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Center for Computational Systems Medicine
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Protein Summary

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AS Summary

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Protein Functional Features

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Gene Isoform Structures and Expression Levels

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Protein Structures

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pLDDT Score Distribution

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Ramachandran Plot of Protein Structures

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Potential Active Site Information

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Protein Structure and Feature Comparision

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Protein-Protein Interaction

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Related Drugs

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Related Diseases

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Clinically Important Variants

Protein:NOD1

Protein Summary

check button Gene summary
Gene name: NOD1
ASpdb.0 ID: 10392
Gene
Gene symbol

NOD1

Gene ID

10392

Gene namenucleotide binding oligomerization domain containing 1
SynonymsCARD4|CLR7.1|NLRC1|hNod1
Cytomap

7p14.3

Type of geneprotein-coding
Descriptionnucleotide-binding oligomerization domain-containing protein 1NLR family, CARD domain containing 1caspase recruitment domain family, member 4caspase recruitment domain-containing protein 4nucleotide-binding oligomerization domain, leucine rich repeat
Modification date20240411
UniProtAcc

Q9Y239


check button Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez
PartnerGeneGO IDGO termPubMed ID
GeneNOD1

GO:0002221

pattern recognition receptor signaling pathway

31649195

GeneNOD1

GO:0005737

cytoplasm

10329646

GeneNOD1

GO:0005829

cytosol

31649195

GeneNOD1

GO:0005886

plasma membrane

17970764|31649195

GeneNOD1

GO:0006919

activation of cysteine-type endopeptidase activity involved in apoptotic process

10329646

GeneNOD1

GO:0016045

detection of bacterium

15653568

GeneNOD1

GO:0016323

basolateral plasma membrane

19043560

GeneNOD1

GO:0032757

positive regulation of interleukin-8 production

15653568

GeneNOD1

GO:0035556

intracellular signal transduction

15653568

GeneNOD1

GO:0038187

pattern recognition receptor activity

11058605|12791997|12796777|12871942|23300079|31649195|33942347

GeneNOD1

GO:0042742

defense response to bacterium

11058605|12791997|15653568

GeneNOD1

GO:0042802

identical protein binding

10329646

GeneNOD1

GO:0042834

peptidoglycan binding

12791997|12796777|12871942|16211083

GeneNOD1

GO:0043123

positive regulation of canonical NF-kappaB signal transduction

10329646

GeneNOD1

GO:0043123

positive regulation of canonical NF-kappaB signal transduction

12791997

GeneNOD1

GO:0043130

ubiquitin binding

23300079

GeneNOD1

GO:0043280

positive regulation of cysteine-type endopeptidase activity involved in apoptotic process

10329646

GeneNOD1

GO:0050700

CARD domain binding

10329646

GeneNOD1

GO:0050829

defense response to Gram-negative bacterium

12791997|12796777

GeneNOD1

GO:0051092

positive regulation of NF-kappaB transcription factor activity

17054981|19043560

GeneNOD1

GO:0070427

nucleotide-binding oligomerization domain containing 1 signaling pathway

11058605|12791997|12796777



AS Summary

check button Information of the canonical protein with experimentally identified structure from PDB (2023).
UniProt AccFile namePDB IDMethodResolutionChainStartEnd
Q9Y239-1Q9Y239-1_2nz7_B.pdb2NZ7X-ray1.9B9106

check button ASpdb's canonical and alternatively spliced isoform information.
accession_idgene_namecanonical_idalternative_idcanonical_lengthalternative_lengthcanonical_startcanonical_endtypeoriginalSEQvariationSEQalternative_startalternative_end
Q9Y239NOD1Q9Y239-1Q9Y239-2953249195249SubstitutionGETIFILGDAGVGKSMLLQRLQSLWATGRLDAGVKFFFHFRCRMFSCFKESDRLCAASRKVTGCVCRTCSSSTTATQSGTPRRCLPSCCASPTWPSSPSMAWTSCTRTWT195249
Q9Y239NOD1Q9Y239-1Q9Y239-2953249250953Deletionnonenone249249

check buttonMultiple sequence alignment of our canonical and alternatively spliced NOD1

check button Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of NOD1
UniProt-idENSGENSTENSP
Q9Y239-1ENSG00000106100.11ENST00000222823.9ENSP00000222823.4

UniProt-idNM IDNP ID
Q9Y239-1NM_006092.2NP_006083.1
Q9Y239-1XM_005249568.1XP_005249625.1
Q9Y239-1XM_005249572.1XP_005249629.1
Q9Y239-1XM_006715633.2XP_006715696.1
Q9Y239-1XM_011515079.1XP_011513381.1

check buttonAmino acid sequences of our canonical and alternatively spliced NOD1
accession_idProtein sequence
Q9Y239-1MEEQGHSEMEIIPSESHPHIQLLKSNRELLVTHIRNTQCLVDNLLKNDYFSAEDAEIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLL
QQLADAYVDLRPWLLEIGFSPSLLTQSKVVVNTDPVSRYTQQLRHHLGRDSKFVLCYAQKEELLLEEIYMDTIMELVGFSNESLGSLNSL
ACLLDHTTGILNEQGETIFILGDAGVGKSMLLQRLQSLWATGRLDAGVKFFFHFRCRMFSCFKESDRLCLQDLLFKHYCYPERDPEEVFA
FLLRFPHVALFTFDGLDELHSDLDLSRVPDSSCPWEPAHPLVLLANLLSGKLLKGASKLLTARTGIEVPRQFLRKKVLLRGFSPSHLRAY
ARRMFPERALQDRLLSQLEANPNLCSLCSVPLFCWIIFRCFQHFRAAFEGSPQLPDCTMTLTDVFLLVTEVHLNRMQPSSLVQRNTRSPV
ETLHAGRDTLCSLGQVAHRGMEKSLFVFTQEEVQASGLQERDMQLGFLRALPELGPGGDQQSYEFFHLTLQAFFTAFFLVLDDRVGTQEL
LRFFQEWMPPAGAATTSCYPPFLPFQCLQGSGPAREDLFKNKDHFQFTNLFLCGLLSKAKQKLLRHLVPAAALRRKRKALWAHLFSSLRG
YLKSLPRVQVESFNQVQAMPTFIWMLRCIYETQSQKVGQLAARGICANYLKLTYCNACSADCSALSFVLHHFPKRLALDLDNNNLNDYGV
RELQPCFSRLTVLRLSVNQITDGGVKVLSEELTKYKIVTYLGLYNNQITDVGARYVTKILDECKGLTHLKLGKNKITSEGGKYLALAVKN
SKSISEVGMWGNQVGDEGAKAFAEALRNHPSLTTLSLASNGISTEGGKSLARALQQNTSLEILWLTQNELNDEVAESLAEMLKVNQTLKH
Q9Y239-2MEEQGHSEMEIIPSESHPHIQLLKSNRELLVTHIRNTQCLVDNLLKNDYFSAEDAEIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLL
QQLADAYVDLRPWLLEIGFSPSLLTQSKVVVNTDPVSRYTQQLRHHLGRDSKFVLCYAQKEELLLEEIYMDTIMELVGFSNESLGSLNSL

Protein Functional Features

check buttonMain function of this protein. (from UniProt)
NOD1 (go to UniProt):Q9Y239

check buttonRetention analysis result of protein across 39 protein features of UniProt such as six molecule processing features, 13 region features, four site features, six amino acid modification features, two natural variation features, five experimental info features, and 3 secondary structure features. Here, because of limited space for viewing, we only show the protein feature retention information belong to the 13 regional features. All retention annotation result can be downloaded at

download page

* Minus value of BPloci means that the break pointn is located before the CDS.
- Retained protein feature among the 13 regional features.
Accession_idSubsectionStartEndFuncitonal featureSplicing information
Q9Y239Domain196531Note=NACHT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00136Type=Substitution;Start=195;End=249
Q9Y239Domain196531Note=NACHT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00136Type=Deletion;Start=250;End=953
Q9Y239Repeat632656Note=LRR 1Type=Deletion;Start=250;End=953
Q9Y239Repeat702725Note=LRR 2Type=Deletion;Start=250;End=953
Q9Y239Repeat727750Note=LRR 3Type=Deletion;Start=250;End=953
Q9Y239Repeat755778Note=LRR 4Type=Deletion;Start=250;End=953
Q9Y239Repeat783806Note=LRR 5Type=Deletion;Start=250;End=953
Q9Y239Repeat839862Note=LRR 6Type=Deletion;Start=250;End=953
Q9Y239Repeat867891Note=LRR 7Type=Deletion;Start=250;End=953
Q9Y239Repeat895918Note=LRR 8Type=Deletion;Start=250;End=953
Q9Y239Repeat923946Note=LRR 9Type=Deletion;Start=250;End=953


Gene Isoform Structures and Expression Levels for NOD1

check buttonGene structures of our canonical and alternative spliced genes of NOD1
* Click on the image to open the UCSC genome browser with custom track showing this image in a new window.
gene isoform structure of NOD1

check button Expression levels of gene isoforms across GTEx.
gtex expression

check button Expression levels of gene isoforms across TCGA.
tcga expression


Protein Structures

check button PDB and CIF files of the predicted protein structures
* Here we show the 3D structure of the proteins using Mol*. AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Model confidence is shown from the pLDDT values per residue. pLDDT corresponds to the model’s prediction of its score on the local Distance Difference Test. It is a measure of local accuracy (from AlphfaFold website). To color code individual residues, we transformed individual PDB files into CIF format.
3D view using mol* of Q9Y239-1
3D view using mol* of Q9Y239-2


pLDDT Score Distribution

check button pLDDT score distribution of the predicted protein structures from AlphaFold2
* AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100.
pLDDT distribution across the protein length of Q9Y239-1
all structure
pLDDT distribution across the protein length of Q9Y239-2
all structure


Ramachandran Plot of Protein Structures


check button Ramachandran plot of the torsional angles - phi (φ)and psi (ψ) - of the residues (amino acids) contained in this protein peptide.
Ramachandran plot of Q9Y239-1
all structure
Ramachandran plot of Q9Y239-2
all structure

Potential Active Site Information


check button The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite.
UniProt-idSite scoreSizeD scoreVolumeExposureEnclosureContactPhobicPhilicBalanceDon/AccResidues
Q9Y239-11.1571941.136284.3470.2710.9331.2231.2351.1151.1081.065373,374,377,378,380,381,383,384,397,401,416,417,41
8,419,420,421,587,590,657,660,661,688,690,691,693,
694,718,722
Q9Y239-21.0112841.067919.5830.5720.6430.8560.8380.7951.0531.021141,144,145,146,147,148,155,158,159,160,161,162,16
3,164,165,166,167,168,169,172,174,177,180,183,190,
191,195,197,198,199,200,201,202,203,204,205,206,20
7,223,224,226,227,228,229,230,231,232,233,234

Protein Structure and Feature Comparision


check button Protein Structure Comparision Using Template Modeling Scores (TM-score).
all structure

check button Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Canonical validated structure (PDB)(green)
3D view using mol* of Q9Y239-1_Q9Y239-1_2nz7_B.pdb

check button Protein Structure Comparision Visualization with mol*. between Canonical validated structure (PDB)(orange) vs Alternative predicted structure (AF2)(green)
3D view using mol* of Q9Y239-1_2nz7_B_Q9Y239-2.pdb

check button Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green)
3D view using mol* of Q9Y239-1_Q9Y239-2.pdb

check button Protein Feature Comparison of the protein sequendary structures among the protiens.
./stats/secondary_structure/figure/Q9Y239-1_vs_Q9Y239-2.png
all structure<

check button Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens.
./stats/relative_asa/Q9Y239-1_vs_Q9Y239-2.png
all structure<


Protein-Protein Interaction


check button Interactors from UniProt.
Accession_idSubsectionStartEndFuncitonal featureSplicing information


check button Interactors from STRING.
Gene nameInteractors


Related Drugs to NOD1


check button Drugs targeting this gene/protein.
(DrugBank)
UniProt accessionGene nameDrugBank IDDrug nameDrug groupActions

Related Diseases to NOD1


check button Previous studies relating to the alternative splicing of NOD1 and disease information from the MeSH term (PubMed)
GenePMIDTitleAbstractMeSH IDMeSH term
NOD120403997Genetic variation in 3-hydroxy-3-methylglutaryl CoA reductase modifies the chemopreventive activity of statins for colorectal cancer.Genetic variation in 3-hydroxy-3-methylglutaryl CoA reductase (HMGCR), the rate-limiting enzyme in cholesterol synthesis, modifies the effect of statins on serum cholesterol levels. Long-term use of statins is associated with a reduced risk of colorectal cancer (CRC) in some, but not all, studies. We genotyped variants in 40 candidate genes important for cholesterol synthesis and metabolism in a population-based case-control study of CRC involving 2,138 incident cases and 2,049 population-based controls. We identified a single-nucleotide polymorphism in the HMGCR gene that significantly modified the protective association between statins and CRC risk. Compared with nonusers, the unadjusted odds ratio of CRC among statin users with the A/A genotype of rs12654264 in HMGCR was 0.3 (95% confidence interval, 0.18-0.51) and among statin users with the T/T genotype was 0.66 (95% confidence interval, 0.41-1.06; P-interaction = 0.0012). This genetic variant (A/A genotype of rs12654264) also was associated with lower serum levels of low-density lipoprotein among all cases and controls. In colon cancer cell lines, the reduction in cholesterol levels after statin treatment was substantially stronger in cells carrying the A/A genotype, and this difference was related to alternative splicing involving the HMGCR statin-binding domain. We anticipate that these data may advance the development of personalized statin use for reducing the risk of cancer as well as cardiovascular disease among the approximately 25 million people currently using statins worldwide.D015179Colorectal Neoplasms


Clinically important variants in NOD1


check button (ClinVar, 04/20/2024)
accession_iduniprot_idgene_nameTypeVariantClinical_significance