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Q9Y239

- NOD1_HUMAN

UniProt

Q9Y239 - NOD1_HUMAN

Protein

Nucleotide-binding oligomerization domain-containing protein 1

Gene

NOD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    Enhances caspase-9-mediated apoptosis. Induces NF-kappa-B activity via RIPK2 and IKK-gamma. Confers responsiveness to intracellular bacterial lipopolysaccharides (LPS). Forms an intracellular sensing system along with ARHGEF2 for the detection of microbial effectors during cell invasion by pathogens. Required for RHOA and RIPK2 dependent NF-kappa-B signaling pathway activation upon S.flexneri cell invasion. Involved not only in sensing peptidoglycan (PGN)-derived muropeptides but also in the activation of NF-kappa-B by Shigella effector proteins IpgB2 and OspB. Recruits NLRP10 to the cell membrane following bacterial infection.4 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi202 – 2098ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. CARD domain binding Source: MGI
    3. cysteine-type endopeptidase activator activity involved in apoptotic process Source: ProtInc
    4. identical protein binding Source: IntAct
    5. peptidoglycan binding Source: HGNC
    6. protein binding Source: UniProtKB
    7. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
    2. activation of MAPK activity Source: Reactome
    3. apoptotic process Source: ProtInc
    4. defense response Source: HGNC
    5. defense response to bacterium Source: HGNC
    6. defense response to Gram-positive bacterium Source: Ensembl
    7. detection of bacterium Source: HGNC
    8. detection of biotic stimulus Source: HGNC
    9. inflammatory response Source: HGNC
    10. innate immune response Source: Reactome
    11. interleukin-8 biosynthetic process Source: HGNC
    12. intracellular signal transduction Source: HGNC
    13. JNK cascade Source: Reactome
    14. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
    15. MyD88-independent toll-like receptor signaling pathway Source: Reactome
    16. nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway Source: Reactome
    17. nucleotide-binding oligomerization domain containing signaling pathway Source: Reactome
    18. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
    19. positive regulation of dendritic cell antigen processing and presentation Source: BHF-UCL
    20. positive regulation of ERK1 and ERK2 cascade Source: Ensembl
    21. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: MGI
    22. positive regulation of interleukin-6 production Source: Ensembl
    23. positive regulation of JNK cascade Source: Ensembl
    24. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    25. positive regulation of tumor necrosis factor production Source: Ensembl
    26. protein oligomerization Source: HGNC
    27. regulation of apoptotic process Source: InterPro
    28. signal transduction Source: HGNC
    29. stress-activated MAPK cascade Source: Reactome
    30. toll-like receptor 10 signaling pathway Source: Reactome
    31. toll-like receptor 2 signaling pathway Source: Reactome
    32. toll-like receptor 3 signaling pathway Source: Reactome
    33. toll-like receptor 4 signaling pathway Source: Reactome
    34. toll-like receptor 5 signaling pathway Source: Reactome
    35. toll-like receptor 9 signaling pathway Source: Reactome
    36. toll-like receptor signaling pathway Source: Reactome
    37. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
    38. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
    39. TRIF-dependent toll-like receptor signaling pathway Source: Reactome

    Keywords - Biological processi

    Apoptosis, Immunity, Innate immunity

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
    REACT_21368. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
    REACT_21399. activated TAK1 mediates p38 MAPK activation.
    REACT_22442. Interleukin-1 signaling.
    REACT_75776. NOD1/2 Signaling Pathway.
    SignaLinkiQ9Y239.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nucleotide-binding oligomerization domain-containing protein 1
    Alternative name(s):
    Caspase recruitment domain-containing protein 4
    Gene namesi
    Name:NOD1
    Synonyms:CARD4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:16390. NOD1.

    Subcellular locationi

    Cytoplasm. Cell membrane. Apical cell membrane. Basolateral cell membrane
    Note: Detected in the cytoplasm and at the cell membrane. Following bacterial infection, localizes to bacterial entry sites in the cell membrane. Recruited to the basolateral and apical membranes in polarized epithelial cells.

    GO - Cellular componenti

    1. apical plasma membrane Source: UniProtKB-SubCell
    2. basolateral plasma membrane Source: UniProtKB
    3. cytoplasm Source: HGNC
    4. cytosol Source: Reactome
    5. intracellular Source: InterPro

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi41 – 411V → A: Abolishes interaction with RIPK2/RICK. 2 Publications
    Mutagenesisi41 – 411V → Q: Abolishes caspase-9 activation. 2 Publications
    Mutagenesisi44 – 441L → A: Abolishes activation of NF-kappa-B. No effect on interaction with RIPK2. 1 Publication
    Mutagenesisi48 – 481D → K: Abolishes activation of NF-kappa-B. No effect on interaction with RIPK2. 1 Publication
    Mutagenesisi53 – 531E → K: No effect on activation of NF-kappa-B. Abolishes interaction with RIPK2. 1 Publication
    Mutagenesisi54 – 541D → K: Abolishes activation of NF-kappa-B. Abolishes interaction with RIPK2. 1 Publication
    Mutagenesisi56 – 561E → K: Abolishes activation of NF-kappa-B. Abolishes interaction with RIPK2. 1 Publication
    Mutagenesisi69 – 691R → E: Abolishes activation of NF-kappa-B. Abolishes interaction with RIPK2. 1 Publication
    Mutagenesisi208 – 2081K → R: Reduces caspase-9 activation. Reduced binding affinity for NLRP10. Does not associate with cell membrane. 3 Publications
    Mutagenesisi287 – 2871D → A: Reduced binding affinity for NLRP10. 1 Publication
    Mutagenesisi711 – 7111D → S: Does not associate with cell membrane. 1 Publication
    Mutagenesisi788 – 7881H → S: No effect on association with cell membrane. 1 Publication
    Mutagenesisi792 – 7921G → S: Does not associate with cell membrane. 1 Publication
    Mutagenesisi877 – 8771Q → S: Does not associate with cell membrane. 1 Publication

    Organism-specific databases

    PharmGKBiPA162398098.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 953953Nucleotide-binding oligomerization domain-containing protein 1PRO_0000144077Add
    BLAST

    Proteomic databases

    PaxDbiQ9Y239.
    PRIDEiQ9Y239.

    PTM databases

    PhosphoSiteiQ9Y239.

    Expressioni

    Tissue specificityi

    Highly expressed in adult heart, skeletal muscle, pancreas, spleen and ovary. Also detected in placenta, lung, liver, kidney, thymus, testis, small intestine and colon.

    Gene expression databases

    ArrayExpressiQ9Y239.
    BgeeiQ9Y239.
    CleanExiHS_NOD1.
    GenevestigatoriQ9Y239.

    Interactioni

    Subunit structurei

    Homodimer. Self-associates. Binds to caspase-9 and RIPK2 by CARD-CARD interaction. Interacts with ARHGEF2. Interacts with NLRP10 and recruits it to the cell membrane following invasive bacterial infection.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-1051262,EBI-1051262

    Protein-protein interaction databases

    BioGridi115664. 21 interactions.
    DIPiDIP-41064N.
    IntActiQ9Y239. 20 interactions.
    MINTiMINT-90728.
    STRINGi9606.ENSP00000222823.

    Structurei

    Secondary structure

    1
    953
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi18 – 258
    Helixi27 – 337
    Helixi38 – 469
    Helixi52 – 598
    Beta strandi61 – 633
    Helixi64 – 7815
    Helixi80 – 9516
    Helixi98 – 1003
    Helixi101 – 1055

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2B1WNMR-A15-138[»]
    2DBDNMR-A17-110[»]
    2NSNX-ray2.00A16-108[»]
    2NZ7X-ray1.90A/B9-106[»]
    4E9MX-ray2.15A/B/C/D/E/F2-138[»]
    4JQWX-ray2.90A16-108[»]
    ProteinModelPortaliQ9Y239.
    SMRiQ9Y239. Positions 9-106, 194-219, 660-939.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y239.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini15 – 10591CARDPROSITE-ProRule annotationAdd
    BLAST
    Domaini196 – 531336NACHTPROSITE-ProRule annotationAdd
    BLAST
    Repeati632 – 65625LRR 1Add
    BLAST
    Repeati702 – 72524LRR 2Add
    BLAST
    Repeati727 – 75024LRR 3Add
    BLAST
    Repeati755 – 77824LRR 4Add
    BLAST
    Repeati783 – 80624LRR 5Add
    BLAST
    Repeati839 – 86224LRR 6Add
    BLAST
    Repeati867 – 89125LRR 7Add
    BLAST
    Repeati895 – 91824LRR 8Add
    BLAST
    Repeati923 – 94624LRR 9Add
    BLAST

    Sequence similaritiesi

    Contains 1 CARD domain.PROSITE-ProRule annotation
    Contains 9 LRR (leucine-rich) repeats.Curated
    Contains 1 NACHT domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Leucine-rich repeat, Repeat

    Phylogenomic databases

    eggNOGiNOG275503.
    HOGENOMiHOG000113813.
    HOVERGENiHBG050793.
    InParanoidiQ9Y239.
    KOiK08727.
    OMAiLCYAQKE.
    OrthoDBiEOG7H4DV9.
    PhylomeDBiQ9Y239.
    TreeFamiTF352118.

    Family and domain databases

    Gene3Di1.10.533.10. 1 hit.
    InterProiIPR001315. CARD.
    IPR011029. DEATH-like_dom.
    IPR007111. NACHT_NTPase.
    [Graphical view]
    PfamiPF00619. CARD. 1 hit.
    [Graphical view]
    SUPFAMiSSF47986. SSF47986. 1 hit.
    PROSITEiPS50209. CARD. 1 hit.
    PS50837. NACHT. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y239-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MEEQGHSEME IIPSESHPHI QLLKSNRELL VTHIRNTQCL VDNLLKNDYF    50
    SAEDAEIVCA CPTQPDKVRK ILDLVQSKGE EVSEFFLYLL QQLADAYVDL 100
    RPWLLEIGFS PSLLTQSKVV VNTDPVSRYT QQLRHHLGRD SKFVLCYAQK 150
    EELLLEEIYM DTIMELVGFS NESLGSLNSL ACLLDHTTGI LNEQGETIFI 200
    LGDAGVGKSM LLQRLQSLWA TGRLDAGVKF FFHFRCRMFS CFKESDRLCL 250
    QDLLFKHYCY PERDPEEVFA FLLRFPHVAL FTFDGLDELH SDLDLSRVPD 300
    SSCPWEPAHP LVLLANLLSG KLLKGASKLL TARTGIEVPR QFLRKKVLLR 350
    GFSPSHLRAY ARRMFPERAL QDRLLSQLEA NPNLCSLCSV PLFCWIIFRC 400
    FQHFRAAFEG SPQLPDCTMT LTDVFLLVTE VHLNRMQPSS LVQRNTRSPV 450
    ETLHAGRDTL CSLGQVAHRG MEKSLFVFTQ EEVQASGLQE RDMQLGFLRA 500
    LPELGPGGDQ QSYEFFHLTL QAFFTAFFLV LDDRVGTQEL LRFFQEWMPP 550
    AGAATTSCYP PFLPFQCLQG SGPAREDLFK NKDHFQFTNL FLCGLLSKAK 600
    QKLLRHLVPA AALRRKRKAL WAHLFSSLRG YLKSLPRVQV ESFNQVQAMP 650
    TFIWMLRCIY ETQSQKVGQL AARGICANYL KLTYCNACSA DCSALSFVLH 700
    HFPKRLALDL DNNNLNDYGV RELQPCFSRL TVLRLSVNQI TDGGVKVLSE 750
    ELTKYKIVTY LGLYNNQITD VGARYVTKIL DECKGLTHLK LGKNKITSEG 800
    GKYLALAVKN SKSISEVGMW GNQVGDEGAK AFAEALRNHP SLTTLSLASN 850
    GISTEGGKSL ARALQQNTSL EILWLTQNEL NDEVAESLAE MLKVNQTLKH 900
    LWLIQNQITA KGTAQLADAL QSNTGITEIC LNGNLIKPEE AKVYEDEKRI 950
    ICF 953
    Length:953
    Mass (Da):107,691
    Last modified:November 1, 1999 - v1
    Checksum:i0A9DF5FC6487E21A
    GO
    Isoform 2 (identifier: Q9Y239-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         195-249: GETIFILGDA...SCFKESDRLC → AASRKVTGCV...AWTSCTRTWT
         250-953: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:249
    Mass (Da):27,949
    Checksum:i9387E0E72FA907A6
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti266 – 2661E → K.
    Corresponds to variant rs2075820 [ dbSNP | Ensembl ].
    VAR_020371
    Natural varianti372 – 3721D → N.
    Corresponds to variant rs5743342 [ dbSNP | Ensembl ].
    VAR_053624
    Natural varianti447 – 4471R → H.1 Publication
    Corresponds to variant rs2975634 [ dbSNP | Ensembl ].
    VAR_053625
    Natural varianti605 – 6051R → W.
    Corresponds to variant rs5743345 [ dbSNP | Ensembl ].
    VAR_053626
    Natural varianti610 – 6101A → T.
    Corresponds to variant rs5743346 [ dbSNP | Ensembl ].
    VAR_053627

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei195 – 24955GETIF…SDRLC → AASRKVTGCVCRTCSSSTTA TQSGTPRRCLPSCCASPTWP SSPSMAWTSCTRTWT in isoform 2. 1 PublicationVSP_055825Add
    BLAST
    Alternative sequencei250 – 953704Missing in isoform 2. 1 PublicationVSP_055826Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF126484 mRNA. Translation: AAD29125.1.
    AF149774 Genomic DNA. Translation: AAD43922.1.
    AF113925 mRNA. Translation: AAD28350.1.
    AK300367 mRNA. Translation: BAG62105.1.
    AC005154 Genomic DNA. No translation available.
    AC006027 Genomic DNA. Translation: AAS46897.1.
    BC040339 mRNA. Translation: AAH40339.1.
    CCDSiCCDS5427.1.
    RefSeqiNP_006083.1. NM_006092.2.
    XP_005249625.1. XM_005249568.1.
    XP_005249629.1. XM_005249572.1.
    XP_006715696.1. XM_006715633.1.
    UniGeneiHs.405153.

    Genome annotation databases

    EnsembliENST00000222823; ENSP00000222823; ENSG00000106100. [Q9Y239-1]
    GeneIDi10392.
    KEGGihsa:10392.
    UCSCiuc003tav.3. human.

    Polymorphism databases

    DMDMi20137579.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF126484 mRNA. Translation: AAD29125.1 .
    AF149774 Genomic DNA. Translation: AAD43922.1 .
    AF113925 mRNA. Translation: AAD28350.1 .
    AK300367 mRNA. Translation: BAG62105.1 .
    AC005154 Genomic DNA. No translation available.
    AC006027 Genomic DNA. Translation: AAS46897.1 .
    BC040339 mRNA. Translation: AAH40339.1 .
    CCDSi CCDS5427.1.
    RefSeqi NP_006083.1. NM_006092.2.
    XP_005249625.1. XM_005249568.1.
    XP_005249629.1. XM_005249572.1.
    XP_006715696.1. XM_006715633.1.
    UniGenei Hs.405153.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2B1W NMR - A 15-138 [» ]
    2DBD NMR - A 17-110 [» ]
    2NSN X-ray 2.00 A 16-108 [» ]
    2NZ7 X-ray 1.90 A/B 9-106 [» ]
    4E9M X-ray 2.15 A/B/C/D/E/F 2-138 [» ]
    4JQW X-ray 2.90 A 16-108 [» ]
    ProteinModelPortali Q9Y239.
    SMRi Q9Y239. Positions 9-106, 194-219, 660-939.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115664. 21 interactions.
    DIPi DIP-41064N.
    IntActi Q9Y239. 20 interactions.
    MINTi MINT-90728.
    STRINGi 9606.ENSP00000222823.

    Chemistry

    BindingDBi Q9Y239.
    ChEMBLi CHEMBL1293222.
    GuidetoPHARMACOLOGYi 1762.

    PTM databases

    PhosphoSitei Q9Y239.

    Polymorphism databases

    DMDMi 20137579.

    Proteomic databases

    PaxDbi Q9Y239.
    PRIDEi Q9Y239.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000222823 ; ENSP00000222823 ; ENSG00000106100 . [Q9Y239-1 ]
    GeneIDi 10392.
    KEGGi hsa:10392.
    UCSCi uc003tav.3. human.

    Organism-specific databases

    CTDi 10392.
    GeneCardsi GC07M030464.
    HGNCi HGNC:16390. NOD1.
    MIMi 605980. gene.
    neXtProti NX_Q9Y239.
    PharmGKBi PA162398098.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG275503.
    HOGENOMi HOG000113813.
    HOVERGENi HBG050793.
    InParanoidi Q9Y239.
    KOi K08727.
    OMAi LCYAQKE.
    OrthoDBi EOG7H4DV9.
    PhylomeDBi Q9Y239.
    TreeFami TF352118.

    Enzyme and pathway databases

    Reactomei REACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
    REACT_21368. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
    REACT_21399. activated TAK1 mediates p38 MAPK activation.
    REACT_22442. Interleukin-1 signaling.
    REACT_75776. NOD1/2 Signaling Pathway.
    SignaLinki Q9Y239.

    Miscellaneous databases

    EvolutionaryTracei Q9Y239.
    GeneWikii NOD1.
    GenomeRNAii 10392.
    NextBioi 39370.
    PROi Q9Y239.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y239.
    Bgeei Q9Y239.
    CleanExi HS_NOD1.
    Genevestigatori Q9Y239.

    Family and domain databases

    Gene3Di 1.10.533.10. 1 hit.
    InterProi IPR001315. CARD.
    IPR011029. DEATH-like_dom.
    IPR007111. NACHT_NTPase.
    [Graphical view ]
    Pfami PF00619. CARD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47986. SSF47986. 1 hit.
    PROSITEi PS50209. CARD. 1 hit.
    PS50837. NACHT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Endothelial cell.
    2. "Nod1, an Apaf-1-like activator of caspase-9 and nuclear factor-kappaB."
      Inohara N., Koseki T., del Peso L., Hu Y., Yee C., Chen S., Carrio R., Merino J., Liu D., Ni J., Nunez G.
      J. Biol. Chem. 274:14560-14567(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), MUTAGENESIS OF VAL-41 AND LYS-208.
      Tissue: Mammary gland.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Placenta.
    4. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT HIS-447.
      Tissue: Lymph.
    6. "Human Nod1 confers responsiveness to bacterial lipopolysaccharides."
      Inohara N., Ogura Y., Chen F.F., Muto A., Nunez G.
      J. Biol. Chem. 276:2551-2554(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "The pattern-recognition molecule Nod1 is localized at the plasma membrane at sites of bacterial interaction."
      Kufer T.A., Kremmer E., Adam A.C., Philpott D.J., Sansonetti P.J.
      Cell. Microbiol. 10:477-486(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-208; ASP-711; HIS-788; GLY-792 AND GLN-877.
    8. "GEF-H1 mediated control of NOD1 dependent NF-kappaB activation by Shigella effectors."
      Fukazawa A., Alonso C., Kurachi K., Gupta S., Lesser C.F., McCormick B.A., Reinecker H.C.
      PLoS Pathog. 4:E1000228-E1000228(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ARHGEF2.
    9. Cited for: FUNCTION, INTERACTION WITH NLRP10, MUTAGENESIS OF LYS-208 AND ASP-287.
    10. "Solution structure of the CARD domain in human caspase recruitment domain protein 4 (NOD1 protein)."
      RIKEN structural genomics initiative (RSGI)
      Submitted (DEC-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 14-110.
    11. "Crystal structure of the Nod1 caspase activation and recruitment domain."
      Coussens N.P., Mowers J.C., McDonald C., Nunez G., Ramaswamy S.
      Biochem. Biophys. Res. Commun. 353:1-5(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 16-108, SUBUNIT.
    12. "Solution structure of NOD1 CARD and mutational analysis of its interaction with the CARD of downstream kinase RICK."
      Manon F., Favier A., Nunez G., Simorre J.P., Cusack S.
      J. Mol. Biol. 365:160-174(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 15-138, FUNCTION, INTERACTION WITH RIPK2, MUTAGENESIS OF VAL-41; LEU-44; ASP-48; GLU-53; ASP-54; GLU-56 AND ARG-69.
    13. "Monomer/dimer transition of the caspase-recruitment domain of human Nod1."
      Srimathi T., Robbins S.L., Dubas R.L., Hasegawa M., Inohara N., Park Y.C.
      Biochemistry 47:1319-1325(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 9-106, SUBUNIT.

    Entry informationi

    Entry nameiNOD1_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y239
    Secondary accession number(s): B4DTU3, Q549U4, Q8IWF5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 31, 2002
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 145 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3