Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - Q96P20 (NLRP3_HUMAN)

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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). 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, 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)DescriptionActionsGraphical viewLength
Nucleotide bindingi226 – 233ATPPROSITE-ProRule annotation8

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
Complete GO annotation...

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: 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 from RNA polymerase II promoter 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
Complete GO annotation...

Keywordsi

Molecular functionActivator
Biological processImmunity, Inflammatory response, Innate immunity, Transcription, Transcription regulation
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-5689901. Metalloprotease DUBs.
R-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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 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)DescriptionActionsGraphical viewLength
Natural variantiVAR_013227200V → M in FCAS1 and MWS. 4 PublicationsCorresponds to variant dbSNP:rs121908147Ensembl.1
Natural variantiVAR_014104262R → W in FCAS1 and MWS; spontaneous polymerization into inflammasome speck. 3 Publications1
Natural variantiVAR_014124307L → P in FCAS1 and MWS. 2 PublicationsCorresponds to variant dbSNP:rs180177431Ensembl.1
Natural variantiVAR_043685355L → P in FCAS1. 1 PublicationCorresponds to variant dbSNP:rs28937896Ensembl.1
Natural variantiVAR_013229441A → V in FCAS1. 1 PublicationCorresponds to variant dbSNP:rs121908146Ensembl.1
Natural variantiVAR_043689490R → K in FCAS1. 1 PublicationCorresponds to variant dbSNP:rs145268073Ensembl.1
Natural variantiVAR_031853525F → C in FCAS1. 1 PublicationCorresponds to variant dbSNP:rs180177478Ensembl.1
Natural variantiVAR_013230629E → 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:191900
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_013227200V → M in FCAS1 and MWS. 4 PublicationsCorresponds to variant dbSNP:rs121908147Ensembl.1
Natural variantiVAR_014104262R → W in FCAS1 and MWS; spontaneous polymerization into inflammasome speck. 3 Publications1
Natural variantiVAR_014105305D → N in CINCA and MWS; spontaneous polymerization into inflammasome speck. 6 PublicationsCorresponds to variant dbSNP:rs121908153Ensembl.1
Natural variantiVAR_014124307L → P in FCAS1 and MWS. 2 PublicationsCorresponds to variant dbSNP:rs180177431Ensembl.1
Natural variantiVAR_014366350T → M in MWS and CINCA; spontaneous polymerization into inflammasome speck. 4 PublicationsCorresponds to variant dbSNP:rs151344629Ensembl.1
Natural variantiVAR_013228354A → V in MWS. 1 PublicationCorresponds to variant dbSNP:rs121908149Ensembl.1
Natural variantiVAR_014369441A → T in MWS. 1 PublicationCorresponds to variant dbSNP:rs180177430Ensembl.1
Natural variantiVAR_014107571G → 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:607115
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_043679174I → T in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177449Ensembl.1
Natural variantiVAR_043680262R → L in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177442Ensembl.1
Natural variantiVAR_043681262R → P in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177442Ensembl.1
Natural variantiVAR_043682266L → H in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177436Ensembl.1
Natural variantiVAR_043683305D → G in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177447Ensembl.1
Natural variantiVAR_014105305D → N in CINCA and MWS; spontaneous polymerization into inflammasome speck. 6 PublicationsCorresponds to variant dbSNP:rs121908153Ensembl.1
Natural variantiVAR_043684308Q → K in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177432Ensembl.1
Natural variantiVAR_014106311F → S in CINCA. 2 PublicationsCorresponds to variant dbSNP:rs121908154Ensembl.1
Natural variantiVAR_014366350T → M in MWS and CINCA; spontaneous polymerization into inflammasome speck. 4 PublicationsCorresponds to variant dbSNP:rs151344629Ensembl.1
Natural variantiVAR_043686356E → D in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177444Ensembl.1
Natural variantiVAR_014367360H → R in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177434Ensembl.1
Natural variantiVAR_043687407T → P in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177445Ensembl.1
Natural variantiVAR_043688438T → I in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177433Ensembl.1
Natural variantiVAR_014368438T → N in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177433Ensembl.1
Natural variantiVAR_043690525F → L in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177439Ensembl.1
Natural variantiVAR_043691572Y → C in CINCA. 2 PublicationsCorresponds to variant dbSNP:rs180177438Ensembl.1
Natural variantiVAR_014108575F → S in CINCA. 1 PublicationCorresponds to variant dbSNP:rs121908152Ensembl.1
Natural variantiVAR_043692634L → F in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177446Ensembl.1
Natural variantiVAR_014370664M → T in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177435Ensembl.1
Natural variantiVAR_023551861Y → C in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177452Ensembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi15E → R: Complete loss of PYCARD filament nucleation. 1 Publication1
Mutagenesisi22 – 23LK → PA: Loss of PYCARD-binding. No effect on GBP5-binding. 1 Publication2
Mutagenesisi23K → E: Complete loss of PYCARD filament nucleation; when associated with E-24. 1 Publication1
Mutagenesisi24K → E: Complete loss of PYCARD filament nucleation; when associated with E-23. 1 Publication1
Mutagenesisi27M → E: Complete loss of PYCARD filament nucleation. 1 Publication1
Mutagenesisi43R → W: Complete loss of PYCARD filament nucleation. 1 Publication1
Mutagenesisi64E → R: Complete loss of PYCARD filament nucleation. 1 Publication1
Mutagenesisi82D → R: Complete loss of PYCARD filament nucleation. 1 Publication1

Keywords - Diseasei

Amyloidosis, Deafness, Disease mutation

Organism-specific databases

DisGeNETi114548.
MalaCardsiNLRP3.
MIMi120100. phenotype.
191900. phenotype.
607115. phenotype.
OpenTargetsiENSG00000162711.
Orphaneti93365. CINCA syndrome with NLRP3 mutations.
47045. Familial cold urticaria.
575. Muckle-Wells syndrome.
PharmGKBiPA26512.

Chemistry databases

ChEMBLiCHEMBL1741208.
GuidetoPHARMACOLOGYi1770.

Polymorphism and mutation databases

BioMutaiNLRP3.
DMDMi262527566.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000808861 – 1036NACHT, LRR and PYD domains-containing protein 3Add BLAST1036

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

EPDiQ96P20.
PaxDbiQ96P20.
PeptideAtlasiQ96P20.
PRIDEiQ96P20.

PTM databases

iPTMnetiQ96P20.
PhosphoSitePlusiQ96P20.

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

BgeeiENSG00000162711.
GenevisibleiQ96P20. HS.

Organism-specific databases

HPAiHPA012878.

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

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • transcription factor binding Source: UniProtKB
Complete GO annotation...

Protein-protein interaction databases

BioGridi125319. 49 interactors.
DIPiDIP-41153N.
IntActiQ96P20. 38 interactors.
MINTiMINT-230535.
STRINGi9606.ENSP00000337383.

Chemistry databases

BindingDBiQ96P20.

Structurei

Secondary structure

11036
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 15Combined sources10
Helixi19 – 30Combined sources12
Beta strandi34 – 37Combined sources4
Helixi43 – 48Combined sources6
Helixi51 – 62Combined sources12
Helixi64 – 77Combined sources14
Helixi81 – 89Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2NAQNMR-A3-93[»]
3QF2X-ray1.70A/B3-112[»]
ProteinModelPortaliQ96P20.
SMRiQ96P20.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 93PyrinPROSITE-ProRule annotationAdd BLAST93
Domaini220 – 536NACHTPROSITE-ProRule annotationAdd BLAST317
Repeati742 – 762LRR 1Add BLAST21
Repeati771 – 792LRR 2Add BLAST22
Repeati799 – 819LRR 3Add BLAST21
Repeati828 – 849LRR 4Add BLAST22
Repeati856 – 876LRR 5Add BLAST21
Repeati885 – 906LRR 6Add BLAST22
Repeati913 – 933LRR 7Add BLAST21
Repeati942 – 963LRR 8Add BLAST22
Repeati970 – 991LRR 9Add BLAST22

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi690 – 697Poly-Glu8

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, Repeat

Phylogenomic databases

eggNOGiENOG410IE5X. Eukaryota.
ENOG4111H3D. LUCA.
GeneTreeiENSGT00860000133669.
HOVERGENiHBG063656.
InParanoidiQ96P20.
KOiK12800.
OMAiPVHTVVF.
OrthoDBiEOG091G01CG.
PhylomeDBiQ96P20.
TreeFamiTF340267.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiView protein in InterPro
IPR004020. DAPIN.
IPR011029. DEATH-like_dom.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR029495. NACHT-assoc.
IPR007111. NACHT_NTPase.
IPR027417. P-loop_NTPase.
PfamiView protein in Pfam
PF14484. FISNA. 1 hit.
PF13516. LRR_6. 4 hits.
PF02758. PYRIN. 1 hit.
SMARTiView protein in SMART
SM01288. FISNA. 1 hit.
SM01289. PYRIN. 1 hit.
SUPFAMiSSF47986. SSF47986. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEiView protein in PROSITE
PS50824. DAPIN. 1 hit.
PS50837. NACHT. 1 hit.

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 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 keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti167R → L in AAL78632 (PubMed:12355493).Curated1
Sequence conflicti167R → L in AAM14669 (PubMed:12355493).Curated1
Sequence conflicti167R → L in AAL14640 (PubMed:12355493).Curated1
Sequence conflicti323Q → H in AAL78632 (PubMed:12355493).Curated1
Sequence conflicti323Q → H in AAM14669 (PubMed:12355493).Curated1
Sequence conflicti323Q → H in AAL14640 (PubMed:12355493).Curated1
Sequence conflicti439T → S in AAC39910 (PubMed:11042152).Curated1
Sequence conflicti523M → V in BAG37494 (Ref. 5) Curated1
Sequence conflicti599K → M in AAC39910 (PubMed:11042152).Curated1
Sequence conflicti617K → N in AAL78632 (PubMed:12355493).Curated1
Sequence conflicti617K → N in AAM14669 (PubMed:12355493).Curated1
Sequence conflicti617K → N in AAL14640 (PubMed:12355493).Curated1
Sequence conflicti622 – 623QI → HD in AAC39910 (PubMed:11042152).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_043679174I → T in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177449Ensembl.1
Natural variantiVAR_013227200V → M in FCAS1 and MWS. 4 PublicationsCorresponds to variant dbSNP:rs121908147Ensembl.1
Natural variantiVAR_043680262R → L in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177442Ensembl.1
Natural variantiVAR_043681262R → P in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177442Ensembl.1
Natural variantiVAR_014104262R → W in FCAS1 and MWS; spontaneous polymerization into inflammasome speck. 3 Publications1
Natural variantiVAR_043682266L → H in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177436Ensembl.1
Natural variantiVAR_043683305D → G in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177447Ensembl.1
Natural variantiVAR_014105305D → N in CINCA and MWS; spontaneous polymerization into inflammasome speck. 6 PublicationsCorresponds to variant dbSNP:rs121908153Ensembl.1
Natural variantiVAR_014124307L → P in FCAS1 and MWS. 2 PublicationsCorresponds to variant dbSNP:rs180177431Ensembl.1
Natural variantiVAR_043684308Q → K in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177432Ensembl.1
Natural variantiVAR_014106311F → S in CINCA. 2 PublicationsCorresponds to variant dbSNP:rs121908154Ensembl.1
Natural variantiVAR_014366350T → M in MWS and CINCA; spontaneous polymerization into inflammasome speck. 4 PublicationsCorresponds to variant dbSNP:rs151344629Ensembl.1
Natural variantiVAR_013228354A → V in MWS. 1 PublicationCorresponds to variant dbSNP:rs121908149Ensembl.1
Natural variantiVAR_043685355L → P in FCAS1. 1 PublicationCorresponds to variant dbSNP:rs28937896Ensembl.1
Natural variantiVAR_043686356E → D in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177444Ensembl.1
Natural variantiVAR_014367360H → R in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177434Ensembl.1
Natural variantiVAR_043687407T → P in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177445Ensembl.1
Natural variantiVAR_043688438T → I in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177433Ensembl.1
Natural variantiVAR_014368438T → N in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177433Ensembl.1
Natural variantiVAR_014369441A → T in MWS. 1 PublicationCorresponds to variant dbSNP:rs180177430Ensembl.1
Natural variantiVAR_013229441A → V in FCAS1. 1 PublicationCorresponds to variant dbSNP:rs121908146Ensembl.1
Natural variantiVAR_043689490R → K in FCAS1. 1 PublicationCorresponds to variant dbSNP:rs145268073Ensembl.1
Natural variantiVAR_031853525F → C in FCAS1. 1 PublicationCorresponds to variant dbSNP:rs180177478Ensembl.1
Natural variantiVAR_043690525F → L in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177439Ensembl.1
Natural variantiVAR_014107571G → R in MWS. 1 PublicationCorresponds to variant dbSNP:rs121908151Ensembl.1
Natural variantiVAR_043691572Y → C in CINCA. 2 PublicationsCorresponds to variant dbSNP:rs180177438Ensembl.1
Natural variantiVAR_014108575F → S in CINCA. 1 PublicationCorresponds to variant dbSNP:rs121908152Ensembl.1
Natural variantiVAR_013230629E → G in FCAS1. 1 PublicationCorresponds to variant dbSNP:rs121908148Ensembl.1
Natural variantiVAR_043692634L → F in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177446Ensembl.1
Natural variantiVAR_014370664M → T in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177435Ensembl.1
Natural variantiVAR_043693705Q → K1 PublicationCorresponds to variant dbSNP:rs35829419Ensembl.1
Natural variantiVAR_023551861Y → C in CINCA. 1 PublicationCorresponds to variant dbSNP:rs180177452Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_005519720 – 1036Missing in isoform 3. 1 PublicationAdd BLAST317
Alternative sequenceiVSP_005520721 – 777Missing in isoform 1 and isoform 4. 6 PublicationsAdd BLAST57
Alternative sequenceiVSP_053714776 – 796WLGRC…LVLSS → C in isoform 6. 1 PublicationAdd BLAST21
Alternative sequenceiVSP_005521836 – 892Missing in isoform 1 and isoform 5. 6 PublicationsAdd BLAST57

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_011542350.1. XM_011544048.2. [Q96P20-1]
XP_016855670.1. XM_017000181.1. [Q96P20-1]
XP_016855671.1. XM_017000182.1. [Q96P20-1]
XP_016855672.1. XM_017000183.1. [Q96P20-4]
XP_016855673.1. XM_017000184.1. [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.4. human. [Q96P20-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

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 historyiIntegrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: November 3, 2009
Last modified: August 30, 2017
This is version 179 of the entry and version 3 of the sequence. See 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