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Nucleotide-binding oligomerization domain-containing protein 2 (Caspase recruitment domain-containing protein 15) (Inflammatory bowel disease protein 1)

 NOD2_HUMAN              Reviewed;        1040 AA.
Q9HC29; E2JEQ6; Q96RH5; Q96RH6; Q96RH8;
31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
31-JUL-2019, entry version 194.
RecName: Full=Nucleotide-binding oligomerization domain-containing protein 2;
AltName: Full=Caspase recruitment domain-containing protein 15;
AltName: Full=Inflammatory bowel disease protein 1;
Name=NOD2; Synonyms=CARD15, IBD1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), MUTAGENESIS OF LYS-305,
AND VARIANT ARG-908.
TISSUE=Mammary gland;
PubMed=11087742; DOI=10.1074/jbc.M008072200;
Ogura Y., Inohara N., Benito A., Chen F.F., Yamaoka S., Nunez G.;
"Nod2, a Nod1/Apaf-1 family member that is restricted to monocytes and
activates NF-kappaB.";
J. Biol. Chem. 276:4812-4818(2001).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2), INVOLVEMENT IN
IBD1, VARIANTS IBD1 THR-140; ARG-157; CYS-235; ARG-248; ASN-291;
SER-294; VAL-301; TRP-311; VAL-348; ARG-352; CYS-373; SER-414;
LEU-431; VAL-432; LYS-441; THR-612; VAL-612; TRP-684; TRP-702;
CYS-703; CYS-713; GLY-725; VAL-755; VAL-758; LYS-778; MET-793;
LYS-843; SER-853; VAL-863; THR-885; ARG-908 AND ASP-924, AND VARIANTS
MET-189; SER-268; SER-289; ASP-918 AND ILE-955.
TISSUE=Leukocyte;
PubMed=11385576; DOI=10.1038/35079107;
Hugot J.-P., Chamaillard M., Zouali H., Lesage S., Cezard J.-P.,
Belaiche J., Almer S., Tysk C., O'Morain C.A., Gassull M., Binder V.,
Finkel Y., Cortot A., Modigliani R., Laurent-Puig P.,
Gower-Rousseau C., Macry J., Colombel J.-F., Sahbatou M., Thomas G.;
"Association of NOD2 leucine-rich repeat variants with susceptibility
to Crohn's disease.";
Nature 411:599-603(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
PubMed=20698950; DOI=10.1186/1756-0500-3-224;
Kramer M., Boeck J., Reichenbach D., Kaether C., Schreiber S.,
Platzer M., Rosenstiel P., Huse K.;
"NOD2-C2 - a novel NOD2 isoform activating NF-kappaB in a muramyl
dipeptide-independent manner.";
BMC Res. Notes 3:224-224(2010).
[4]
INTERACTION WITH ERBBI2P, AND SUBCELLULAR LOCATION.
PubMed=16203728; DOI=10.1074/jbc.M508538200;
McDonald C., Chen F.F., Ollendorff V., Ogura Y., Marchetto S.,
Lecine P., Borg J.P., Nunez G.;
"A role for Erbin in the regulation of Nod2-dependent NF-kappaB
signaling.";
J. Biol. Chem. 280:40301-40309(2005).
[5]
FUNCTION, INTERACTION WITH CASP1; CASP4 AND NLRP1, AUTOINHIBITION, AND
DOMAIN.
PubMed=18511561; DOI=10.1073/pnas.0802726105;
Hsu L.C., Ali S.R., McGillivray S., Tseng P.H., Mariathasan S.,
Humke E.W., Eckmann L., Powell J.J., Nizet V., Dixit V.M., Karin M.;
"A NOD2-NALP1 complex mediates caspase-1-dependent IL-1beta secretion
in response to Bacillus anthracis infection and muramyl dipeptide.";
Proc. Natl. Acad. Sci. U.S.A. 105:7803-7808(2008).
[6]
INTERACTION WITH RIPK2.
PubMed=19592251; DOI=10.1016/j.cub.2009.06.038;
Tao M., Scacheri P.C., Marinis J.M., Harhaj E.W., Matesic L.E.,
Abbott D.W.;
"ITCH K63-ubiquitinates the NOD2 binding protein, RIP2, to influence
inflammatory signaling pathways.";
Curr. Biol. 19:1255-1263(2009).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MAVS.
PubMed=19701189; DOI=10.1038/ni.1782;
Sabbah A., Chang T.H., Harnack R., Frohlich V., Tominaga K.,
Dube P.H., Xiang Y., Bose S.;
"Activation of innate immune antiviral responses by Nod2.";
Nat. Immunol. 10:1073-1080(2009).
[8]
FUNCTION, AND INTERACTION WITH ATG16L1.
PubMed=20637199; DOI=10.1053/j.gastro.2010.07.006;
Homer C.R., Richmond A.L., Rebert N.A., Achkar J.P., McDonald C.;
"ATG16L1 and NOD2 interact in an autophagy-dependent antibacterial
pathway implicated in Crohn's disease pathogenesis.";
Gastroenterology 139:1630-1641(2010).
[9]
IDENTIFICATION IN A COMPLEX WITH ARHGEF2 AND RIPK2, AND INTERACTION
WITH RIPK2.
PubMed=21887730; DOI=10.1002/ibd.21851;
Zhao Y., Alonso C., Ballester I., Song J.H., Chang S.Y., Guleng B.,
Arihiro S., Murray P.J., Xavier R., Kobayashi K.S., Reinecker H.C.;
"Control of NOD2 and Rip2-dependent innate immune activation by GEF-
H1.";
Inflamm. Bowel Dis. 18:603-612(2012).
[10]
TISSUE SPECIFICITY, AND INTERACTION WITH MAPKBP1.
PubMed=22700971; DOI=10.1074/jbc.M112.355545;
Lecat A., Di Valentin E., Somja J., Jourdan S., Fillet M., Kufer T.A.,
Habraken Y., Sadzot C., Louis E., Delvenne P., Piette J.,
Legrand-Poels S.;
"The c-Jun N-terminal kinase (JNK)-binding protein (JNKBP1) acts as a
negative regulator of NOD2 protein signaling by inhibiting its
oligomerization process.";
J. Biol. Chem. 287:29213-29226(2012).
[11]
INTERACTION WITH HSP90 AND SOCS3, AND POLYUBIQUITINATION.
PubMed=23019338; DOI=10.1074/jbc.M112.410027;
Lee K.H., Biswas A., Liu Y.J., Kobayashi K.S.;
"Proteasomal degradation of Nod2 protein mediates tolerance to
bacterial cell wall components.";
J. Biol. Chem. 287:39800-39811(2012).
[12]
INTERACTION WITH ATG16L1.
PubMed=23376921; DOI=10.1038/emboj.2013.8;
Boada-Romero E., Letek M., Fleischer A., Pallauf K., Ramon-Barros C.,
Pimentel-Muinos F.X.;
"TMEM59 defines a novel ATG16L1-binding motif that promotes local
activation of LC3.";
EMBO J. 32:566-582(2013).
[13]
INTERACTION WITH ANKRD17.
PubMed=23711367; DOI=10.1016/j.febslet.2013.05.037;
Menning M., Kufer T.A.;
"A role for the Ankyrin repeat containing protein Ankrd17 in Nod1- and
Nod2-mediated inflammatory responses.";
FEBS Lett. 587:2137-2142(2013).
[14]
FUNCTION.
PubMed=23806334; DOI=10.1016/j.molcel.2013.06.004;
Fiil B.K., Damgaard R.B., Wagner S.A., Keusekotten K., Fritsch M.,
Bekker-Jensen S., Mailand N., Choudhary C., Komander D.,
Gyrd-Hansen M.;
"OTULIN restricts Met1-linked ubiquitination to control innate immune
signaling.";
Mol. Cell 50:818-830(2013).
[15]
INTERACTION WITH CARD9, VARIANTS IBD1 ALA-357; PHE-363 AND VAL-550,
VARIANT ALA-463, CHARACTERIZATION OF VARIANTS IBD1 ARG-248; ALA-357;
PHE-363; LEU-431; LYS-441; VAL-550; VAL-612 AND TRP-702,
CHARACTERIZATION OF VARIANT BLAUS TRP-334, CHARACTERIZATION OF VARIANT
ALA-463, AND MUTAGENESIS OF ASP-379.
PubMed=24960071; DOI=10.1016/j.febslet.2014.06.035;
Parkhouse R., Boyle J.P., Mayle S., Sawmynaden K., Rittinger K.,
Monie T.P.;
"Interaction between NOD2 and CARD9 involves the NOD2 NACHT and the
linker region between the NOD2 CARDs and NACHT domain.";
FEBS Lett. 588:2830-2836(2014).
[16]
SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS BLAUS GLN-334;
TRP-334; GLY-383; LYS-383; PHE-469; ASP-481; LEU-490; TYR-495;
LEU-496; THR-513; CYS-587; ASN-605; PRO-605 AND LYS-670, AND
CHARACTERIZATION OF VARIANTS AND CYS-471.
PubMed=25093298; DOI=10.1016/j.febslet.2014.07.029;
Parkhouse R., Boyle J.P., Monie T.P.;
"Blau syndrome polymorphisms in NOD2 identify nucleotide hydrolysis
and helical domain 1 as signalling regulators.";
FEBS Lett. 588:3382-3389(2014).
[17]
INTERACTION WITH HSPA1A, SUBCELLULAR LOCATION, AND CHARACTERIZATION OF
VARIANTS IBD1 TRP-702 AND ARG-908.
PubMed=24790089; DOI=10.1074/jbc.M114.557686;
Mohanan V., Grimes C.L.;
"The molecular chaperone HSP70 binds to and stabilizes NOD2, an
important protein involved in Crohn disease.";
J. Biol. Chem. 289:18987-18998(2014).
[18]
INTERACTION WITH ANKHD1; C10ORF67; CHMP5; DOCK7; ENTR1; KRT15; LDOC1;
PPP1R12C; PPP2R3B; RIPK2; TRIM41 AND VIM, INDUCTION, CHARACTERIZATION
OF VARIANTS IBD1 TRP-702 AND ARG-908, AND CHARACTERIZATION OF VARIANT
BLAUS GLN-334.
PubMed=27812135; DOI=10.1371/journal.pone.0165420;
Thiebaut R., Esmiol S., Lecine P., Mahfouz B., Hermant A.,
Nicoletti C., Parnis S., Perroy J., Borg J.P., Pascoe L., Hugot J.P.,
Ollendorff V.;
"Characterization and Genetic Analyses of New Genes Coding for NOD2
Interacting Proteins.";
PLoS ONE 11:E0165420-E0165420(2016).
[19]
FUNCTION, AND INTERACTION WITH INAVA.
PubMed=28436939; DOI=10.1172/JCI86282;
Yan J., Hedl M., Abraham C.;
"An inflammatory bowel disease-risk variant in INAVA decreases pattern
recognition receptor-induced outcomes.";
J. Clin. Invest. 127:2192-2205(2017).
[20]
INTERACTION WITH NLRP12.
PubMed=30559449; DOI=10.1038/s41467-018-07750-5;
Normand S., Waldschmitt N., Neerincx A., Martinez-Torres R.J.,
Chauvin C., Couturier-Maillard A., Boulard O., Cobret L., Awad F.,
Huot L., Ribeiro-Ribeiro A., Lautz K., Ruez R., Delacre M., Bondu C.,
Guilliams M., Scott C., Segal A., Amselem S., Hot D., Karabina S.,
Bohn E., Ryffel B., Poulin L.F., Kufer T.A., Chamaillard M.;
"Proteasomal degradation of NOD2 by NLRP12 in monocytes promotes
bacterial tolerance and colonization by enteropathogens.";
Nat. Commun. 9:5338-5338(2018).
[21]
VARIANTS BLAUS GLN-334; TRP-334 AND PHE-469.
PubMed=11528384; DOI=10.1038/ng720;
Miceli-Richard C., Lesage S., Rybojad M., Prieur A.M.,
Manouvrier-Hanu S., Hafner R., Chamaillard M., Zouali H., Thomas G.,
Hugot J.-P.;
"CARD15 mutations in Blau syndrome.";
Nat. Genet. 29:19-20(2001).
[22]
VARIANTS IBD1 ASN-113; ALA-357; PHE-363; VAL-550 AND SER-852.
PubMed=15024686; DOI=10.1086/382226;
Tukel T., Shalata A., Present D., Rachmilewitz D., Mayer L., Grant D.,
Risch N., Desnick R.J.;
"Crohn disease: frequency and nature of CARD15 mutations in Ashkenazi
and Sephardi/Oriental Jewish families.";
Am. J. Hum. Genet. 74:623-636(2004).
[23]
VARIANTS BLAUS TRP-334; GLU-382; LEU-496; THR-513; PRO-605; THR-612
AND LYS-670, AND CHARACTERIZATION OF VARIANTS BLAUS GLU-382; LEU-496;
THR-513; PRO-605 AND LYS-670.
PubMed=15459013; DOI=10.1182/blood-2004-07-2972;
Kanazawa N., Okafuji I., Kambe N., Nishikomori R., Nakata-Hizume M.,
Nagai S., Fuji A., Yuasa T., Manki A., Sakurai Y., Nakajima M.,
Kobayashi H., Fujiwara I., Tsutsumi H., Utani A., Nishigori C.,
Heike T., Nakahata T., Miyachi Y.;
"Early-onset sarcoidosis and CARD15 mutations with constitutive
nuclear factor-kappaB activation: common genetic etiology with Blau
syndrome.";
Blood 105:1195-1197(2005).
[24]
VARIANT BLAUS LYS-383.
PubMed=15812565; DOI=10.1038/sj.ejhg.5201404;
van Duist M.M., Albrecht M., Podswiadek M., Giachino D., Lengauer T.,
Punzi L., De Marchi M.;
"A new CARD15 mutation in Blau syndrome.";
Eur. J. Hum. Genet. 13:742-747(2005).
[25]
VARIANTS IBD1 TRP-311; TRP-702; CYS-703; HIS-713; VAL-755; CYS-760;
TRP-790 AND ARG-908, AND VARIANTS SER-268; SER-289; CYS-391; ALA-463;
TRP-791; LYS-825 AND VAL-849.
PubMed=16485124; DOI=10.1007/s00251-005-0073-2;
Schnitzler F., Brand S., Staudinger T., Pfennig S., Hofbauer K.,
Seiderer J., Tillack C., Goke B., Ochsenkuhn T., Lohse P.;
"Eight novel CARD15 variants detected by DNA sequence analysis of the
CARD15 gene in 111 patients with inflammatory bowel disease.";
Immunogenetics 58:99-106(2006).
[26]
VARIANTS BLAUS GLN-334; TRP-334; LYS-383; LEU-490; TYR-495 AND
CYS-587.
PubMed=19479837; DOI=10.1002/art.24533;
Rose C.D., Arostegui J.I., Martin T.M., Espada G., Scalzi L.,
Yague J., Rosenbaum J.T., Modesto C., Cristina Arnal M., Merino R.,
Garcia-Consuegra J., Carballo Silva M.A., Wouters C.H.;
"NOD2-associated pediatric granulomatous arthritis, an expanding
phenotype: study of an international registry and a national cohort in
Spain.";
Arthritis Rheum. 60:1797-1803(2009).
[27]
VARIANTS BLAUS GLN-334; TRP-334; GLU-382; GLY-383; TYR-495; LEU-496;
THR-513; PRO-605 AND LYS-670.
PubMed=19116920; DOI=10.1002/art.24134;
Okafuji I., Nishikomori R., Kanazawa N., Kambe N., Fujisawa A.,
Yamazaki S., Saito M., Yoshioka T., Kawai T., Sakai H., Tanizaki H.,
Heike T., Miyachi Y., Nakahata T.;
"Role of the NOD2 genotype in the clinical phenotype of Blau syndrome
and early-onset sarcoidosis.";
Arthritis Rheum. 60:242-250(2009).
[28]
VARIANT BLAUS ASP-481.
PubMed=19359344; DOI=10.1093/rheumatology/kep061;
Okada S., Konishi N., Tsumura M., Shirao K., Yasunaga S., Sakai H.,
Nishikomori R., Takihara Y., Kobayashi M.;
"Cardiac infiltration in early-onset sarcoidosis associated with a
novel heterozygous mutation, G481D, in CARD15.";
Rheumatology 48:706-707(2009).
[29]
VARIANT BLAUS ASN-605.
PubMed=19169908; DOI=10.1080/03009740802464194;
Milman N., Ursin K., Rodevand E., Nielsen F.C., Hansen T.V.;
"A novel mutation in the NOD2 gene associated with Blau syndrome: a
Norwegian family with four affected members.";
Scand. J. Rheumatol. 38:190-197(2009).
[30]
VARIANT BLAUS TRP-334.
PubMed=20199415; DOI=10.1111/j.1525-1470.2009.01060.x;
Stoevesandt J., Morbach H., Martin T.M., Zierhut M., Girschick H.,
Hamm H.;
"Sporadic Blau syndrome with onset of widespread granulomatous
dermatitis in the newborn period.";
Pediatr. Dermatol. 27:69-73(2010).
[31]
INVOLVEMENT IN YAOS, AND VARIANT YAOS TRP-702.
PubMed=21914217; DOI=10.1186/ar3462;
Yao Q., Zhou L., Cusumano P., Bose N., Piliang M., Jayakar B.,
Su L.C., Shen B.;
"A new category of autoinflammatory disease associated with NOD2 gene
mutations.";
Arthritis Res. Ther. 13:R148-R148(2011).
[32]
VARIANT BLAUS SER-507.
PubMed=25692065; DOI=10.1155/2015/463959;
Zeybek C., Basbozkurt G., Gul D., Demirkaya E., Gok F.;
"A new mutation in blau syndrome.";
Case Rep. Rheumatol. 2015:463959-463959(2015).
[33]
VARIANT BLAUS GLN-334, AND VARIANT SER-268.
PubMed=25724124; DOI=10.1016/j.jaci.2014.12.1941;
de Inocencio J., Mensa-Vilaro A., Tejada-Palacios P.,
Enriquez-Merayo E., Gonzalez-Roca E., Magri G., Ruiz-Ortiz E.,
Cerutti A., Yaguee J., Arostegui J.I.;
"Somatic NOD2 mosaicism in Blau syndrome.";
J. Allergy Clin. Immunol. 0:0-0(2015).
[34]
INVOLVEMENT IN YAOS, AND VARIANT YAOS ARG-908.
PubMed=26070941; DOI=10.1093/rheumatology/kev207;
Yao Q., Shen M., McDonald C., Lacbawan F., Moran R., Shen B.;
"NOD2-associated autoinflammatory disease: a large cohort study.";
Rheumatology 54:1904-1912(2015).
-!- FUNCTION: Involved in gastrointestinal immunity. Upon stimulation
by muramyl dipeptide (MDP), a fragment of bacterial peptidoglycan,
binds the proximal adapter receptor-interacting RIPK2, which
recruits ubiquitin ligases as XIAP, BIRC2, BIRC3, INAVA and the
LUBAC complex, triggering activation of MAP kinases and activation
of NF-kappa-B signaling. This in turn leads to the transcriptional
activation of hundreds of genes involved in immune response.
Required for MDP-induced NLRP1-dependent CASP1 activation and IL1B
release in macrophages (PubMed:18511561). Component of an
autophagy-mediated antibacterial pathway together with ATG16L1
(PubMed:20637199). Plays also a role in sensing single-stranded
RNA (ssRNA) from viruses. Interacts with mitochondrial antiviral
signaling/MAVS, leading to activation of interferon regulatory
factor-3/IRF3 and expression of type I interferon
(PubMed:19701189). {ECO:0000269|PubMed:18511561,
ECO:0000269|PubMed:19701189, ECO:0000269|PubMed:20637199,
ECO:0000269|PubMed:23806334, ECO:0000269|PubMed:28436939}.
-!- SUBUNIT: Component of a signaling complex consisting of ARHGEF2,
NOD2 and RIPK2 (PubMed:21887730). Interacts (via CARD domain) with
RIPK2 (via CARD domain) (PubMed:19592251, PubMed:21887730,
PubMed:27812135). Interacts with ATG16L1 (PubMed:20637199,
PubMed:23376921). Interacts (via NACHT domain) with CARD9
(PubMed:24960071). Interacts with ANKRD17 (via N-terminus)
(PubMed:23711367). Interacts with HSPA1A; the interaction enhances
NOD2 stability (PubMed:24790089). Interacts (via both CARD
domains) with HSP90; the interaction enhances NOD2 stability
(PubMed:23019338). Interacts (via CARD domain) with SOCS3; the
interaction promotes NOD2 degradation (PubMed:23019338). Interacts
(via CARD domain) with ERBBI2P; the interaction inhibits
activation of NOD2 (PubMed:16203728). Interacts (via CARD domain)
with CASP1; this interaction leads to IL1B processing. Also
interacts with CASP4. Interacts with NLRP1; this interaction is
enhanced in the presence of muramyl dipeptide (MDP) and leads to
increased IL1B release (PubMed:18511561). Interacts with MAPKBP1;
the interaction is enhanced in the presence of muramyl dipeptide
(MDP) (PubMed:22700971). Interacts with INAVA; the interaction
takes place upon PRR stimulation (PubMed:28436939). Interacts with
ANKHD1, C10ORF67, CHMP5, DOCK7, ENTR1, KRT15, LDOC1, PPP1R12C,
PPP2R3B, TRIM41 and VIM (PubMed:27812135). Interacts with NLRP12;
this interaction promotes degradation of NOD2 through the
ubiquitin-proteasome pathway (PubMed:30559449).
{ECO:0000269|PubMed:16203728, ECO:0000269|PubMed:18511561,
ECO:0000269|PubMed:19592251, ECO:0000269|PubMed:20637199,
ECO:0000269|PubMed:21887730, ECO:0000269|PubMed:22700971,
ECO:0000269|PubMed:23019338, ECO:0000269|PubMed:23376921,
ECO:0000269|PubMed:23711367, ECO:0000269|PubMed:24790089,
ECO:0000269|PubMed:24960071, ECO:0000269|PubMed:27812135,
ECO:0000269|PubMed:28436939, ECO:0000269|PubMed:30559449}.
-!- INTERACTION:
P29466:CASP1; NbExp=4; IntAct=EBI-7445625, EBI-516667;
Q96RT1:ERBIN; NbExp=5; IntAct=EBI-7445625, EBI-993903;
Q96RT1-2:ERBIN; NbExp=5; IntAct=EBI-7445625, EBI-8449250;
Q9Y3D6:FIS1; NbExp=2; IntAct=EBI-7445625, EBI-3385283;
Q10471:GALNT2; NbExp=2; IntAct=EBI-7445625, EBI-10226985;
Q92993:KAT5; NbExp=2; IntAct=EBI-7445625, EBI-399080;
Q9P0J0:NDUFA13; NbExp=6; IntAct=EBI-7445625, EBI-372742;
Q6UX06:OLFM4; NbExp=2; IntAct=EBI-7445625, EBI-2804156;
Q16537:PPP2R5E; NbExp=2; IntAct=EBI-7445625, EBI-968374;
O43353:RIPK2; NbExp=3; IntAct=EBI-7445625, EBI-358522;
Q8IY34:SLC15A3; NbExp=2; IntAct=EBI-7445625, EBI-12179023;
Q8N697:SLC15A4; NbExp=2; IntAct=EBI-7445625, EBI-4319594;
Q04724:TLE1; NbExp=2; IntAct=EBI-7445625, EBI-711424;
P14373:TRIM27; NbExp=10; IntAct=EBI-7445625, EBI-719493;
P08670:VIM; NbExp=7; IntAct=EBI-7445625, EBI-353844;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19701189,
ECO:0000269|PubMed:24790089, ECO:0000269|PubMed:25093298}.
Membrane {ECO:0000269|PubMed:25093298}. Mitochondrion
{ECO:0000269|PubMed:19701189}. Basolateral cell membrane
{ECO:0000269|PubMed:16203728}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=3;
Name=1; Synonyms=Nod2;
IsoId=Q9HC29-1; Sequence=Displayed;
Note=Can activate NF-kappa-B. More abundant.;
Name=2; Synonyms=Nod2b;
IsoId=Q9HC29-2; Sequence=VSP_018689;
Note=Can activate NF-kappa-B.;
Name=3; Synonyms=NOD2-C2;
IsoId=Q9HC29-3; Sequence=VSP_018689, VSP_046567, VSP_046568;
Note=Can activate NF-kappa-B.;
-!- TISSUE SPECIFICITY: Expressed in intestinal mucosa, mainly in
Paneth cells and, at lower extent, in the glandular epithelium.
{ECO:0000269|PubMed:22700971}.
-!- INDUCTION: Up-regulated by muramyl-dipeptide and
lipopolysaccharide. {ECO:0000269|PubMed:27812135}.
-!- DOMAIN: The ATG16L1-binding motif mediates interaction with
ATG16L1. {ECO:0000269|PubMed:23376921}.
-!- DOMAIN: Intramolecular interactions between the N-terminal moiety
and the leucine-rich repeats (LRR) may be important for
autoinhibition in the absence of activating signal. In the absence
of LRRs, the protein becomes a constitutive activator of CASP1
cleavage and proIL1B processing. {ECO:0000269|PubMed:18511561}.
-!- PTM: Polyubiquitinated following MDP stimulation, leading to
proteasome-mediated degradation (PubMed:23019338).
{ECO:0000269|PubMed:23019338}.
-!- DISEASE: Blau syndrome (BLAUS) [MIM:186580]: An autosomal dominant
inflammatory disorder characterized by the formation of immune
granulomas invading the skin, joints and eye. Other organs may be
involved. Clinical manifestations are variable and include early-
onset granulomatous arthritis, uveitis and skin rash. Blindness,
joint destruction and visceral involvement have been reported in
severe cases. {ECO:0000269|PubMed:11528384,
ECO:0000269|PubMed:15459013, ECO:0000269|PubMed:15812565,
ECO:0000269|PubMed:19116920, ECO:0000269|PubMed:19169908,
ECO:0000269|PubMed:19359344, ECO:0000269|PubMed:19479837,
ECO:0000269|PubMed:20199415, ECO:0000269|PubMed:24960071,
ECO:0000269|PubMed:25093298, ECO:0000269|PubMed:25692065,
ECO:0000269|PubMed:25724124, ECO:0000269|PubMed:27812135}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Inflammatory bowel disease 1 (IBD1) [MIM:266600]: A
chronic, relapsing inflammation of the gastrointestinal tract with
a complex etiology. It is subdivided into Crohn disease and
ulcerative colitis phenotypes. Crohn disease may affect any part
of the gastrointestinal tract from the mouth to the anus, but most
frequently it involves the terminal ileum and colon. Bowel
inflammation is transmural and discontinuous; it may contain
granulomas or be associated with intestinal or perianal fistulas.
In contrast, in ulcerative colitis, the inflammation is continuous
and limited to rectal and colonic mucosal layers; fistulas and
granulomas are not observed. Both diseases include extraintestinal
inflammation of the skin, eyes, or joints.
{ECO:0000269|PubMed:11385576, ECO:0000269|PubMed:15024686,
ECO:0000269|PubMed:16485124, ECO:0000269|PubMed:24790089,
ECO:0000269|PubMed:24960071, ECO:0000269|PubMed:27812135}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- DISEASE: Yao syndrome (YAOS) [MIM:617321]: An autoinflammatory
disease characterized by periodic fever, dermatitis,
polyarthritis, leg swelling, and gastrointestinal and sicca-like
symptoms. YAOS is a complex disease with multifactorial
inheritance. {ECO:0000269|PubMed:21914217,
ECO:0000269|PubMed:26070941}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- WEB RESOURCE: Name=INFEVERS; Note=Repertory of FMF and hereditary
autoinflammatory disorders mutations;
URL="https://infevers.umai-montpellier.fr/web/search.php?n=6";
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EMBL; AF178930; AAG33677.1; -; mRNA.
EMBL; AF385089; AAK70867.1; -; Genomic_DNA.
EMBL; AF385090; AAK70868.1; -; Genomic_DNA.
EMBL; AJ303140; CAC42117.1; -; Genomic_DNA.
EMBL; HQ204571; ADN95581.1; -; mRNA.
CCDS; CCDS10746.1; -. [Q9HC29-1]
CCDS; CCDS86525.1; -. [Q9HC29-2]
RefSeq; NP_001280486.1; NM_001293557.1. [Q9HC29-2]
RefSeq; NP_071445.1; NM_022162.2. [Q9HC29-1]
RefSeq; XP_005256141.1; XM_005256084.3.
SMR; Q9HC29; -.
BioGrid; 122077; 66.
DIP; DIP-41998N; -.
IntAct; Q9HC29; 46.
MINT; Q9HC29; -.
STRING; 9606.ENSP00000300589; -.
BindingDB; Q9HC29; -.
ChEMBL; CHEMBL1293266; -.
GuidetoPHARMACOLOGY; 1763; -.
iPTMnet; Q9HC29; -.
PhosphoSitePlus; Q9HC29; -.
BioMuta; NOD2; -.
DMDM; 20137973; -.
EPD; Q9HC29; -.
jPOST; Q9HC29; -.
PaxDb; Q9HC29; -.
PeptideAtlas; Q9HC29; -.
PRIDE; Q9HC29; -.
ProteomicsDB; 81629; -. [Q9HC29-1]
ProteomicsDB; 81630; -. [Q9HC29-2]
DNASU; 64127; -.
Ensembl; ENST00000300589; ENSP00000300589; ENSG00000167207. [Q9HC29-1]
Ensembl; ENST00000647318; ENSP00000495993; ENSG00000167207. [Q9HC29-2]
GeneID; 64127; -.
KEGG; hsa:64127; -.
UCSC; uc002egm.2; human. [Q9HC29-1]
CTD; 64127; -.
DisGeNET; 64127; -.
GeneCards; NOD2; -.
HGNC; HGNC:5331; NOD2.
HPA; HPA041985; -.
HPA; HPA054494; -.
MalaCards; NOD2; -.
MIM; 186580; phenotype.
MIM; 266600; phenotype.
MIM; 605956; gene.
MIM; 617321; phenotype.
neXtProt; NX_Q9HC29; -.
OpenTargets; ENSG00000167207; -.
Orphanet; 90340; Blau syndrome.
Orphanet; 206; NON RARE IN EUROPE: Crohn disease.
Orphanet; 771; NON RARE IN EUROPE: Ulcerative colitis.
PharmGKB; PA26074; -.
eggNOG; KOG4308; Eukaryota.
eggNOG; ENOG410ZBX3; LUCA.
GeneTree; ENSGT00940000160934; -.
HOGENOM; HOG000113814; -.
InParanoid; Q9HC29; -.
KO; K10165; -.
OMA; LHCEQLQ; -.
OrthoDB; 651627at2759; -.
PhylomeDB; Q9HC29; -.
TreeFam; TF352118; -.
Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
Reactome; R-HSA-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
Reactome; R-HSA-450302; activated TAK1 mediates p38 MAPK activation.
Reactome; R-HSA-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
Reactome; R-HSA-5689896; Ovarian tumor domain proteases.
Reactome; R-HSA-9020702; Interleukin-1 signaling.
SignaLink; Q9HC29; -.
SIGNOR; Q9HC29; -.
GeneWiki; NOD2; -.
GenomeRNAi; 64127; -.
PRO; PR:Q9HC29; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000167207; Expressed in 126 organ(s), highest expression level in ectocervix.
ExpressionAtlas; Q9HC29; baseline and differential.
Genevisible; Q9HC29; HS.
GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HGNC.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
GO; GO:0031982; C:vesicle; IDA:UniProtKB.
GO; GO:0003779; F:actin binding; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0050700; F:CARD domain binding; IPI:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0030544; F:Hsp70 protein binding; IPI:UniProtKB.
GO; GO:0051879; F:Hsp90 protein binding; IDA:UniProtKB.
GO; GO:0032500; F:muramyl dipeptide binding; IDA:HGNC.
GO; GO:0042834; F:peptidoglycan binding; IDA:HGNC.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0044877; F:protein-containing complex binding; IPI:UniProtKB.
GO; GO:0000187; P:activation of MAPK activity; TAS:Reactome.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:UniProtKB.
GO; GO:0071225; P:cellular response to muramyl dipeptide; IDA:UniProtKB.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
GO; GO:0071224; P:cellular response to peptidoglycan; IEA:Ensembl.
GO; GO:0002367; P:cytokine production involved in immune response; IMP:UniProtKB.
GO; GO:0002374; P:cytokine secretion involved in immune response; IMP:CACAO.
GO; GO:0006952; P:defense response; TAS:HGNC.
GO; GO:0042742; P:defense response to bacterium; IDA:HGNC.
GO; GO:0016045; P:detection of bacterium; IDA:HGNC.
GO; GO:0009595; P:detection of biotic stimulus; TAS:HGNC.
GO; GO:0032498; P:detection of muramyl dipeptide; IDA:HGNC.
GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
GO; GO:0070498; P:interleukin-1-mediated signaling pathway; TAS:Reactome.
GO; GO:0035556; P:intracellular signal transduction; IDA:HGNC.
GO; GO:0007254; P:JNK cascade; TAS:Reactome.
GO; GO:0030277; P:maintenance of gastrointestinal epithelium; IMP:UniProtKB.
GO; GO:2000110; P:negative regulation of macrophage apoptotic process; ISS:BHF-UCL.
GO; GO:0070431; P:nucleotide-binding oligomerization domain containing 2 signaling pathway; IDA:UniProtKB.
GO; GO:0070423; P:nucleotide-binding oligomerization domain containing signaling pathway; TAS:Reactome.
GO; GO:0050871; P:positive regulation of B cell activation; IDA:BHF-UCL.
GO; GO:1900017; P:positive regulation of cytokine production involved in inflammatory response; IDA:CACAO.
GO; GO:0002606; P:positive regulation of dendritic cell antigen processing and presentation; ISS:BHF-UCL.
GO; GO:0002732; P:positive regulation of dendritic cell cytokine production; IEA:Ensembl.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISS:BHF-UCL.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:BHF-UCL.
GO; GO:0046645; P:positive regulation of gamma-delta T cell activation; ISS:BHF-UCL.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IMP:BHF-UCL.
GO; GO:0050718; P:positive regulation of interleukin-1 beta secretion; IDA:HGNC.
GO; GO:0032733; P:positive regulation of interleukin-10 production; ISS:BHF-UCL.
GO; GO:0032740; P:positive regulation of interleukin-17 production; IMP:UniProtKB.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:BHF-UCL.
GO; GO:0032757; P:positive regulation of interleukin-8 production; IMP:UniProtKB.
GO; GO:0046330; P:positive regulation of JNK cascade; IDA:MGI.
GO; GO:0043406; P:positive regulation of MAP kinase activity; ISS:BHF-UCL.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; ISS:BHF-UCL.
GO; GO:0045747; P:positive regulation of Notch signaling pathway; ISS:BHF-UCL.
GO; GO:0051353; P:positive regulation of oxidoreductase activity; ISS:BHF-UCL.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; ISS:BHF-UCL.
GO; GO:2000363; P:positive regulation of prostaglandin-E synthase activity; ISS:BHF-UCL.
GO; GO:0060585; P:positive regulation of prostaglandin-endoperoxide synthase activity; ISS:BHF-UCL.
GO; GO:1902523; P:positive regulation of protein K63-linked ubiquitination; IMP:UniProtKB.
GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; IDA:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:MGI.
GO; GO:0002830; P:positive regulation of type 2 immune response; IMP:BHF-UCL.
GO; GO:0051259; P:protein complex oligomerization; TAS:HGNC.
GO; GO:0050727; P:regulation of inflammatory response; IC:BHF-UCL.
GO; GO:0032495; P:response to muramyl dipeptide; IDA:HGNC.
GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
Gene3D; 3.80.10.10; -; 1.
InterPro; IPR001315; CARD.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR007111; NACHT_NTPase.
InterPro; IPR041267; NLRC_HD2.
InterPro; IPR041075; NOD2_WH.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF00619; CARD; 1.
Pfam; PF13516; LRR_6; 3.
Pfam; PF05729; NACHT; 1.
Pfam; PF17776; NLRC4_HD2; 1.
Pfam; PF17779; NOD2_WH; 1.
SUPFAM; SSF47986; SSF47986; 2.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50209; CARD; 2.
PROSITE; PS51450; LRR; 4.
PROSITE; PS50837; NACHT; 1.
1: Evidence at protein level;
Alternative initiation; ATP-binding; Cell membrane; Complete proteome;
Cytoplasm; Disease mutation; Immunity; Innate immunity;
Leucine-rich repeat; Membrane; Mitochondrion; Nucleotide-binding;
Polymorphism; Reference proteome; Repeat; Ubl conjugation.
CHAIN 1 1040 Nucleotide-binding oligomerization
domain-containing protein 2.
/FTId=PRO_0000004418.
DOMAIN 26 122 CARD 1. {ECO:0000255|PROSITE-
ProRule:PRU00046}.
DOMAIN 126 218 CARD 2. {ECO:0000255|PROSITE-
ProRule:PRU00046}.
DOMAIN 293 618 NACHT. {ECO:0000255|PROSITE-
ProRule:PRU00136}.
REPEAT 791 812 LRR 1.
REPEAT 816 839 LRR 2.
REPEAT 844 865 LRR 3.
REPEAT 872 884 LRR 4.
REPEAT 900 920 LRR 5.
REPEAT 928 949 LRR 6.
REPEAT 956 976 LRR 7.
REPEAT 984 1005 LRR 8.
REPEAT 1012 1032 LRR 9.
NP_BIND 299 306 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00136}.
REGION 241 274 Required for CARD9 binding.
{ECO:0000269|PubMed:24960071}.
MOTIF 63 77 ATG16L1-binding motif.
VAR_SEQ 1 27 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:11087742,
ECO:0000303|PubMed:20698950}.
/FTId=VSP_018689.
VAR_SEQ 216 224 AATCKKYMA -> DERTEAQKG (in isoform 3).
{ECO:0000303|PubMed:20698950}.
/FTId=VSP_046567.
VAR_SEQ 225 1040 Missing (in isoform 3).
{ECO:0000303|PubMed:20698950}.
/FTId=VSP_046568.
VARIANT 81 81 L -> V (in dbSNP:rs34936594).
/FTId=VAR_036871.
VARIANT 113 113 D -> N (in IBD1; unknown pathological
significance; dbSNP:rs104895468).
{ECO:0000269|PubMed:15024686}.
/FTId=VAR_073228.
VARIANT 140 140 A -> T (in IBD1; also found in patients
with ulcerative colitis; unknown
pathological significance;
dbSNP:rs34684955).
{ECO:0000269|PubMed:11385576}.
/FTId=VAR_012665.
VARIANT 157 157 W -> R (in IBD1; unknown pathological
significance; dbSNP:rs104895420).
{ECO:0000269|PubMed:11385576}.
/FTId=VAR_012666.
VARIANT 189 189 T -> M (in dbSNP:rs61755182).
{ECO:0000269|PubMed:11385576}.
/FTId=VAR_012667.
VARIANT 235 235 R -> C (in IBD1; unknown pathological
significance; dbSNP:rs104895422).
{ECO:0000269|PubMed:11385576}.
/FTId=VAR_012668.
VARIANT 248 248 L -> R (in IBD1; unknown pathological
significance; no disruption of NOD2-CARD9
interaction; dbSNP:rs104895423).
{ECO:0000269|PubMed:11385576,
ECO:0000269|PubMed:24960071}.
/FTId=VAR_012669.
VARIANT 268 268 P -> S (in dbSNP:rs2066842).
{ECO:0000269|PubMed:11385576,
ECO:0000269|PubMed:16485124,
ECO:0000269|PubMed:25724124}.
/FTId=VAR_012670.
VARIANT 289 289 N -> S (in dbSNP:rs5743271).
{ECO:0000269|PubMed:11385576,
ECO:0000269|PubMed:16485124}.
/FTId=VAR_012671.
VARIANT 291 291 D -> N (in IBD1; unknown pathological
significance; dbSNP:rs104895424).
{ECO:0000269|PubMed:11385576}.
/FTId=VAR_012672.
VARIANT 294 294 T -> S (in IBD1; unknown pathological
significance; dbSNP:rs104895425).
{ECO:0000269|PubMed:11385576}.
/FTId=VAR_012673.
VARIANT 301 301 A -> V (in IBD1; unknown pathological
significance; dbSNP:rs104895426).
{ECO:0000269|PubMed:11385576}.
/FTId=VAR_012674.
VARIANT 311 311 R -> W (in IBD1; also found in patients
with ulcerative colitis; unknown
pathological significance;
dbSNP:rs104895427).
{ECO:0000269|PubMed:11385576,
ECO:0000269|PubMed:16485124}.
/FTId=VAR_012675.
VARIANT 334 334 R -> Q (in BLAUS; somatic mosaicism in
4.9% to 11% of peripheral blood cells;
hyperactive; abolishes interaction with
LDOC1, ANKHD1, PPP2R3B, ENTR1 and TRIM41;
decreases interaction with RIPK2 and
PPP1R12C; no effect on interaction with
CHMP5; dbSNP:rs104895461).
{ECO:0000269|PubMed:11528384,
ECO:0000269|PubMed:19116920,
ECO:0000269|PubMed:19479837,
ECO:0000269|PubMed:25093298,
ECO:0000269|PubMed:25724124,
ECO:0000269|PubMed:27812135}.
/FTId=VAR_012676.
VARIANT 334 334 R -> W (in BLAUS; no disruption of NOD2-
CARD9 interaction; hyperactive;
dbSNP:rs104895462).
{ECO:0000269|PubMed:11528384,
ECO:0000269|PubMed:15459013,
ECO:0000269|PubMed:19116920,
ECO:0000269|PubMed:19479837,
ECO:0000269|PubMed:20199415,
ECO:0000269|PubMed:24960071,
ECO:0000269|PubMed:25093298}.
/FTId=VAR_012677.
VARIANT 348 348 L -> V (in IBD1; unknown pathological
significance; dbSNP:rs104895428).
{ECO:0000269|PubMed:11385576}.
/FTId=VAR_012678.
VARIANT 352 352 H -> R (in IBD1; unknown pathological
significance; dbSNP:rs5743272).
{ECO:0000269|PubMed:11385576}.
/FTId=VAR_012679.
VARIANT 357 357 D -> A (in IBD1; unknown pathological
significance; no disruption of NOD2-CARD9
interaction; dbSNP:rs104895469).
{ECO:0000269|PubMed:15024686,
ECO:0000269|PubMed:24960071}.
/FTId=VAR_073229.
VARIANT 363 363 I -> F (in IBD1; unknown pathological
significance; no disruption of NOD2-CARD9
interaction; dbSNP:rs104895470).
{ECO:0000269|PubMed:15024686,
ECO:0000269|PubMed:24960071}.
/FTId=VAR_073230.
VARIANT 373 373 R -> C (in IBD1; unknown pathological
significance; dbSNP:rs145293873).
{ECO:0000269|PubMed:11385576}.
/FTId=VAR_012680.
VARIANT 382 382 D -> E (in BLAUS; hyperactive;
dbSNP:rs104895476).
{ECO:0000269|PubMed:15459013,
ECO:0000269|PubMed:19116920}.
/FTId=VAR_023822.
VARIANT 383 383 E -> G (in BLAUS; unknown pathological
significance; hyperactive;
dbSNP:rs104895493).
{ECO:0000269|PubMed:19116920,
ECO:0000269|PubMed:25093298}.
/FTId=VAR_073231.
VARIANT 383 383 E -> K (in BLAUS; hyperactive;
dbSNP:rs104895477).
{ECO:0000269|PubMed:15812565,
ECO:0000269|PubMed:19479837,
ECO:0000269|PubMed:25093298}.
/FTId=VAR_023823.
VARIANT 391 391 R -> C (in dbSNP:rs104895481).
{ECO:0000269|PubMed:16485124}.
/FTId=VAR_073232.
VARIANT 414 414 N -> S (in IBD1; unknown pathological
significance; dbSNP:rs104895429).
{ECO:0000269|PubMed:11385576}.
/FTId=VAR_012681.
VARIANT 431 431 S -> L (in IBD1; unknown pathological
significance; no disruption of NOD2-CARD9
interaction; dbSNP:rs104895431).
{ECO:0000269|PubMed:11385576,
ECO:0000269|PubMed:24960071}.
/FTId=VAR_012682.
VARIANT 432 432 A -> V (in IBD1; unknown pathological
significance; dbSNP:rs2076754).
{ECO:0000269|PubMed:11385576}.
/FTId=VAR_012683.
VARIANT 441 441 E -> K (in IBD1; unknown pathological
significance; no disruption of NOD2-CARD9
interaction; dbSNP:rs104895432).
{ECO:0000269|PubMed:11385576,
ECO:0000269|PubMed:24960071}.
/FTId=VAR_012684.
VARIANT 463 463 P -> A (polymorphism; no disruption of
NOD2-CARD9 interaction;
dbSNP:rs104895482).
{ECO:0000269|PubMed:16485124,
ECO:0000269|PubMed:24960071}.
/FTId=VAR_073233.
VARIANT 464 464 G -> W (polymorphism; hyperactive;
dbSNP:rs104895492).
{ECO:0000269|PubMed:25093298}.
/FTId=VAR_073234.
VARIANT 469 469 L -> F (in BLAUS; hyperactive;
dbSNP:rs104895460).
{ECO:0000269|PubMed:11528384,
ECO:0000269|PubMed:25093298}.
/FTId=VAR_012685.
VARIANT 471 471 R -> C (polymorphism; does not affect
activity; dbSNP:rs1078327).
{ECO:0000269|PubMed:25093298}.
/FTId=VAR_036872.
VARIANT 481 481 G -> D (in BLAUS; atypical form with
cardiac infiltration; sporadic case;
unknown pathological significance;
hyperactive; dbSNP:rs104895494).
{ECO:0000269|PubMed:19359344,
ECO:0000269|PubMed:25093298}.
/FTId=VAR_073235.
VARIANT 490 490 W -> L (in BLAUS; unknown pathological
significance; hyperactive;
dbSNP:rs104895480).
{ECO:0000269|PubMed:19479837,
ECO:0000269|PubMed:25093298}.
/FTId=VAR_073236.
VARIANT 495 495 C -> Y (in BLAUS; unknown pathological
significance; hyperactive;
dbSNP:rs104895478).
{ECO:0000269|PubMed:19116920,
ECO:0000269|PubMed:19479837,
ECO:0000269|PubMed:25093298}.
/FTId=VAR_073237.
VARIANT 496 496 H -> L (in BLAUS; hyperactive;
dbSNP:rs104895472).
{ECO:0000269|PubMed:15459013,
ECO:0000269|PubMed:19116920,
ECO:0000269|PubMed:25093298}.
/FTId=VAR_023824.
VARIANT 507 507 P -> S (in BLAUS).
{ECO:0000269|PubMed:25692065}.
/FTId=VAR_073180.
VARIANT 513 513 M -> T (in BLAUS; hyperactive;
dbSNP:rs104895473).
{ECO:0000269|PubMed:15459013,
ECO:0000269|PubMed:19116920,
ECO:0000269|PubMed:25093298}.
/FTId=VAR_073238.
VARIANT 550 550 L -> V (in IBD1; unknown pathological
significance; no disruption of NOD2-CARD9
interaction; dbSNP:rs104895471).
{ECO:0000269|PubMed:15024686,
ECO:0000269|PubMed:24960071}.
/FTId=VAR_073239.
VARIANT 587 587 R -> C (in BLAUS; unknown pathological
significance; not hyperactive;
dbSNP:rs104895479).
{ECO:0000269|PubMed:19479837,
ECO:0000269|PubMed:25093298}.
/FTId=VAR_073240.
VARIANT 605 605 T -> N (in BLAUS; hyperactive).
{ECO:0000269|PubMed:19169908,
ECO:0000269|PubMed:25093298}.
/FTId=VAR_065228.
VARIANT 605 605 T -> P (in BLAUS; hyperactive;
dbSNP:rs104895474).
{ECO:0000269|PubMed:15459013,
ECO:0000269|PubMed:19116920,
ECO:0000269|PubMed:25093298}.
/FTId=VAR_073241.
VARIANT 612 612 A -> T (in BLAUS and IBD1; unknown
pathological significance;
dbSNP:rs104895438).
{ECO:0000269|PubMed:11385576,
ECO:0000269|PubMed:15459013}.
/FTId=VAR_012686.
VARIANT 612 612 A -> V (in IBD1; unknown pathological
significance; no disruption of NOD2-CARD9
interaction; dbSNP:rs104895439).
{ECO:0000269|PubMed:11385576,
ECO:0000269|PubMed:24960071}.
/FTId=VAR_012687.
VARIANT 670 670 N -> K (in BLAUS; hyperactive;
dbSNP:rs104895475).
{ECO:0000269|PubMed:15459013,
ECO:0000269|PubMed:19116920,
ECO:0000269|PubMed:25093298}.
/FTId=VAR_073242.
VARIANT 684 684 R -> W (in IBD1; unknown pathological
significance; dbSNP:rs5743276).
{ECO:0000269|PubMed:11385576}.
/FTId=VAR_012688.
VARIANT 702 702 R -> W (in IBD1 and YAOS; associated with
disease susceptibility; no disruption of
NOD2-CARD9 interaction; decreases half-
life of protein; abolishes interaction
with ANKHD1, ENTR1 and TRIM41; increases
interaction with RIPK2 and PPP2R3B;
decreases interaction with LDOC1 and
PPP1R12C; no effect on interaction with
CHMP5; dbSNP:rs2066844).
{ECO:0000269|PubMed:11385576,
ECO:0000269|PubMed:16485124,
ECO:0000269|PubMed:21914217,
ECO:0000269|PubMed:24790089,
ECO:0000269|PubMed:24960071,
ECO:0000269|PubMed:27812135}.
/FTId=VAR_012689.
VARIANT 703 703 R -> C (in IBD1; also found in patients
with ulcerative colitis; unknown
pathological significance;
dbSNP:rs5743277).
{ECO:0000269|PubMed:11385576,
ECO:0000269|PubMed:16485124}.
/FTId=VAR_012690.
VARIANT 713 713 R -> C (in IBD1; unknown pathological
significance; dbSNP:rs104895440).
{ECO:0000269|PubMed:11385576}.
/FTId=VAR_012691.
VARIANT 713 713 R -> H (in IBD1; unknown pathological
significance; dbSNP:rs104895483).
{ECO:0000269|PubMed:16485124}.
/FTId=VAR_073243.
VARIANT 725 725 A -> G (in IBD1; unknown pathological
significance; dbSNP:rs5743278).
{ECO:0000269|PubMed:11385576}.
/FTId=VAR_012692.
VARIANT 755 755 A -> V (in IBD1; also found in patients
with ulcerative colitis; unknown
pathological significance;
dbSNP:rs61747625).
{ECO:0000269|PubMed:11385576,
ECO:0000269|PubMed:16485124}.
/FTId=VAR_012693.
VARIANT 758 758 A -> V (in IBD1; unknown pathological
significance; dbSNP:rs104895442).
{ECO:0000269|PubMed:11385576}.
/FTId=VAR_012694.
VARIANT 760 760 R -> C (in IBD1; unknown pathological
significance; dbSNP:rs3813758).
{ECO:0000269|PubMed:16485124}.
/FTId=VAR_073244.
VARIANT 778 778 E -> K (in IBD1; unknown pathological
significance; dbSNP:rs104895443).
{ECO:0000269|PubMed:11385576}.
/FTId=VAR_012695.
VARIANT 790 790 R -> Q (in dbSNP:rs5743279).
/FTId=VAR_024402.
VARIANT 790 790 R -> W (in IBD1; unknown pathological
significance; dbSNP:rs62029861).
{ECO:0000269|PubMed:16485124}.
/FTId=VAR_073245.
VARIANT 791 791 R -> W (in dbSNP:rs104895484).
{ECO:0000269|PubMed:16485124}.
/FTId=VAR_073246.
VARIANT 793 793 V -> M (in IBD1; unknown pathological
significance; dbSNP:rs104895444).
{ECO:0000269|PubMed:11385576}.
/FTId=VAR_012696.
VARIANT 825 825 N -> K (in dbSNP:rs104895485).
{ECO:0000269|PubMed:16485124}.
/FTId=VAR_073247.
VARIANT 843 843 E -> K (in IBD1; unknown pathological
significance; dbSNP:rs104895445).
{ECO:0000269|PubMed:11385576}.
/FTId=VAR_012697.
VARIANT 849 849 A -> V (in dbSNP:rs104895486).
{ECO:0000269|PubMed:16485124}.
/FTId=VAR_073248.
VARIANT 852 852 N -> S (in IBD1; unknown pathological
significance; dbSNP:rs104895467).
{ECO:0000269|PubMed:15024686}.
/FTId=VAR_073249.
VARIANT 853 853 N -> S (in IBD1; unknown pathological
significance; dbSNP:rs104895446).
{ECO:0000269|PubMed:11385576}.
/FTId=VAR_012698.
VARIANT 863 863 M -> V (in IBD1; unknown pathological
significance; dbSNP:rs104895447).
{ECO:0000269|PubMed:11385576}.
/FTId=VAR_012699.
VARIANT 885 885 A -> T (in IBD1; unknown pathological
significance).
{ECO:0000269|PubMed:11385576}.
/FTId=VAR_012700.
VARIANT 908 908 G -> R (in IBD1 and YAOS; associated with
disease susceptibility; decreases half-
life of protein; abolishes interaction
with ANKHD1, ENTR1 and TRIM41; decreases
interaction with RIPK2 and PPP1R12C; no
effect on interaction with CHMP5, LDOC1
and PPP2R3B; dbSNP:rs2066845).
{ECO:0000269|PubMed:11087742,
ECO:0000269|PubMed:11385576,
ECO:0000269|PubMed:16485124,
ECO:0000269|PubMed:24790089,
ECO:0000269|PubMed:26070941,
ECO:0000269|PubMed:27812135}.
/FTId=VAR_012701.
VARIANT 918 918 A -> D (in dbSNP:rs104895452).
{ECO:0000269|PubMed:11385576}.
/FTId=VAR_012702.
VARIANT 924 924 G -> D (in IBD1; unknown pathological
significance; dbSNP:rs104895453).
{ECO:0000269|PubMed:11385576}.
/FTId=VAR_012703.
VARIANT 955 955 V -> I (in dbSNP:rs5743291).
{ECO:0000269|PubMed:11385576}.
/FTId=VAR_012704.
MUTAGEN 305 305 K->R: No activation.
{ECO:0000269|PubMed:11087742}.
MUTAGEN 379 379 D->A: No disruption in NOD2-CARD9
interaction.
{ECO:0000269|PubMed:24960071}.
SEQUENCE 1040 AA; 115283 MW; 0037592D96D7DDFF CRC64;
MGEEGGSASH DEEERASVLL GHSPGCEMCS QEAFQAQRSQ LVELLVSGSL EGFESVLDWL
LSWEVLSWED YEGFHLLGQP LSHLARRLLD TVWNKGTWAC QKLIAAAQEA QADSQSPKLH
GCWDPHSLHP ARDLQSHRPA IVRRLHSHVE NMLDLAWERG FVSQYECDEI RLPIFTPSQR
ARRLLDLATV KANGLAAFLL QHVQELPVPL ALPLEAATCK KYMAKLRTTV SAQSRFLSTY
DGAETLCLED IYTENVLEVW ADVGMAGPPQ KSPATLGLEE LFSTPGHLND DADTVLVVGE
AGSGKSTLLQ RLHLLWAAGQ DFQEFLFVFP FSCRQLQCMA KPLSVRTLLF EHCCWPDVGQ
EDIFQLLLDH PDRVLLTFDG FDEFKFRFTD RERHCSPTDP TSVQTLLFNL LQGNLLKNAR
KVVTSRPAAV SAFLRKYIRT EFNLKGFSEQ GIELYLRKRH HEPGVADRLI RLLQETSALH
GLCHLPVFSW MVSKCHQELL LQEGGSPKTT TDMYLLILQH FLLHATPPDS ASQGLGPSLL
RGRLPTLLHL GRLALWGLGM CCYVFSAQQL QAAQVSPDDI SLGFLVRAKG VVPGSTAPLE
FLHITFQCFF AAFYLALSAD VPPALLRHLF NCGRPGNSPM ARLLPTMCIQ ASEGKDSSVA
ALLQKAEPHN LQITAAFLAG LLSREHWGLL AECQTSEKAL LRRQACARWC LARSLRKHFH
SIPPAAPGEA KSVHAMPGFI WLIRSLYEMQ EERLARKAAR GLNVGHLKLT FCSVGPTECA
ALAFVLQHLR RPVALQLDYN SVGDIGVEQL LPCLGVCKAL YLRDNNISDR GICKLIECAL
HCEQLQKLAL FNNKLTDGCA HSMAKLLACR QNFLALRLGN NYITAAGAQV LAEGLRGNTS
LQFLGFWGNR VGDEGAQALA EALGDHQSLR WLSLVGNNIG SVGAQALALM LAKNVMLEEL
CLEENHLQDE GVCSLAEGLK KNSSLKILKL SNNCITYLGA EALLQALERN DTILEVWLRG
NTFSLEEVDK LGCRDTRLLL


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EIAAB27463 Bos taurus,Bovine,CARD15,Caspase recruitment domain-containing protein 15,NOD2,Nucleotide-binding oligomerization domain-containing protein 2
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EIAAB27350 Caterpiller protein 11.3,CLR11.3,Homo sapiens,Human,NLR family member X1,NLRX1,NOD26,NOD5,NOD9,Nucleotide-binding oligomerization domain protein 26,Nucleotide-binding oligomerization domain protein 5,
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EIAAB26309 Homo sapiens,Human,NACHT, LRR and PYD domains-containing protein 11,NALP11,NLRP11,NOD17,Nucleotide-binding oligomerization domain protein 17,PAAD-and NACHT domain-containing protein 10,PAN10,PYPAF6,PY
EIAAB05320 CARD17,Caspase recruitment domain-containing protein 17,Caspase-1 inhibitor INCA,Homo sapiens,Human,INCA,Inhibitory caspase recruitment domain protein
EIAAB26342 Homo sapiens,Human,NACHT, LRR and PYD domains-containing protein 7,NALP7,NLRP7,NOD12,Nucleotide-binding oligomerization domain protein 12,PYPAF3,PYRIN-containing APAF1-like protein 3
EIAAB27347 CARD15-like protein,Caterpiller protein 16.2,CLR16.2,Homo sapiens,Human,NLRC3,NOD3,Nucleotide-binding oligomerization domain protein 3,Protein NLRC3
EIAAB26313 Homo sapiens,Human,NACHT, LRR and PYD domains-containing protein 14,NALP14,NLRP14,NOD5,Nucleotide-binding oligomerization domain protein 5
EIAAB26311 Homo sapiens,Human,NACHT, LRR and PYD domains-containing protein 13,NALP13,NLRP13,NOD14,Nucleotide-binding oligomerization domain protein 14
EIAAB26307 Homo sapiens,Human,NACHT, LRR and PYD domains-containing protein 10,NALP10,NLRP10,NOD8,Nucleotide-binding oligomerization domain protein 8,PYNOD
EIAAB26343 Homo sapiens,Human,NACHT, LRR and PYD domains-containing protein 8,NALP8,NLRP8,NOD16,Nucleotide-binding oligomerization domain protein 16,PAN4,PYRIN and NACHT-containing protein 4
EIAAB26344 Homo sapiens,Human,NACHT, LRR and PYD domains-containing protein 9,NALP9,NLRP9,NOD6,Nucleotide-binding oligomerization domain protein 6,PAN12,PYRIN and NACHT-containing protein 12
CSB-EL015915HU Human Nucleotide-binding oligomerization domain-containing protein 2(NOD2) ELISA kit 96T
CSB-EL015915MO Mouse Nucleotide-binding oligomerization domain-containing protein 2(NOD2) ELISA kit 96T
CSB-EL015914HU Human Nucleotide-binding oligomerization domain-containing protein 1(NOD1) ELISA kit 96T
CSB-EL015914MO Mouse Nucleotide-binding oligomerization domain-containing protein 1(NOD1) ELISA kit 96T
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CSB-EL015914MO Mouse Nucleotide-binding oligomerization domain-containing protein 1(NOD1) ELISA kit SpeciesMouse 96T
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Pathways :
WP2292: Chemokine signaling pathway
WP1689: Porphyrin and chlorophyll metabolism
WP2371: Parkinsons Disease Pathway
WP1531: Vitamin D synthesis
WP1616: ABC transporters
WP1678: Nucleotide excision repair
WP731: Sterol regulatory element binding protein related
WP2199: Seed Development
WP525: Mitochondrial Unfolded-Protein Response
WP1675: Nitrogen metabolism
WP1566: Citrate cycle (TCA cycle)
WP1892: Protein folding
WP1939: Unfolded Protein Response
WP73: G Protein Signaling Pathways
WP1049: G Protein Signaling Pathways
WP1685: Peptidoglycan biosynthesis
WP232: G Protein Signaling Pathways
WP1692: Protein export
WP1644: DNA replication
WP1657: Glycerolipid metabolism
WP1700: Selenoamino acid metabolism
WP346: Protein Modifications
WP1663: Homologous recombination
WP211: BMP signaling pathway
WP1673: Naphthalene and anthracene degradation

Related Genes :
[NOD2 CARD15 IBD1] Nucleotide-binding oligomerization domain-containing protein 2 (Caspase recruitment domain-containing protein 15) (Inflammatory bowel disease protein 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 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)
[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)
[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)
[CARD14 CARMA2] Caspase recruitment domain-containing protein 14 (CARD-containing MAGUK protein 2) (Carma 2)
[Nlrc4 Card12 Ipaf] NLR family CARD domain-containing protein 4 (Caspase recruitment domain-containing protein 12) (Ice protease-activating factor) (Ipaf)
[NLRP10 NALP10 NOD8 PYNOD] NACHT, LRR and PYD domains-containing protein 10 (Nucleotide-binding oligomerization domain protein 8)
[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)
[CARD11 CARMA1] Caspase recruitment domain-containing protein 11 (CARD-containing MAGUK protein 1) (Carma 1)
[CARD9] Caspase recruitment domain-containing protein 9 (hCARD9)
[NLRC5 NOD27 NOD4] Protein NLRC5 (Caterpiller protein 16.1) (CLR16.1) (Nucleotide-binding oligomerization domain protein 27) (Nucleotide-binding oligomerization domain protein 4)
[APP A4 AD1] Amyloid-beta precursor protein (APP) (ABPP) (APPI) (Alzheimer disease amyloid protein) (Amyloid precursor protein) (Amyloid-beta A4 protein) (Cerebral vascular amyloid peptide) (CVAP) (PreA4) (Protease nexin-II) (PN-II) [Cleaved into: N-APP; Soluble APP-alpha (S-APP-alpha); Soluble APP-beta (S-APP-beta); C99 (Beta-secretase C-terminal fragment) (Beta-CTF); Amyloid-beta protein 42 (Abeta42) (Beta-APP42); Amyloid-beta protein 40 (Abeta40) (Beta-APP40); C83 (Alpha-secretase C-terminal fragment) (Alpha-CTF); P3(42); P3(40); C80; Gamma-secretase C-terminal fragment 59 (Amyloid intracellular domain 59) (AICD-59) (AID(59)) (Gamma-CTF(59)); Gamma-secretase C-terminal fragment 57 (Amyloid intracellular domain 57) (AICD-57) (AID(57)) (Gamma-CTF(57)); Gamma-secretase C-terminal fragment 50 (Amyloid intracellular domain 50) (AICD-50) (AID(50)) (Gamma-CTF(50)); C31]
[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)
[MAPK14 CSBP CSBP1 CSBP2 CSPB1 MXI2 SAPK2A] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (Cytokine suppressive anti-inflammatory drug-binding protein) (CSAID-binding protein) (CSBP) (MAP kinase MXI2) (MAX-interacting protein 2) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha) (Stress-activated protein kinase 2a) (SAPK2a)
[CASP4 ICH2] Caspase-4 (CASP-4) (EC 3.4.22.57) (ICE and Ced-3 homolog 2) (ICH-2) (ICE(rel)-II) (Mih1) (Protease TX) [Cleaved into: Caspase-4 subunit 1; Caspase-4 subunit 2]
[Card11] Caspase recruitment domain-containing protein 11
[RRS1 RCH2 RRS1-S RSH4 SLH1 WRKY52 At5g45260/At5g45270 K9E15.2/K9E15.3] Disease resistance protein RRS1 (Disease resistance protein RCH2) (Disease resistance protein SLH1) (Probable WRKY transcription factor 52) (Protein RPS4-homolog) (Protein SENSITIVE TO LOW HUMIDITY 1) (Resistance to Colletotrichum higginsianum 2 protein) (Resistance to Ralstonia solanacearum 1 protein) (WRKY DNA-binding protein 52)
[CARD10 CARMA3] Caspase recruitment domain-containing protein 10 (CARD-containing MAGUK protein 3) (Carma 3)
[] Genome polyprotein [Cleaved into: Leader protease (Lb(pro)) (EC 3.4.22.46); Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protein 2A (P2A) (P52); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Protein 3B-1 (P3B-1) (Genome-linked protein VPg1); Protein 3B-2 (P3B-2) (Genome-linked protein VPg2); Protein 3B-3 (P3B-3) (Genome-linked protein VPg3); Protease 3C (EC 3.4.22.28) (Picornain 3C) (P3C) (Protease P20B); RNA-directed RNA polymerase 3D-POL (P3D-POL) (EC 2.7.7.48) (P56A)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[Casp4 Casp11 Caspl Ich3] Caspase-4 (CASP-4) (EC 3.4.22.64) (Caspase-11) (CASP-11) (Protease ICH-3) [Cleaved into: Caspase-4 subunit p10; Caspase-4 subunit p20]
[App] Amyloid-beta A4 protein (ABPP) (APP) (Alzheimer disease amyloid A4 protein homolog) (Amyloid precursor protein) (Amyloid-beta precursor protein) (Amyloidogenic glycoprotein) (AG) [Cleaved into: N-APP; Soluble APP-alpha (S-APP-alpha); Soluble APP-beta (S-APP-beta); C99 (APP-C99) (Beta-secretase C-terminal fragment) (Beta-CTF); Amyloid-beta protein 42 (Abeta42) (Beta-APP42); Amyloid-beta protein 40 (Abeta40) (Beta-APP40); C83 (Alpha-secretase C-terminal fragment) (Alpha-CTF); P3(42); P3(40); C80; Gamma-secretase C-terminal fragment 59 (APP-C59) (Amyloid intracellular domain 59) (AID(59)) (Gamma-CTF(59)); Gamma-secretase C-terminal fragment 57 (APP-C57) (Amyloid intracellular domain 57) (AID(57)) (Gamma-CTF(57)); Gamma-secretase C-terminal fragment 50 (Amyloid intracellular domain 50) (AID(50)) (Gamma-CTF(50)); C31]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); Viroporin p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[RIPK1 RIP RIP1] Receptor-interacting serine/threonine-protein kinase 1 (EC 2.7.11.1) (Cell death protein RIP) (Receptor-interacting protein 1) (RIP-1)
[CCL15 MIP5 NCC3 SCYA15] C-C motif chemokine 15 (Chemokine CC-2) (HCC-2) (Leukotactin-1) (LKN-1) (MIP-1 delta) (Macrophage inflammatory protein 5) (MIP-5) (Mrp-2b) (NCC-3) (Small-inducible cytokine A15) [Cleaved into: CCL15(22-92); CCL15(25-92); CCL15(29-92)]
[ced-3 C48D1.2] Cell death protein 3 (EC 3.4.22.60) (Caspase ced-3) [Cleaved into: Cell death protein 3 subunit p17; Cell death protein 3 subunit p15; Cell death protein 3 subunit p13]
[] Genome polyprotein [Cleaved into: Leader protease (Lpro) (EC 3.4.22.46); Protein VP0 (VP4-VP2); Protein VP4 (P1A) (Virion protein 4); Protein VP2 (P1B) (Virion protein 2); Protein VP3 (P1C) (Virion protein 3); Protein VP1 (P1D) (Virion protein 1); Protein 2A (P2A) (P52); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Protein 3B-1 (P3B-1) (Genome-linked protein VPg1); Protein 3B-2 (P3B-2) (Genome-linked protein VPg2); Protein 3B-3 (P3B-3) (Genome-linked protein VPg3); Protease 3C (EC 3.4.22.28) (Picornain 3C) (P3C) (Protease P20B); RNA-directed RNA polymerase 3D-POL (P3D-POL) (EC 2.7.7.48) (P56A)]
[] Genome polyprotein [Cleaved into: Leader protease (Lpro) (EC 3.4.22.46); Protein VP0 (VP4-VP2); Protein VP4 (P1A) (Virion protein 4); Protein VP2 (P1B) (Virion protein 2); Protein VP3 (P1C) (Virion protein 3); Protein VP1 (P1D) (Virion protein 1); Protein 2A (P2A) (P52); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Protein 3B-1 (P3B-1) (Genome-linked protein VPg1); Protein 3B-2 (P3B-2) (Genome-linked protein VPg2); Protein 3B-3 (P3B-3) (Genome-linked protein VPg3); Protease 3C (EC 3.4.22.28) (Picornain 3C) (P3C) (Protease P20B); RNA-directed RNA polymerase 3D-POL (P3D-POL) (EC 2.7.7.48) (P56A)]
[] Genome polyprotein [Cleaved into: Leader protease (Lpro) (EC 3.4.22.46); Protein VP0 (VP4-VP2); Protein VP4 (P1A) (Virion protein 4); Protein VP2 (P1B) (Virion protein 2); Protein VP3 (P1C) (Virion protein 3); Protein VP1 (P1D) (Virion protein 1); Protein 2A (P2A) (P52); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Protein 3B-1 (P3B-1) (Genome-linked protein VPg1); Protein 3B-2 (P3B-2) (Genome-linked protein VPg2); Protein 3B-3 (P3B-3) (Genome-linked protein VPg3); Protease 3C (EC 3.4.22.28) (Picornain 3C) (P3C) (Protease P20B); RNA-directed RNA polymerase 3D-POL (P3D-POL) (EC 2.7.7.48) (P56A)]

Bibliography :
[23352252] Nucleotide-binding oligomerization domain containing 2: structure, function, and diseases.
[21206965] IL23R, NOD2/CARD15, ATG16L1 and PHOX2B polymorphisms in a group of patients with Crohn's disease and correlation with sub-phenotypes.
[17661913] The role of the selenoprotein S (SELS) gene -105G>A promoter polymorphism in inflammatory bowel disease and regulation of SELS gene expression in intestinal inflammation.