NOD1
entrez
10392
canonical
uniprot
Q9Y239
canonical
ensembl
ENSG00000106100
resolver
ensp
ENSP00000222823
resolver
ensp
ENSP00000416946
resolver
ensp
ENSP00000525608
resolver
ensp
ENSP00000525610
resolver
ensp
ENSP00000525613
resolver
ensp
ENSP00000525615
resolver
ensp
ENSP00000601910
resolver
ensp
ENSP00000626047
resolver
ensp
ENSP00000626049
resolver
ensp
ENSP00000626055
resolver
ensp
ENSP00000626056
resolver
ensp
ENSP00000699641
resolver
ensp
ENSP00000699645
resolver
ensp
ENSP00000782095
resolver
enst
ENST00000434755
resolver
genesymbol
NOD1
resolver
genesymbol_syn
CARD4
resolver
hgnc
HGNC:16390
resolver
uniprot
A0A024RA73
resolver
uniprot
B4DTU3
resolver
uniprot
G3XAL1
resolver
uniprot
Q549U4
resolver
uniprot
Q8IWF5
resolver
uniprot_entry
A0A024RA73_HUMAN
resolver
uniprot_entry
G3XAL1_HUMAN
resolver
uniprot_entry
NOD1_HUMAN
resolver
uniprot_sec
B4DTU3
resolver
uniprot_sec
Q549U4
resolver
uniprot_sec
Q8IWF5
resolver
amino_acid_sequence
MEEQGHSEMEIIPSESHPHIQLLKSNRELLVTHIRNTQCLVDNLLKNDYFSAEDAEIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLLQQLADAYVDLRPWLLEIGFSPSLLTQSKVVVNTDPVSRYTQQLRHHLGRDSKFVLCYAQKEELLLEEIYMDTIMELVGFSNESLGSLNSLACLLDHTTGILNEQGETIFILGDAGVGKSMLLQRLQSLWATGRLDAGVKFFFHFRCRMFSCFKESDRLCLQDLLFKHYCYPERDPEEVFAFLLRFPHVALFTFDGLDELHSDLDLSRVPDSSCPWEPAHPLVLLANLLSGKLLKGASKLLTARTGIEVPRQFLRKKVLLRGFSPSHLRAYARRMFPERALQDRLLSQLEANPNLCSLCSVPLFCWIIFRCFQHFRAAFEGSPQLPDCTMTLTDVFLLVTEVHLNRMQPSSLVQRNTRSPVETLHAGRDTLCSLGQVAHRGMEKSLFVFTQEEVQASGLQERDMQLGFLRALPELGPGGDQQSYEFFHLTLQAFFTAFFLVLDDRVGTQELLRFFQEWMPPAGAATTSCYPPFLPFQCLQGSGPAREDLFKNKDHFQFTNLFLCGLLSKAKQKLLRHLVPAAALRRKRKALWAHLFSSLRGYLKSLPRVQVESFNQVQAMPTFIWMLRCIYETQSQKVGQLAARGICANYLKLTYCNACSADCSALSFVLHHFPKRLALDLDNNNLNDYGVRELQPCFSRLTVLRLSVNQITDGGVKVLSEELTKYKIVTYLGLYNNQITDVGARYVTKILDECKGLTHLKLGKNKITSEGGKYLALAVKNSKSISEVGMWGNQVGDEGAKAFAEALRNHPSLTTLSLASNGISTEGGKSLARALQQNTSLEILWLTQNELNDEVAESLAEMLKVNQTLKHLWLIQNQITAKGTAQLADALQSNTGITEICLNGNLIKPEEAKVYEDEKRIICF
uniprot
proteins
function
FUNCTION: Pattern recognition receptor (PRR) that detects bacterial peptidoglycan fragments and other danger signals and thus participates in both innate and adaptive immune responses (PubMed:11058605, PubMed:12791997, PubMed:12796777, PubMed:15044951, PubMed:16172124, PubMed:19043560, PubMed:22672233, PubMed:27099311). Specifically recognizes and binds gamma-D-glutamyl-meso-diaminopimelic acid (iE-DAP), a dipeptide present in peptidoglycan of Gram-negative bacteria (PubMed:12791997, PubMed:12796777, PubMed:12871942, PubMed:16172124, PubMed:16211083). Preferentially binds iE-DAP in tripeptide-containing muropeptides (MurNAc-TriDAP or TriDAP) (PubMed:16211083). Ligand binding triggers oligomerization that facilitates the binding and subsequent activation of the proximal adapter receptor-interacting RIPK2 (PubMed:12791997, PubMed:12796777, PubMed:17054981). Following recruitment, RIPK2 undergoes 'Met-1'- (linear) and 'Lys-63'-linked polyubiquitination by E3 ubiquitin-protein ligases XIAP, BIRC2, BIRC3 and the LUBAC complex, becoming a scaffolding protein for downstream effectors, triggering activation of the NF-kappa-B and MAP kinases signaling (PubMed:10880512, PubMed:12791997, PubMed:19043560). This in turn leads to the transcriptional activation of hundreds of genes involved in immune response (PubMed:10880512, PubMed:19043560). Also acts as a regulator of antiviral response elicited by dsRNA and the expression of RLR pathway members by targeting IFIH1 and TRAF3 to modulate the formation of IFIH1-MAVS and TRAF3-MAVS complexes leading to increased transcription of type I IFNs (PubMed:32169843). Also acts as a regulator of autophagy via its interaction with ATG16L1, possibly by recruiting ATG16L1 at the site of bacterial entry (By similarity). Besides recognizing pathogens, also involved in the endoplasmic reticulum stress response: acts by sensing and binding to the cytosolic metabolite sphingosine-1-phosphate generated in response to endoplasmic reticulum stress, initiating an inflammation process that leads to activation of the NF-kappa-B and MAP kinases signaling (PubMed:27007849, PubMed:33942347). In addition, plays a role in insulin trafficking in beta cells in a cell-autonomous manner (By similarity). Mechanistically, upon recognizing cognate ligands, NOD1 and RIPK2 localize to insulin vesicles where they recruit RAB1A to direct insulin trafficking through the cytoplasm (By similarity). {ECO:0000250|UniProtKB:Q8BHB0, ECO:0000269|PubMed:10880512, ECO:0000269|PubMed:11058605, ECO:0000269|PubMed:12791997, ECO:0000269|PubMed:12796777, ECO:0000269|PubMed:12871942, ECO:0000269|PubMed:15044951, ECO:0000269|PubMed:16172124, ECO:0000269|PubMed:16211083, ECO:0000269|PubMed:17054981, ECO:0000269|PubMed:19043560, ECO:0000269|PubMed:22672233, ECO:0000269|PubMed:27007849, ECO:0000269|PubMed:27099311, ECO:0000269|PubMed:32169843, ECO:0000269|PubMed:33942347}.; FUNCTION: [Isoform 3]: In contrast to isoform 1, does not efficiently recognize and bind gamma-D-glutamyl-meso-diaminopimelic acid (iE-DAP) ligand. {ECO:0000269|PubMed:16172124}.
uniprot
proteins
mass_dalton
107691
uniprot
proteins
mutagenesis
MUTAGEN 41; /note="V->A: Abolishes interaction with RIPK2/RICK."; /evidence="ECO:0000269|PubMed:10329646, ECO:0000269|PubMed:17054981"; MUTAGEN 41; /note="V->Q: Abolishes caspase-9 activation."; /evidence="ECO:0000269|PubMed:10329646, ECO:0000269|PubMed:17054981"; MUTAGEN 44; /note="L->A: Abolishes activation of NF-kappa-B. No effect on interaction with RIPK2."; /evidence="ECO:0000269|PubMed:17054981"; MUTAGEN 48; /note="D->K: Abolishes activation of NF-kappa-B. No effect on interaction with RIPK2."; /evidence="ECO:0000269|PubMed:17054981"; MUTAGEN 53; /note="E->K: No effect on activation of NF-kappa-B. Abolishes interaction with RIPK2."; /evidence="ECO:0000269|PubMed:17054981"; MUTAGEN 54; /note="D->K: Abolishes activation of NF-kappa-B. Abolishes interaction with RIPK2."; /evidence="ECO:0000269|PubMed:17054981"; MUTAGEN 56; /note="E->K: Abolishes activation of NF-kappa-B. Abolishes interaction with RIPK2."; /evidence="ECO:0000269|PubMed:17054981"; MUTAGEN 69; /note="R->E: Abolishes activation of NF-kappa-B. Abolished interaction with ubiquitin and RIPK2."; /evidence="ECO:0000269|PubMed:17054981, ECO:0000269|PubMed:23300079"; MUTAGEN 84..88; /note="EFFLY->AFFLR: Abolished interaction with ubiquitin without affecting interaction with RIPK2."; /evidence="ECO:0000269|PubMed:23300079"; MUTAGEN 208; /note="K->R: Reduces caspase-9 activation. Reduced binding affinity for NLRP10. Does not associate with cell membrane. Reduced NF-kappa-B activation in response to ligand binding."; /evidence="ECO:0000269|PubMed:10329646, ECO:0000269|PubMed:15044951, ECO:0000269|PubMed:17970764, ECO:0000269|PubMed:22672233"; MUTAGEN 284; /note="D->A: Reduced NF-kappa-B activation in response to ligand binding."; /evidence="ECO:0000269|PubMed:15044951"; MUTAGEN 287; /note="D->A: Reduced binding affinity for NLRP10."; /evidence="ECO:0000269|PubMed:22672233"; MUTAGEN 517; /note="H->A: Loss of activation by sphingosine-1-phosphate."; /evidence="ECO:0000269|PubMed:33942347"; MUTAGEN 558; /note="C->S: Strongly reduced palmitoylation and localization to the cell membrane; when associated with S-567 and S-952."; /evidence="ECO:0000269|PubMed:31649195"; MUTAGEN 567; /note="C->S: Strongly reduced palmitoylation and localization to the cell membrane; when associated with S-558 and S-952."; /evidence="ECO:0000269|PubMed:31649195"; MUTAGEN 711; /note="D->S: Does not associate with cell membrane."; /evidence="ECO:0000269|PubMed:17970764"; MUTAGEN 788; /note="H->S: No effect on association with cell membrane. Reduced binding to gamma-D-glutamyl-meso-diaminopimelic acid (iE-DAP)."; /evidence="ECO:0000269|PubMed:16172124, ECO:0000269|PubMed:17970764"; MUTAGEN 790; /note="K->T: Reduced binding to gamma-D-glutamyl-meso-diaminopimelic acid (iE-DAP)."; /evidence="ECO:0000269|PubMed:16172124"; MUTAGEN 792; /note="G->S: Does not associate with cell membrane. Reduced binding to gamma-D-glutamyl-meso-diaminopimelic acid (iE-DAP)."; /evidence="ECO:0000269|PubMed:16172124, ECO:0000269|PubMed:17970764"; MUTAGEN 816; /note="E->D: Increased binding to gamma-D-glutamyl-meso-diaminopimelic acid (iE-DAP) in tetrapeptide-containing muropeptides (MurNAc-TetraDAP or TetraDAP)."; /evidence="ECO:0000269|PubMed:16172124"; MUTAGEN 816; /note="E->S: Reduced binding to gamma-D-glutamyl-meso-diaminopimelic acid (iE-DAP)."; /evidence="ECO:0000269|PubMed:16172124"; MUTAGEN 818; /note="G->S: Reduced binding to gamma-D-glutamyl-meso-diaminopimelic acid (iE-DAP)."; /evidence="ECO:0000269|PubMed:16172124"; MUTAGEN 820; /note="W->S: Reduced binding to gamma-D-glutamyl-meso-diaminopimelic acid (iE-DAP)."; /evidence="ECO:0000269|PubMed:16172124"; MUTAGEN 874; /note="W->S: Reduced binding to gamma-D-glutamyl-meso-diaminopimelic acid (iE-DAP)."; /evidence="ECO:0000269|PubMed:16172124"; MUTAGEN 877; /note="Q->S: Does not associate with cell membrane."; /evidence="ECO:0000269|PubMed:17970764"; MUTAGEN 952; /note="C->S: Strongly reduced palmitoylation and localization to the cell membrane; when associated with S-558 and S-567."; /evidence="ECO:0000269|PubMed:31649195
uniprot
proteins
post_translational_modification
PTM: Palmitoylated. Palmitoylation is required for proper recruitment to the bacterial entry site and hence for proper signaling upon cognate peptidoglycan detection. {ECO:0000269|PubMed:31649195}.; PTM: Ubiquitinated. 'Lys-48'-linked polyubiquitination by RNF34 promotes proteasomal degradation and thereby negatively regulates NOD1 for instance in NF-kappa-B activation. {ECO:0000269|PubMed:25012219}.; PTM: Degraded via selective autophagy following interaction with IRGM (PubMed:36221902). IRGM promotes NOD1-RIPK2 RIPosome recruitment to autophagosome membranes, promoting their SQSTM1/p62-dependent autophagic degradation (PubMed:36221902). {ECO:0000269|PubMed:36221902}.
uniprot
proteins
protein_family
NOD1-NOD2 family
uniprot
proteins
pubmed
10224040
uniprot
proteins
pubmed
10329646
uniprot
proteins
pubmed
10880512
uniprot
proteins
pubmed
11058605
uniprot
proteins
pubmed
12791997
uniprot
proteins
pubmed
12796777
uniprot
proteins
pubmed
12853948
uniprot
proteins
pubmed
12871942
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15044951
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16172124
uniprot
proteins
pubmed
16211083
uniprot
proteins
pubmed
17054981
uniprot
proteins
pubmed
17173864
uniprot
proteins
pubmed
17970764
uniprot
proteins
pubmed
18186648
uniprot
proteins
pubmed
19043560
uniprot
proteins
pubmed
22672233
uniprot
proteins
pubmed
23300079
uniprot
proteins
pubmed
25012219
uniprot
proteins
pubmed
25127239
uniprot
proteins
pubmed
27007849
uniprot
proteins
pubmed
27099311
uniprot
proteins
pubmed
30478312
uniprot
proteins
pubmed
31649195
uniprot
proteins
pubmed
32169843
uniprot
proteins
pubmed
33942347
uniprot
proteins
pubmed
36221902
uniprot
proteins
sequence_length
953
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:31649195}; Lipid-anchor {ECO:0000269|PubMed:31649195}. Apical cell membrane {ECO:0000269|PubMed:19043560}. Basolateral cell membrane {ECO:0000269|PubMed:19043560}. Cytoplasm {ECO:0000269|PubMed:10329646, ECO:0000269|PubMed:31649195}. Note=Detected in the cytoplasm and at the cell membrane (PubMed:31649195). Following bacterial infection, localizes to bacterial entry sites in the cell membrane (PubMed:31649195). Recruited to the basolateral and apical membranes in polarized epithelial cells (PubMed:19043560). {ECO:0000269|PubMed:19043560, ECO:0000269|PubMed:31649195}.
uniprot
proteins