M.;
"Activation of a caspase-9-mediated apoptotic pathway by subcellular
redistribution of the novel caspase recruitment domain protein TMS1.";
Cancer Res. 60:6243-6247(2000).
[9]
INTERACTION WITH NLRC4.
PubMed=11374873; DOI=10.1006/bbrc.2001.4928;
Geddes B.J., Wang L., Huang W.-J., Lavellee M., Manji G.A., Brown M.,
Jurman M., Cao J., Morgenstern J., Merriam S., Glucksmann M.A.,
DiStefano P.S., Bertin J.;
"Human CARD12 is a novel CED4/Apaf-1 family member that induces
apoptosis.";
Biochem. Biophys. Res. Commun. 284:77-82(2001).
[10]
INTERACTION WITH MEFV.
PubMed=11498534; DOI=10.1074/jbc.M104730200;
Richards N., Schaner P., Diaz A., Stuckey J., Shelden E., Wadhwa A.,
Gumucio D.L.;
"Interaction between pyrin and the apoptotic speck protein (ASC)
modulates ASC-induced apoptosis.";
J. Biol. Chem. 276:39320-39329(2001).
[11]
INTERACTION WITH NLRP3, AND DOMAIN.
PubMed=11786556; DOI=10.1074/jbc.M112208200;
Manji G.A., Wang L., Geddes B.J., Brown M., Merriam S., Al-Garawi A.,
Mak S., Lora J.M., Briskin M., Jurman M., Cao J., DiStefano P.S.,
Bertin J.;
"PYPAF1: a PYRIN-containing APAF1-like protein that assembles with ASC
and activates NF-kB.";
J. Biol. Chem. 277:11570-11575(2002).
[12]
INTERACTION WITH CASP1; NLRC4 AND CARD16.
PubMed=11967258; DOI=10.1074/jbc.C200179200;
Srinivasula S.M., Poyet J.L., Razmara M., Datta P., Zhang Z.,
Alnemri E.S.;
"The PYRIN-CARD protein ASC is an activating adaptor for caspase-1.";
J. Biol. Chem. 277:21119-21122(2002).
[13]
FUNCTION, AND INTERACTION WITH CHUK AND IKBKB.
PubMed=12486103; DOI=10.1084/jem.20021552;
Stehlik C., Fiorentino L., Dorfleutner A., Bruey J.M., Ariza E.M.,
Sagara J., Reed J.C.;
"The PAAD/PYRIN-family protein ASC is a dual regulator of a conserved
step in nuclear factor kappaB activation pathways.";
J. Exp. Med. 196:1605-1615(2002).
[14]
IDENTIFICATION IN NLPR1 INFLAMMASOME.
PubMed=12191486; DOI=10.1016/S1097-2765(02)00599-3;
Martinon F., Burns K., Tschopp J.;
"The inflammasome: a molecular platform triggering activation of
inflammatory caspases and processing of proIL-beta.";
Mol. Cell 10:417-426(2002).
[15]
FUNCTION IN APOPTOSIS, INTERACTION WITH CASP8, AND MUTAGENESIS OF
LEU-12.
PubMed=12646168; DOI=10.1016/S0006-291X(03)00309-7;
Masumoto J., Dowds T.A., Schaner P., Chen F.F., Ogura Y., Li M.,
Zhu L., Katsuyama T., Sagara J., Taniguchi S., Gumucio D.L., Nunez G.,
Inohara N.;
"ASC is an activating adaptor for NF-kappa B and caspase-8-dependent
apoptosis.";
Biochem. Biophys. Res. Commun. 303:69-73(2003).
[16]
INTERACTION WITH PYDC1, DOMAIN, AND PHOSPHORYLATION.
PubMed=12656673; DOI=10.1042/BJ20030304;
Stehlik C., Krajewska M., Welsh K., Krajewski S., Godzik A.,
Reed J.C.;
"The PAAD/PYRIN-only protein POP1/ASC2 is a modulator of ASC-mediated
nuclear-factor-kappa B and pro-caspase-1 regulation.";
Biochem. J. 373:101-113(2003).
[17]
INTERACTION WITH CASP1 AND RIPK2.
PubMed=14634131; DOI=10.4049/jimmunol.171.11.6154;
Stehlik C., Lee S.H., Dorfleutner A., Stassinopoulos A., Sagara J.,
Reed J.C.;
"Apoptosis-associated speck-like protein containing a caspase
recruitment domain is a regulator of procaspase-1 activation.";
J. Immunol. 171:6154-6163(2003).
[18]
FUNCTION IN NLRP2 AND NLRP3 INFLAMMASOMES, INTERACTION WITH NLRP2 AND
NLRP3, AND SUBCELLULAR LOCATION.
PubMed=15030775; DOI=10.1016/S1074-7613(04)00046-9;
Agostini L., Martinon F., Burns K., McDermott M.F., Hawkins P.N.,
Tschopp J.;
"NALP3 forms an IL-1beta-processing inflammasome with increased
activity in Muckle-Wells autoinflammatory disorder.";
Immunity 20:319-325(2004).
[19]
INTERACTION WITH NLRP10.
PubMed=15096476; DOI=10.1093/intimm/dxh081;
Wang Y., Hasegawa M., Imamura R., Kinoshita T., Kondo C., Konaka K.,
Suda T.;
"PYNOD, a novel Apaf-1/CED4-like protein is an inhibitor of ASC and
caspase-1.";
Int. Immunol. 16:777-786(2004).
[20]
INTERACTION WITH NLRP3.
PubMed=15020601; DOI=10.1074/jbc.M401178200;
Dowds T.A., Masumoto J., Zhu L., Inohara N., Nunez G.;
"Cryopyrin-induced interleukin 1beta secretion in monocytic cells:
enhanced activity of disease-associated mutants and requirement for
ASC.";
J. Biol. Chem. 279:21924-21928(2004).
[21]
INTERACTION WITH NLRP2, AND MUTAGENESIS OF GLU-13.
PubMed=15456791; DOI=10.1074/jbc.M406741200;
Bruey J.-M., Bruey-Sedano N., Newman R., Chandler S., Stehlik C.,
Reed J.C.;
"PAN1/NALP2/PYPAF2, an inducible inflammatory mediator that regulates
NF-kappaB and caspase-1 activation in macrophages.";
J. Biol. Chem. 279:51897-51907(2004).
[22]
FUNCTION IN APOPTOSIS, SUBCELLULAR LOCATION, AND INTERACTION WITH BAX.
PubMed=14730312; DOI=10.1038/ncb1087;
Ohtsuka T., Ryu H., Minamishima Y.A., Macip S., Sagara J.,
Nakayama K.I., Aaronson S.A., Lee S.W.;
"ASC is a Bax adaptor and regulates the p53-Bax mitochondrial
apoptosis pathway.";
Nat. Cell Biol. 6:121-128(2004).
[23]
SELF-ASSOCIATION, AND MUTAGENESIS OF ILE-8; LEU-12; GLU-13; LEU-15;
GLU-19; LEU-20; LYS-21; PHE-23; LEU-25; LYS-26; LEU-27; PRO-40;
ARG-41; LEU-45; MET-47; ASP-48; LEU-52; LEU-56; GLU-62; GLU-67;
LEU-68; VAL-72 AND MET-76.
PubMed=15641782; DOI=10.1021/bi048374i;
Moriya M., Taniguchi S., Wu P., Liepinsh E., Otting G., Sagara J.;
"Role of charged and hydrophobic residues in the oligomerization of
the PYRIN domain of ASC.";
Biochemistry 44:575-583(2005).
[24]
ASSOCIATION WITH INFLAMMASOMES.
PubMed=16037825; DOI=10.1038/sj.cdd.4401734;
Yu J.W., Wu J., Zhang Z., Datta P., Ibrahimi I., Taniguchi S.,
Sagara J., Fernandes-Alnemri T., Alnemri E.S.;
"Cryopyrin and pyrin activate caspase-1, but not NF-kappaB, via ASC
oligomerization.";
Cell Death Differ. 13:236-249(2006).
[25]
FUNCTION, AND INTERACTION WITH CASP1.
PubMed=16585594; DOI=10.4049/jimmunol.176.8.4979;
Sarkar A., Duncan M., Hart J., Hertlein E., Guttridge D.C.,
Wewers M.D.;
"ASC directs NF-kappaB activation by regulating receptor interacting
protein-2 (RIP2) caspase-1 interactions.";
J. Immunol. 176:4979-4986(2006).
[26]
FUNCTION.
PubMed=16982856; DOI=10.4049/jimmunol.177.7.4252;
Taxman D.J., Zhang J., Champagne C., Bergstralh D.T., Iocca H.A.,
Lich J.D., Ting J.P.;
"ASC mediates the induction of multiple cytokines by Porphyromonas
gingivalis via caspase-1-dependent and -independent pathways.";
J. Immunol. 177:4252-4256(2006).
[27]
FUNCTION, AND SUBUNIT.
PubMed=17599095; DOI=10.1038/sj.cdd.4402194;
Fernandes-Alnemri T., Wu J., Yu J.W., Datta P., Miller B.,
Jankowski W., Rosenberg S., Zhang J., Alnemri E.S.;
"The pyroptosome: a supramolecular assembly of ASC dimers mediating
inflammatory cell death via caspase-1 activation.";
Cell Death Differ. 14:1590-1604(2007).
[28]
FUNCTION IN NLRP1 INFLAMMASOME.
PubMed=17349957; DOI=10.1016/j.molcel.2007.01.032;
Faustin B., Lartigue L., Bruey J.-M., Luciano F., Sergienko E.,
Bailly-Maitre B., Volkmann N., Hanein D., Rouiller I., Reed J.C.;
"Reconstituted NALP1 inflammasome reveals two-step mechanism of
caspase-1 activation.";
Mol. Cell 25:713-724(2007).
[29]
FUNCTION IN APOPTOSIS.
PubMed=16964285; DOI=10.1038/sj.onc.1209965;
Hasegawa M., Kawase K., Inohara N., Imamura R., Yeh W.C.,
Kinoshita T., Suda T.;
"Mechanism of ASC-mediated apoptosis: bid-dependent apoptosis in type
II cells.";
Oncogene 26:1748-1756(2007).
[30]
INTERACTION WITH PYDC1 AND PYDC2, AND DOMAIN.
PubMed=17178784; DOI=10.1128/IAI.01315-06;
Dorfleutner A., Bryan N.B., Talbott S.J., Funya K.N., Rellick S.L.,
Reed J.C., Shi X., Rojanasakul Y., Flynn D.C., Stehlik C.;
"Cellular pyrin domain-only protein 2 is a candidate regulator of
inflammasome activation.";
Infect. Immun. 75:1484-1492(2007).
[31]
INTERACTION WITH PYDC2.
PubMed=17339483; DOI=10.4049/jimmunol.178.6.3837;
Bedoya F., Sandler L.L., Harton J.A.;
"Pyrin-only protein 2 modulates NF-kappaB and disrupts ASC:CLR
interactions.";
J. Immunol. 178:3837-3845(2007).
[32]
INTERACTION WITH PYDC1, AND MUTAGENESIS OF GLU-13; TYR-36 AND ASP-48.
PubMed=18362139; DOI=10.1074/jbc.M801589200;
Srimathi T., Robbins S.L., Dubas R.L., Chang H., Cheng H., Roder H.,
Park Y.C.;
"Mapping of POP1-binding site on pyrin domain of ASC.";
J. Biol. Chem. 283:15390-15398(2008).
[33]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19234215; DOI=10.4049/jimmunol.0802367;
Bryan N.B., Dorfleutner A., Rojanasakul Y., Stehlik C.;
"Activation of inflammasomes requires intracellular redistribution of
the apoptotic speck-like protein containing a caspase recruitment
domain.";
J. Immunol. 182:3173-3182(2009).
[34]
FUNCTION.
PubMed=19494289; DOI=10.4049/jimmunol.0800448;
Hasegawa M., Imamura R., Motani K., Nishiuchi T., Matsumoto N.,
Kinoshita T., Suda T.;
"Mechanism and repertoire of ASC-mediated gene expression.";
J. Immunol. 182:7655-7662(2009).
[35]
FUNCTION IN AIM2 INFLAMMASOME, INTERACTION WITH AIM2, AND DOMAIN.
PubMed=19158676; DOI=10.1038/nature07710;
Fernandes-Alnemri T., Yu J.W., Datta P., Wu J., Alnemri E.S.;
"AIM2 activates the inflammasome and cell death in response to
cytoplasmic DNA.";
Nature 458:509-513(2009).
[36]
FUNCTION IN AIM2 INFLAMMASOME, INTERACTION WITH AIM2, AND DOMAIN.
PubMed=19158675; DOI=10.1038/nature07725;
Hornung V., Ablasser A., Charrel-Dennis M., Bauernfeind F.,
Horvath G., Caffrey D.R., Latz E., Fitzgerald K.A.;
"AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating
inflammasome with ASC.";
Nature 458:514-518(2009).
[37]
FUNCTION (ISOFORMS 2 AND 3).
PubMed=20482797; DOI=10.1186/1476-9255-7-23;
Bryan N.B., Dorfleutner A., Kramer S.J., Yun C., Rojanasakul Y.,
Stehlik C.;
"Differential splicing of the apoptosis-associated speck like protein
containing a caspase recruitment domain (ASC) regulates
inflammasomes.";
J. Inflamm. (Lond.) 7:23-23(2010).
[38]
INTERACTION WITH DDX58.
PubMed=19915568; DOI=10.1038/ni.1824;
Poeck H., Bscheider M., Gross O., Finger K., Roth S., Rebsamen M.,
Hannesschlager N., Schlee M., Rothenfusser S., Barchet W., Kato H.,
Akira S., Inoue S., Endres S., Peschel C., Hartmann G., Hornung V.,
Ruland J.;
"Recognition of RNA virus by RIG-I results in activation of CARD9 and
inflammasome signaling for interleukin 1 beta production.";
Nat. Immunol. 11:63-69(2010).
[39]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[40]
INTERACTION WITH IFI16.
PubMed=21575908; DOI=10.1016/j.chom.2011.04.008;
Kerur N., Veettil M.V., Sharma-Walia N., Bottero V., Sadagopan S.,
Otageri P., Chandran B.;
"IFI16 acts as a nuclear pathogen sensor to induce the inflammasome in
response to Kaposi Sarcoma-associated herpesvirus infection.";
Cell Host Microbe 9:363-375(2011).
[41]
FUNCTION.
PubMed=21487011; DOI=10.1074/jbc.M111.221077;
Taxman D.J., Holley-Guthrie E.A., Huang M.T., Moore C.B.,
Bergstralh D.T., Allen I.C., Lei Y., Gris D., Ting J.P.;
"The NLR adaptor ASC/PYCARD regulates DUSP10, mitogen-activated
protein kinase (MAPK), and chemokine induction independent of the
inflammasome.";
J. Biol. Chem. 286:19605-19616(2011).
[42]
FUNCTION.
PubMed=22732093; DOI=10.1016/j.humimm.2012.06.008;
Guo X., Dhodapkar K.M.;
"Central and overlapping role of cathepsin B and inflammasome adaptor
ASC in antigen presenting function of human dendritic cells.";
Hum. Immunol. 73:871-878(2012).
[43]
SUBCELLULAR LOCATION.
PubMed=21124315; DOI=10.1038/nature09663;
Zhou R., Yazdi A.S., Menu P., Tschopp J.;
"A role for mitochondria in NLRP3 inflammasome activation.";
Nature 469:221-225(2011).
[44]
INDUCTION BY ENDOCANNABINOID ANANDAMIDE.
PubMed=23955712; DOI=10.1038/nm.3265;
Jourdan T., Godlewski G., Cinar R., Bertola A., Szanda G., Liu J.,
Tam J., Han T., Mukhopadhyay B., Skarulis M.C., Ju C., Aouadi M.,
Czech M.P., Kunos G.;
"Activation of the Nlrp3 inflammasome in infiltrating macrophages by
endocannabinoids mediates beta cell loss in type 2 diabetes.";
Nat. Med. 19:1132-1140(2013).
[45]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[46]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[47]
FUNCTION.
PubMed=28314590; DOI=10.1016/j.immuni.2017.02.011;
Wang Y., Ning X., Gao P., Wu S., Sha M., Lv M., Zhou X., Gao J.,
Fang R., Meng G., Su X., Jiang Z.;
"Inflammasome activation triggers caspase-1-mediated cleavage of cGAS
to regulate responses to DNA virus infection.";
Immunity 46:393-404(2017).
[48]
STRUCTURE BY NMR OF 1-91, AND DOMAIN.
PubMed=14499617; DOI=10.1016/j.jmb.2003.07.007;
Liepinsh E., Barbals R., Dahl E., Sharipo A., Staub E., Otting G.;
"The death-domain fold of the ASC PYRIN domain, presenting a basis for
PYRIN/PYRIN recognition.";
J. Mol. Biol. 332:1155-1163(2003).
[49]
STRUCTURE BY NMR.
PubMed=19759015; DOI=10.1074/jbc.M109.024273;
de Alba E.;
"Structure and interdomain dynamics of apoptosis-associated speck-like
protein containing a CARD (ASC).";
J. Biol. Chem. 284:32932-32941(2009).
-!- FUNCTION: Functions as key mediator in apoptosis and inflammation.
Promotes caspase-mediated apoptosis involving predominantly
caspase-8 and also caspase-9 in a probable cell type-specific
manner. Involved in activation of the mitochondrial apoptotic
pathway, promotes caspase-8-dependent proteolytic maturation of
BID independently of FADD in certain cell types and also mediates
mitochondrial translocation of BAX and activates BAX-dependent
apoptosis coupled to activation of caspase-9, -2 and -3. Involved
in macrophage pyroptosis, a caspase-1-dependent inflammatory form
of cell death and is the major constituent of the ASC pyroptosome
which forms upon potassium depletion and rapidly recruits and
activates caspase-1. In innate immune response believed to act as
an integral adapter in the assembly of the inflammasome which
activates caspase-1 leading to processing and secretion of
proinflammatory cytokines. The function as activating adapter in
different types of inflammasomes is mediated by the pyrin and CARD
domains and their homotypic interactions. Required for recruitment
of caspase-1 to inflammasomes containing certain pattern
recognition receptors, such as NLRP2, NLRP3, AIM2 and probably
IFI16. In the NLRP1 and NLRC4 inflammasomes seems not be required
but facilitates the processing of procaspase-1. In cooperation
with NOD2 involved in an inflammasome activated by bacterial
muramyl dipeptide leading to caspase-1 activation. May be involved
in DDX58-triggered proinflammatory responses and inflammasome
activation. Isoform 2 may have a regulating effect on the function
as inflammasome adapter. Isoform 3 seems to inhibit inflammasome-
mediated maturation of interleukin-1 beta. In collaboration with
AIM2 which detects cytosolic double-stranded DNA may also be
involved in a caspase-1-independent cell death that involves
caspase-8. In adaptive immunity may be involved in maturation of
dendritic cells to stimulate T-cell immunity and in cytoskeletal
rearrangements coupled to chemotaxis and antigen uptake may be
involved in post-transcriptional regulation of the guanine
nucleotide exchange factor DOCK2; the latter function is proposed
to involve the nuclear form. Also involved in transcriptional
activation of cytokines and chemokines independent of the
inflammasome; this function may involve AP-1, NF-kappa-B, MAPK and
caspase-8 signaling pathways. For regulation of NF-kappa-B
activating and inhibiting functions have been reported. Modulates
NF-kappa-B induction at the level of the IKK complex by inhibiting
kinase activity of CHUK and IKBK. Proposed to compete with RIPK2
for association with CASP1 thereby down-regulating CASP1-mediated
RIPK2-dependent NF-kappa-B activation and activating interleukin-1
beta processing. Modulates host resistance to DNA virus infection,
probably by inducing the cleavage of and inactivating MB21D1 in
presence of cytoplasmic double-stranded DNA (PubMed:28314590).
{ECO:0000269|PubMed:11103777, ECO:0000269|PubMed:12486103,
ECO:0000269|PubMed:12646168, ECO:0000269|PubMed:14499617,
ECO:0000269|PubMed:14730312, ECO:0000269|PubMed:15030775,
ECO:0000269|PubMed:16585594, ECO:0000269|PubMed:16964285,
ECO:0000269|PubMed:16982856, ECO:0000269|PubMed:17349957,
ECO:0000269|PubMed:17599095, ECO:0000269|PubMed:19158675,
ECO:0000269|PubMed:19158676, ECO:0000269|PubMed:19234215,
ECO:0000269|PubMed:19494289, ECO:0000269|PubMed:21487011,
ECO:0000269|PubMed:22732093, ECO:0000269|PubMed:28314590}.
-!- SUBUNIT: Self-associates; enforced oligomerization induces
apoptosis, NF-kappa-B regulation and interleukin-1 beta secretion.
Homooligomers can form disk-like particles of approximately 12 nm
diameter and approximately 1 nm height. Next to isorm 1 also
isoform 2 and isoform 3 may be involved in oligomerization leading
to functional regulation. Component of several inflammasomes
containing one pattern recognition receptor/sensor, such as NLRP1,
NLRP2, NLRP3, AIM2, MEFV or NOD2, and probably NLRC4, NLRP12 or
IFI16. Major component of the ASC pyroptosome, a 1-2 um
supramolecular assembly (one per macrophage cell) which consists
of oligomerized PYCARD dimers and CASP1. Interacts with CASP1
(precursor form); the interaction induces activation of CASP1
leading to the processing of interleukin-1 beta; PYCARD competes
with RIPK2 for binding to CASP1. Interacts with NLRP3; the
interaction requires the homooligomerization of NLRP3. Interacts
with NLRP2, NLRC4, MEFV, CARD16, AIM2, IFI16, NOD2, DDX58, RIPK2,
PYDC1, PYDC2, NLRP10, CASP8, CHUK, IKBKB and BAX.
{ECO:0000269|PubMed:11374873, ECO:0000269|PubMed:11498534,
ECO:0000269|PubMed:11786556, ECO:0000269|PubMed:11967258,
ECO:0000269|PubMed:12191486, ECO:0000269|PubMed:12486103,
ECO:0000269|PubMed:12646168, ECO:0000269|PubMed:12656673,
ECO:0000269|PubMed:14634131, ECO:0000269|PubMed:14730312,
ECO:0000269|PubMed:15020601, ECO:0000269|PubMed:15030775,
ECO:0000269|PubMed:15096476, ECO:0000269|PubMed:15456791,
ECO:0000269|PubMed:16585594, ECO:0000269|PubMed:17178784,
ECO:0000269|PubMed:17339483, ECO:0000269|PubMed:17599095,
ECO:0000269|PubMed:18362139, ECO:0000269|PubMed:19158675,
ECO:0000269|PubMed:19158676, ECO:0000269|PubMed:19915568,
ECO:0000269|PubMed:21575908}.
-!- INTERACTION:
Self; NbExp=8; IntAct=EBI-751215, EBI-751215;
O14862:AIM2; NbExp=13; IntAct=EBI-751215, EBI-6253193;
Q07812:BAX; NbExp=7; IntAct=EBI-751215, EBI-516580;
P29466:CASP1; NbExp=9; IntAct=EBI-751215, EBI-516667;
O00471:EXOC5; NbExp=5; IntAct=EBI-751215, EBI-949824;
O15553:MEFV; NbExp=8; IntAct=EBI-751215, EBI-7644532;
Q7RTR2:NLRC3; NbExp=3; IntAct=EBI-751215, EBI-1042625;
Q9C000:NLRP1; NbExp=5; IntAct=EBI-751215, EBI-1220518;
Q96P20:NLRP3; NbExp=9; IntAct=EBI-751215, EBI-6253230;
Q56P42:PYDC2; NbExp=4; IntAct=EBI-751215, EBI-6374418;
Q13546:RIPK1; NbExp=2; IntAct=EBI-751215, EBI-358507;
P43405:SYK; NbExp=4; IntAct=EBI-751215, EBI-78302;
-!- SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum.
Mitochondrion. Nucleus. Note=Upstream of caspase activation, a
redistribution from the cytoplasm to the aggregates occurs. These
appear as hollow, perinuclear spherical, ball-like structures.
Upon NLRP3 inflammasome activation redistributes to the
perinuclear space localizing to endoplasmic reticulum and
mitochondria. Localized primarily to the nucleus in resting
monocytes/macrophages and rapidly redistributed to the cytoplasm
upon pathogen infection. Localized to large cytoplasmic aggregate
appearing as a speck containing AIM2, PYCARD, CASP8 and bacterial
DNA after infection with Francisella tularensis (By similarity).
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=fASC;
IsoId=Q9ULZ3-1; Sequence=Displayed;
Name=2; Synonyms=Asc-b, vASC;
IsoId=Q9ULZ3-2; Sequence=VSP_004119;
Name=3; Synonyms=Asc-c;
IsoId=Q9ULZ3-3; Sequence=VSP_004118;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed at low levels. Detected in
peripheral blood leukocytes, lung, small intestine, spleen,
thymus, colon and at lower levels in placenta, liver and kidney.
Very low expression in skeletal muscle, heart and brain. Detected
in the leukemia cell lines HL-60 and U-937, but not in Jurkat T-
cell lymphoma and Daudi Burkitt's lymphoma. Detected in the
melanoma cell line WM35, but not in WM793. Not detected in HeLa
cervical carcinoma cells and MOLT-4 lymphocytic leukemia cells.
-!- INDUCTION: In macrophages, up-regulated by endocannabinoid
anandamide/AEA. {ECO:0000269|PubMed:23955712}.
-!- DOMAIN: The CARD domain mediates interaction with CASP1 and NLRC4
(PubMed:14634131 and PubMed:11967258).
{ECO:0000269|PubMed:11786556}.
-!- DOMAIN: The pyrin domain mediates homotypic interactions with
pyrin domains of proteins such as of NLRP3, PYDC1, PYDC2 and AIM2.
{ECO:0000269|PubMed:11786556, ECO:0000269|PubMed:12656673,
ECO:0000269|PubMed:14499617, ECO:0000269|PubMed:17178784,
ECO:0000269|PubMed:19158675, ECO:0000269|PubMed:19158676}.
-!- PTM: Phosphorylated. {ECO:0000269|PubMed:12656673}.
-!- MISCELLANEOUS: In breast tumorigenesis, methylation-mediated
silencing may affect genes and proteins that act as positive
mediators of cell death.
-!- SEQUENCE CAUTION:
Sequence=BAA91012.1; Type=Frameshift; Positions=4; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AB023416; BAA87339.2; -; mRNA.
EMBL; AF184072; AAG01187.1; -; Genomic_DNA.
EMBL; AF184073; AAG01188.1; -; mRNA.
EMBL; AF255794; AAF99665.1; -; mRNA.
EMBL; AF310103; AAG30286.1; -; mRNA.
EMBL; AF384665; AAK63850.1; -; mRNA.
EMBL; AK000211; BAA91012.1; ALT_FRAME; mRNA.
EMBL; BC004470; AAH04470.1; -; mRNA.
EMBL; BC013569; AAH13569.2; -; mRNA.
CCDS; CCDS10708.1; -. [Q9ULZ3-1]
CCDS; CCDS10709.1; -. [Q9ULZ3-2]
RefSeq; NP_037390.2; NM_013258.4. [Q9ULZ3-1]
RefSeq; NP_660183.1; NM_145182.2. [Q9ULZ3-2]
UniGene; Hs.499094; -.
PDB; 1UCP; NMR; -; A=1-91.
PDB; 2KN6; NMR; -; A=1-195.
PDB; 3J63; EM; 3.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=1-91.
PDB; 5H8O; X-ray; 4.21 A; B=115-195.
PDBsum; 1UCP; -.
PDBsum; 2KN6; -.
PDBsum; 3J63; -.
PDBsum; 5H8O; -.
ProteinModelPortal; Q9ULZ3; -.
SMR; Q9ULZ3; -.
BioGrid; 118876; 44.
CORUM; Q9ULZ3; -.
DIP; DIP-27618N; -.
IntAct; Q9ULZ3; 48.
MINT; MINT-206960; -.
STRING; 9606.ENSP00000247470; -.
iPTMnet; Q9ULZ3; -.
PhosphoSitePlus; Q9ULZ3; -.
BioMuta; PYCARD; -.
DMDM; 18203507; -.
EPD; Q9ULZ3; -.
PaxDb; Q9ULZ3; -.
PeptideAtlas; Q9ULZ3; -.
PRIDE; Q9ULZ3; -.
DNASU; 29108; -.
Ensembl; ENST00000247470; ENSP00000247470; ENSG00000103490. [Q9ULZ3-1]
Ensembl; ENST00000350605; ENSP00000340441; ENSG00000103490. [Q9ULZ3-2]
GeneID; 29108; -.
KEGG; hsa:29108; -.
UCSC; uc002ebm.4; human. [Q9ULZ3-1]
CTD; 29108; -.
DisGeNET; 29108; -.
EuPathDB; HostDB:ENSG00000103490.13; -.
GeneCards; PYCARD; -.
H-InvDB; HIX0012985; -.
HGNC; HGNC:16608; PYCARD.
HPA; CAB006853; -.
HPA; CAB015948; -.
HPA; HPA049074; -.
HPA; HPA054496; -.
MIM; 606838; gene.
neXtProt; NX_Q9ULZ3; -.
OpenTargets; ENSG00000103490; -.
PharmGKB; PA134950175; -.
eggNOG; ENOG410J02A; Eukaryota.
eggNOG; ENOG4111XEQ; LUCA.
GeneTree; ENSGT00440000033973; -.
HOGENOM; HOG000034090; -.
HOVERGEN; HBG018739; -.
InParanoid; Q9ULZ3; -.
KO; K12799; -.
OMA; AWNLTCK; -.
OrthoDB; EOG091G0OWO; -.
PhylomeDB; Q9ULZ3; -.
TreeFam; TF337882; -.
Reactome; R-HSA-5660668; CLEC7A/inflammasome pathway.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-844456; The NLRP3 inflammasome.
Reactome; R-HSA-844615; The AIM2 inflammasome.
SIGNOR; Q9ULZ3; -.
EvolutionaryTrace; Q9ULZ3; -.
GeneWiki; PYCARD; -.
GenomeRNAi; 29108; -.
PRO; PR:Q9ULZ3; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000103490; -.
CleanEx; HS_PYCARD; -.
ExpressionAtlas; Q9ULZ3; baseline and differential.
Genevisible; Q9ULZ3; HS.
GO; GO:0097169; C:AIM2 inflammasome complex; IDA:UniProtKB.
GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0008385; C:IkappaB kinase complex; TAS:HGNC.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0072558; C:NLRP1 inflammasome complex; IDA:UniProtKB.
GO; GO:0072559; C:NLRP3 inflammasome complex; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0070700; F:BMP receptor binding; IPI:AgBase.
GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; NAS:UniProtKB.
GO; GO:0097153; F:cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
GO; GO:0019899; F:enzyme binding; IPI:AgBase.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005138; F:interleukin-6 receptor binding; IPI:AgBase.
GO; GO:0017024; F:myosin I binding; IPI:AgBase.
GO; GO:0002020; F:protease binding; IPI:AgBase.
GO; GO:0042803; F:protein homodimerization activity; IDA:HGNC.
GO; GO:0032090; F:Pyrin domain binding; IPI:HGNC.
GO; GO:0005523; F:tropomyosin binding; IPI:AgBase.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; NAS:UniProtKB.
GO; GO:0002218; P:activation of innate immune response; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
GO; GO:0071347; P:cellular response to interleukin-1; IDA:UniProtKB.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:UniProtKB.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:UniProtKB.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IMP:UniProtKB.
GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IMP:UniProtKB.
GO; GO:0044351; P:macropinocytosis; ISS:UniProtKB.
GO; GO:0001773; P:myeloid dendritic cell activation; IMP:UniProtKB.
GO; GO:0002277; P:myeloid dendritic cell activation involved in immune response; ISS:UniProtKB.
GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
GO; GO:0032688; P:negative regulation of interferon-beta production; IMP:UniProtKB.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0030838; P:positive regulation of actin filament polymerization; ISS:UniProtKB.
GO; GO:0042104; P:positive regulation of activated T cell proliferation; ISS:UniProtKB.
GO; GO:0002821; P:positive regulation of adaptive immune response; IMP:UniProtKB.
GO; GO:0002588; P:positive regulation of antigen processing and presentation of peptide antigen via MHC class II; ISS:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0090197; P:positive regulation of chemokine secretion; IMP:UniProtKB.
GO; GO:2001056; P:positive regulation of cysteine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:HGNC.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IDA:UniProtKB.
GO; GO:0032729; P:positive regulation of interferon-gamma production; ISS:UniProtKB.
GO; GO:0050718; P:positive regulation of interleukin-1 beta secretion; IDA:HGNC.
GO; GO:2001181; P:positive regulation of interleukin-10 secretion; IMP:UniProtKB.
GO; GO:0032755; P:positive regulation of interleukin-6 production; ISS:UniProtKB.
GO; GO:2000778; P:positive regulation of interleukin-6 secretion; IMP:UniProtKB.
GO; GO:2000484; P:positive regulation of interleukin-8 secretion; IMP:UniProtKB.
GO; GO:0046330; P:positive regulation of JNK cascade; IMP:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:0050766; P:positive regulation of phagocytosis; ISS:UniProtKB.
GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IDA:UniProtKB.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IDA:UniProtKB.
GO; GO:0050870; P:positive regulation of T cell activation; IMP:UniProtKB.
GO; GO:2000406; P:positive regulation of T cell migration; ISS:UniProtKB.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:UniProtKB.
GO; GO:2001242; P:regulation of intrinsic apoptotic signaling pathway; IDA:UniProtKB.
GO; GO:0031647; P:regulation of protein stability; ISS:UniProtKB.
GO; GO:0010803; P:regulation of tumor necrosis factor-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IDA:HGNC.
CDD; cd08330; CARD_ASC_NALP1; 1.
InterPro; IPR001315; CARD.
InterPro; IPR033516; CARD8/ASC/NALP1_CARD.
InterPro; IPR004020; DAPIN.
InterPro; IPR011029; DEATH-like_dom_sf.
Pfam; PF00619; CARD; 1.
Pfam; PF02758; PYRIN; 1.
SMART; SM01289; PYRIN; 1.
SUPFAM; SSF47986; SSF47986; 2.
PROSITE; PS50209; CARD; 1.
PROSITE; PS50824; DAPIN; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Apoptosis; Complete proteome;
Cytoplasm; Endoplasmic reticulum; Immunity; Inflammatory response;
Innate immunity; Mitochondrion; Nucleus; Phosphoprotein;
Reference proteome; Tumor suppressor.
CHAIN 1 195 Apoptosis-associated speck-like protein
containing a CARD.
/FTId=PRO_0000064692.
DOMAIN 1 91 Pyrin. {ECO:0000255|PROSITE-
ProRule:PRU00061}.
DOMAIN 107 195 CARD. {ECO:0000255|PROSITE-
ProRule:PRU00046}.
MOD_RES 195 195 Phosphoserine.
{ECO:0000250|UniProtKB:Q9EPB4}.
VAR_SEQ 26 85 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_004118.
VAR_SEQ 93 111 Missing (in isoform 2).
{ECO:0000303|PubMed:11103776}.
/FTId=VSP_004119.
MUTAGEN 8 8 I->A: Abolishes homooligomerization.
{ECO:0000269|PubMed:15641782}.
MUTAGEN 12 12 L->A: Abolishes homooligomerization.
{ECO:0000269|PubMed:12646168,
ECO:0000269|PubMed:15641782}.
MUTAGEN 12 12 L->Q: Abolishes promotion of apoptosis
and NF-kappa-B activation.
{ECO:0000269|PubMed:12646168,
ECO:0000269|PubMed:15641782}.
MUTAGEN 13 13 E->A: Abolishes interaction with PYDC1.
{ECO:0000269|PubMed:15456791,
ECO:0000269|PubMed:15641782,
ECO:0000269|PubMed:18362139}.
MUTAGEN 13 13 E->W: Abolishes interaction with NLRP2.
{ECO:0000269|PubMed:15456791,
ECO:0000269|PubMed:15641782,
ECO:0000269|PubMed:18362139}.
MUTAGEN 15 15 L->A: Abolishes homooligomerization.
{ECO:0000269|PubMed:15641782}.
MUTAGEN 19 19 E->A: Abolishes homooligomerization.
{ECO:0000269|PubMed:15641782}.
MUTAGEN 20 20 L->A: Abolishes homooligomerization.
{ECO:0000269|PubMed:15641782}.
MUTAGEN 21 21 K->A,E,Q: Abolishes homooligomerization.
{ECO:0000269|PubMed:15641782}.
MUTAGEN 23 23 F->A: Abolishes homooligomerization.
{ECO:0000269|PubMed:15641782}.
MUTAGEN 25 25 L->A,E,G,K,N,Q: Abolishes
homooligomerization.
{ECO:0000269|PubMed:15641782}.
MUTAGEN 26 26 K->A,Q: Abolishes homooligomerization.
{ECO:0000269|PubMed:15641782}.
MUTAGEN 27 27 L->A: Abolishes homooligomerization.
{ECO:0000269|PubMed:15641782}.
MUTAGEN 36 36 Y->A: Abolishes interaction with PYDC1.
{ECO:0000269|PubMed:18362139}.
MUTAGEN 40 40 P->A: Abolishes homooligomerization.
{ECO:0000269|PubMed:15641782}.
MUTAGEN 41 41 R->A,Q,W: Abolishes homooligomerization.
{ECO:0000269|PubMed:15641782}.
MUTAGEN 45 45 L->A: Abolishes homooligomerization.
{ECO:0000269|PubMed:15641782}.
MUTAGEN 47 47 M->A,N,Q: Abolishes homooligomerization.
{ECO:0000269|PubMed:15641782}.
MUTAGEN 48 48 D->A,K: Abolishes homooligomerization.
{ECO:0000269|PubMed:15641782,
ECO:0000269|PubMed:18362139}.
MUTAGEN 48 48 D->A: Abolishes interaction with PYDC1.
{ECO:0000269|PubMed:15641782,
ECO:0000269|PubMed:18362139}.
MUTAGEN 52 52 L->A: Abolishes homooligomerization.
{ECO:0000269|PubMed:15641782}.
MUTAGEN 56 56 L->A: Abolishes homooligomerization.
{ECO:0000269|PubMed:15641782}.
MUTAGEN 62 62 E->A: Abolishes homooligomerization.
{ECO:0000269|PubMed:15641782}.
MUTAGEN 67 67 E->A: Abolishes homooligomerization.
{ECO:0000269|PubMed:15641782}.
MUTAGEN 68 68 L->A: Abolishes homooligomerization.
{ECO:0000269|PubMed:15641782}.
MUTAGEN 72 72 V->A: Abolishes homooligomerization.
{ECO:0000269|PubMed:15641782}.
MUTAGEN 76 76 M->A: Abolishes homooligomerization.
{ECO:0000269|PubMed:15641782}.
HELIX 3 14 {ECO:0000244|PDB:1UCP}.
HELIX 17 26 {ECO:0000244|PDB:1UCP}.
TURN 27 29 {ECO:0000244|PDB:1UCP}.
STRAND 34 36 {ECO:0000244|PDB:1UCP}.
HELIX 41 46 {ECO:0000244|PDB:1UCP}.
HELIX 49 58 {ECO:0000244|PDB:1UCP}.
HELIX 62 75 {ECO:0000244|PDB:1UCP}.
HELIX 80 90 {ECO:0000244|PDB:1UCP}.
HELIX 117 126 {ECO:0000244|PDB:2KN6}.
HELIX 129 135 {ECO:0000244|PDB:2KN6}.
TURN 136 140 {ECO:0000244|PDB:2KN6}.
HELIX 143 150 {ECO:0000244|PDB:2KN6}.
HELIX 155 164 {ECO:0000244|PDB:2KN6}.
HELIX 166 168 {ECO:0000244|PDB:2KN6}.
HELIX 171 184 {ECO:0000244|PDB:2KN6}.
HELIX 186 193 {ECO:0000244|PDB:2KN6}.
SEQUENCE 195 AA; 21627 MW; 455987286586F46A CRC64;
MGRARDAILD ALENLTAEEL KKFKLKLLSV PLREGYGRIP RGALLSMDAL DLTDKLVSFY
LETYGAELTA NVLRDMGLQE MAGQLQAATH QGSGAAPAGI QAPPQSAAKP GLHFIDQHRA
ALIARVTNVE WLLDALYGKV LTDEQYQAVR AEPTNPSKMR KLFSFTPAWN WTCKDLLLQA
LRESQSYLVE DLERS


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18-661-15141 Caspase recruitment domain-containing protein 12 - Ice protease-activating factor; Ipaf; CARD. LRR. and NACHT-containing protein; Clan protein Polyclonal 0.1 mg
18-001-30061 Caspase recruitment domain-containing protein 12 - Ice protease-activating factor; Ipaf; CARD. LRR. and NACHT-containing protein; Clan protein Polyclonal 0.1 mg
18-003-42864 Caspase recruitment domain-containing protein 12 - Ice protease-activating factor; Ipaf; CARD. LRR. and NACHT-containing protein; Clan protein Polyclonal 0.05 mg Aff Pur
10-288-21980F Caspase recruitment domain-containing protein 14 - CARD-containing MAGUK protein 2; Carma 2 0.1 mg
10-288-21980F Caspase recruitment domain-containing protein 14 - CARD-containing MAGUK protein 2; Carma 2 0.05 mg
15-288-21980A Caspase recruitment domain-containing protein 14 - CARD-containing MAGUK protein 2; Carma 2 Polyclonal 0.05 mg
15-288-21980B Caspase recruitment domain-containing protein 14 - CARD-containing MAGUK protein 2; Carma 2 Polyclonal 0.1 mg
15-288-21980B Caspase recruitment domain-containing protein 14 - CARD-containing MAGUK protein 2; Carma 2 Polyclonal 0.05 mg
15-288-21980A Caspase recruitment domain-containing protein 14 - CARD-containing MAGUK protein 2; Carma 2 Polyclonal 0.1 mg
18-661-15160 Caspase recruitment domain-containing protein 11 - CARD-containing MAGUK protein 3; Carma 1 Polyclonal 0.1 mg
20-272-191255 NALP1 - Mouse monoclonal [Nalpy1 - 4] to NALP1; Death effector filament-forming ced-4-like apoptosis protein; Nucleotide-binding domain and caspase recruitment domain; Caspase recruitment domain prote 0.05 mg
EIAAB05316 CARD11,CARD-containing MAGUK protein 1,Carma 1,CARMA1,Caspase recruitment domain-containing protein 11,Homo sapiens,Human
EIAAB05313 CARD10,CARD-containing MAGUK protein 3,Carma 3,CARMA3,Caspase recruitment domain-containing protein 10,Homo sapiens,Human
EIAAB05318 CARD14,CARD-containing MAGUK protein 2,Carma 2,CARMA2,Caspase recruitment domain-containing protein 14,Homo sapiens,Human
32-115 B-cell CLL_lymphoma 10, also known as CLAP, Me10, CIPER, c-E10, CARMEN. Entrez Protein NP_003912. It is a protein containing a caspase recruitment domain (CARD). It plays an important role in apoptosi 0.1 mg
E1535h ELISA kit CARD, LRR, and NACHT-containing protein,CARD12,Caspase recruitment domain-containing protein 12,CLAN,Clan protein,CLAN1,Homo sapiens,Human,Ice protease-activating factor,Ipaf,IPAF,NLR famil 96T
E1535h ELISA CARD, LRR, and NACHT-containing protein,CARD12,Caspase recruitment domain-containing protein 12,CLAN,Clan protein,CLAN1,Homo sapiens,Human,Ice protease-activating factor,Ipaf,IPAF,NLR family CAR 96T
EIAAB05323 Apoptotic protein NDPP1,CARD8,CARDINAL,CARD-inhibitor of NF-kappa-B-activating ligand,Caspase recruitment domain-containing protein 8,DACAR,Homo sapiens,Human,KIAA0955,NDPP1,TUCAN,Tumor up-regulated C
EIAAB05320 CARD17,Caspase recruitment domain-containing protein 17,Caspase-1 inhibitor INCA,Homo sapiens,Human,INCA,Inhibitory caspase recruitment domain protein
CSB-EL019114MO Mouse Apoptosis-associated speck-like protein containing a CARD(PYCARD) ELISA kit 96T


 

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