Details for: NOD2

Gene ID: 64127

Symbol: NOD2

Ensembl ID: ENSG00000167207

Description: nucleotide binding oligomerization domain containing 2

Associated with

Other Information

Genular Protein ID: 421911463

Symbol: NOD2_HUMAN

Name: Inflammatory bowel disease protein 1

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 11087742

Title: Nod2, a Nod1/Apaf-1 family member that is restricted to monocytes and activates NF-kappaB.

PubMed ID: 11087742

DOI: 10.1074/jbc.m008072200

PubMed ID: 11385576

Title: Association of NOD2 leucine-rich repeat variants with susceptibility to Crohn's disease.

PubMed ID: 11385576

DOI: 10.1038/35079107

PubMed ID: 20698950

Title: NOD2-C2 - a novel NOD2 isoform activating NF-kappaB in a muramyl dipeptide-independent manner.

PubMed ID: 20698950

DOI: 10.1186/1756-0500-3-224

PubMed ID: 14570728

Title: Expression of NOD2 in Paneth cells: a possible link to Crohn's ileitis.

PubMed ID: 14570728

DOI: 10.1136/gut.52.11.1591

PubMed ID: 12514169

Title: Host recognition of bacterial muramyl dipeptide mediated through NOD2. Implications for Crohn's disease.

PubMed ID: 12514169

DOI: 10.1074/jbc.c200673200

PubMed ID: 12527755

Title: Nod2 is a general sensor of peptidoglycan through muramyl dipeptide (MDP) detection.

PubMed ID: 12527755

DOI: 10.1074/jbc.c200651200

PubMed ID: 12871942

Title: Peptidoglycan molecular requirements allowing detection by Nod1 and Nod2.

PubMed ID: 12871942

DOI: 10.1074/jbc.m307198200

PubMed ID: 12626759

Title: Gene-environment interaction modulated by allelic heterogeneity in inflammatory diseases.

PubMed ID: 12626759

DOI: 10.1073/pnas.0530276100

PubMed ID: 15044951

Title: Regulatory regions and critical residues of NOD2 involved in muramyl dipeptide recognition.

PubMed ID: 15044951

DOI: 10.1038/sj.emboj.7600175

PubMed ID: 15998797

Title: Membrane recruitment of NOD2 in intestinal epithelial cells is essential for nuclear factor-{kappa}B activation in muramyl dipeptide recognition.

PubMed ID: 15998797

DOI: 10.1083/jcb.200502153

PubMed ID: 16203728

Title: A role for Erbin in the regulation of Nod2-dependent NF-kappaB signaling.

PubMed ID: 16203728

DOI: 10.1074/jbc.m508538200

PubMed ID: 17355968

Title: The NOD2-RICK complex signals from the plasma membrane.

PubMed ID: 17355968

DOI: 10.1074/jbc.m606242200

PubMed ID: 18511561

Title: A NOD2-NALP1 complex mediates caspase-1-dependent IL-1beta secretion in response to Bacillus anthracis infection and muramyl dipeptide.

PubMed ID: 18511561

DOI: 10.1073/pnas.0802726105

PubMed ID: 19592251

Title: ITCH K63-ubiquitinates the NOD2 binding protein, RIP2, to influence inflammatory signaling pathways.

PubMed ID: 19592251

DOI: 10.1016/j.cub.2009.06.038

PubMed ID: 19701189

Title: Activation of innate immune antiviral responses by Nod2.

PubMed ID: 19701189

DOI: 10.1038/ni.1782

PubMed ID: 20637199

Title: ATG16L1 and NOD2 interact in an autophagy-dependent antibacterial pathway implicated in Crohn's disease pathogenesis.

PubMed ID: 20637199

DOI: 10.1053/j.gastro.2010.07.006

PubMed ID: 21887730

Title: Control of NOD2 and Rip2-dependent innate immune activation by GEF-H1.

PubMed ID: 21887730

DOI: 10.1002/ibd.21851

PubMed ID: 22857257

Title: The innate immune protein Nod2 binds directly to MDP, a bacterial cell wall fragment.

PubMed ID: 22857257

DOI: 10.1021/ja303883c

PubMed ID: 22700971

Title: The c-Jun N-terminal kinase (JNK)-binding protein (JNKBP1) acts as a negative regulator of NOD2 protein signaling by inhibiting its oligomerization process.

PubMed ID: 22700971

DOI: 10.1074/jbc.m112.355545

PubMed ID: 23019338

Title: Proteasomal degradation of Nod2 protein mediates tolerance to bacterial cell wall components.

PubMed ID: 23019338

DOI: 10.1074/jbc.m112.410027

PubMed ID: 22829933

Title: TRIM27 negatively regulates NOD2 by ubiquitination and proteasomal degradation.

PubMed ID: 22829933

DOI: 10.1371/journal.pone.0041255

PubMed ID: 23376921

Title: TMEM59 defines a novel ATG16L1-binding motif that promotes local activation of LC3.

PubMed ID: 23376921

DOI: 10.1038/emboj.2013.8

PubMed ID: 23711367

Title: A role for the Ankyrin repeat containing protein Ankrd17 in Nod1- and Nod2-mediated inflammatory responses.

PubMed ID: 23711367

DOI: 10.1016/j.febslet.2013.05.037

PubMed ID: 23806334

Title: OTULIN restricts Met1-linked ubiquitination to control innate immune signaling.

PubMed ID: 23806334

DOI: 10.1016/j.molcel.2013.06.004

PubMed ID: 23322906

Title: A genome-wide siRNA screen reveals positive and negative regulators of the NOD2 and NF-kappaB signaling pathways.

PubMed ID: 23322906

DOI: 10.1126/scisignal.2003305

PubMed ID: 24960071

Title: Interaction between NOD2 and CARD9 involves the NOD2 NACHT and the linker region between the NOD2 CARDs and NACHT domain.

PubMed ID: 24960071

DOI: 10.1016/j.febslet.2014.06.035

PubMed ID: 25093298

Title: Blau syndrome polymorphisms in NOD2 identify nucleotide hydrolysis and helical domain 1 as signalling regulators.

PubMed ID: 25093298

DOI: 10.1016/j.febslet.2014.07.029

PubMed ID: 24790089

Title: The molecular chaperone HSP70 binds to and stabilizes NOD2, an important protein involved in Crohn disease.

PubMed ID: 24790089

DOI: 10.1074/jbc.m114.557686

PubMed ID: 25891078

Title: IRGM governs the core autophagy machinery to conduct antimicrobial defense.

PubMed ID: 25891078

DOI: 10.1016/j.molcel.2015.03.020

PubMed ID: 26369908

Title: Identification and biological consequences of the O-GlcNAc modification of the human innate immune receptor, Nod2.

PubMed ID: 26369908

DOI: 10.1093/glycob/cwv076

PubMed ID: 27007849

Title: NOD1 and NOD2 signalling links ER stress with inflammation.

PubMed ID: 27007849

DOI: 10.1038/nature17631

PubMed ID: 27283905

Title: Crystal structure of NOD2 and its implications in human disease.

PubMed ID: 27283905

DOI: 10.1038/ncomms11813

PubMed ID: 27812135

Title: Characterization and Genetic Analyses of New Genes Coding for NOD2 Interacting Proteins.

PubMed ID: 27812135

DOI: 10.1371/journal.pone.0165420

PubMed ID: 27748583

Title: Molecular recognition of muramyl dipeptide occurs in the leucine-rich repeat domain of Nod2.

PubMed ID: 27748583

DOI: 10.1021/acsinfecdis.6b00154

PubMed ID: 23300079

Title: Ubiquitin regulates caspase recruitment domain-mediated signaling by nucleotide-binding oligomerization domain-containing proteins NOD1 and NOD2.

PubMed ID: 23300079

DOI: 10.1074/jbc.m112.413781

PubMed ID: 28436939

Title: An inflammatory bowel disease-risk variant in INAVA decreases pattern recognition receptor-induced outcomes.

PubMed ID: 28436939

DOI: 10.1172/jci86282

PubMed ID: 30279485

Title: RIP2 filament formation is required for NOD2 dependent NF-kappaB signalling.

PubMed ID: 30279485

DOI: 10.1038/s41467-018-06451-3

PubMed ID: 30478312

Title: Structural basis of RIP2 activation and signaling.

PubMed ID: 30478312

DOI: 10.1038/s41467-018-07447-9

PubMed ID: 30559449

Title: Proteasomal degradation of NOD2 by NLRP12 in monocytes promotes bacterial tolerance and colonization by enteropathogens.

PubMed ID: 30559449

DOI: 10.1038/s41467-018-07750-5

PubMed ID: 31649195

Title: Palmitoylation of NOD1 and NOD2 is required for bacterial sensing.

PubMed ID: 31649195

DOI: 10.1126/science.aau6391

PubMed ID: 33942347

Title: Cellular stress promotes NOD1/2-dependent inflammation via the endogenous metabolite sphingosine-1-phosphate.

PubMed ID: 33942347

DOI: 10.15252/embj.2020106272

PubMed ID: 34293401

Title: S-palmitoylation of NOD2 controls its localization to the plasma membrane.

PubMed ID: 34293401

DOI: 10.1016/j.jlr.2021.100097

PubMed ID: 35066577

Title: Palmitoylation restricts SQSTM1/p62-mediated autophagic degradation of NOD2 to modulate inflammation.

PubMed ID: 35066577

DOI: 10.1038/s41418-022-00942-z

PubMed ID: 36221902

Title: Selective autophagy of RIPosomes maintains innate immune homeostasis during bacterial infection.

PubMed ID: 36221902

DOI: 10.15252/embj.2022111289

PubMed ID: 36002575

Title: Phosphorylation of muramyl peptides by NAGK is required for NOD2 activation.

PubMed ID: 36002575

DOI: 10.1038/s41586-022-05125-x

PubMed ID: 11385577

Title: A frameshift mutation in NOD2 associated with susceptibility to Crohn's disease.

PubMed ID: 11385577

DOI: 10.1038/35079114

PubMed ID: 11528384

Title: CARD15 mutations in Blau syndrome.

PubMed ID: 11528384

DOI: 10.1038/ng720

PubMed ID: 15024686

Title: Crohn disease: frequency and nature of CARD15 mutations in Ashkenazi and Sephardi/Oriental Jewish families.

PubMed ID: 15024686

DOI: 10.1086/382226

PubMed ID: 15198989

Title: Regulation of IL-8 and IL-1beta expression in Crohn's disease associated NOD2/CARD15 mutations.

PubMed ID: 15198989

DOI: 10.1093/hmg/ddh182

PubMed ID: 15459013

Title: Early-onset sarcoidosis and CARD15 mutations with constitutive nuclear factor-kappaB activation: common genetic etiology with Blau syndrome.

PubMed ID: 15459013

DOI: 10.1182/blood-2004-07-2972

PubMed ID: 15812565

Title: A new CARD15 mutation in Blau syndrome.

PubMed ID: 15812565

DOI: 10.1038/sj.ejhg.5201404

PubMed ID: 16485124

Title: Eight novel CARD15 variants detected by DNA sequence analysis of the CARD15 gene in 111 patients with inflammatory bowel disease.

PubMed ID: 16485124

DOI: 10.1007/s00251-005-0073-2

PubMed ID: 19479837

Title: NOD2-associated pediatric granulomatous arthritis, an expanding phenotype: study of an international registry and a national cohort in Spain.

PubMed ID: 19479837

DOI: 10.1002/art.24533

PubMed ID: 19116920

Title: Role of the NOD2 genotype in the clinical phenotype of Blau syndrome and early-onset sarcoidosis.

PubMed ID: 19116920

DOI: 10.1002/art.24134

PubMed ID: 19359344

Title: Cardiac infiltration in early-onset sarcoidosis associated with a novel heterozygous mutation, G481D, in CARD15.

PubMed ID: 19359344

DOI: 10.1093/rheumatology/kep061

PubMed ID: 19169908

Title: A novel mutation in the NOD2 gene associated with Blau syndrome: a Norwegian family with four affected members.

PubMed ID: 19169908

DOI: 10.1080/03009740802464194

PubMed ID: 20199415

Title: Sporadic Blau syndrome with onset of widespread granulomatous dermatitis in the newborn period.

PubMed ID: 20199415

DOI: 10.1111/j.1525-1470.2009.01060.x

PubMed ID: 21914217

Title: A new category of autoinflammatory disease associated with NOD2 gene mutations.

PubMed ID: 21914217

DOI: 10.1186/ar3462

PubMed ID: 25692065

Title: A new mutation in blau syndrome.

PubMed ID: 25692065

DOI: 10.1155/2015/463959

PubMed ID: 25724124

Title: Somatic NOD2 mosaicism in Blau syndrome.

PubMed ID: 25724124

DOI: 10.1016/j.jaci.2014.12.1941

PubMed ID: 26070941

Title: NOD2-associated autoinflammatory disease: a large cohort study.

PubMed ID: 26070941

DOI: 10.1093/rheumatology/kev207

PubMed ID: 34251956

Title: A novel pathogenic NOD2 variant in a mother and daughter with Blau syndrome.

PubMed ID: 34251956

DOI: 10.1080/13816810.2021.1946701

Sequence Information:

  • Length: 1040
  • Mass: 115283
  • Checksum: 0037592D96D7DDFF
  • Sequence:
  • 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

Genular Protein ID: 1327207586

Symbol: A0A286YF65_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 15616553

Title: The sequence and analysis of duplication-rich human chromosome 16.

PubMed ID: 15616553

DOI: 10.1038/nature03187

Sequence Information:

  • Length: 793
  • Mass: 88448
  • Checksum: E3D34A4652F34C44
  • Sequence:
  • MCSQEAFQAQ RSQLVELLVS GSLEGFESVL DWLLSWEVLS WEDYEGFHLL GQPLSHLARR 
    LLDTVWNKGT WACQKLIAAA QEAQADSQSP KLHGCWDPHS LHPARDLQSH RPAIVRRLHS 
    HVENMLDLAW ERGFVSQYEC DEIRLPIFTP SQRARRLLDL ATVKANGLAA FLLQHVQELP 
    VPLALPLEAA TCKKYMAKLR TTVSAQSRFL STYDGAETLC LEDIYTENVL EVWADVGMAG 
    PPQKSPATLG LEELFSTPGH LNDDADTVLV VGEAGSGKST LLQRLHLLWA AGQDFQEFLF 
    VFPFSCRQLQ CMAKPLSVRT LLFEHCCWPD VGQEDIFQLL LDHPDRVLLT FDGFDEFKFR 
    FTDRERHCSP TDPTSVQTLL FNLLQGNLLK NARKVVTSRP AAVSAFLRKY IRTEFNLKGF 
    SEQGIELYLR KRHHEPGVAD RLIRLLQETS ALHGLCHLPV FSWMVSKCHQ ELLLQEGGSP 
    KTTTDMYLLI LQHFLLHATP PDSASQGLGP SLLRGRLPTL LHLGRLALWG LGMCCYVFSA 
    QQLQAAQVSP DDISLGFLVR AKGVVPGSTA PLEFLHITFQ CFFAAFYLAL SADVPPALLR 
    HLFNCGRPGN SPMARLLPTM CIQASEGKDS SVAALLQKAE PHNLQITAAF LAGLLSREHW 
    GLLAECQTSE KALLRRQACA RWCLARSLRK HFHSIPPAAP GEAKSVHAMP GFIWLIRSLY 
    EMQEERLARK AARGLNVGHL KLTFCSVGPT ECAALAFVLQ HLRRPVALQL DYNSVGDIGV 
    EQLLPCLGVC KAL

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.