Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

Q9C000

- NALP1_HUMAN

UniProt

Q9C000 - NALP1_HUMAN

Protein

NACHT, LRR and PYD domains-containing protein 1

Gene

NLRP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Able to form cytoplasmic structures termed death effector filaments. Enhances APAF1 and cytochrome c-dependent activation of pro-caspase-9 and consecutive apoptosis. Stimulates apoptosis through activation of caspase-3. Involved in activation of caspase-1 and caspase-5 as part of the NALP1 inflammasome complex which leads to processing and release of IL1B and IL18. Binds ATP.3 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi334 – 3418ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: HGNC
    2. cysteine-type endopeptidase activator activity involved in apoptotic process Source: UniProtKB
    3. enzyme binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein domain specific binding Source: UniProtKB

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    2. apoptotic process Source: UniProtKB
    3. defense response to bacterium Source: BHF-UCL
    4. innate immune response Source: Reactome
    5. neuron apoptotic process Source: HGNC
    6. nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway Source: Reactome
    7. positive regulation of interleukin-1 beta secretion Source: BHF-UCL
    8. regulation of inflammatory response Source: BHF-UCL
    9. response to muramyl dipeptide Source: BHF-UCL

    Keywords - Biological processi

    Apoptosis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_75927. The NLRP1 inflammasome.

    Protein family/group databases

    MEROPSiS79.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NACHT, LRR and PYD domains-containing protein 1
    Alternative name(s):
    Caspase recruitment domain-containing protein 7
    Death effector filament-forming ced-4-like apoptosis protein
    Nucleotide-binding domain and caspase recruitment domain
    Gene namesi
    Name:NLRP1
    Synonyms:CARD7, DEFCAP, KIAA0926, NAC, NALP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:14374. NLRP1.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. intracellular Source: UniProtKB
    3. NLRP1 inflammasome complex Source: UniProtKB
    4. nucleus Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Vitiligo (VTLG) [MIM:193200]: A pigmentary disorder of the skin and mucous membranes. It is characterized by circumscribed depigmented macules and patches, commonly on extensor aspects of extremities, on the face or neck and in skin folds. Vitiligo is a progressive disorder in which some or all of the melanocytes in the affected skin are selectively destroyed. It is a multifactorial disorder with a complex etiology probably including autoimmune mechanisms, and is associated with an elevated risk of other autoimmune diseases.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
    Vitiligo-associated multiple autoimmune disease 1 (VAMAS1) [MIM:606579]: A disorder characterized by the association of vitiligo with several autoimmune and autoinflammatory diseases including autoimmune thyroid disease, rheumatoid arthritis and systemic lupus erythematosus.
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
    Corneal intraepithelial dyskeratosis and ectodermal dysplasia (CIDED) [MIM:615225]: A disease characterized by keratopathy with neovascularization, bilateral corneal opacification, palmoplantar hyperkeratosis, dyshidrosis, and dystrophic nails.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti77 – 771M → T in CIDED. 1 Publication
    VAR_069901

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi339 – 3402GK → EA: Abolishes binding to ATP. 1 Publication
    Mutagenesisi340 – 3401K → L or S: No effect. 2 Publications

    Keywords - Diseasei

    Disease mutation, Ectodermal dysplasia

    Organism-specific databases

    MIMi193200. phenotype.
    606579. phenotype.
    615225. phenotype.
    Orphaneti352662. Corneal intraepithelial dyskeratosis with palmoplantar hyperkeratosis and laryngeal dyskeratosis.
    3435. Vitiligo.
    247871. Vitiligo-associated autoimmune disease.
    PharmGKBiPA162397797.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14731473NACHT, LRR and PYD domains-containing protein 1PRO_0000096710Add
    BLAST

    Proteomic databases

    PaxDbiQ9C000.
    PRIDEiQ9C000.

    PTM databases

    PhosphoSiteiQ9C000.

    Expressioni

    Tissue specificityi

    Widely expressed. Isoform 1 and isoform 2 are expressed in peripheral blood leukocytes and chronic myelogenous leukemia cell line K-562, followed by thymus, spleen and heart. Also detected in brain, lung, placenta, small intestine, colon, kidney, liver, muscle, testis and epithelial cells. Absent from hematopoietic progenitor cells but expressed upon differentiation of cells into granulocytes and, to a lesser extent, monocytes. In peripheral blood cells, highest levels are found in T-lymphocytes, granulocytes and monocytes. Expression is significantly increased in bone marrow blast cells of some acute leukemia patients but not in solid tumors. Expressed in adult cornea as well as adult and 24-week fetal tissues, including choroid, sclera, cornea, optic nerve, and adult retina and fetal retina/retinal pigment epithelium. In addition, expressed in corneal epithelia obtained during photorefractive keratectomy.3 Publications

    Gene expression databases

    ArrayExpressiQ9C000.
    BgeeiQ9C000.
    CleanExiHS_NLRP1.
    GenevestigatoriQ9C000.

    Organism-specific databases

    HPAiCAB009189.

    Interactioni

    Subunit structurei

    Interacts strongly with caspase-2, weakly with caspase-9 and with APAF1 in a cytochrome c-inducible way, leading to the formation of an apoptosome. This interaction may be ATP-dependent. Part of the NALP1 inflammasome complex which is involved in activation of caspase-1 and caspase-5, leading to processing of IL1B and IL18. The complex is activated by bacterial muramyl dipeptide which triggers ATP-binding and oligomerization of NALP1. Interacts with EIF2AK2/PKR and MEFV.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BCL2P1041512EBI-1220518,EBI-77694
    BCL2L1Q078179EBI-1220518,EBI-78035
    PYCARDQ9ULZ35EBI-1220518,EBI-751215

    Protein-protein interaction databases

    BioGridi116529. 5 interactions.
    DIPiDIP-38407N.
    IntActiQ9C000. 9 interactions.
    MINTiMINT-150191.

    Structurei

    Secondary structure

    1
    1473
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 157
    Helixi18 – 3114
    Helixi50 – 6011
    Helixi63 – 7715
    Helixi80 – 856
    Beta strandi88 – 914
    Helixi794 – 80411
    Beta strandi812 – 8143
    Helixi822 – 83312
    Beta strandi840 – 8434
    Helixi851 – 86212
    Beta strandi869 – 8713
    Helixi878 – 88912
    Beta strandi898 – 9003
    Helixi908 – 9103
    Helixi911 – 92010
    Beta strandi926 – 9283
    Beta strandi931 – 9333
    Helixi935 – 94612
    Beta strandi955 – 9573
    Helixi965 – 97713
    Beta strandi982 – 9843
    Helixi1381 – 13844
    Helixi1386 – 13927
    Helixi1396 – 14038
    Turni1405 – 14073
    Helixi1410 – 14178
    Beta strandi1419 – 14213
    Helixi1422 – 143312
    Helixi1438 – 145114
    Helixi1453 – 146210

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1PN5NMR-A1-93[»]
    3KATX-ray3.10A1371-1467[»]
    4IFPX-ray1.99A/B/C1379-1462[»]
    4IM6X-ray1.65A791-990[»]
    DisProtiDP00554.
    ProteinModelPortaliQ9C000.
    SMRiQ9C000. Positions 1-93, 325-350, 763-1035, 1379-1462.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9C000.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 9292DAPINPROSITE-ProRule annotationAdd
    BLAST
    Domaini328 – 637310NACHTPROSITE-ProRule annotationAdd
    BLAST
    Repeati809 – 83022LRR 1Add
    BLAST
    Repeati838 – 85821LRR 2Add
    BLAST
    Repeati866 – 88722LRR 3Add
    BLAST
    Repeati895 – 91521LRR 4Add
    BLAST
    Repeati923 – 94422LRR 5Add
    BLAST
    Repeati950 – 97324LRR 6Add
    BLAST
    Domaini1374 – 146390CARDPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the NLRP family.Curated
    Contains 1 CARD domain.PROSITE-ProRule annotation
    Contains 1 DAPIN domain.PROSITE-ProRule annotation
    Contains 6 LRR (leucine-rich) repeats.Curated
    Contains 1 NACHT domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Leucine-rich repeat, Repeat

    Phylogenomic databases

    eggNOGiNOG146295.
    HOGENOMiHOG000230509.
    HOVERGENiHBG052573.
    InParanoidiQ9C000.
    KOiK12798.
    OMAiHPHLIME.
    OrthoDBiEOG7P5T07.
    PhylomeDBiQ9C000.
    TreeFamiTF340267.

    Family and domain databases

    Gene3Di1.10.533.10. 2 hits.
    InterProiIPR001315. CARD.
    IPR004020. DAPIN.
    IPR011029. DEATH-like_dom.
    IPR000767. Disease_R.
    IPR025307. FIIND_dom.
    IPR001611. Leu-rich_rpt.
    IPR007111. NACHT_NTPase.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF00619. CARD. 1 hit.
    PF13553. FIIND. 1 hit.
    PF02758. PYRIN. 1 hit.
    [Graphical view]
    PRINTSiPR00364. DISEASERSIST.
    SUPFAMiSSF47986. SSF47986. 2 hits.
    SSF52540. SSF52540. 2 hits.
    PROSITEiPS50209. CARD. 1 hit.
    PS50824. DAPIN. 1 hit.
    PS51450. LRR. 3 hits.
    PS50837. NACHT. 1 hit.
    [Graphical view]

    Sequences (7)i

    Sequence statusi: Complete.

    This entry describes 7 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9C000-1) [UniParc]FASTAAdd to Basket

    Also known as: NAC beta, DEFCAP-L

    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

    MAGGAWGRLA CYLEFLKKEE LKEFQLLLAN KAHSRSSSGE TPAQPEKTSG     50
    MEVASYLVAQ YGEQRAWDLA LHTWEQMGLR SLCAQAQEGA GHSPSFPYSP 100
    SEPHLGSPSQ PTSTAVLMPW IHELPAGCTQ GSERRVLRQL PDTSGRRWRE 150
    ISASLLYQAL PSSPDHESPS QESPNAPTST AVLGSWGSPP QPSLAPREQE 200
    APGTQWPLDE TSGIYYTEIR EREREKSEKG RPPWAAVVGT PPQAHTSLQP 250
    HHHPWEPSVR ESLCSTWPWK NEDFNQKFTQ LLLLQRPHPR SQDPLVKRSW 300
    PDYVEENRGH LIEIRDLFGP GLDTQEPRIV ILQGAAGIGK STLARQVKEA 350
    WGRGQLYGDR FQHVFYFSCR ELAQSKVVSL AELIGKDGTA TPAPIRQILS 400
    RPERLLFILD GVDEPGWVLQ EPSSELCLHW SQPQPADALL GSLLGKTILP 450
    EASFLITART TALQNLIPSL EQARWVEVLG FSESSRKEYF YRYFTDERQA 500
    IRAFRLVKSN KELWALCLVP WVSWLACTCL MQQMKRKEKL TLTSKTTTTL 550
    CLHYLAQALQ AQPLGPQLRD LCSLAAEGIW QKKTLFSPDD LRKHGLDGAI 600
    ISTFLKMGIL QEHPIPLSYS FIHLCFQEFF AAMSYVLEDE KGRGKHSNCI 650
    IDLEKTLEAY GIHGLFGAST TRFLLGLLSD EGEREMENIF HCRLSQGRNL 700
    MQWVPSLQLL LQPHSLESLH CLYETRNKTF LTQVMAHFEE MGMCVETDME 750
    LLVCTFCIKF SRHVKKLQLI EGRQHRSTWS PTMVVLFRWV PVTDAYWQIL 800
    FSVLKVTRNL KELDLSGNSL SHSAVKSLCK TLRRPRCLLE TLRLAGCGLT 850
    AEDCKDLAFG LRANQTLTEL DLSFNVLTDA GAKHLCQRLR QPSCKLQRLQ 900
    LVSCGLTSDC CQDLASVLSA SPSLKELDLQ QNNLDDVGVR LLCEGLRHPA 950
    CKLIRLGLDQ TTLSDEMRQE LRALEQEKPQ LLIFSRRKPS VMTPTEGLDT 1000
    GEMSNSTSSL KRQRLGSERA ASHVAQANLK LLDVSKIFPI AEIAEESSPE 1050
    VVPVELLCVP SPASQGDLHT KPLGTDDDFW GPTGPVATEV VDKEKNLYRV 1100
    HFPVAGSYRW PNTGLCFVMR EAVTVEIEFC VWDQFLGEIN PQHSWMVAGP 1150
    LLDIKAEPGA VEAVHLPHFV ALQGGHVDTS LFQMAHFKEE GMLLEKPARV 1200
    ELHHIVLENP SFSPLGVLLK MIHNALRFIP VTSVVLLYHR VHPEEVTFHL 1250
    YLIPSDCSIR KAIDDLEMKF QFVRIHKPPP LTPLYMGCRY TVSGSGSGML 1300
    EILPKELELC YRSPGEDQLF SEFYVGHLGS GIRLQVKDKK DETLVWEALV 1350
    KPGDLMPATT LIPPARIAVP SPLDAPQLLH FVDQYREQLI ARVTSVEVVL 1400
    DKLHGQVLSQ EQYERVLAEN TRPSQMRKLF SLSQSWDRKC KDGLYQALKE 1450
    THPHLIMELW EKGSKKGLLP LSS 1473
    Length:1,473
    Mass (Da):165,866
    Last modified:June 1, 2001 - v1
    Checksum:i438F0DCE45C2562D
    GO
    Isoform 2 (identifier: Q9C000-2) [UniParc]FASTAAdd to Basket

    Also known as: NAC alpha, DEFCAP-S

    The sequence of this isoform differs from the canonical sequence as follows:
         1262-1305: Missing.

    Show »
    Length:1,429
    Mass (Da):160,946
    Checksum:i6C5CBE8FD2819435
    GO
    Isoform 3 (identifier: Q9C000-3) [UniParc]FASTAAdd to Basket

    Also known as: NAC gamma

    The sequence of this isoform differs from the canonical sequence as follows:
         958-987: Missing.
         1262-1305: Missing.

    Show »
    Length:1,399
    Mass (Da):157,319
    Checksum:i59C172B75766F38F
    GO
    Isoform 4 (identifier: Q9C000-4) [UniParc]FASTAAdd to Basket

    Also known as: NAC delta

    The sequence of this isoform differs from the canonical sequence as follows:
         958-987: Missing.

    Show »
    Length:1,443
    Mass (Da):162,239
    Checksum:iC30E9BE9EC82FE96
    GO
    Isoform 5 (identifier: Q9C000-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1044-1044: A → AGKSH
         1354-1371: DLMPATTLIPPARIAVPS → RNTSQPWNLRCNRDARRY
         1372-1473: Missing.

    Show »
    Length:1,375
    Mass (Da):154,881
    Checksum:iBC6844DC6B4FDB0A
    GO
    Isoform 6 (identifier: Q9C000-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-734: Missing.

    Show »
    Length:739
    Mass (Da):83,100
    Checksum:i41E23E686642323B
    GO
    Isoform 7 (identifier: Q9C000-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-966: Missing.
         1044-1044: A → AGKSH
         1354-1371: DLMPATTLIPPARIAVPS → RNTSQPWNLRCNRDARRY
         1372-1473: Missing.

    Show »
    Length:409
    Mass (Da):46,068
    Checksum:i07CC5FACF3EB7236
    GO

    Sequence cautioni

    The sequence BAB15469.1 differs from that shown. Reason: Frameshift at position 1241.
    The sequence BAA76770.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti287 – 2871P → S in AAH51787. (PubMed:15489334)Curated
    Sequence conflicti782 – 7821T → S in AAG15254. (PubMed:11270363)Curated
    Sequence conflicti995 – 9951T → I in AAG15254. (PubMed:11270363)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti77 – 771M → T in CIDED. 1 Publication
    VAR_069901
    Natural varianti155 – 1551L → H Associated with susceptibility to vitiligo and vitiligo-associated autoimmune diseases. 2 Publications
    Corresponds to variant rs12150220 [ dbSNP | Ensembl ].
    VAR_033239
    Natural varianti246 – 2461T → S.1 Publication
    Corresponds to variant rs11651595 [ dbSNP | Ensembl ].
    VAR_024238
    Natural varianti404 – 4041R → Q.
    Corresponds to variant rs3744718 [ dbSNP | Ensembl ].
    VAR_021886
    Natural varianti878 – 8781T → M.1 Publication
    Corresponds to variant rs11657747 [ dbSNP | Ensembl ].
    VAR_033240
    Natural varianti1059 – 10591V → M.
    Corresponds to variant rs2301582 [ dbSNP | Ensembl ].
    VAR_024239
    Natural varianti1069 – 10691H → Y.
    Corresponds to variant rs9907167 [ dbSNP | Ensembl ].
    VAR_033241
    Natural varianti1119 – 11191M → V.1 Publication
    Corresponds to variant rs35596958 [ dbSNP | Ensembl ].
    VAR_033242
    Natural varianti1184 – 11841M → V.2 Publications
    Corresponds to variant rs11651270 [ dbSNP | Ensembl ].
    VAR_033243
    Natural varianti1241 – 12411V → L.1 Publication
    Corresponds to variant rs11653832 [ dbSNP | Ensembl ].
    VAR_033244
    Natural varianti1366 – 13661R → C.1 Publication
    Corresponds to variant rs2137722 [ dbSNP | Ensembl ].
    VAR_020437

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 966966Missing in isoform 7. 1 PublicationVSP_053801Add
    BLAST
    Alternative sequencei1 – 734734Missing in isoform 6. 1 PublicationVSP_053802Add
    BLAST
    Alternative sequencei958 – 98730Missing in isoform 3 and isoform 4. 1 PublicationVSP_004326Add
    BLAST
    Alternative sequencei1044 – 10441A → AGKSH in isoform 5 and isoform 7. 2 PublicationsVSP_053803
    Alternative sequencei1262 – 130544Missing in isoform 2 and isoform 3. 5 PublicationsVSP_004327Add
    BLAST
    Alternative sequencei1354 – 137118DLMPA…IAVPS → RNTSQPWNLRCNRDARRY in isoform 5 and isoform 7. 2 PublicationsVSP_053804Add
    BLAST
    Alternative sequencei1372 – 1473102Missing in isoform 5 and isoform 7. 2 PublicationsVSP_053805Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF298548 mRNA. Translation: AAG15254.1.
    AF310105 mRNA. Translation: AAG30288.1.
    AF229059 mRNA. Translation: AAK00748.1.
    AF229060 mRNA. Translation: AAK00749.1.
    AF229061 mRNA. Translation: AAK00750.1.
    AF229062 mRNA. Translation: AAK00751.1.
    AB023143 mRNA. Translation: BAA76770.2. Different initiation.
    AK026393 mRNA. Translation: BAB15469.1. Frameshift.
    AK026398 mRNA. Translation: BAB15470.1.
    AC055839 Genomic DNA. No translation available.
    BC051787 mRNA. Translation: AAH51787.1.
    AL117470 mRNA. Translation: CAB55945.1.
    CCDSiCCDS32537.1. [Q9C000-5]
    CCDS42244.1. [Q9C000-4]
    CCDS42245.1. [Q9C000-2]
    CCDS42246.1. [Q9C000-1]
    CCDS58508.1. [Q9C000-3]
    PIRiT17255.
    RefSeqiNP_001028225.1. NM_001033053.2. [Q9C000-5]
    NP_055737.1. NM_014922.4. [Q9C000-2]
    NP_127497.1. NM_033004.3. [Q9C000-1]
    NP_127499.1. NM_033006.3. [Q9C000-4]
    NP_127500.1. NM_033007.3. [Q9C000-3]
    UniGeneiHs.652273.

    Genome annotation databases

    EnsembliENST00000262467; ENSP00000262467; ENSG00000091592. [Q9C000-5]
    ENST00000269280; ENSP00000269280; ENSG00000091592. [Q9C000-2]
    ENST00000345221; ENSP00000324366; ENSG00000091592. [Q9C000-2]
    ENST00000354411; ENSP00000346390; ENSG00000091592. [Q9C000-4]
    ENST00000544378; ENSP00000442029; ENSG00000091592. [Q9C000-5]
    ENST00000572272; ENSP00000460475; ENSG00000091592. [Q9C000-1]
    ENST00000577119; ENSP00000460216; ENSG00000091592. [Q9C000-3]
    GeneIDi22861.
    KEGGihsa:22861.
    UCSCiuc002gch.4. human. [Q9C000-2]
    uc002gci.3. human. [Q9C000-1]
    uc002gcj.3. human. [Q9C000-4]
    uc002gcl.3. human. [Q9C000-3]

    Polymorphism databases

    DMDMi17380146.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF298548 mRNA. Translation: AAG15254.1 .
    AF310105 mRNA. Translation: AAG30288.1 .
    AF229059 mRNA. Translation: AAK00748.1 .
    AF229060 mRNA. Translation: AAK00749.1 .
    AF229061 mRNA. Translation: AAK00750.1 .
    AF229062 mRNA. Translation: AAK00751.1 .
    AB023143 mRNA. Translation: BAA76770.2 . Different initiation.
    AK026393 mRNA. Translation: BAB15469.1 . Frameshift.
    AK026398 mRNA. Translation: BAB15470.1 .
    AC055839 Genomic DNA. No translation available.
    BC051787 mRNA. Translation: AAH51787.1 .
    AL117470 mRNA. Translation: CAB55945.1 .
    CCDSi CCDS32537.1. [Q9C000-5 ]
    CCDS42244.1. [Q9C000-4 ]
    CCDS42245.1. [Q9C000-2 ]
    CCDS42246.1. [Q9C000-1 ]
    CCDS58508.1. [Q9C000-3 ]
    PIRi T17255.
    RefSeqi NP_001028225.1. NM_001033053.2. [Q9C000-5 ]
    NP_055737.1. NM_014922.4. [Q9C000-2 ]
    NP_127497.1. NM_033004.3. [Q9C000-1 ]
    NP_127499.1. NM_033006.3. [Q9C000-4 ]
    NP_127500.1. NM_033007.3. [Q9C000-3 ]
    UniGenei Hs.652273.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1PN5 NMR - A 1-93 [» ]
    3KAT X-ray 3.10 A 1371-1467 [» ]
    4IFP X-ray 1.99 A/B/C 1379-1462 [» ]
    4IM6 X-ray 1.65 A 791-990 [» ]
    DisProti DP00554.
    ProteinModelPortali Q9C000.
    SMRi Q9C000. Positions 1-93, 325-350, 763-1035, 1379-1462.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116529. 5 interactions.
    DIPi DIP-38407N.
    IntActi Q9C000. 9 interactions.
    MINTi MINT-150191.

    Chemistry

    BindingDBi Q9C000.
    ChEMBLi CHEMBL1741214.
    GuidetoPHARMACOLOGYi 1768.

    Protein family/group databases

    MEROPSi S79.002.

    PTM databases

    PhosphoSitei Q9C000.

    Polymorphism databases

    DMDMi 17380146.

    Proteomic databases

    PaxDbi Q9C000.
    PRIDEi Q9C000.

    Protocols and materials databases

    DNASUi 22861.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262467 ; ENSP00000262467 ; ENSG00000091592 . [Q9C000-5 ]
    ENST00000269280 ; ENSP00000269280 ; ENSG00000091592 . [Q9C000-2 ]
    ENST00000345221 ; ENSP00000324366 ; ENSG00000091592 . [Q9C000-2 ]
    ENST00000354411 ; ENSP00000346390 ; ENSG00000091592 . [Q9C000-4 ]
    ENST00000544378 ; ENSP00000442029 ; ENSG00000091592 . [Q9C000-5 ]
    ENST00000572272 ; ENSP00000460475 ; ENSG00000091592 . [Q9C000-1 ]
    ENST00000577119 ; ENSP00000460216 ; ENSG00000091592 . [Q9C000-3 ]
    GeneIDi 22861.
    KEGGi hsa:22861.
    UCSCi uc002gch.4. human. [Q9C000-2 ]
    uc002gci.3. human. [Q9C000-1 ]
    uc002gcj.3. human. [Q9C000-4 ]
    uc002gcl.3. human. [Q9C000-3 ]

    Organism-specific databases

    CTDi 22861.
    GeneCardsi GC17M005407.
    HGNCi HGNC:14374. NLRP1.
    HPAi CAB009189.
    MIMi 193200. phenotype.
    606579. phenotype.
    606636. gene.
    615225. phenotype.
    neXtProti NX_Q9C000.
    Orphaneti 352662. Corneal intraepithelial dyskeratosis with palmoplantar hyperkeratosis and laryngeal dyskeratosis.
    3435. Vitiligo.
    247871. Vitiligo-associated autoimmune disease.
    PharmGKBi PA162397797.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG146295.
    HOGENOMi HOG000230509.
    HOVERGENi HBG052573.
    InParanoidi Q9C000.
    KOi K12798.
    OMAi HPHLIME.
    OrthoDBi EOG7P5T07.
    PhylomeDBi Q9C000.
    TreeFami TF340267.

    Enzyme and pathway databases

    Reactomei REACT_75927. The NLRP1 inflammasome.

    Miscellaneous databases

    ChiTaRSi NLRP1. human.
    EvolutionaryTracei Q9C000.
    GeneWikii NLRP1.
    GenomeRNAii 22861.
    NextBioi 35533902.
    PROi Q9C000.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9C000.
    Bgeei Q9C000.
    CleanExi HS_NLRP1.
    Genevestigatori Q9C000.

    Family and domain databases

    Gene3Di 1.10.533.10. 2 hits.
    InterProi IPR001315. CARD.
    IPR004020. DAPIN.
    IPR011029. DEATH-like_dom.
    IPR000767. Disease_R.
    IPR025307. FIIND_dom.
    IPR001611. Leu-rich_rpt.
    IPR007111. NACHT_NTPase.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    Pfami PF00619. CARD. 1 hit.
    PF13553. FIIND. 1 hit.
    PF02758. PYRIN. 1 hit.
    [Graphical view ]
    PRINTSi PR00364. DISEASERSIST.
    SUPFAMi SSF47986. SSF47986. 2 hits.
    SSF52540. SSF52540. 2 hits.
    PROSITEi PS50209. CARD. 1 hit.
    PS50824. DAPIN. 1 hit.
    PS51450. LRR. 3 hits.
    PS50837. NACHT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The PYRIN domain: a novel motif found in apoptosis and inflammation proteins."
      Bertin J., DiStefano P.S.
      Cell Death Differ. 7:1273-1274(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANTS HIS-155; SER-246; MET-878; VAL-1119; VAL-1184; LEU-1241 AND CYS-1366.
    2. "The pyrin domain: a possible member of the death domain-fold family implicated in apoptosis and inflammation."
      Martinon F., Hofmann K., Tschopp J.
      Curr. Biol. 11:R118-R120(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    3. "Molecular cloning and characterization of DEFCAP-L and -S, two isoforms of a novel member of the mammalian Ced-4 family of apoptosis proteins."
      Hlaing T., Guo R.-F., Dilley K.A., Loussia J.M., Morrish T.A., Shi M.M., Vincenz C., Ward P.A.
      J. Biol. Chem. 276:9230-9238(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), MUTAGENESIS OF LYS-340.
      Tissue: Erythroleukemia.
    4. "A novel enhancer of the Apaf1 apoptosome involved in cytochrome c-dependent caspase activation and apoptosis."
      Chu Z.-L., Pio F., Xie Z., Welsh K., Krajewska M., Krajewski S., Godzik A., Reed J.C.
      J. Biol. Chem. 276:9239-9245(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), INTERACTION WITH CASP2 AND CASP9.
      Tissue: T-cell.
    5. "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    6. "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] (ISOFORMS 6 AND 7).
    7. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
      Tissue: Blood.
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 282-1473 (ISOFORM 1), VARIANT VAL-1184.
      Tissue: Uterus.
    10. "The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta."
      Martinon F., Burns K., Tschopp J.
      Mol. Cell 10:417-426(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN NALP1 INFLAMMASOME COMPLEX.
    11. "NALP1 is a transcriptional target for cAMP-response-element-binding protein (CREB) in myeloid leukaemia cells."
      Sanz C., Calasanz M.J., Andreu E., Richard C., Prosper F., Fernandez-Luna J.L.
      Biochem. J. 384:281-286(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    12. Cited for: FUNCTION, MUTAGENESIS OF 339-GLY-LYS-340.
    13. "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.
    14. "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.
    15. "Reconstituted NALP1 inflammasome reveals two-step mechanism of caspase-1 activation."
      Faustin B., Lartigue L., Bruey J.-M., Luciano F., Sergienko E., Bailly-Maitre B., Volkmann N., Hanein D., Rouiller I., Reed J.C.
      Mol. Cell 25:713-724(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. Cited for: INTERACTION WITH EIF2AK2.
    17. Cited for: TISSUE SPECIFICITY, VARIANT CIDED THR-77.
    18. "NMR structure of the apoptosis- and inflammation-related NALP1 pyrin domain."
      Hiller S., Kohl A., Fiorito F., Herrmann T., Wider G., Tschopp J., Gruetter M.G., Wuethrich K.
      Structure 11:1199-1205(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-93.
    19. Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO VITILIGO AND VITILIGO-ASSOCIATED AUTOIMMUNE DISEASES, VARIANT HIS-155.
    20. "Northeast structural genomics consortium target HR3486E."
      Northeast structural genomics consortium (NESG)
      Submitted (OCT-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1371-1467.

    Entry informationi

    Entry nameiNALP1_HUMAN
    AccessioniPrimary (citable) accession number: Q9C000
    Secondary accession number(s): E9PE50
    , I6L9D9, Q9BZZ8, Q9BZZ9, Q9H5Z7, Q9H5Z8, Q9HAV8, Q9UFT4, Q9Y2E0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 18, 2001
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 154 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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