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Q96P20

- NALP3_HUMAN

UniProt

Q96P20 - NALP3_HUMAN

Protein

NACHT, LRR and PYD domains-containing protein 3

Gene

NLRP3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 3 (03 Nov 2009)
      Previous versions | rss
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    Functioni

    May function as an inducer of apoptosis. Interacts selectively with ASC and this complex may function as an upstream activator of NF-kappa-B signaling. Inhibits TNF-alpha induced activation and nuclear translocation of RELA/NF-KB p65. Also inhibits transcriptional activity of RELA. Activates caspase-1 in response to a number of triggers including bacterial or viral infection which leads to processing and release of IL1B and IL18.2 Publications

    Regions

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

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. peptidoglycan binding Source: HGNC
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
    2. apoptotic process Source: UniProtKB
    3. cellular response to lipopolysaccharide Source: BHF-UCL
    4. defense response Source: HGNC
    5. defense response to virus Source: Ensembl
    6. detection of biotic stimulus Source: HGNC
    7. inflammatory response Source: UniProtKB
    8. innate immune response Source: Reactome
    9. interleukin-18 production Source: Ensembl
    10. interleukin-1 beta production Source: Ensembl
    11. interleukin-1 secretion Source: Ensembl
    12. negative regulation of acute inflammatory response Source: BHF-UCL
    13. negative regulation of inflammatory response Source: BHF-UCL
    14. negative regulation of interleukin-1 beta secretion Source: BHF-UCL
    15. negative regulation of NF-kappaB import into nucleus Source: HGNC
    16. negative regulation of NF-kappaB transcription factor activity Source: HGNC
    17. NLRP3 inflammasome complex assembly Source: Ensembl
    18. nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway Source: Reactome
    19. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: HGNC
    20. positive regulation of interleukin-1 beta secretion Source: HGNC
    21. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    22. protein oligomerization Source: HGNC
    23. signal transduction Source: UniProtKB

    Keywords - Biological processi

    Apoptosis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_75808. 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 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: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:16400. NLRP3.

    Subcellular locationi

    Cytoplasm 3 Publications

    GO - Cellular componenti

    1. cytoplasm Source: BHF-UCL
    2. cytosol Source: Reactome
    3. NLRP3 inflammasome complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Familial cold autoinflammatory syndrome 1 (FCAS1) [MIM:120100]: A 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.6 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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. 2 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) [MIM:191900]: A 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.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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. 2 Publications
    VAR_014104
    Natural varianti305 – 3051D → N in CINCA and MWS. 5 Publications
    VAR_014105
    Natural varianti307 – 3071L → P in FCAS1 and MWS. 2 Publications
    VAR_014124
    Natural varianti350 – 3501T → M in MWS and CINCA. 3 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) [MIM:607115]: Rare congenital inflammatory disorder characterized by a triad of neonatal onset of cutaneous symptoms, chronic meningitis, and joint manifestations with recurrent fever and inflammation.6 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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. 5 Publications
    VAR_014105
    Natural varianti308 – 3081Q → L in CINCA. 1 Publication
    VAR_043684
    Natural varianti311 – 3111F → S in CINCA. 2 Publications
    VAR_014106
    Natural varianti350 – 3501T → M in MWS and CINCA. 3 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

    Keywords - Diseasei

    Amyloidosis, Deafness, Disease mutation

    Organism-specific databases

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

    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 DAPIN domain may play a role in inflammation activation by reactive oxygen species.

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiQ96P20.
    PRIDEiQ96P20.

    PTM databases

    PhosphoSiteiQ96P20.

    Expressioni

    Tissue specificityi

    Expressed in blood leukocytes. Strongly expressed in polymorphonuclear cells and osteoblasts. Undetectable or expressed at a lower magnitude in B- and T-lymphoblasts, respectively. High level of expression detected in chondrocytes. Detected in non-keratinizing epithelia of oropharynx, esophagus and ectocervix and in the urothelial layer of the bladder.4 Publications

    Inductioni

    By TNF.1 Publication

    Gene expression databases

    ArrayExpressiQ96P20.
    BgeeiQ96P20.
    GenevestigatoriQ96P20.

    Organism-specific databases

    HPAiCAB009190.
    HPA012878.
    HPA017374.

    Interactioni

    Subunit structurei

    Part of the NALP3 inflammasome complex which is involved in activation of caspase-1 and caspase-5, leading to processing of IL1B and IL18. Interacts with PYCARD/ASC, PML (isoform PML-1), EIF2AK2/PKR and MEFV.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MAVSQ7Z4344EBI-6253230,EBI-995373
    PYCARDQ9ULZ34EBI-6253230,EBI-751215

    Protein-protein interaction databases

    BioGridi125319. 4 interactions.
    DIPiDIP-41153N.
    IntActiQ96P20. 3 interactions.
    MINTiMINT-230535.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3QF2X-ray1.70A/B3-112[»]
    ProteinModelPortaliQ96P20.
    SMRiQ96P20. Positions 5-110, 223-531, 666-1031.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 9393DAPINPROSITE-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

    Sequence similaritiesi

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

    Keywords - Domaini

    Leucine-rich repeat, Repeat

    Phylogenomic databases

    eggNOGiNOG82860.
    HOVERGENiHBG063656.
    InParanoidiQ96P20.
    KOiK12800.
    OMAiQRAMDYF.
    OrthoDBiEOG7P5T07.
    PhylomeDBiQ96P20.
    TreeFamiTF340267.

    Family and domain databases

    Gene3Di1.10.533.10. 1 hit.
    InterProiIPR004020. DAPIN.
    IPR011029. DEATH-like_dom.
    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. Align

    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

    MKMASTRCKL ARYLEDLEDV DLKKFKMHLE DYPPQKGCIP LPRGQTEKAD     50
    HVDLATLMID FNGEEKAWAM AVWIFAAINR RDLYEKAKRD EPKWGSDNAR 100
    VSNPTVICQE DSIEEEWMGL LEYLSRISIC KMKKDYRKKY RKYVRSRFQC 150
    IEDRNARLGE SVSLNKRYTR LRLIKEHRSQ QEREQELLAI GKTKTCESPV 200
    SPIKMELLFD PDDEHSEPVH TVVFQGAAGI GKTILARKMM LDWASGTLYQ 250
    DRFDYLFYIH CREVSLVTQR SLGDLIMSCC PDPNPPIHKI VRKPSRILFL 300
    MDGFDELQGA FDEHIGPLCT DWQKAERGDI LLSSLIRKKL LPEASLLITT 350
    RPVALEKLQH LLDHPRHVEI LGFSEAKRKE YFFKYFSDEA QARAAFSLIQ 400
    ENEVLFTMCF IPLVCWIVCT GLKQQMESGK SLAQTSKTTT AVYVFFLSSL 450
    LQPRGGSQEH GLCAHLWGLC SLAADGIWNQ KILFEESDLR NHGLQKADVS 500
    AFLRMNLFQK EVDCEKFYSF IHMTFQEFFA AMYYLLEEEK EGRTNVPGSR 550
    LKLPSRDVTV LLENYGKFEK GYLIFVVRFL FGLVNQERTS YLEKKLSCKI 600
    SQQIRLELLK WIEVKAKAKK LQIQPSQLEL FYCLYEMQEE DFVQRAMDYF 650
    PKIEINLSTR MDHMVSSFCI ENCHRVESLS LGFLHNMPKE EEEEEKEGRH 700
    LDMVQCVLPS SSHAACSHGL VNSHLTSSFC RGLFSVLSTS QSLTELDLSD 750
    NSLGDPGMRV LCETLQHPGC NIRRLWLGRC GLSHECCFDI SLVLSSNQKL 800
    VELDLSDNAL GDFGIRLLCV GLKHLLCNLK KLWLVSCCLT SACCQDLASV 850
    LSTSHSLTRL YVGENALGDS GVAILCEKAK NPQCNLQKLG LVNSGLTSVC 900
    CSALSSVLST NQNLTHLYLR GNTLGDKGIK LLCEGLLHPD CKLQVLELDN 950
    CNLTSHCCWD LSTLLTSSQS LRKLSLGNND LGDLGVMMFC EVLKQQSCLL 1000
    QNLGLSEMYF NYETKSALET LQEEKPELTV VFEPSW 1036
    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.
    The sequence AAL12497.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAL12498.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAL33908.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAL65136.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAQ98889.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAD92128.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAG37494.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAI17155.1 differs from that shown. Reason: Erroneous initiation.

    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. (PubMed:14702039)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. 2 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. 5 Publications
    VAR_014105
    Natural varianti307 – 3071L → P in FCAS1 and MWS. 2 Publications
    VAR_014124
    Natural varianti308 – 3081Q → L in CINCA. 1 Publication
    VAR_043684
    Natural varianti311 – 3111F → S in CINCA. 2 Publications
    VAR_014106
    Natural varianti350 – 3501T → M in MWS and CINCA. 3 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:
    EMBL
    GenBank
    DDBJ
    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.
    AY422168 mRNA. Translation: AAQ98889.1. Different initiation.
    AK314998 mRNA. Translation: BAG37494.1. Different initiation.
    AB208891 mRNA. Translation: BAD92128.1. Different initiation.
    AL606804, AC104335 Genomic DNA. Translation: CAI17153.1.
    AL606804, AC104335 Genomic DNA. Translation: CAI17154.1.
    AL606804, AC104335 Genomic DNA. Translation: CAI17155.1. Different initiation.
    CH471148 Genomic DNA. Translation: EAW77184.1.
    BC117211 mRNA. Translation: AAI17212.1.
    BC143359 mRNA. Translation: AAI43360.1.
    BC143362 mRNA. Translation: AAI43363.1.
    BC143363 mRNA. Translation: AAI43364.1.
    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_005273036.1. [Q96P20-1]
    XP_005273094.1. XM_005273037.1. [Q96P20-1]
    XP_005273095.1. XM_005273038.1. [Q96P20-4]
    XP_006711796.1. XM_006711733.1. [Q96P20-1]
    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]

    Polymorphism databases

    DMDMi262527566.

    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:
    EMBL
    GenBank
    DDBJ
    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 .
    AY422168 mRNA. Translation: AAQ98889.1 . Different initiation.
    AK314998 mRNA. Translation: BAG37494.1 . Different initiation.
    AB208891 mRNA. Translation: BAD92128.1 . Different initiation.
    AL606804 , AC104335 Genomic DNA. Translation: CAI17153.1 .
    AL606804 , AC104335 Genomic DNA. Translation: CAI17154.1 .
    AL606804 , AC104335 Genomic DNA. Translation: CAI17155.1 . Different initiation.
    CH471148 Genomic DNA. Translation: EAW77184.1 .
    BC117211 mRNA. Translation: AAI17212.1 .
    BC143359 mRNA. Translation: AAI43360.1 .
    BC143362 mRNA. Translation: AAI43363.1 .
    BC143363 mRNA. Translation: AAI43364.1 .
    AF054176 mRNA. Translation: AAC39910.1 . Frameshift.
    CCDSi CCDS1632.1. [Q96P20-1 ]
    CCDS1633.1. [Q96P20-2 ]
    CCDS44346.1. [Q96P20-5 ]
    CCDS44347.1. [Q96P20-4 ]
    RefSeqi NP_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_005273036.1. [Q96P20-1 ]
    XP_005273094.1. XM_005273037.1. [Q96P20-1 ]
    XP_005273095.1. XM_005273038.1. [Q96P20-4 ]
    XP_006711796.1. XM_006711733.1. [Q96P20-1 ]
    UniGenei Hs.159483.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3QF2 X-ray 1.70 A/B 3-112 [» ]
    ProteinModelPortali Q96P20.
    SMRi Q96P20. Positions 5-110, 223-531, 666-1031.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 125319. 4 interactions.
    DIPi DIP-41153N.
    IntActi Q96P20. 3 interactions.
    MINTi MINT-230535.

    Chemistry

    ChEMBLi CHEMBL1741208.

    PTM databases

    PhosphoSitei Q96P20.

    Polymorphism databases

    DMDMi 262527566.

    Proteomic databases

    PaxDbi Q96P20.
    PRIDEi Q96P20.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000336119 ; 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 ]
    GeneIDi 114548.
    KEGGi hsa:114548.
    UCSCi uc001icr.3. human. [Q96P20-1 ]
    uc001ics.3. human. [Q96P20-5 ]
    uc001icv.3. human. [Q96P20-2 ]
    uc001icw.3. human. [Q96P20-4 ]

    Organism-specific databases

    CTDi 114548.
    GeneCardsi GC01P247579.
    HGNCi HGNC:16400. NLRP3.
    HPAi CAB009190.
    HPA012878.
    HPA017374.
    MIMi 120100. phenotype.
    191900. phenotype.
    606416. gene.
    607115. phenotype.
    neXtProti NX_Q96P20.
    Orphaneti 93365. CINCA syndrome with NLRP3 mutations.
    47045. Familial cold urticaria.
    575. Muckle-Wells syndrome.
    PharmGKBi PA26512.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG82860.
    HOVERGENi HBG063656.
    InParanoidi Q96P20.
    KOi K12800.
    OMAi QRAMDYF.
    OrthoDBi EOG7P5T07.
    PhylomeDBi Q96P20.
    TreeFami TF340267.

    Enzyme and pathway databases

    Reactomei REACT_75808. The NLRP3 inflammasome.

    Miscellaneous databases

    GeneWikii NALP3.
    GenomeRNAii 114548.
    NextBioi 35481188.
    PROi Q96P20.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96P20.
    Bgeei Q96P20.
    Genevestigatori Q96P20.

    Family and domain databases

    Gene3Di 1.10.533.10. 1 hit.
    InterProi IPR004020. DAPIN.
    IPR011029. DEATH-like_dom.
    IPR003590. Leu-rich_rpt_RNase_inh_sub-typ.
    IPR007111. NACHT_NTPase.
    IPR029495. NATCH-assoc.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    Pfami PF14484. FISNA. 1 hit.
    PF02758. PYRIN. 1 hit.
    [Graphical view ]
    SMARTi SM00368. LRR_RI. 3 hits.
    [Graphical view ]
    SUPFAMi SSF47986. SSF47986. 1 hit.
    SSF52540. SSF52540. 2 hits.
    PROSITEi PS50824. DAPIN. 1 hit.
    PS50837. NACHT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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), FUNCTION, INTERACTION WITH PYCARD/ASC, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    4. "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] (ISOFORMS 1; 2 AND 4), FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY TNF.
    5. "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.
    6. 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.
    7. "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].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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.
    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 IN NALP3 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.
    15. Cited for: INTERACTION WITH EIF2AK2.
    16. "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.
    17. "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.
    18. "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 FCAS/MWS TRP-262.
    19. "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; LEU-308; SER-311; ARG-360; ASN-438; SER-575 AND THR-664, TISSUE SPECIFICITY.
    20. "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.
    21. "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.
    22. "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.
    23. "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.
    24. "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.
    25. "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.
    26. "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 nameiNALP3_HUMAN
    AccessioniPrimary (citable) accession number: Q96P20
    Secondary accession number(s): 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: October 1, 2014
    This is version 148 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

    External Data

    Dasty 3