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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.
03-JUL-2019, entry version 188.
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]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION UPON HRSV (MICROBIAL
INFECTION).
PubMed=23229815; DOI=10.1136/thoraxjnl-2012-202182;
Triantafilou K., Kar S., Vakakis E., Kotecha S., Triantafilou M.;
"Human respiratory syncytial virus viroporin SH: a viral recognition
pathway used by the host to signal inflammasome activation.";
Thorax 68:66-75(2013).
[46]
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).
[47]
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).
[48]
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).
[49]
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).
[50]
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 CGAS 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 isoform 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}.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane. Note=(Microbial
infection) Upon HRSV infection, the protein is mainly located in
lipid rafts in the Golgi membrane. {ECO:0000269|PubMed:23229815}.
-!- 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. Expressed
in lung epithelial cells (at protein level) (PubMed:23229815).
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. {ECO:0000269|PubMed:23229815}.
-!- 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]
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.
PDB; 6N1H; EM; 3.17 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=112-194.
PDBsum; 1UCP; -.
PDBsum; 2KN6; -.
PDBsum; 3J63; -.
PDBsum; 5H8O; -.
PDBsum; 6N1H; -.
SMR; Q9ULZ3; -.
BioGrid; 118876; 45.
CORUM; Q9ULZ3; -.
DIP; DIP-27618N; -.
IntAct; Q9ULZ3; 48.
MINT; Q9ULZ3; -.
STRING; 9606.ENSP00000247470; -.
iPTMnet; Q9ULZ3; -.
PhosphoSitePlus; Q9ULZ3; -.
BioMuta; PYCARD; -.
DMDM; 18203507; -.
EPD; Q9ULZ3; -.
jPOST; Q9ULZ3; -.
PaxDb; Q9ULZ3; -.
PeptideAtlas; Q9ULZ3; -.
PRIDE; Q9ULZ3; -.
ProteomicsDB; 85158; -.
ProteomicsDB; 85159; -. [Q9ULZ3-2]
ProteomicsDB; 85160; -. [Q9ULZ3-3]
ABCD; 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; -.
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; ENSGT00940000161873; -.
HOGENOM; HOG000034090; -.
InParanoid; Q9ULZ3; -.
KO; K12799; -.
OMA; FSFAPAW; -.
OrthoDB; 1494108at2759; -.
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; -.
ChiTaRS; PYCARD; human.
EvolutionaryTrace; Q9ULZ3; -.
GeneWiki; PYCARD; -.
GenomeRNAi; 29108; -.
PRO; PR:Q9ULZ3; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000103490; Expressed in 188 organ(s), highest expression level in blood.
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:0000139; C:Golgi membrane; IDA:UniProtKB.
GO; GO:0008385; C:IkappaB kinase complex; TAS:HGNC.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
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:0032991; C:protein-containing complex; IDA:ARUK-UCL.
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:0044325; F:ion channel binding; IEA:Ensembl.
GO; GO:0017024; F:myosin I binding; IPI:AgBase.
GO; GO:0002020; F:protease binding; IPI:AgBase.
GO; GO:0046983; F:protein dimerization activity; IDA:UniProtKB.
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:0097202; P:activation of cysteine-type endopeptidase activity; IEA:Ensembl.
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; IBA:GO_Central.
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:0032611; P:interleukin-1 beta production; IEA:Ensembl.
GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IMP:UniProtKB.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IBA:GO_Central.
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:1900016; P:negative regulation of cytokine production involved in inflammatory response; IMP: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:0002230; P:positive regulation of defense response to virus by host; IEA:Ensembl.
GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
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:0032731; P:positive regulation of interleukin-1 beta production; IMP:ARUK-UCL.
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: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:0051260; P:protein homooligomerization; IDA:UniProtKB.
GO; GO:0010506; P:regulation of autophagy; IEA:Ensembl.
GO; GO:0043087; P:regulation of GTPase activity; IEA:Ensembl.
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.
InterPro; IPR002398; Pept_C14.
PANTHER; PTHR10454; PTHR10454; 1.
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; Golgi apparatus; Immunity;
Inflammatory response; Innate immunity; Membrane; 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 114 117 {ECO:0000244|PDB:6N1H}.
HELIX 119 125 {ECO:0000244|PDB:6N1H}.
HELIX 129 136 {ECO:0000244|PDB:6N1H}.
TURN 138 140 {ECO:0000244|PDB:6N1H}.
HELIX 143 149 {ECO:0000244|PDB:6N1H}.
STRAND 152 154 {ECO:0000244|PDB:6N1H}.
HELIX 155 162 {ECO:0000244|PDB:6N1H}.
HELIX 166 168 {ECO:0000244|PDB:6N1H}.
HELIX 171 184 {ECO:0000244|PDB:6N1H}.
HELIX 188 193 {ECO:0000244|PDB:6N1H}.
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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WP1939: Unfolded Protein Response
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WP2032: TSH signaling pathway
WP1694: Pyrimidine metabolism
WP2371: Parkinsons Disease Pathway
WP1714: Tyrosine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP211: BMP signaling pathway
WP1165: G Protein Signaling Pathways
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Related Genes :
[PYCARD ASC CARD5 TMS1] 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)
[NLRP1 CARD7 DEFCAP KIAA0926 NAC NALP1] NACHT, LRR and PYD domains-containing protein 1 (Caspase recruitment domain-containing protein 7) (Death effector filament-forming ced-4-like apoptosis protein) (Nucleotide-binding domain and caspase recruitment domain)
[Pycard Asc] Apoptosis-associated speck-like protein containing a CARD (mASC) (PYD and CARD domain-containing protein)
[CARD16 COP COP1] Caspase recruitment domain-containing protein 16 (Caspase recruitment domain-only protein 1) (CARD-only protein 1) (Caspase-1 inhibitor COP) (Pseudo interleukin-1 beta converting enzyme) (Pseudo-ICE) (Pseudo-IL1B-converting enzyme)
[PYCARD ASC] Apoptosis-associated speck-like protein containing a CARD (PYD and CARD domain-containing protein)
[CARD14 CARMA2] Caspase recruitment domain-containing protein 14 (CARD-containing MAGUK protein 2) (Carma 2)
[NLRC4 CARD12 CLAN CLAN1 IPAF UNQ6189/PRO20215] NLR family CARD domain-containing protein 4 (CARD, LRR, and NACHT-containing protein) (Clan protein) (Caspase recruitment domain-containing protein 12) (Ice protease-activating factor) (Ipaf)
[Nlrc4 Card12 Ipaf] NLR family CARD domain-containing protein 4 (Caspase recruitment domain-containing protein 12) (Ice protease-activating factor) (Ipaf)
[CARD11 CARMA1] Caspase recruitment domain-containing protein 11 (CARD-containing MAGUK protein 1) (Carma 1)
[CARD9] Caspase recruitment domain-containing protein 9 (hCARD9)
[IFIH1 MDA5 RH116] Interferon-induced helicase C domain-containing protein 1 (EC 3.6.4.13) (Clinically amyopathic dermatomyositis autoantigen 140 kDa) (CADM-140 autoantigen) (Helicase with 2 CARD domains) (Helicard) (Interferon-induced with helicase C domain protein 1) (Melanoma differentiation-associated protein 5) (MDA-5) (Murabutide down-regulated protein) (RIG-I-like receptor 2) (RLR-2) (RNA helicase-DEAD box protein 116)
[NOD2 CARD15 IBD1] Nucleotide-binding oligomerization domain-containing protein 2 (Caspase recruitment domain-containing protein 15) (Inflammatory bowel disease protein 1)
[Card11] Caspase recruitment domain-containing protein 11
[Ifih1] Interferon-induced helicase C domain-containing protein 1 (EC 3.6.4.13) (Helicase with 2 CARD domains) (Helicard) (Interferon induced with helicase C domain protein 1) (Melanoma differentiation-associated protein 5) (MDA-5) (RIG-I-like receptor 2) (RLR-2)
[CARD10 CARMA3] Caspase recruitment domain-containing protein 10 (CARD-containing MAGUK protein 3) (Carma 3)
[MAVS IPS1 KIAA1271 VISA] Mitochondrial antiviral-signaling protein (MAVS) (CARD adapter inducing interferon beta) (Cardif) (Interferon beta promoter stimulator protein 1) (IPS-1) (Putative NF-kappa-B-activating protein 031N) (Virus-induced-signaling adapter) (VISA)
[NOL3 ARC NOP] Nucleolar protein 3 (Apoptosis repressor with CARD) (Muscle-enriched cytoplasmic protein) (Myp) (Nucleolar protein of 30 kDa) (Nop30)
[Nol3 Arc] Nucleolar protein 3 (Apoptosis repressor with CARD)
[BCL10 CIPER CLAP] B-cell lymphoma/leukemia 10 (B-cell CLL/lymphoma 10) (Bcl-10) (CARD-containing molecule enhancing NF-kappa-B) (CARD-like apoptotic protein) (hCLAP) (CED-3/ICH-1 prodomain homologous E10-like regulator) (CIPER) (Cellular homolog of vCARMEN) (cCARMEN) (Cellular-E10) (c-E10) (Mammalian CARD-containing adapter molecule E10) (mE10)
[NLRP3 C1orf7 CIAS1 NALP3 PYPAF1] NACHT, LRR and PYD domains-containing protein 3 (Angiotensin/vasopressin receptor AII/AVP-like) (Caterpiller protein 1.1) (CLR1.1) (Cold-induced autoinflammatory syndrome 1 protein) (Cryopyrin) (PYRIN-containing APAF1-like protein 1)
[RIPK2 CARDIAK RICK RIP2 UNQ277/PRO314/PRO34092] Receptor-interacting serine/threonine-protein kinase 2 (EC 2.7.11.1) (CARD-containing interleukin-1 beta-converting enzyme-associated kinase) (CARD-containing IL-1 beta ICE-kinase) (RIP-like-interacting CLARP kinase) (Receptor-interacting protein 2) (RIP-2) (Tyrosine-protein kinase RIPK2) (EC 2.7.10.2)
[Mavs Ips1 Visa] Mitochondrial antiviral-signaling protein (MAVS) (CARD adapter inducing interferon beta) (Cardif) (Interferon beta promoter stimulator protein 1) (IPS-1) (Virus-induced-signaling adapter) (VISA)
[Nlrp1b Nalp1b] NACHT, LRR and PYD domains-containing protein 1b allele 5
[Nlrp1b Nalp1b] NACHT, LRR and PYD domains-containing protein 1b allele 1
[Nlrp1b Nalp1b] NACHT, LRR and PYD domains-containing protein 1b allele 2
[NLRC3 NOD3] NLR family CARD domain-containing protein 3 (CARD15-like protein) (Caterpiller protein 16.2) (CLR16.2) (NACHT, LRR and CARD domains-containing protein 3) (Nucleotide-binding oligomerization domain protein 3)
[CFLAR CASH CASP8AP1 CLARP MRIT] CASP8 and FADD-like apoptosis regulator (Caspase homolog) (CASH) (Caspase-eight-related protein) (Casper) (Caspase-like apoptosis regulatory protein) (CLARP) (Cellular FLICE-like inhibitory protein) (c-FLIP) (FADD-like antiapoptotic molecule 1) (FLAME-1) (Inhibitor of FLICE) (I-FLICE) (MACH-related inducer of toxicity) (MRIT) (Usurpin) [Cleaved into: CASP8 and FADD-like apoptosis regulator subunit p43; CASP8 and FADD-like apoptosis regulator subunit p12]
[Nlrp6 Nalp6 Navr Pypaf5] NACHT, LRR and PYD domains-containing protein 6 (Angiotensin II/vasopressin receptor) (Non-angiotensin-vasopressin receptor) (Non-AVR) (PYRIN-containing APAF1-like protein 5-like)
[Birc2] Baculoviral IAP repeat-containing protein 2 (EC 2.3.2.27) (Cellular inhibitor of apoptosis 1) (C-IAP1) (Inhibitor of apoptosis protein 2) (mIAP2) (RING-type E3 ubiquitin transferase BIRC2)
[Nlrp3 Cias1 Mmig1 Nalp3 Pypaf1] NACHT, LRR and PYD domains-containing protein 3 (Cold autoinflammatory syndrome 1 protein homolog) (Cryopyrin) (Mast cell maturation-associated-inducible protein 1) (PYRIN-containing APAF1-like protein 1)

Bibliography :