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Protein

Nucleotide-binding oligomerization domain-containing protein 1

Gene

NOD1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 – 2098ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • CARD domain binding Source: MGI
  • cysteine-type endopeptidase activator activity involved in apoptotic process Source: ProtInc
  • identical protein binding Source: IntAct
  • peptidoglycan binding Source: HGNC
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

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 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:16390. NOD1.

Subcellular locationi

GO - Cellular componenti

  • apical plasma membrane Source: UniProtKB-SubCell
  • basolateral plasma membrane Source: UniProtKB
  • cytoplasm Source: HGNC
  • 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.

Polymorphism and mutation databases

BioMutaiNOD1.
DMDMi20137579.

PTM / Processingi

Molecule processing

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

Post-translational modificationi

Ubiquitinated. 'Lys-48'-linked polyubiquitination by RNF34 promotes proteasomal degradation and thereby negatively regulates NOD1 for instance in NF-kappa-B activition.1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiQ9Y239.
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

BgeeiQ9Y239.
CleanExiHS_NOD1.
ExpressionAtlasiQ9Y239. baseline and differential.
GenevisibleiQ9Y239. HS.

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. Interacts with RNF34.5 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi115664. 25 interactions.
DIPiDIP-41064N.
IntActiQ9Y239. 19 interactions.
MINTiMINT-90728.
STRINGi9606.ENSP00000222823.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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, 642-953.
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.
GeneTreeiENSGT00790000123007.
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. AlignAdd to basket

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

        10         20         30         40         50
MEEQGHSEME IIPSESHPHI QLLKSNRELL VTHIRNTQCL VDNLLKNDYF
60 70 80 90 100
SAEDAEIVCA CPTQPDKVRK ILDLVQSKGE EVSEFFLYLL QQLADAYVDL
110 120 130 140 150
RPWLLEIGFS PSLLTQSKVV VNTDPVSRYT QQLRHHLGRD SKFVLCYAQK
160 170 180 190 200
EELLLEEIYM DTIMELVGFS NESLGSLNSL ACLLDHTTGI LNEQGETIFI
210 220 230 240 250
LGDAGVGKSM LLQRLQSLWA TGRLDAGVKF FFHFRCRMFS CFKESDRLCL
260 270 280 290 300
QDLLFKHYCY PERDPEEVFA FLLRFPHVAL FTFDGLDELH SDLDLSRVPD
310 320 330 340 350
SSCPWEPAHP LVLLANLLSG KLLKGASKLL TARTGIEVPR QFLRKKVLLR
360 370 380 390 400
GFSPSHLRAY ARRMFPERAL QDRLLSQLEA NPNLCSLCSV PLFCWIIFRC
410 420 430 440 450
FQHFRAAFEG SPQLPDCTMT LTDVFLLVTE VHLNRMQPSS LVQRNTRSPV
460 470 480 490 500
ETLHAGRDTL CSLGQVAHRG MEKSLFVFTQ EEVQASGLQE RDMQLGFLRA
510 520 530 540 550
LPELGPGGDQ QSYEFFHLTL QAFFTAFFLV LDDRVGTQEL LRFFQEWMPP
560 570 580 590 600
AGAATTSCYP PFLPFQCLQG SGPAREDLFK NKDHFQFTNL FLCGLLSKAK
610 620 630 640 650
QKLLRHLVPA AALRRKRKAL WAHLFSSLRG YLKSLPRVQV ESFNQVQAMP
660 670 680 690 700
TFIWMLRCIY ETQSQKVGQL AARGICANYL KLTYCNACSA DCSALSFVLH
710 720 730 740 750
HFPKRLALDL DNNNLNDYGV RELQPCFSRL TVLRLSVNQI TDGGVKVLSE
760 770 780 790 800
ELTKYKIVTY LGLYNNQITD VGARYVTKIL DECKGLTHLK LGKNKITSEG
810 820 830 840 850
GKYLALAVKN SKSISEVGMW GNQVGDEGAK AFAEALRNHP SLTTLSLASN
860 870 880 890 900
GISTEGGKSL ARALQQNTSL EILWLTQNEL NDEVAESLAE MLKVNQTLKH
910 920 930 940 950
LWLIQNQITA KGTAQLADAL QSNTGITEIC LNGNLIKPEE AKVYEDEKRI

ICF
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:
EMBLi
GenBanki
DDBJi
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. [Q9Y239-1]
RefSeqiNP_006083.1. NM_006092.2. [Q9Y239-1]
XP_005249625.1. XM_005249568.1. [Q9Y239-1]
XP_005249629.1. XM_005249572.1. [Q9Y239-1]
XP_006715696.1. XM_006715633.2. [Q9Y239-1]
UniGeneiHs.405153.

Genome annotation databases

EnsembliENST00000222823; ENSP00000222823; ENSG00000106100. [Q9Y239-1]
GeneIDi10392.
KEGGihsa:10392.
UCSCiuc003tav.3. human. [Q9Y239-1]
uc010kvs.2. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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. [Q9Y239-1]
RefSeqiNP_006083.1. NM_006092.2. [Q9Y239-1]
XP_005249625.1. XM_005249568.1. [Q9Y239-1]
XP_005249629.1. XM_005249572.1. [Q9Y239-1]
XP_006715696.1. XM_006715633.2. [Q9Y239-1]
UniGeneiHs.405153.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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, 642-953.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115664. 25 interactions.
DIPiDIP-41064N.
IntActiQ9Y239. 19 interactions.
MINTiMINT-90728.
STRINGi9606.ENSP00000222823.

Chemistry

BindingDBiQ9Y239.
ChEMBLiCHEMBL1293222.
GuidetoPHARMACOLOGYi1762.

PTM databases

PhosphoSiteiQ9Y239.

Polymorphism and mutation databases

BioMutaiNOD1.
DMDMi20137579.

Proteomic databases

MaxQBiQ9Y239.
PaxDbiQ9Y239.
PRIDEiQ9Y239.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000222823; ENSP00000222823; ENSG00000106100. [Q9Y239-1]
GeneIDi10392.
KEGGihsa:10392.
UCSCiuc003tav.3. human. [Q9Y239-1]
uc010kvs.2. human.

Organism-specific databases

CTDi10392.
GeneCardsiGC07M030464.
HGNCiHGNC:16390. NOD1.
MIMi605980. gene.
neXtProtiNX_Q9Y239.
PharmGKBiPA162398098.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG275503.
GeneTreeiENSGT00790000123007.
HOGENOMiHOG000113813.
HOVERGENiHBG050793.
InParanoidiQ9Y239.
KOiK08727.
OMAiLCYAQKE.
OrthoDBiEOG7H4DV9.
PhylomeDBiQ9Y239.
TreeFamiTF352118.

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.

Miscellaneous databases

ChiTaRSiNOD1. human.
EvolutionaryTraceiQ9Y239.
GeneWikiiNOD1.
GenomeRNAii10392.
NextBioi35475018.
PROiQ9Y239.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y239.
CleanExiHS_NOD1.
ExpressionAtlasiQ9Y239. baseline and differential.
GenevisibleiQ9Y239. HS.

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]
ProtoNetiSearch...

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. "The E3 ligase RNF34 is a novel negative regulator of the NOD1 pathway."
    Zhang R., Zhao J., Song Y., Wang X., Wang L., Xu J., Song C., Liu F.
    Cell. Physiol. Biochem. 33:1954-1962(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RNF34, UBIQUITINATION BY RNF34.
  11. "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.
  12. "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.
  13. "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.
  14. "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: June 24, 2015
This is version 154 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.