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Q9Y239

- NOD1_HUMAN

UniProt

Q9Y239 - NOD1_HUMAN

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Protein
Nucleotide-binding oligomerization domain-containing protein 1
Gene
NOD1, CARD4
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 2098ATP Reviewed prediction

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

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.2 Publications

GO - Cellular componenti

  1. apical plasma membrane Source: UniProtKB-SubCell
  2. basolateral plasma membrane Source: UniProtKB
  3. cytoplasm Source: HGNC
  4. cytosol Source: Reactome
Complete GO annotation...

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 1
PRO_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. 3 interactions.
MINTiMINT-90728.
STRINGi9606.ENSP00000222823.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiQ9Y239.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Contains 1 CARD domain.
Contains 1 NACHT domain.

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.
VSP_055825Add
BLAST
Alternative sequencei250 – 953704Missing in isoform 2.
VSP_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.
ENST00000423334; ENSP00000409416; ENSG00000106100.
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. 3 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 .
ENST00000423334 ; ENSP00000409416 ; ENSG00000106100 .
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 144 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

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