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Protein

NACHT, LRR and PYD domains-containing protein 3

Gene

NLRP3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

As the sensor component of the NLRP3 inflammasome, plays a crucial role in innate immunity and inflammation. In response to pathogens and other damage-associated signals, initiates the formation of the inflammasome polymeric complex, made of NLRP3, PYCARD and CASP1 (and possibly CASP4 and CASP5). Recruitement of proCASP1 to the inflammasome promotes its activation and CASP1-catalyzed IL1B and IL18 maturation and secretion in the extracellular milieu. Activation of NLRP3 inflammasome is also required for HMGB1 secretion (PubMed:22801494). The active cytokines and HMGB1 stimulate inflammatory responses. Inflammasomes can also induce pyroptosis, an inflammatory form of programmed cell death. Under resting conditions, NLRP3 is autoinhibited. NLRP3 activation stimuli include extracellular ATP, reactive oxygen species, K+ efflux, crystals of monosodium urate or cholesterol, beta-amyloid fibers, environmental or industrial particles and nanoparticles, etc. However, it is unclear what constitutes the direct NLRP3 activator. Independently of inflammasome activation, regulates the differentiation of T helper 2 (Th2) cells and has a role in Th2 cell-dependent asthma and tumor growth (By similarity). During Th2 differentiation, required for optimal IRF4 binding to IL4 promoter and for IRF4-dependent IL4 transcription. Binds to the consensus DNA sequence 5'-GRRGGNRGAG-3'. May also participate in the transcription of IL5, IL13, GATA3, CCR3, CCR4 and MAF (By similarity).By similarity1 Publication1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi226 – 2338ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • peptidoglycan binding Source: HGNC
  • sequence-specific DNA binding Source: UniProtKB
  • transcription factor binding Source: UniProtKB

GO - Biological processi

  • activation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
  • apoptotic process Source: UniProtKB
  • cellular response to lipopolysaccharide Source: BHF-UCL
  • defense response Source: HGNC
  • defense response to virus Source: Ensembl
  • detection of biotic stimulus Source: HGNC
  • inflammatory response Source: UniProtKB
  • innate immune response Source: Reactome
  • interleukin-18 production Source: Ensembl
  • interleukin-1 beta production Source: Ensembl
  • interleukin-1 secretion Source: Ensembl
  • negative regulation of acute inflammatory response Source: BHF-UCL
  • negative regulation of inflammatory response Source: BHF-UCL
  • negative regulation of interleukin-1 beta secretion Source: BHF-UCL
  • negative regulation of NF-kappaB import into nucleus Source: HGNC
  • negative regulation of NF-kappaB transcription factor activity Source: HGNC
  • NLRP3 inflammasome complex assembly Source: Ensembl
  • nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway Source: Reactome
  • positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: HGNC
  • positive regulation of interleukin-1 beta secretion Source: HGNC
  • positive regulation of interleukin-4 production Source: UniProtKB
  • positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • positive regulation of T-helper 2 cell cytokine production Source: UniProtKB
  • positive regulation of T-helper 2 cell differentiation Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • positive regulation of type 2 immune response Source: UniProtKB
  • protein oligomerization Source: HGNC
  • signal transduction Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Immunity, Inflammatory response, Innate immunity, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-844456. The NLRP3 inflammasome.

Names & Taxonomyi

Protein namesi
Recommended name:
NACHT, LRR and PYD domains-containing protein 3
Alternative name(s):
Angiotensin/vasopressin receptor AII/AVP-like
Caterpiller protein 1.1
Short name:
CLR1.1
Cold-induced autoinflammatory syndrome 1 protein
Cryopyrin
PYRIN-containing APAF1-like protein 1
Gene namesi
Name:NLRP3
Synonyms:C1orf7, CIAS1, NALP3, PYPAF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:16400. NLRP3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: BHF-UCL
  • cytosol Source: Reactome
  • endoplasmic reticulum Source: UniProtKB-SubCell
  • extracellular region Source: UniProtKB-SubCell
  • NLRP3 inflammasome complex Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Inflammasome, Nucleus, Secreted

Pathology & Biotechi

Involvement in diseasei

Familial cold autoinflammatory syndrome 1 (FCAS1)7 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare autosomal dominant systemic inflammatory disease characterized by recurrent episodes of maculopapular rash associated with arthralgias, myalgias, fever and chills, swelling of the extremities, and conjunctivitis after generalized exposure to cold. Rarely, some patients may also develop late-onset renal amyloidosis.
See also OMIM:120100
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti200 – 2001V → M in FCAS1 and MWS. 4 Publications
Corresponds to variant rs121908147 [ dbSNP | Ensembl ].
VAR_013227
Natural varianti262 – 2621R → W in FCAS1 and MWS; spontaneous polymerization into inflammasome speck. 3 Publications
VAR_014104
Natural varianti307 – 3071L → P in FCAS1 and MWS. 2 Publications
VAR_014124
Natural varianti355 – 3551L → P in FCAS1. 1 Publication
Corresponds to variant rs28937896 [ dbSNP | Ensembl ].
VAR_043685
Natural varianti441 – 4411A → V in FCAS1. 1 Publication
VAR_013229
Natural varianti490 – 4901R → K in FCAS1. 1 Publication
Corresponds to variant rs145268073 [ dbSNP | Ensembl ].
VAR_043689
Natural varianti525 – 5251F → C in FCAS1. 1 Publication
VAR_031853
Natural varianti629 – 6291E → G in FCAS1. 1 Publication
VAR_013230
Muckle-Wells syndrome (MWS)5 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA hereditary periodic fever syndrome characterized by fever, chronic recurrent urticaria, arthralgias, progressive sensorineural deafness, and reactive renal amyloidosis. The disease may be severe if generalized reactive amyloidosis occurs.
See also OMIM:191900
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti200 – 2001V → M in FCAS1 and MWS. 4 Publications
Corresponds to variant rs121908147 [ dbSNP | Ensembl ].
VAR_013227
Natural varianti262 – 2621R → W in FCAS1 and MWS; spontaneous polymerization into inflammasome speck. 3 Publications
VAR_014104
Natural varianti305 – 3051D → N in CINCA and MWS; spontaneous polymerization into inflammasome speck. 6 Publications
VAR_014105
Natural varianti307 – 3071L → P in FCAS1 and MWS. 2 Publications
VAR_014124
Natural varianti350 – 3501T → M in MWS and CINCA; spontaneous polymerization into inflammasome speck. 4 Publications
VAR_014366
Natural varianti354 – 3541A → V in MWS. 1 Publication
VAR_013228
Natural varianti441 – 4411A → T in MWS. 1 Publication
VAR_014369
Natural varianti571 – 5711G → R in MWS. 1 Publication
VAR_014107
Chronic infantile neurologic cutaneous and articular syndrome (CINCA)7 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionRare congenital inflammatory disorder characterized by a triad of neonatal onset of cutaneous symptoms, chronic meningitis, and joint manifestations with recurrent fever and inflammation.
See also OMIM:607115
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti174 – 1741I → T in CINCA. 1 Publication
VAR_043679
Natural varianti262 – 2621R → L in CINCA. 1 Publication
VAR_043680
Natural varianti262 – 2621R → P in CINCA. 1 Publication
VAR_043681
Natural varianti266 – 2661L → H in CINCA. 1 Publication
VAR_043682
Natural varianti305 – 3051D → G in CINCA. 1 Publication
VAR_043683
Natural varianti305 – 3051D → N in CINCA and MWS; spontaneous polymerization into inflammasome speck. 6 Publications
VAR_014105
Natural varianti308 – 3081Q → K in CINCA. 1 Publication
VAR_043684
Natural varianti311 – 3111F → S in CINCA. 2 Publications
VAR_014106
Natural varianti350 – 3501T → M in MWS and CINCA; spontaneous polymerization into inflammasome speck. 4 Publications
VAR_014366
Natural varianti356 – 3561E → D in CINCA. 1 Publication
VAR_043686
Natural varianti360 – 3601H → R in CINCA. 1 Publication
VAR_014367
Natural varianti407 – 4071T → P in CINCA. 1 Publication
VAR_043687
Natural varianti438 – 4381T → I in CINCA. 1 Publication
VAR_043688
Natural varianti438 – 4381T → N in CINCA. 1 Publication
VAR_014368
Natural varianti525 – 5251F → L in CINCA. 1 Publication
VAR_043690
Natural varianti572 – 5721Y → C in CINCA. 2 Publications
VAR_043691
Natural varianti575 – 5751F → S in CINCA. 1 Publication
VAR_014108
Natural varianti634 – 6341L → F in CINCA. 1 Publication
VAR_043692
Natural varianti664 – 6641M → T in CINCA. 1 Publication
VAR_014370
Natural varianti861 – 8611Y → C in CINCA. 1 Publication
VAR_023551

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi15 – 151E → R: Complete loss of PYCARD filament nucleation. 1 Publication
Mutagenesisi22 – 232LK → PA: Loss of PYCARD-binding. No effect on GBP5-binding. 1 Publication
Mutagenesisi23 – 231K → E: Complete loss of PYCARD filament nucleation; when associated with E-24. 1 Publication
Mutagenesisi24 – 241K → E: Complete loss of PYCARD filament nucleation; when associated with E-23. 1 Publication
Mutagenesisi27 – 271M → E: Complete loss of PYCARD filament nucleation. 1 Publication
Mutagenesisi43 – 431R → W: Complete loss of PYCARD filament nucleation. 1 Publication
Mutagenesisi64 – 641E → R: Complete loss of PYCARD filament nucleation. 1 Publication
Mutagenesisi82 – 821D → R: Complete loss of PYCARD filament nucleation. 1 Publication

Keywords - Diseasei

Amyloidosis, Deafness, Disease mutation

Organism-specific databases

MalaCardsiNLRP3.
MIMi120100. phenotype.
191900. phenotype.
607115. phenotype.
Orphaneti93365. CINCA syndrome with NLRP3 mutations.
47045. Familial cold urticaria.
575. Muckle-Wells syndrome.
PharmGKBiPA26512.

Chemistry

ChEMBLiCHEMBL1741208.
GuidetoPHARMACOLOGYi1770.

Polymorphism and mutation databases

BioMutaiNLRP3.
DMDMi262527566.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10361036NACHT, LRR and PYD domains-containing protein 3PRO_0000080886Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi8 ↔ 108Redox-active1 Publication

Post-translational modificationi

The disulfide bond in the pyrin domain might play a role in reactive oxygen species-mediated activation.1 Publication
Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked polyubiquitination. Ubiquitination does not lead to degradation, but inhibits inflammasome activation (By similarity). Deubiquitination is catalyzed by BRCC3 and associated with NLRP3 activation and inflammasome assembly. This process can be induced by the activation of Toll-like receptors (by LPS), through a non-transcriptional pathway dependent on the mitochondrial production of reactive oxygen species, and by ATP.By similarity1 Publication

Keywords - PTMi

Disulfide bond, Ubl conjugation

Proteomic databases

PaxDbiQ96P20.
PRIDEiQ96P20.

PTM databases

iPTMnetiQ96P20.
PhosphoSiteiQ96P20.

Expressioni

Tissue specificityi

Predominantly expressed in macrophages. Also expressed in dendritic cells, B- and T-cells (at protein level) (PubMed:11786556) (PubMed:17164409). Expressed in LPS-treated granulocytes, but not in resting cells (at protein level) (PubMed:17164409). Expression in monocytes is very weak (at protein level) (PubMed:17164409). Expressed in stratified non-keratinizing squamous epithelium, including oral, esophageal and ectocervical mucosa and in the Hassall's corpuscles in the thymus. Also, detected in the stratified epithelium covering the bladder and ureter (transitional mucosa) (at protein level) (PubMed:17164409). Expressed in chondrocytes (PubMed:12032915). Expressed at low levels in resting osteoblasts (PubMed:17907925).4 Publications

Inductioni

By activators of Toll-like receptors, such as lipoteichoic acid (LTA) (TLR2), polyinosine-polycytidylic acid (poly(I:C), a synthetic analog of dsRNA) (TLR3) and bacterial lipopolysaccharides (LPS) (TLR4), and by TNF (PubMed:14662828). Up-regulated in osteoblasts after exposure to invasive, but not invasion-defective, strains of Salmonella typhimurium (at protein level) (PubMed:17907925).2 Publications

Gene expression databases

BgeeiQ96P20.
ExpressionAtlasiQ96P20. baseline and differential.
GenevisibleiQ96P20. HS.

Organism-specific databases

HPAiCAB009190.
HPA012878.
HPA017374.

Interactioni

Subunit structurei

Sensor component of NLRP3 inflammasomes. Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation. The core of NLRP3 inflammasomes consists of a signal sensor component (NLRP3), an adapter (ASC/PYCARD), which recruits an effector proinflammatory caspase (CASP1 and, possibly, CASP4 and CASP5). Within the complex, NLRP3 and PYCARD interact via their respective DAPIN/pyrin domains. This interaction initiates speck formation (nucleation) which greatly enhances further addition of soluble PYCARD molecules to the speck in a prion-like polymerization process (PubMed:24630722). NLRP3 localizes at the end of each PYCARD filament (PubMed:24630722). Clustered PYCARD nucleates the formation of CASP1 filaments through the interaction of their respective CARD domains, acting as a platform for CASP1 polymerization (PubMed:24630722). CASP1 filament formation increases local enzyme concentration, resulting in trans-autocleavage and activation. Active CASP1 then processes IL1B and IL18 precursors, leading to the release of mature cytokines in the extracellular milieu and inflammatory response. Reconstituted ternary inflammasomes show star-shaped structures, in which multiple filaments, containing CASP1, protrude radially from a single central hub, containing the sensor protein and PYCARD (PubMed:24630722). In this complex, the sensor protein is sub-stoichiometric to PYCARD, and PYCARD is further substoichiometric to CASP1, suggesting amplifications of signal transduction from the sensor, via the adapter, to the effector (PubMed:24630722). Interacts with MEFV; this interaction targets NLRP3 to degradation by autophagy, hence preventing excessive IL1B- and IL18-mediated inflammation (PubMed:17431422) (PubMed:26347139). Interacts with GBP5 (via DAPIN domain); this interaction promotes inflammasome assembly in response to microbial and soluble, but not crystalline, agents (PubMed:22461501). Interacts with EIF2AK2/PKR; this interaction requires EIF2AK2 activity, is accompanied by EIF2AK2 autophosphorylation and promotes inflammasome assembly in response to specific stimuli (PubMed:22801494). Interacts with PML (isoform PML-1) (via the leucine-rich repeat (LRR) domain); PML-mediated increase in NLRP3 inflammasome activation does not depend upon this interaction (PubMed:23430110). Directly interacts with IRF4 (via the LRR domain); this interaction is required for optimal IRF4 binding to IL4 promoter and efficient IL4 transactivation during differentiation of Th2 helper T cells (By similarity).By similarity2 Publications9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MAVSQ7Z4344EBI-6253230,EBI-995373
PYCARDQ9ULZ38EBI-6253230,EBI-751215

Protein-protein interaction databases

BioGridi125319. 8 interactions.
DIPiDIP-41153N.
IntActiQ96P20. 36 interactions.
MINTiMINT-230535.
STRINGi9606.ENSP00000337383.

Structurei

Secondary structure

1
1036
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 1510Combined sources
Helixi19 – 3012Combined sources
Beta strandi34 – 374Combined sources
Helixi43 – 486Combined sources
Helixi51 – 6212Combined sources
Helixi64 – 7714Combined sources
Helixi81 – 899Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3QF2X-ray1.70A/B3-112[»]
ProteinModelPortaliQ96P20.
SMRiQ96P20. Positions 5-110.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9393PyrinPROSITE-ProRule annotationAdd
BLAST
Domaini220 – 536317NACHTPROSITE-ProRule annotationAdd
BLAST
Repeati742 – 76221LRR 1Add
BLAST
Repeati771 – 79222LRR 2Add
BLAST
Repeati799 – 81921LRR 3Add
BLAST
Repeati828 – 84922LRR 4Add
BLAST
Repeati856 – 87621LRR 5Add
BLAST
Repeati885 – 90622LRR 6Add
BLAST
Repeati913 – 93321LRR 7Add
BLAST
Repeati942 – 96322LRR 8Add
BLAST
Repeati970 – 99122LRR 9Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi690 – 6978Poly-Glu

Domaini

The pyrin domain (also called DAPIN domain or PYD) is involved in PYCARD-binding.1 Publication
The LRR domain mediates the interaction with IRF4 and PML.By similarity1 Publication
Intramolecular interactions between NACHT and leucine-rich repeat (LRR) domains may be important for autoinhibition in the absence of activating signal.By similarity1 Publication

Sequence similaritiesi

Belongs to the NLRP family.Curated
Contains 9 LRR (leucine-rich) repeats.Curated
Contains 1 NACHT domain.PROSITE-ProRule annotation
Contains 1 pyrin domain.PROSITE-ProRule annotation

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiENOG410IE5X. Eukaryota.
ENOG4111H3D. LUCA.
GeneTreeiENSGT00820000126959.
HOVERGENiHBG063656.
InParanoidiQ96P20.
KOiK12800.
OMAiNCHRVES.
OrthoDBiEOG7P5T07.
PhylomeDBiQ96P20.
TreeFamiTF340267.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
3.80.10.10. 1 hit.
InterProiIPR004020. DAPIN.
IPR011029. DEATH-like_dom.
IPR032675. L_dom-like.
IPR003590. Leu-rich_rpt_RNase_inh_sub-typ.
IPR007111. NACHT_NTPase.
IPR029495. NATCH-assoc.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF14484. FISNA. 1 hit.
PF02758. PYRIN. 1 hit.
[Graphical view]
SMARTiSM00368. LRR_RI. 3 hits.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEiPS50824. DAPIN. 1 hit.
PS50837. NACHT. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 2 (identifier: Q96P20-1) [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
MKMASTRCKL ARYLEDLEDV DLKKFKMHLE DYPPQKGCIP LPRGQTEKAD
60 70 80 90 100
HVDLATLMID FNGEEKAWAM AVWIFAAINR RDLYEKAKRD EPKWGSDNAR
110 120 130 140 150
VSNPTVICQE DSIEEEWMGL LEYLSRISIC KMKKDYRKKY RKYVRSRFQC
160 170 180 190 200
IEDRNARLGE SVSLNKRYTR LRLIKEHRSQ QEREQELLAI GKTKTCESPV
210 220 230 240 250
SPIKMELLFD PDDEHSEPVH TVVFQGAAGI GKTILARKMM LDWASGTLYQ
260 270 280 290 300
DRFDYLFYIH CREVSLVTQR SLGDLIMSCC PDPNPPIHKI VRKPSRILFL
310 320 330 340 350
MDGFDELQGA FDEHIGPLCT DWQKAERGDI LLSSLIRKKL LPEASLLITT
360 370 380 390 400
RPVALEKLQH LLDHPRHVEI LGFSEAKRKE YFFKYFSDEA QARAAFSLIQ
410 420 430 440 450
ENEVLFTMCF IPLVCWIVCT GLKQQMESGK SLAQTSKTTT AVYVFFLSSL
460 470 480 490 500
LQPRGGSQEH GLCAHLWGLC SLAADGIWNQ KILFEESDLR NHGLQKADVS
510 520 530 540 550
AFLRMNLFQK EVDCEKFYSF IHMTFQEFFA AMYYLLEEEK EGRTNVPGSR
560 570 580 590 600
LKLPSRDVTV LLENYGKFEK GYLIFVVRFL FGLVNQERTS YLEKKLSCKI
610 620 630 640 650
SQQIRLELLK WIEVKAKAKK LQIQPSQLEL FYCLYEMQEE DFVQRAMDYF
660 670 680 690 700
PKIEINLSTR MDHMVSSFCI ENCHRVESLS LGFLHNMPKE EEEEEKEGRH
710 720 730 740 750
LDMVQCVLPS SSHAACSHGL VNSHLTSSFC RGLFSVLSTS QSLTELDLSD
760 770 780 790 800
NSLGDPGMRV LCETLQHPGC NIRRLWLGRC GLSHECCFDI SLVLSSNQKL
810 820 830 840 850
VELDLSDNAL GDFGIRLLCV GLKHLLCNLK KLWLVSCCLT SACCQDLASV
860 870 880 890 900
LSTSHSLTRL YVGENALGDS GVAILCEKAK NPQCNLQKLG LVNSGLTSVC
910 920 930 940 950
CSALSSVLST NQNLTHLYLR GNTLGDKGIK LLCEGLLHPD CKLQVLELDN
960 970 980 990 1000
CNLTSHCCWD LSTLLTSSQS LRKLSLGNND LGDLGVMMFC EVLKQQSCLL
1010 1020 1030
QNLGLSEMYF NYETKSALET LQEEKPELTV VFEPSW
Length:1,036
Mass (Da):118,173
Last modified:November 3, 2009 - v3
Checksum:i4C1DFB2B5B283CE8
GO
Isoform 1 (identifier: Q96P20-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     721-777: Missing.
     836-892: Missing.

Show »
Length:922
Mass (Da):105,975
Checksum:i8680FA0F4259B6F8
GO
Isoform 3 (identifier: Q96P20-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     720-1036: Missing.

Show »
Length:719
Mass (Da):83,533
Checksum:i0BF2090304B74886
GO
Isoform 4 (identifier: Q96P20-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     721-777: Missing.

Show »
Length:979
Mass (Da):111,884
Checksum:iDB355ECE3BF0A226
GO
Isoform 5 (identifier: Q96P20-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     836-892: Missing.

Note: No experimental confirmation available.
Show »
Length:979
Mass (Da):112,263
Checksum:i8E46F79B1A816B5E
GO
Isoform 6 (identifier: Q96P20-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     776-796: WLGRCGLSHECCFDISLVLSS → C

Note: No experimental confirmation available.
Show »
Length:1,016
Mass (Da):115,968
Checksum:iCE6980B309C3322D
GO

Sequence cautioni

The sequence AAC39910.1 differs from that shown. Reason: Frameshift at positions 893, 918 and 926. Curated
The sequence AAL12497.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAL12498.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAL33908.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAL65136.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAD92128.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAG37494.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti167 – 1671R → L in AAL78632 (PubMed:12355493).Curated
Sequence conflicti167 – 1671R → L in AAM14669 (PubMed:12355493).Curated
Sequence conflicti167 – 1671R → L in AAL14640 (PubMed:12355493).Curated
Sequence conflicti323 – 3231Q → H in AAL78632 (PubMed:12355493).Curated
Sequence conflicti323 – 3231Q → H in AAM14669 (PubMed:12355493).Curated
Sequence conflicti323 – 3231Q → H in AAL14640 (PubMed:12355493).Curated
Sequence conflicti439 – 4391T → S in AAC39910 (PubMed:11042152).Curated
Sequence conflicti523 – 5231M → V in BAG37494 (Ref. 5) Curated
Sequence conflicti599 – 5991K → M in AAC39910 (PubMed:11042152).Curated
Sequence conflicti617 – 6171K → N in AAL78632 (PubMed:12355493).Curated
Sequence conflicti617 – 6171K → N in AAM14669 (PubMed:12355493).Curated
Sequence conflicti617 – 6171K → N in AAL14640 (PubMed:12355493).Curated
Sequence conflicti622 – 6232QI → HD in AAC39910 (PubMed:11042152).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti174 – 1741I → T in CINCA. 1 Publication
VAR_043679
Natural varianti200 – 2001V → M in FCAS1 and MWS. 4 Publications
Corresponds to variant rs121908147 [ dbSNP | Ensembl ].
VAR_013227
Natural varianti262 – 2621R → L in CINCA. 1 Publication
VAR_043680
Natural varianti262 – 2621R → P in CINCA. 1 Publication
VAR_043681
Natural varianti262 – 2621R → W in FCAS1 and MWS; spontaneous polymerization into inflammasome speck. 3 Publications
VAR_014104
Natural varianti266 – 2661L → H in CINCA. 1 Publication
VAR_043682
Natural varianti305 – 3051D → G in CINCA. 1 Publication
VAR_043683
Natural varianti305 – 3051D → N in CINCA and MWS; spontaneous polymerization into inflammasome speck. 6 Publications
VAR_014105
Natural varianti307 – 3071L → P in FCAS1 and MWS. 2 Publications
VAR_014124
Natural varianti308 – 3081Q → K in CINCA. 1 Publication
VAR_043684
Natural varianti311 – 3111F → S in CINCA. 2 Publications
VAR_014106
Natural varianti350 – 3501T → M in MWS and CINCA; spontaneous polymerization into inflammasome speck. 4 Publications
VAR_014366
Natural varianti354 – 3541A → V in MWS. 1 Publication
VAR_013228
Natural varianti355 – 3551L → P in FCAS1. 1 Publication
Corresponds to variant rs28937896 [ dbSNP | Ensembl ].
VAR_043685
Natural varianti356 – 3561E → D in CINCA. 1 Publication
VAR_043686
Natural varianti360 – 3601H → R in CINCA. 1 Publication
VAR_014367
Natural varianti407 – 4071T → P in CINCA. 1 Publication
VAR_043687
Natural varianti438 – 4381T → I in CINCA. 1 Publication
VAR_043688
Natural varianti438 – 4381T → N in CINCA. 1 Publication
VAR_014368
Natural varianti441 – 4411A → T in MWS. 1 Publication
VAR_014369
Natural varianti441 – 4411A → V in FCAS1. 1 Publication
VAR_013229
Natural varianti490 – 4901R → K in FCAS1. 1 Publication
Corresponds to variant rs145268073 [ dbSNP | Ensembl ].
VAR_043689
Natural varianti525 – 5251F → C in FCAS1. 1 Publication
VAR_031853
Natural varianti525 – 5251F → L in CINCA. 1 Publication
VAR_043690
Natural varianti571 – 5711G → R in MWS. 1 Publication
VAR_014107
Natural varianti572 – 5721Y → C in CINCA. 2 Publications
VAR_043691
Natural varianti575 – 5751F → S in CINCA. 1 Publication
VAR_014108
Natural varianti629 – 6291E → G in FCAS1. 1 Publication
VAR_013230
Natural varianti634 – 6341L → F in CINCA. 1 Publication
VAR_043692
Natural varianti664 – 6641M → T in CINCA. 1 Publication
VAR_014370
Natural varianti705 – 7051Q → K.1 Publication
Corresponds to variant rs35829419 [ dbSNP | Ensembl ].
VAR_043693
Natural varianti861 – 8611Y → C in CINCA. 1 Publication
VAR_023551

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei720 – 1036317Missing in isoform 3. 1 PublicationVSP_005519Add
BLAST
Alternative sequencei721 – 77757Missing in isoform 1 and isoform 4. 6 PublicationsVSP_005520Add
BLAST
Alternative sequencei776 – 79621WLGRC…LVLSS → C in isoform 6. 1 PublicationVSP_053714Add
BLAST
Alternative sequencei836 – 89257Missing in isoform 1 and isoform 5. 6 PublicationsVSP_005521Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF410477 mRNA. Translation: AAL33908.1. Different initiation.
AF427617 mRNA. Translation: AAL33911.1.
AY051117
, AY051112, AY051113, AY051114, AY051115, AY051116, AY056059, AY056060 Genomic DNA. Translation: AAL12497.1. Different initiation.
AY051117
, AY051112, AY051113, AY051114, AY051115, AY051116 Genomic DNA. Translation: AAL12498.1. Different initiation.
AF468522 mRNA. Translation: AAL78632.1.
AF420469 mRNA. Translation: AAL65136.1. Different initiation.
AY092033 mRNA. Translation: AAM14669.1.
AF418985 mRNA. Translation: AAL14640.2.
AK314998 mRNA. Translation: BAG37494.1. Different initiation.
AB208891 mRNA. Translation: BAD92128.1. Different initiation.
AC104335 Genomic DNA. No translation available.
AL606804 Genomic DNA. No translation available.
CH471148 Genomic DNA. Translation: EAW77184.1.
CH471148 Genomic DNA. Translation: EAW77186.1.
BC117211 mRNA. Translation: AAI17212.1.
BC143359 mRNA. Translation: AAI43360.1.
BC143362 mRNA. Translation: AAI43363.1.
BC143363 mRNA. Translation: AAI43364.1.
AY422168 mRNA. Translation: AAQ98889.1.
AF054176 mRNA. Translation: AAC39910.1. Frameshift.
CCDSiCCDS1632.1. [Q96P20-1]
CCDS1633.1. [Q96P20-2]
CCDS44346.1. [Q96P20-5]
CCDS44347.1. [Q96P20-4]
RefSeqiNP_001073289.1. NM_001079821.2. [Q96P20-1]
NP_001120933.1. NM_001127461.2. [Q96P20-5]
NP_001120934.1. NM_001127462.2. [Q96P20-4]
NP_001230062.1. NM_001243133.1.
NP_004886.3. NM_004895.4. [Q96P20-1]
NP_899632.1. NM_183395.2. [Q96P20-2]
XP_005273093.1. XM_005273036.2. [Q96P20-1]
XP_005273094.1. XM_005273037.2. [Q96P20-1]
XP_011542350.1. XM_011544048.1. [Q96P20-1]
XP_011542351.1. XM_011544049.1. [Q96P20-1]
XP_011542352.1. XM_011544050.1. [Q96P20-1]
XP_011542353.1. XM_011544051.1. [Q96P20-1]
XP_011542354.1. XM_011544052.1. [Q96P20-4]
XP_011542356.1. XM_011544054.1. [Q96P20-2]
UniGeneiHs.159483.

Genome annotation databases

EnsembliENST00000336119; ENSP00000337383; ENSG00000162711. [Q96P20-1]
ENST00000348069; ENSP00000294752; ENSG00000162711. [Q96P20-2]
ENST00000366496; ENSP00000355452; ENSG00000162711. [Q96P20-5]
ENST00000366497; ENSP00000355453; ENSG00000162711. [Q96P20-5]
ENST00000391827; ENSP00000375703; ENSG00000162711. [Q96P20-4]
ENST00000391828; ENSP00000375704; ENSG00000162711. [Q96P20-1]
GeneIDi114548.
KEGGihsa:114548.
UCSCiuc001icr.3. human. [Q96P20-1]
uc001ics.3. human. [Q96P20-5]
uc001icv.3. human. [Q96P20-2]
uc001icw.3. human. [Q96P20-4]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

INFEVERS

Repertory of FMF and hereditary autoinflammatory disorders mutations

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF410477 mRNA. Translation: AAL33908.1. Different initiation.
AF427617 mRNA. Translation: AAL33911.1.
AY051117
, AY051112, AY051113, AY051114, AY051115, AY051116, AY056059, AY056060 Genomic DNA. Translation: AAL12497.1. Different initiation.
AY051117
, AY051112, AY051113, AY051114, AY051115, AY051116 Genomic DNA. Translation: AAL12498.1. Different initiation.
AF468522 mRNA. Translation: AAL78632.1.
AF420469 mRNA. Translation: AAL65136.1. Different initiation.
AY092033 mRNA. Translation: AAM14669.1.
AF418985 mRNA. Translation: AAL14640.2.
AK314998 mRNA. Translation: BAG37494.1. Different initiation.
AB208891 mRNA. Translation: BAD92128.1. Different initiation.
AC104335 Genomic DNA. No translation available.
AL606804 Genomic DNA. No translation available.
CH471148 Genomic DNA. Translation: EAW77184.1.
CH471148 Genomic DNA. Translation: EAW77186.1.
BC117211 mRNA. Translation: AAI17212.1.
BC143359 mRNA. Translation: AAI43360.1.
BC143362 mRNA. Translation: AAI43363.1.
BC143363 mRNA. Translation: AAI43364.1.
AY422168 mRNA. Translation: AAQ98889.1.
AF054176 mRNA. Translation: AAC39910.1. Frameshift.
CCDSiCCDS1632.1. [Q96P20-1]
CCDS1633.1. [Q96P20-2]
CCDS44346.1. [Q96P20-5]
CCDS44347.1. [Q96P20-4]
RefSeqiNP_001073289.1. NM_001079821.2. [Q96P20-1]
NP_001120933.1. NM_001127461.2. [Q96P20-5]
NP_001120934.1. NM_001127462.2. [Q96P20-4]
NP_001230062.1. NM_001243133.1.
NP_004886.3. NM_004895.4. [Q96P20-1]
NP_899632.1. NM_183395.2. [Q96P20-2]
XP_005273093.1. XM_005273036.2. [Q96P20-1]
XP_005273094.1. XM_005273037.2. [Q96P20-1]
XP_011542350.1. XM_011544048.1. [Q96P20-1]
XP_011542351.1. XM_011544049.1. [Q96P20-1]
XP_011542352.1. XM_011544050.1. [Q96P20-1]
XP_011542353.1. XM_011544051.1. [Q96P20-1]
XP_011542354.1. XM_011544052.1. [Q96P20-4]
XP_011542356.1. XM_011544054.1. [Q96P20-2]
UniGeneiHs.159483.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3QF2X-ray1.70A/B3-112[»]
ProteinModelPortaliQ96P20.
SMRiQ96P20. Positions 5-110.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125319. 8 interactions.
DIPiDIP-41153N.
IntActiQ96P20. 36 interactions.
MINTiMINT-230535.
STRINGi9606.ENSP00000337383.

Chemistry

ChEMBLiCHEMBL1741208.
GuidetoPHARMACOLOGYi1770.

PTM databases

iPTMnetiQ96P20.
PhosphoSiteiQ96P20.

Polymorphism and mutation databases

BioMutaiNLRP3.
DMDMi262527566.

Proteomic databases

PaxDbiQ96P20.
PRIDEiQ96P20.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000336119; ENSP00000337383; ENSG00000162711. [Q96P20-1]
ENST00000348069; ENSP00000294752; ENSG00000162711. [Q96P20-2]
ENST00000366496; ENSP00000355452; ENSG00000162711. [Q96P20-5]
ENST00000366497; ENSP00000355453; ENSG00000162711. [Q96P20-5]
ENST00000391827; ENSP00000375703; ENSG00000162711. [Q96P20-4]
ENST00000391828; ENSP00000375704; ENSG00000162711. [Q96P20-1]
GeneIDi114548.
KEGGihsa:114548.
UCSCiuc001icr.3. human. [Q96P20-1]
uc001ics.3. human. [Q96P20-5]
uc001icv.3. human. [Q96P20-2]
uc001icw.3. human. [Q96P20-4]

Organism-specific databases

CTDi114548.
GeneCardsiNLRP3.
HGNCiHGNC:16400. NLRP3.
HPAiCAB009190.
HPA012878.
HPA017374.
MalaCardsiNLRP3.
MIMi120100. phenotype.
191900. phenotype.
606416. gene.
607115. phenotype.
neXtProtiNX_Q96P20.
Orphaneti93365. CINCA syndrome with NLRP3 mutations.
47045. Familial cold urticaria.
575. Muckle-Wells syndrome.
PharmGKBiPA26512.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IE5X. Eukaryota.
ENOG4111H3D. LUCA.
GeneTreeiENSGT00820000126959.
HOVERGENiHBG063656.
InParanoidiQ96P20.
KOiK12800.
OMAiNCHRVES.
OrthoDBiEOG7P5T07.
PhylomeDBiQ96P20.
TreeFamiTF340267.

Enzyme and pathway databases

ReactomeiR-HSA-844456. The NLRP3 inflammasome.

Miscellaneous databases

GeneWikiiNALP3.
GenomeRNAii114548.
NextBioi35481188.
PROiQ96P20.
SOURCEiSearch...

Gene expression databases

BgeeiQ96P20.
ExpressionAtlasiQ96P20. baseline and differential.
GenevisibleiQ96P20. HS.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
3.80.10.10. 1 hit.
InterProiIPR004020. DAPIN.
IPR011029. DEATH-like_dom.
IPR032675. L_dom-like.
IPR003590. Leu-rich_rpt_RNase_inh_sub-typ.
IPR007111. NACHT_NTPase.
IPR029495. NATCH-assoc.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF14484. FISNA. 1 hit.
PF02758. PYRIN. 1 hit.
[Graphical view]
SMARTiSM00368. LRR_RI. 3 hits.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEiPS50824. DAPIN. 1 hit.
PS50837. NACHT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mutation of a new gene encoding a putative pyrin-like protein causes familial cold autoinflammatory syndrome and Muckle-Wells syndrome."
    Hoffman H.M., Mueller J.L., Broide D.H., Wanderer A.A., Kolodner R.D.
    Nat. Genet. 29:301-305(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), VARIANTS FCAS1 MET-200; VAL-441 AND GLY-629, VARIANT MWS VAL-354.
  2. "Association of mutations in the NALP3/CIAS1/PYPAF1 gene with a broad phenotype including recurrent fever, cold sensitivity, sensorineural deafness, and AA amyloidosis."
    Aganna E., Martinon F., Hawkins P.N., Ross J.B., Swan D.C., Booth D.R., Lachmann H.J., Gaudet R., Woo P., Feighery C., Cotter F.E., Thome M., Hitman G.A., Tschopp J., McDermott M.F.
    Arthritis Rheum. 46:2445-2452(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), VARIANT MWS MET-200, VARIANTS FCAS1/MWS TRP-262 AND PRO-307.
  3. "PYPAF1: a PYRIN-containing APAF1-like protein that assembles with ASC and activates NF-kB."
    Manji G.A., Wang L., Geddes B.J., Brown M., Merriam S., Al-Garawi A., Mak S., Lora J.M., Briskin M., Jurman M., Cao J., DiStefano P.S., Bertin J.
    J. Biol. Chem. 277:11570-11575(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH PYCARD, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AUTOINHIBITION.
  4. "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 1).
    Tissue: Brain.
  5. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
    Tissue: Brain.
  6. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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] (ISOFORMS 2; 4 AND 6).
    Tissue: Colon.
  9. "CIAS1/cryopyrin/PYPAF1/NALP3/CATERPILLER 1.1 is an inducible inflammatory mediator with NF-kappa B suppressive properties."
    O'Connor W. Jr., Harton J.A., Zhu X., Linhoff M.W., Ting J.-P.
    J. Immunol. 171:6329-6333(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-1036 (ISOFORM 4), ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, INDUCTION BY LPS; LTA; POLY(I:C) AND TNF.
  10. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 393-1036 (ISOFORM 1).
    Tissue: Umbilical cord blood.
  11. "NALP3 forms an IL-1beta-processing inflammasome with increased activity in Muckle-Wells autoinflammatory disorder."
    Agostini L., Martinon F., Burns K., McDermott M.F., Hawkins P.N., Tschopp J.
    Immunity 20:319-325(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF NRLP3 INFLAMMASOME COMPLEX.
  12. "The SPRY domain of Pyrin, mutated in familial Mediterranean fever patients, interacts with inflammasome components and inhibits proIL-1beta processing."
    Papin S., Cuenin S., Agostini L., Martinon F., Werner S., Beer H.D., Grutter C., Grutter M., Tschopp J.
    Cell Death Differ. 14:1457-1466(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MEFV.
  13. "Inflammasome components NALP 1 and 3 Show distinct but separate expression profiles in human tissues suggesting a site-specific role in the inflammatory response."
    Kummer J.A., Broekhuizen R., Everett H., Agostini L., Kuijk L., Martinon F., van Bruggen R., Tschopp J.
    J. Histochem. Cytochem. 55:443-452(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  14. "Osteoblasts express NLRP3, a nucleotide-binding domain and leucine-rich repeat region containing receptor implicated in bacterially induced cell death."
    McCall S.H., Sahraei M., Young A.B., Worley C.S., Duncan J.A., Ting J.P., Marriott I.
    J. Bone Miner. Res. 23:30-40(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INDUCTION BY SALMONELLA.
  15. "Non-transcriptional priming and deubiquitination regulate NLRP3 inflammasome activation."
    Juliana C., Fernandes-Alnemri T., Kang S., Farias A., Qin F., Alnemri E.S.
    J. Biol. Chem. 287:36617-36622(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION.
  16. Cited for: FUNCTION, INTERACTION WITH EIF2AK2.
  17. "GBP5 promotes NLRP3 inflammasome assembly and immunity in mammals."
    Shenoy A.R., Wellington D.A., Kumar P., Kassa H., Booth C.J., Cresswell P., MacMicking J.D.
    Science 336:481-485(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GBP5, MUTAGENESIS OF 22-LEU-LYS-23.
  18. "Selective inhibition of the NLRP3 inflammasome by targeting to promyelocytic leukemia protein in mouse and human."
    Lo Y.H., Huang Y.W., Wu Y.H., Tsai C.S., Lin Y.C., Mo S.T., Kuo W.C., Chuang Y.T., Jiang S.T., Shih H.M., Lai M.Z.
    Blood 121:3185-3194(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PML.
  19. "Modulatory mechanisms controlling the NLRP3 inflammasome in inflammation: recent developments."
    Haneklaus M., O'Neill L.A., Coll R.C.
    Curr. Opin. Immunol. 25:40-45(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  20. "Unified polymerization mechanism for the assembly of ASC-dependent inflammasomes."
    Lu A., Magupalli V.G., Ruan J., Yin Q., Atianand M.K., Vos M.R., Schroder G.F., Fitzgerald K.A., Wu H., Egelman E.H.
    Cell 156:1193-1206(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: MECHANISM OF INFLAMMASOME ASSEMBLY, MUTAGENESIS OF GLU-15; LYS-23; LYS-24; MET-27; ARG-43; GLU-64 AND ASP-82.
  21. Cited for: SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT FCAS1/MWS TRP-262, CHARACTERIZATION OF VARIANT CINCA ASN-305, CHARACTERIZATION OF VARIANT CINCA/MWS MET-350.
  22. "Structural mechanisms of inflammasome assembly."
    Lu A., Wu H.
    FEBS J. 282:435-444(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON INFLAMMASOME ASSEMBLY.
  23. "TRIM-mediated precision autophagy targets cytoplasmic regulators of innate immunity."
    Kimura T., Jain A., Choi S.W., Mandell M.A., Schroder K., Johansen T., Deretic V.
    J. Cell Biol. 210:973-989(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MEFV.
  24. "Crystal structure of NALP3 protein pyrin domain (PYD) and its implications in inflammasome assembly."
    Bae J.Y., Park H.H.
    J. Biol. Chem. 286:39528-39536(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 3-112, SUBUNIT, DISULFIDE BOND.
  25. "New mutations of CIAS1 that are responsible for Muckle-Wells syndrome and familial cold urticaria: a novel mutation underlies both syndromes."
    Dode C., Le Du N., Cuisset L., Letourneur F., Berthelot J.-M., Vaudour G., Meyrier A., Watts R.A., Scott D.G.I., Nicholls A., Granel B., Frances C., Garcier F., Edery P., Boulinguez S., Domergues J.-P., Delpech M., Grateau G.
    Am. J. Hum. Genet. 70:1498-1506(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT FCAS1 MET-200, VARIANTS MWS ASN-305; MET-350; THR-441 AND ARG-571, VARIANT FCAS1/MWS TRP-262.
  26. "Chronic infantile neurological cutaneous and articular syndrome is caused by mutations in CIAS1, a gene highly expressed in polymorphonuclear cells and chondrocytes."
    Feldmann J., Prieur A.-M., Quartier P., Berquin P., Certain S., Cortis E., Teillac-Hamel D., Fischer A., de Saint Basile G.
    Am. J. Hum. Genet. 71:198-203(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CINCA ASN-305; LYS-308; SER-311; ARG-360; ASN-438; SER-575 AND THR-664, TISSUE SPECIFICITY.
  27. "De novo CIAS1 mutations, cytokine activation, and evidence for genetic heterogeneity in patients with neonatal-onset multisystem inflammatory disease (NOMID): a new member of the expanding family of pyrin-associated autoinflammatory diseases."
    Aksentijevich I., Nowak M., Mallah M., Chae J.J., Watford W.T., Hofmann S.R., Stein L., Russo R., Goldsmith D., Dent P., Rosenberg H.F., Austin F., Remmers E.F., Balow J.E. Jr., Rosenzweig S., Komarow H., Shoham N.G., Wood G.
    , Jones J., Mangra N., Carrero H., Adams B.S., Moore T.L., Schikler K., Hoffman H., Lovell D.J., Lipnick R., Barron K., O'Shea J.J., Kastner D.L., Goldbach-Mansky R.
    Arthritis Rheum. 46:3340-3348(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CINCA HIS-266; ASN-305; LEU-525 AND CYS-572.
  28. "Fine structure mapping of CIAS1: identification of an ancestral haplotype and a common FCAS mutation, L353P."
    Hoffman H.M., Gregory S.G., Mueller J.L., Tresierras M., Broide D.H., Wanderer A.A., Kolodner R.D.
    Hum. Genet. 112:209-216(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT FCAS1 PRO-355, VARIANT LYS-705.
  29. "Variant chronic infantile neurologic, cutaneous, articular syndrome due to a mutation within the leucine-rich repeat domain of CIAS1."
    Frenkel J., van Kempen M.J., Kuis W., van Amstel H.K.
    Arthritis Rheum. 50:2719-2720(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CINCA CYS-861.
  30. "Clinical and genetic heterogeneity among Spanish patients with recurrent autoinflammatory syndromes associated with the CIAS1/PYPAF1/NALP3 gene."
    Arostegui J.I., Aldea A., Modesto C., Rua M.J., Argueelles F., Gonzalez-Ensenat M.A., Ramos E., Rius J., Plaza S., Vives J., Yaguee J.
    Arthritis Rheum. 50:4045-4050(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS FCAS1 MET-200; PRO-307 AND LYS-490, VARIANT CINCA ASN-305, VARIANT MWS MET-350.
  31. "Molecular basis of the spectral expression of CIAS1 mutations associated with phagocytic cell-mediated autoinflammatory disorders CINCA/NOMID, MWS, and FCU."
    Neven B., Callebaut I., Prieur A.-M., Feldmann J., Bodemer C., Lepore L., Derfalvi B., Benjaponpitak S., Vesely R., Sauvain M.J., Oertle S., Allen R., Morgan G., Borkhardt A., Hill C., Gardner-Medwin J., Fischer A., de Saint Basile G.
    Blood 103:2809-2815(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CINCA LEU-262; PRO-262; ASN-305; GLY-305; SER-311; MET-350; ASP-356; PRO-407; ILE-438; CYS-572 AND PHE-634.
  32. "A novel CIAS1 mutation and plasma/cerebrospinal fluid cytokine profile in a German patient with neonatal-onset multisystem inflammatory disease responsive to methotrexate therapy."
    Stojanov S., Weiss M., Lohse P., Belohradsky B.H.
    Pediatrics 114:E124-E127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CINCA THR-174.
  33. "A novel missense mutation in CIAS1 encoding the pyrin-like protein, cryopyrin, causes familial cold autoinflammatory syndrome in a family of Ethiopian origin."
    Shalev S.A., Sprecher E., Indelman M., Hujirat Y., Bergman R., Rottem M.
    Int. Arch. Allergy Immunol. 143:190-193(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT FCAS1 CYS-525.

Entry informationi

Entry nameiNLRP3_HUMAN
AccessioniPrimary (citable) accession number: Q96P20
Secondary accession number(s): A0A024R5Q0
, B2RC97, B7ZKS9, B7ZKT2, B7ZKT3, O75434, Q17RS2, Q59H68, Q5JQS8, Q5JQS9, Q6TG35, Q8TCW0, Q8TEU9, Q8WXH9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: November 3, 2009
Last modified: January 20, 2016
This is version 162 of the entry and version 3 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 1
    Human chromosome 1: 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

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 one 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.