UniProtKB - Q96P20 (NLRP3_HUMAN)
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Protein
NACHT, LRR and PYD domains-containing protein 3
Gene
NLRP3
Organism
Homo sapiens (Human)
Status
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). Recruitment 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, amyloid-beta 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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 226 – 233 | ATPPROSITE-ProRule annotation | 8 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- identical protein binding Source: IntAct
- 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
- cellular response to peptidoglycan Source: Ensembl
- cytokine secretion involved in immune response Source: Ensembl
- defense response Source: HGNC
- defense response to Gram-positive bacterium Source: Ensembl
- defense response to virus Source: Ensembl
- detection of biotic stimulus Source: HGNC
- inflammatory response Source: UniProtKB
- innate immune response Source: UniProtKB-KW
- 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
- positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: HGNC
- positive regulation of interleukin-13 production Source: Ensembl
- positive regulation of interleukin-1 beta secretion Source: HGNC
- positive regulation of interleukin-4 production Source: UniProtKB
- positive regulation of interleukin-5 production Source: Ensembl
- positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
- positive regulation of T-helper 17 cell differentiation Source: Ensembl
- 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 by RNA polymerase II Source: UniProtKB
- positive regulation of type 2 immune response Source: UniProtKB
- protein deubiquitination Source: Reactome
- protein oligomerization Source: HGNC
- signal transduction Source: UniProtKB
- transcription, DNA-templated Source: UniProtKB-KW
Keywordsi
Molecular function | Activator |
Biological process | Immunity, Inflammatory response, Innate immunity, Transcription, Transcription regulation |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
Reactomei | R-HSA-5689901. Metalloprotease DUBs. R-HSA-844456. The NLRP3 inflammasome. |
Names & Taxonomyi
Protein namesi | Recommended name: NACHT, LRR and PYD domains-containing protein 3Alternative 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 |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
EuPathDBi | HostDB:ENSG00000162711.16. |
HGNCi | HGNC:16400. NLRP3. |
MIMi | 606416. gene. |
neXtProti | NX_Q96P20. |
Subcellular locationi
Keywords - Cellular componenti
Cytoplasm, Endoplasmic reticulum, Inflammasome, Nucleus, SecretedPathology & 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:120100Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_043685 | 355 | L → P in FCAS1. 1 PublicationCorresponds to variant dbSNP:rs28937896Ensembl. | 1 | |
Natural variantiVAR_013229 | 441 | A → V in FCAS1. 1 PublicationCorresponds to variant dbSNP:rs121908146Ensembl. | 1 | |
Natural variantiVAR_043689 | 490 | R → K in FCAS1. 1 PublicationCorresponds to variant dbSNP:rs145268073Ensembl. | 1 | |
Natural variantiVAR_031853 | 525 | F → C in FCAS1. 1 PublicationCorresponds to variant dbSNP:rs180177478Ensembl. | 1 | |
Natural variantiVAR_013230 | 629 | E → G in FCAS1. 1 PublicationCorresponds to variant dbSNP:rs121908148Ensembl. | 1 |
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:191900Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_013228 | 354 | A → V in MWS. 1 PublicationCorresponds to variant dbSNP:rs121908149Ensembl. | 1 | |
Natural variantiVAR_014369 | 441 | A → T in MWS. 1 PublicationCorresponds to variant dbSNP:rs180177430Ensembl. | 1 | |
Natural variantiVAR_014107 | 571 | G → R in MWS. 1 PublicationCorresponds to variant dbSNP:rs121908151Ensembl. | 1 |
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:607115Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_043679 | 174 | I → T in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177449Ensembl. | 1 | |
Natural variantiVAR_043680 | 262 | R → L in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177442Ensembl. | 1 | |
Natural variantiVAR_043681 | 262 | R → P in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177442Ensembl. | 1 | |
Natural variantiVAR_043682 | 266 | L → H in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177436Ensembl. | 1 | |
Natural variantiVAR_043683 | 305 | D → G in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177447Ensembl. | 1 | |
Natural variantiVAR_043684 | 308 | Q → K in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177432Ensembl. | 1 | |
Natural variantiVAR_014106 | 311 | F → S in CINCA. 2 PublicationsCorresponds to variant dbSNP:rs121908154Ensembl. | 1 | |
Natural variantiVAR_043686 | 356 | E → D in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177444Ensembl. | 1 | |
Natural variantiVAR_014367 | 360 | H → R in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177434Ensembl. | 1 | |
Natural variantiVAR_043687 | 407 | T → P in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177445Ensembl. | 1 | |
Natural variantiVAR_043688 | 438 | T → I in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177433Ensembl. | 1 | |
Natural variantiVAR_014368 | 438 | T → N in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177433Ensembl. | 1 | |
Natural variantiVAR_043690 | 525 | F → L in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177439Ensembl. | 1 | |
Natural variantiVAR_043691 | 572 | Y → C in CINCA. 2 PublicationsCorresponds to variant dbSNP:rs180177438Ensembl. | 1 | |
Natural variantiVAR_014108 | 575 | F → S in CINCA. 1 PublicationCorresponds to variant dbSNP:rs121908152Ensembl. | 1 | |
Natural variantiVAR_043692 | 634 | L → F in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177446Ensembl. | 1 | |
Natural variantiVAR_014370 | 664 | M → T in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177435Ensembl. | 1 | |
Natural variantiVAR_023551 | 861 | Y → C in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177452Ensembl. | 1 |
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 15 | E → R: Complete loss of PYCARD filament nucleation. 1 Publication | 1 | |
Mutagenesisi | 22 – 23 | LK → PA: Loss of PYCARD-binding. No effect on GBP5-binding. 1 Publication | 2 | |
Mutagenesisi | 23 | K → E: Complete loss of PYCARD filament nucleation; when associated with E-24. 1 Publication | 1 | |
Mutagenesisi | 24 | K → E: Complete loss of PYCARD filament nucleation; when associated with E-23. 1 Publication | 1 | |
Mutagenesisi | 27 | M → E: Complete loss of PYCARD filament nucleation. 1 Publication | 1 | |
Mutagenesisi | 43 | R → W: Complete loss of PYCARD filament nucleation. 1 Publication | 1 | |
Mutagenesisi | 64 | E → R: Complete loss of PYCARD filament nucleation. 1 Publication | 1 | |
Mutagenesisi | 82 | D → R: Complete loss of PYCARD filament nucleation. 1 Publication | 1 |
Keywords - Diseasei
Amyloidosis, Deafness, Disease mutationOrganism-specific databases
DisGeNETi | 114548. |
MalaCardsi | NLRP3. |
MIMi | 120100. phenotype. 191900. phenotype. 607115. phenotype. |
OpenTargetsi | ENSG00000162711. |
Orphaneti | 93365. CINCA syndrome with NLRP3 mutations. 47045. Familial cold urticaria. 575. Muckle-Wells syndrome. |
PharmGKBi | PA26512. |
Chemistry databases
ChEMBLi | CHEMBL1741208. |
GuidetoPHARMACOLOGYi | 1770. |
Polymorphism and mutation databases
BioMutai | NLRP3. |
DMDMi | 262527566. |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000080886 | 1 – 1036 | NACHT, LRR and PYD domains-containing protein 3Add BLAST | 1036 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 8 ↔ 108 | Redox-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 conjugationProteomic databases
EPDi | Q96P20. |
PaxDbi | Q96P20. |
PeptideAtlasi | Q96P20. |
PRIDEi | Q96P20. |
PTM databases
iPTMneti | Q96P20. |
PhosphoSitePlusi | Q96P20. |
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). In macrophages, up-regulated by endocannabinoid anandamide/AEA (PubMed:23955712).3 Publications
Gene expression databases
Bgeei | ENSG00000162711. |
Genevisiblei | Q96P20. HS. |
Organism-specific databases
HPAi | HPA012878. |
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
GO - Molecular functioni
- identical protein binding Source: IntAct
- transcription factor binding Source: UniProtKB
Protein-protein interaction databases
BioGridi | 125319. 49 interactors. |
CORUMi | Q96P20. |
DIPi | DIP-41153N. |
IntActi | Q96P20. 41 interactors. |
STRINGi | 9606.ENSP00000337383. |
Chemistry databases
BindingDBi | Q96P20. |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Helixi | 6 – 15 | Combined sources | 10 | |
Helixi | 19 – 30 | Combined sources | 12 | |
Beta strandi | 34 – 37 | Combined sources | 4 | |
Helixi | 43 – 48 | Combined sources | 6 | |
Helixi | 51 – 62 | Combined sources | 12 | |
Helixi | 64 – 77 | Combined sources | 14 | |
Helixi | 81 – 89 | Combined sources | 9 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2NAQ | NMR | - | A | 3-93 | [»] | |
3QF2 | X-ray | 1.70 | A/B | 3-112 | [»] | |
ProteinModelPortali | Q96P20. | |||||
SMRi | Q96P20. | |||||
ModBasei | Search... | |||||
MobiDBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 1 – 93 | PyrinPROSITE-ProRule annotationAdd BLAST | 93 | |
Domaini | 220 – 536 | NACHTPROSITE-ProRule annotationAdd BLAST | 317 | |
Repeati | 742 – 762 | LRR 1Add BLAST | 21 | |
Repeati | 771 – 792 | LRR 2Add BLAST | 22 | |
Repeati | 799 – 819 | LRR 3Add BLAST | 21 | |
Repeati | 828 – 849 | LRR 4Add BLAST | 22 | |
Repeati | 856 – 876 | LRR 5Add BLAST | 21 | |
Repeati | 885 – 906 | LRR 6Add BLAST | 22 | |
Repeati | 913 – 933 | LRR 7Add BLAST | 21 | |
Repeati | 942 – 963 | LRR 8Add BLAST | 22 | |
Repeati | 970 – 991 | LRR 9Add BLAST | 22 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 690 – 697 | Poly-Glu | 8 |
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
Keywords - Domaini
Leucine-rich repeat, RepeatPhylogenomic databases
eggNOGi | ENOG410IE5X. Eukaryota. ENOG4111H3D. LUCA. |
GeneTreei | ENSGT00900000140813. |
HOVERGENi | HBG063656. |
InParanoidi | Q96P20. |
KOi | K12800. |
OMAi | PVHTVVF. |
OrthoDBi | EOG091G01CG. |
PhylomeDBi | Q96P20. |
TreeFami | TF340267. |
Family and domain databases
Gene3Di | 3.80.10.10. 1 hit. |
InterProi | View protein in InterPro IPR004020. DAPIN. IPR011029. DEATH-like_dom_sf. IPR001611. Leu-rich_rpt. IPR032675. LRR_dom_sf. IPR029495. NACHT-assoc. IPR007111. NACHT_NTPase. IPR027417. P-loop_NTPase. |
Pfami | View protein in Pfam PF14484. FISNA. 1 hit. PF13516. LRR_6. 4 hits. PF02758. PYRIN. 1 hit. |
SMARTi | View protein in SMART SM01288. FISNA. 1 hit. SM01289. PYRIN. 1 hit. |
SUPFAMi | SSF47986. SSF47986. 1 hit. SSF52540. SSF52540. 2 hits. |
PROSITEi | View protein in PROSITE PS50824. DAPIN. 1 hit. PS50837. NACHT. 1 hit. |
s (6)i Sequence
Sequence statusi: Complete.
This entry describes 6 produced by isoformsialternative 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.
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
Sequence cautioni
The sequence AAC39910 differs from that shown. Reason: Frameshift at positions 893, 918 and 926.Curated
The sequence AAL12497 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAL12498 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAL33908 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAL65136 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAD92128 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAG37494 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 167 | R → L in AAL78632 (PubMed:12355493).Curated | 1 | |
Sequence conflicti | 167 | R → L in AAM14669 (PubMed:12355493).Curated | 1 | |
Sequence conflicti | 167 | R → L in AAL14640 (PubMed:12355493).Curated | 1 | |
Sequence conflicti | 323 | Q → H in AAL78632 (PubMed:12355493).Curated | 1 | |
Sequence conflicti | 323 | Q → H in AAM14669 (PubMed:12355493).Curated | 1 | |
Sequence conflicti | 323 | Q → H in AAL14640 (PubMed:12355493).Curated | 1 | |
Sequence conflicti | 439 | T → S in AAC39910 (PubMed:11042152).Curated | 1 | |
Sequence conflicti | 523 | M → V in BAG37494 (Ref. 5) Curated | 1 | |
Sequence conflicti | 599 | K → M in AAC39910 (PubMed:11042152).Curated | 1 | |
Sequence conflicti | 617 | K → N in AAL78632 (PubMed:12355493).Curated | 1 | |
Sequence conflicti | 617 | K → N in AAM14669 (PubMed:12355493).Curated | 1 | |
Sequence conflicti | 617 | K → N in AAL14640 (PubMed:12355493).Curated | 1 | |
Sequence conflicti | 622 – 623 | QI → HD in AAC39910 (PubMed:11042152).Curated | 2 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_043679 | 174 | I → T in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177449Ensembl. | 1 | |
Natural variantiVAR_013227 | 200 | V → M in FCAS1 and MWS. 4 PublicationsCorresponds to variant dbSNP:rs121908147Ensembl. | 1 | |
Natural variantiVAR_043680 | 262 | R → L in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177442Ensembl. | 1 | |
Natural variantiVAR_043681 | 262 | R → P in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177442Ensembl. | 1 | |
Natural variantiVAR_014104 | 262 | R → W in FCAS1 and MWS; spontaneous polymerization into inflammasome speck. 3 Publications | 1 | |
Natural variantiVAR_043682 | 266 | L → H in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177436Ensembl. | 1 | |
Natural variantiVAR_043683 | 305 | D → G in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177447Ensembl. | 1 | |
Natural variantiVAR_014105 | 305 | D → N in CINCA and MWS; spontaneous polymerization into inflammasome speck. 6 PublicationsCorresponds to variant dbSNP:rs121908153Ensembl. | 1 | |
Natural variantiVAR_014124 | 307 | L → P in FCAS1 and MWS. 2 PublicationsCorresponds to variant dbSNP:rs180177431Ensembl. | 1 | |
Natural variantiVAR_043684 | 308 | Q → K in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177432Ensembl. | 1 | |
Natural variantiVAR_014106 | 311 | F → S in CINCA. 2 PublicationsCorresponds to variant dbSNP:rs121908154Ensembl. | 1 | |
Natural variantiVAR_014366 | 350 | T → M in MWS and CINCA; spontaneous polymerization into inflammasome speck. 4 PublicationsCorresponds to variant dbSNP:rs151344629Ensembl. | 1 | |
Natural variantiVAR_013228 | 354 | A → V in MWS. 1 PublicationCorresponds to variant dbSNP:rs121908149Ensembl. | 1 | |
Natural variantiVAR_043685 | 355 | L → P in FCAS1. 1 PublicationCorresponds to variant dbSNP:rs28937896Ensembl. | 1 | |
Natural variantiVAR_043686 | 356 | E → D in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177444Ensembl. | 1 | |
Natural variantiVAR_014367 | 360 | H → R in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177434Ensembl. | 1 | |
Natural variantiVAR_043687 | 407 | T → P in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177445Ensembl. | 1 | |
Natural variantiVAR_043688 | 438 | T → I in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177433Ensembl. | 1 | |
Natural variantiVAR_014368 | 438 | T → N in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177433Ensembl. | 1 | |
Natural variantiVAR_014369 | 441 | A → T in MWS. 1 PublicationCorresponds to variant dbSNP:rs180177430Ensembl. | 1 | |
Natural variantiVAR_013229 | 441 | A → V in FCAS1. 1 PublicationCorresponds to variant dbSNP:rs121908146Ensembl. | 1 | |
Natural variantiVAR_043689 | 490 | R → K in FCAS1. 1 PublicationCorresponds to variant dbSNP:rs145268073Ensembl. | 1 | |
Natural variantiVAR_031853 | 525 | F → C in FCAS1. 1 PublicationCorresponds to variant dbSNP:rs180177478Ensembl. | 1 | |
Natural variantiVAR_043690 | 525 | F → L in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177439Ensembl. | 1 | |
Natural variantiVAR_014107 | 571 | G → R in MWS. 1 PublicationCorresponds to variant dbSNP:rs121908151Ensembl. | 1 | |
Natural variantiVAR_043691 | 572 | Y → C in CINCA. 2 PublicationsCorresponds to variant dbSNP:rs180177438Ensembl. | 1 | |
Natural variantiVAR_014108 | 575 | F → S in CINCA. 1 PublicationCorresponds to variant dbSNP:rs121908152Ensembl. | 1 | |
Natural variantiVAR_013230 | 629 | E → G in FCAS1. 1 PublicationCorresponds to variant dbSNP:rs121908148Ensembl. | 1 | |
Natural variantiVAR_043692 | 634 | L → F in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177446Ensembl. | 1 | |
Natural variantiVAR_014370 | 664 | M → T in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177435Ensembl. | 1 | |
Natural variantiVAR_043693 | 705 | Q → K1 PublicationCorresponds to variant dbSNP:rs35829419Ensembl. | 1 | |
Natural variantiVAR_023551 | 861 | Y → C in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177452Ensembl. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_005519 | 720 – 1036 | Missing in isoform 3. 1 PublicationAdd BLAST | 317 | |
Alternative sequenceiVSP_005520 | 721 – 777 | Missing in isoform 1 and isoform 4. 6 PublicationsAdd BLAST | 57 | |
Alternative sequenceiVSP_053714 | 776 – 796 | WLGRC…LVLSS → C in isoform 6. 1 PublicationAdd BLAST | 21 | |
Alternative sequenceiVSP_005521 | 836 – 892 | Missing in isoform 1 and isoform 5. 6 PublicationsAdd BLAST | 57 |
Sequence databases
Genome annotation databases
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Entry informationi
Entry namei | NLRP3_HUMAN | |
Accessioni | Q96P20Primary (citable) accession number: Q96P20 Secondary accession number(s): A0A024R5Q0 Q8WXH9 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 2, 2002 |
Last sequence update: | November 3, 2009 | |
Last modified: | March 28, 2018 | |
This is version 185 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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. |