Nucleotide-binding oligomerization domain-containing protein 2

Details

Name
Nucleotide-binding oligomerization domain-containing protein 2
Synonyms
  • CARD15
  • Caspase recruitment domain-containing protein 15
  • IBD1
  • Inflammatory bowel disease protein 1
Gene Name
NOD2
Organism
Humans
Amino acid sequence
>lcl|BSEQ0051572|Nucleotide-binding oligomerization domain-containing protein 2
MGEEGGSASHDEEERASVLLGHSPGCEMCSQEAFQAQRSQLVELLVSGSLEGFESVLDWL
LSWEVLSWEDYEGFHLLGQPLSHLARRLLDTVWNKGTWACQKLIAAAQEAQADSQSPKLH
GCWDPHSLHPARDLQSHRPAIVRRLHSHVENMLDLAWERGFVSQYECDEIRLPIFTPSQR
ARRLLDLATVKANGLAAFLLQHVQELPVPLALPLEAATCKKYMAKLRTTVSAQSRFLSTY
DGAETLCLEDIYTENVLEVWADVGMAGPPQKSPATLGLEELFSTPGHLNDDADTVLVVGE
AGSGKSTLLQRLHLLWAAGQDFQEFLFVFPFSCRQLQCMAKPLSVRTLLFEHCCWPDVGQ
EDIFQLLLDHPDRVLLTFDGFDEFKFRFTDRERHCSPTDPTSVQTLLFNLLQGNLLKNAR
KVVTSRPAAVSAFLRKYIRTEFNLKGFSEQGIELYLRKRHHEPGVADRLIRLLQETSALH
GLCHLPVFSWMVSKCHQELLLQEGGSPKTTTDMYLLILQHFLLHATPPDSASQGLGPSLL
RGRLPTLLHLGRLALWGLGMCCYVFSAQQLQAAQVSPDDISLGFLVRAKGVVPGSTAPLE
FLHITFQCFFAAFYLALSADVPPALLRHLFNCGRPGNSPMARLLPTMCIQASEGKDSSVA
ALLQKAEPHNLQITAAFLAGLLSREHWGLLAECQTSEKALLRRQACARWCLARSLRKHFH
SIPPAAPGEAKSVHAMPGFIWLIRSLYEMQEERLARKAARGLNVGHLKLTFCSVGPTECA
ALAFVLQHLRRPVALQLDYNSVGDIGVEQLLPCLGVCKALYLRDNNISDRGICKLIECAL
HCEQLQKLALFNNKLTDGCAHSMAKLLACRQNFLALRLGNNYITAAGAQVLAEGLRGNTS
LQFLGFWGNRVGDEGAQALAEALGDHQSLRWLSLVGNNIGSVGAQALALMLAKNVMLEEL
CLEENHLQDEGVCSLAEGLKKNSSLKILKLSNNCITYLGAEALLQALERNDTILEVWLRG
NTFSLEEVDKLGCRDTRLLL
Number of residues
1040
Molecular Weight
115281.675
Theoretical pI
Not Available
GO Classification
Functions
actin binding / ATP binding / CARD domain binding / enzyme binding / Hsp70 protein binding / Hsp90 protein binding / muramyl dipeptide binding / peptidoglycan binding / protein kinase binding
Processes
activation of MAPK activity / cellular response to muramyl dipeptide / cellular response to organic cyclic compound / cellular response to peptidoglycan / cytokine production involved in immune response / cytokine secretion involved in immune response / defense response / defense response to bacterium / detection of bacterium / detection of biotic stimulus / detection of muramyl dipeptide / innate immune response / intracellular signal transduction / JNK cascade / maintenance of gastrointestinal epithelium / negative regulation of macrophage apoptotic process / nucleotide-binding oligomerization domain containing 2 signaling pathway / nucleotide-binding oligomerization domain containing signaling pathway / positive regulation of B cell activation / positive regulation of cytokine production involved in inflammatory response / positive regulation of dendritic cell antigen processing and presentation / positive regulation of dendritic cell cytokine production / positive regulation of epithelial cell proliferation / positive regulation of ERK1 and ERK2 cascade / positive regulation of gamma-delta T cell activation / positive regulation of I-kappaB kinase/NF-kappaB signaling / positive regulation of interleukin-1 beta production / positive regulation of interleukin-1 beta secretion / positive regulation of interleukin-10 production / positive regulation of interleukin-17 production / positive regulation of interleukin-6 production / positive regulation of interleukin-8 production / positive regulation of JNK cascade / positive regulation of MAP kinase activity / positive regulation of NF-kappaB transcription factor activity / positive regulation of NIK/NF-kappaB signaling / positive regulation of nitric-oxide synthase biosynthetic process / positive regulation of Notch signaling pathway / positive regulation of oxidoreductase activity / positive regulation of phosphatidylinositol 3-kinase activity / positive regulation of prostaglandin-E synthase activity / positive regulation of prostaglandin-endoperoxide synthase activity / positive regulation of protein K63-linked ubiquitination / positive regulation of stress-activated MAPK cascade / positive regulation of transcription from RNA polymerase II promoter / positive regulation of tumor necrosis factor production / positive regulation of type 2 immune response / protein deubiquitination / protein oligomerization / regulation of inflammatory response / response to muramyl dipeptide / response to nutrient
Components
basolateral plasma membrane / cell surface / cytoplasm / cytoskeleton / cytosol / Golgi apparatus / plasma membrane / protein complex / vesicle
General 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).
Specific Function
Actin binding
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0051573|Nucleotide-binding oligomerization domain-containing protein 2 (NOD2)
ATGGGGGAAGAGGGTGGTTCAGCCTCTCACGATGAGGAGGAAAGAGCAAGTGTCCTCCTC
GGACATTCTCCGGGTTGTGAAATGTGCTCGCAGGAGGCTTTTCAGGCACAGAGGAGCCAG
CTGGTCGAGCTGCTGGTCTCAGGGTCCCTGGAAGGCTTCGAGAGTGTCCTGGACTGGCTG
CTGTCCTGGGAGGTCCTCTCCTGGGAGGACTACGAGGGCTTCCACCTCCTGGGCCAGCCT
CTCTCCCACTTGGCCAGGCGCCTTCTGGACACCGTCTGGAATAAGGGTACTTGGGCCTGT
CAGAAGCTCATCGCGGCTGCCCAAGAAGCCCAGGCCGACAGCCAGTCCCCCAAGCTGCAT
GGCTGCTGGGACCCCCACTCGCTCCACCCAGCCCGAGACCTGCAGAGTCACCGGCCAGCC
ATTGTCAGGAGGCTCCACAGCCATGTGGAGAACATGCTGGACCTGGCATGGGAGCGGGGT
TTCGTCAGCCAGTATGAATGTGATGAAATCAGGTTGCCGATCTTCACACCGTCCCAGAGG
GCAAGAAGGCTGCTTGATCTTGCCACGGTGAAAGCGAATGGATTGGCTGCCTTCCTTCTA
CAACATGTTCAGGAATTACCAGTCCCATTGGCCCTGCCTTTGGAAGCTGCCACATGCAAG
AAGTATATGGCCAAGCTGAGGACCACGGTGTCTGCTCAGTCTCGCTTCCTCAGTACCTAT
GATGGAGCAGAGACGCTCTGCCTGGAGGACATATACACAGAGAATGTCCTGGAGGTCTGG
GCAGATGTGGGCATGGCTGGACCCCCGCAGAAGAGCCCAGCCACCCTGGGCCTGGAGGAG
CTCTTCAGCACCCCTGGCCACCTCAATGACGATGCGGACACTGTGCTGGTGGTGGGTGAG
GCGGGCAGTGGCAAGAGCACGCTCCTGCAGCGGCTGCACTTGCTGTGGGCTGCAGGGCAA
GACTTCCAGGAATTTCTCTTTGTCTTCCCATTCAGCTGCCGGCAGCTGCAGTGCATGGCC
AAACCACTCTCTGTGCGGACTCTACTCTTTGAGCACTGCTGTTGGCCTGATGTTGGTCAA
GAAGACATCTTCCAGTTACTCCTTGACCACCCTGACCGTGTCCTGTTAACCTTTGATGGC
TTTGACGAGTTCAAGTTCAGGTTCACGGATCGTGAACGCCACTGCTCCCCGACCGACCCC
ACCTCTGTCCAGACCCTGCTCTTCAACCTTCTGCAGGGCAACCTGCTGAAGAATGCCCGC
AAGGTGGTGACCAGCCGTCCGGCCGCTGTGTCGGCGTTCCTCAGGAAGTACATCCGCACC
GAGTTCAACCTCAAGGGCTTCTCTGAACAGGGCATCGAGCTGTACCTGAGGAAGCGCCAT
CATGAGCCCGGGGTGGCGGACCGCCTCATCCGCCTGCTCCAAGAGACCTCAGCCCTGCAC
GGTTTGTGCCACCTGCCTGTCTTCTCATGGATGGTGTCCAAATGCCACCAGGAACTGTTG
CTGCAGGAGGGGGGGTCCCCAAAGACCACTACAGATATGTACCTGCTGATTCTGCAGCAT
TTTCTGCTGCATGCCACCCCCCCAGACTCAGCTTCCCAAGGTCTGGGACCCAGTCTTCTT
CGGGGCCGCCTCCCCACCCTCCTGCACCTGGGCAGACTGGCTCTGTGGGGCCTGGGCATG
TGCTGCTACGTGTTCTCAGCCCAGCAGCTCCAGGCAGCACAGGTCAGCCCTGATGACATT
TCTCTTGGCTTCCTGGTGCGTGCCAAAGGTGTCGTGCCAGGGAGTACGGCGCCCCTGGAA
TTCCTTCACATCACTTTCCAGTGCTTCTTTGCCGCGTTCTACCTGGCACTCAGTGCTGAT
GTGCCACCAGCTTTGCTCAGACACCTCTTCAATTGTGGCAGGCCAGGCAACTCACCAATG
GCCAGGCTCCTGCCCACGATGTGCATCCAGGCCTCGGAGGGAAAGGACAGCAGCGTGGCA
GCTTTGCTGCAGAAGGCCGAGCCGCACAACCTTCAGATCACAGCAGCCTTCCTGGCAGGG
CTGTTGTCCCGGGAGCACTGGGGCCTGCTGGCTGAGTGCCAGACATCTGAGAAGGCCCTG
CTCCGGCGCCAGGCCTGTGCCCGCTGGTGTCTGGCCCGCAGCCTCCGCAAGCACTTCCAC
TCCATCCCGCCAGCTGCACCGGGTGAGGCCAAGAGCGTGCATGCCATGCCCGGGTTCATC
TGGCTCATCCGGAGCCTGTACGAGATGCAGGAGGAGCGGCTGGCTCGGAAGGCTGCACGT
GGCCTGAATGTTGGGCACCTCAAGTTGACATTTTGCAGTGTGGGCCCCACTGAGTGTGCT
GCCCTGGCCTTTGTGCTGCAGCACCTCCGGCGGCCCGTGGCCCTGCAGCTGGACTACAAC
TCTGTGGGTGACATTGGCGTGGAGCAGCTGCTGCCTTGCCTTGGTGTCTGCAAGGCTCTG
TATTTGCGCGATAACAATATCTCAGACCGAGGCATCTGCAAGCTCATTGAATGTGCTCTT
CACTGCGAGCAATTGCAGAAGTTAGCTCTATTCAACAACAAATTGACTGACGGCTGTGCA
CACTCCATGGCTAAGCTCCTTGCATGCAGGCAGAACTTCTTGGCATTGAGGCTGGGGAAT
AACTACATCACTGCCGCGGGAGCCCAAGTGCTGGCCGAGGGGCTCCGAGGCAACACCTCC
TTGCAGTTCCTGGGATTCTGGGGCAACAGAGTGGGTGACGAGGGGGCCCAGGCCCTGGCT
GAAGCCTTGGGTGATCACCAGAGCTTGAGGTGGCTCAGCCTGGTGGGGAACAACATTGGC
AGTGTGGGTGCCCAAGCCTTGGCACTGATGCTGGCAAAGAACGTCATGCTAGAAGAACTC
TGCCTGGAGGAGAACCATCTCCAGGATGAAGGTGTATGTTCTCTCGCAGAAGGACTGAAG
AAAAATTCAAGTTTGAAAATCCTGAAGTTGTCCAATAACTGCATCACCTACCTAGGGGCA
GAAGCCCTCCTGCAGGCCCTTGAAAGGAATGACACCATCCTGGAAGTCTGGCTCCGAGGG
AACACTTTCTCTCTAGAGGAGGTTGACAAGCTCGGCTGCAGGGACACCAGACTCTTGCTT
TGA
Chromosome Location
16
Locus
16q12.1
External Identifiers
ResourceLink
UniProtKB IDQ9HC29
UniProtKB Entry NameNOD2_HUMAN
HGNC IDHGNC:5331
General References
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  2. Hugot JP, Chamaillard M, Zouali H, Lesage S, Cezard JP, Belaiche J, Almer S, Tysk C, O'Morain CA, Gassull M, Binder V, Finkel Y, Cortot A, Modigliani R, Laurent-Puig P, Gower-Rousseau C, Macry J, Colombel JF, Sahbatou M, Thomas G: Association of NOD2 leucine-rich repeat variants with susceptibility to Crohn's disease. Nature. 2001 May 31;411(6837):599-603. doi: 10.1038/35079107. [PubMed:11385576]
  3. 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. 2010 Aug 10;3:224. doi: 10.1186/1756-0500-3-224. [PubMed:20698950]
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  5. Hsu LC, Ali SR, McGillivray S, Tseng PH, Mariathasan S, Humke EW, Eckmann L, Powell JJ, Nizet V, Dixit VM, 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. 2008 Jun 3;105(22):7803-8. doi: 10.1073/pnas.0802726105. Epub 2008 May 29. [PubMed:18511561]
  6. Tao M, Scacheri PC, Marinis JM, Harhaj EW, Matesic LE, Abbott DW: ITCH K63-ubiquitinates the NOD2 binding protein, RIP2, to influence inflammatory signaling pathways. Curr Biol. 2009 Aug 11;19(15):1255-63. doi: 10.1016/j.cub.2009.06.038. Epub 2009 Jul 9. [PubMed:19592251]
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  8. Lecat A, Di Valentin E, Somja J, Jourdan S, Fillet M, Kufer TA, 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. 2012 Aug 24;287(35):29213-26. doi: 10.1074/jbc.M112.355545. Epub 2012 Jun 14. [PubMed:22700971]
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  12. Fiil BK, Damgaard RB, Wagner SA, 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. 2013 Jun 27;50(6):818-30. doi: 10.1016/j.molcel.2013.06.004. [PubMed:23806334]
  13. Parkhouse R, Boyle JP, Mayle S, Sawmynaden K, Rittinger K, Monie TP: Interaction between NOD2 and CARD9 involves the NOD2 NACHT and the linker region between the NOD2 CARDs and NACHT domain. FEBS Lett. 2014 Aug 25;588(17):2830-6. doi: 10.1016/j.febslet.2014.06.035. Epub 2014 Jun 21. [PubMed:24960071]
  14. Parkhouse R, Boyle JP, Monie TP: Blau syndrome polymorphisms in NOD2 identify nucleotide hydrolysis and helical domain 1 as signalling regulators. FEBS Lett. 2014 Sep 17;588(18):3382-9. doi: 10.1016/j.febslet.2014.07.029. Epub 2014 Aug 2. [PubMed:25093298]
  15. Mohanan V, Grimes CL: The molecular chaperone HSP70 binds to and stabilizes NOD2, an important protein involved in Crohn disease. J Biol Chem. 2014 Jul 4;289(27):18987-98. doi: 10.1074/jbc.M114.557686. Epub 2014 Apr 30. [PubMed:24790089]
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  29. de Inocencio J, Mensa-Vilaro A, Tejada-Palacios P, Enriquez-Merayo E, Gonzalez-Roca E, Magri G, Ruiz-Ortiz E, Cerutti A, Yague J, Arostegui JI: Somatic NOD2 mosaicism in Blau syndrome. J Allergy Clin Immunol. 2015 Aug;136(2):484-7.e2. doi: 10.1016/j.jaci.2014.12.1941. Epub 2015 Feb 25. [PubMed:25724124]
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Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB13615Mifamurtideapproved, experimentalyesligandDetails