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Q9C000 (NALP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:NLRP1
Synonyms:CARD7, DEFCAP, KIAA0926, NAC, NALP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1473 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.10 Ref.12 Ref.15

Subunit structure

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. Ref.4 Ref.10 Ref.13 Ref.16

Subcellular location

Cytoplasm. Nucleus Ref.14.

Tissue specificity

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. Ref.11 Ref.14 Ref.17

Involvement in disease

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.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.19

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. Ref.19

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.17 Ref.19

Sequence similarities

Belongs to the NLRP family.

Contains 1 CARD domain.

Contains 1 DAPIN domain.

Contains 6 LRR (leucine-rich) repeats.

Contains 1 NACHT domain.

Sequence caution

The sequence BAA76770.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAB15469.1 differs from that shown. Reason: Frameshift at position 1241.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Ectodermal dysplasia
   DomainLeucine-rich repeat
Repeat
   LigandATP-binding
Nucleotide-binding
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of cysteine-type endopeptidase activity involved in apoptotic process

Non-traceable author statement Ref.3. Source: UniProtKB

apoptotic process

Non-traceable author statement Ref.3. Source: UniProtKB

defense response to bacterium

Inferred from sequence or structural similarity. Source: BHF-UCL

innate immune response

Traceable author statement. Source: Reactome

neuron apoptotic process

Inferred from direct assay Ref.12. Source: HGNC

nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway

Traceable author statement. Source: Reactome

positive regulation of interleukin-1 beta secretion

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of inflammatory response

Inferred by curator Ref.12. Source: BHF-UCL

response to muramyl dipeptide

Inferred from sequence or structural similarity. Source: BHF-UCL

   Cellular_componentNLRP1 inflammasome complex

Inferred from direct assay Ref.10. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

intracellular

Inferred by curator Ref.3. Source: UniProtKB

nucleus

Inferred from direct assay Ref.14. Source: BHF-UCL

   Molecular_functionATP binding

Inferred from direct assay Ref.12. Source: HGNC

cysteine-type endopeptidase activator activity involved in apoptotic process

Non-traceable author statement Ref.3. Source: UniProtKB

enzyme binding

Inferred from physical interaction Ref.3. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 11472070Ref.16. Source: UniProtKB

protein domain specific binding

Inferred from physical interaction PubMed 16575408. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9C000-1)

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.
Isoform 2 (identifier: Q9C000-2)

Also known as: NAC alpha; DEFCAP-S;

The sequence of this isoform differs from the canonical sequence as follows:
     1262-1305: Missing.
Isoform 3 (identifier: Q9C000-3)

Also known as: NAC gamma;

The sequence of this isoform differs from the canonical sequence as follows:
     958-987: Missing.
     1262-1305: Missing.
Isoform 4 (identifier: Q9C000-4)

Also known as: NAC delta;

The sequence of this isoform differs from the canonical sequence as follows:
     958-987: Missing.
Isoform 5 (identifier: Q9C000-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1044-1044: A → AGKSH
     1354-1371: DLMPATTLIPPARIAVPS → RNTSQPWNLRCNRDARRY
     1372-1473: Missing.
Isoform 6 (identifier: Q9C000-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-734: Missing.
Isoform 7 (identifier: Q9C000-7)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14731473NACHT, LRR and PYD domains-containing protein 1
PRO_0000096710

Regions

Domain1 – 9292DAPIN
Domain328 – 637310NACHT
Repeat809 – 83022LRR 1
Repeat838 – 85821LRR 2
Repeat866 – 88722LRR 3
Repeat895 – 91521LRR 4
Repeat923 – 94422LRR 5
Repeat950 – 97324LRR 6
Domain1374 – 146390CARD
Nucleotide binding334 – 3418ATP Potential

Natural variations

Alternative sequence1 – 966966Missing in isoform 7.
VSP_053801
Alternative sequence1 – 734734Missing in isoform 6.
VSP_053802
Alternative sequence958 – 98730Missing in isoform 3 and isoform 4.
VSP_004326
Alternative sequence10441A → AGKSH in isoform 5 and isoform 7.
VSP_053803
Alternative sequence1262 – 130544Missing in isoform 2 and isoform 3.
VSP_004327
Alternative sequence1354 – 137118DLMPA…IAVPS → RNTSQPWNLRCNRDARRY in isoform 5 and isoform 7.
VSP_053804
Alternative sequence1372 – 1473102Missing in isoform 5 and isoform 7.
VSP_053805
Natural variant771M → T in CIDED. Ref.17
VAR_069901
Natural variant1551L → H Associated with susceptibility to vitiligo and vitiligo-associated autoimmune diseases. Ref.1 Ref.19
Corresponds to variant rs12150220 [ dbSNP | Ensembl ].
VAR_033239
Natural variant2461T → S. Ref.1
Corresponds to variant rs11651595 [ dbSNP | Ensembl ].
VAR_024238
Natural variant4041R → Q.
Corresponds to variant rs3744718 [ dbSNP | Ensembl ].
VAR_021886
Natural variant8781T → M. Ref.1
Corresponds to variant rs11657747 [ dbSNP | Ensembl ].
VAR_033240
Natural variant10591V → M.
Corresponds to variant rs2301582 [ dbSNP | Ensembl ].
VAR_024239
Natural variant10691H → Y.
Corresponds to variant rs9907167 [ dbSNP | Ensembl ].
VAR_033241
Natural variant11191M → V. Ref.1
Corresponds to variant rs35596958 [ dbSNP | Ensembl ].
VAR_033242
Natural variant11841M → V. Ref.1 Ref.9
Corresponds to variant rs11651270 [ dbSNP | Ensembl ].
VAR_033243
Natural variant12411V → L. Ref.1
Corresponds to variant rs11653832 [ dbSNP | Ensembl ].
VAR_033244
Natural variant13661R → C. Ref.1
Corresponds to variant rs2137722 [ dbSNP | Ensembl ].
VAR_020437

Experimental info

Mutagenesis339 – 3402GK → EA: Abolishes binding to ATP. Ref.3 Ref.12
Mutagenesis3401K → L or S: No effect. Ref.3 Ref.12
Sequence conflict2871P → S in AAH51787. Ref.8
Sequence conflict7821T → S in AAG15254. Ref.1
Sequence conflict9951T → I in AAG15254. Ref.1

Secondary structure

............................................................. 1473
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (NAC beta) (DEFCAP-L) [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 438F0DCE45C2562D

FASTA1,473165,866
        10         20         30         40         50         60 
MAGGAWGRLA CYLEFLKKEE LKEFQLLLAN KAHSRSSSGE TPAQPEKTSG MEVASYLVAQ 

        70         80         90        100        110        120 
YGEQRAWDLA LHTWEQMGLR SLCAQAQEGA GHSPSFPYSP SEPHLGSPSQ PTSTAVLMPW 

       130        140        150        160        170        180 
IHELPAGCTQ GSERRVLRQL PDTSGRRWRE ISASLLYQAL PSSPDHESPS QESPNAPTST 

       190        200        210        220        230        240 
AVLGSWGSPP QPSLAPREQE APGTQWPLDE TSGIYYTEIR EREREKSEKG RPPWAAVVGT 

       250        260        270        280        290        300 
PPQAHTSLQP HHHPWEPSVR ESLCSTWPWK NEDFNQKFTQ LLLLQRPHPR SQDPLVKRSW 

       310        320        330        340        350        360 
PDYVEENRGH LIEIRDLFGP GLDTQEPRIV ILQGAAGIGK STLARQVKEA WGRGQLYGDR 

       370        380        390        400        410        420 
FQHVFYFSCR ELAQSKVVSL AELIGKDGTA TPAPIRQILS RPERLLFILD GVDEPGWVLQ 

       430        440        450        460        470        480 
EPSSELCLHW SQPQPADALL GSLLGKTILP EASFLITART TALQNLIPSL EQARWVEVLG 

       490        500        510        520        530        540 
FSESSRKEYF YRYFTDERQA IRAFRLVKSN KELWALCLVP WVSWLACTCL MQQMKRKEKL 

       550        560        570        580        590        600 
TLTSKTTTTL CLHYLAQALQ AQPLGPQLRD LCSLAAEGIW QKKTLFSPDD LRKHGLDGAI 

       610        620        630        640        650        660 
ISTFLKMGIL QEHPIPLSYS FIHLCFQEFF AAMSYVLEDE KGRGKHSNCI IDLEKTLEAY 

       670        680        690        700        710        720 
GIHGLFGAST TRFLLGLLSD EGEREMENIF HCRLSQGRNL MQWVPSLQLL LQPHSLESLH 

       730        740        750        760        770        780 
CLYETRNKTF LTQVMAHFEE MGMCVETDME LLVCTFCIKF SRHVKKLQLI EGRQHRSTWS 

       790        800        810        820        830        840 
PTMVVLFRWV PVTDAYWQIL FSVLKVTRNL KELDLSGNSL SHSAVKSLCK TLRRPRCLLE 

       850        860        870        880        890        900 
TLRLAGCGLT AEDCKDLAFG LRANQTLTEL DLSFNVLTDA GAKHLCQRLR QPSCKLQRLQ 

       910        920        930        940        950        960 
LVSCGLTSDC CQDLASVLSA SPSLKELDLQ QNNLDDVGVR LLCEGLRHPA CKLIRLGLDQ 

       970        980        990       1000       1010       1020 
TTLSDEMRQE LRALEQEKPQ LLIFSRRKPS VMTPTEGLDT GEMSNSTSSL KRQRLGSERA 

      1030       1040       1050       1060       1070       1080 
ASHVAQANLK LLDVSKIFPI AEIAEESSPE VVPVELLCVP SPASQGDLHT KPLGTDDDFW 

      1090       1100       1110       1120       1130       1140 
GPTGPVATEV VDKEKNLYRV HFPVAGSYRW PNTGLCFVMR EAVTVEIEFC VWDQFLGEIN 

      1150       1160       1170       1180       1190       1200 
PQHSWMVAGP LLDIKAEPGA VEAVHLPHFV ALQGGHVDTS LFQMAHFKEE GMLLEKPARV 

      1210       1220       1230       1240       1250       1260 
ELHHIVLENP SFSPLGVLLK MIHNALRFIP VTSVVLLYHR VHPEEVTFHL YLIPSDCSIR 

      1270       1280       1290       1300       1310       1320 
KAIDDLEMKF QFVRIHKPPP LTPLYMGCRY TVSGSGSGML EILPKELELC YRSPGEDQLF 

      1330       1340       1350       1360       1370       1380 
SEFYVGHLGS GIRLQVKDKK DETLVWEALV KPGDLMPATT LIPPARIAVP SPLDAPQLLH 

      1390       1400       1410       1420       1430       1440 
FVDQYREQLI ARVTSVEVVL DKLHGQVLSQ EQYERVLAEN TRPSQMRKLF SLSQSWDRKC 

      1450       1460       1470 
KDGLYQALKE THPHLIMELW EKGSKKGLLP LSS 

« Hide

Isoform 2 (NAC alpha) (DEFCAP-S) [UniParc].

Checksum: 6C5CBE8FD2819435
Show »

FASTA1,429160,946
Isoform 3 (NAC gamma) [UniParc].

Checksum: 59C172B75766F38F
Show »

FASTA1,399157,319
Isoform 4 (NAC delta) [UniParc].

Checksum: C30E9BE9EC82FE96
Show »

FASTA1,443162,239
Isoform 5 [UniParc].

Checksum: BC6844DC6B4FDB0A
Show »

FASTA1,375154,881
Isoform 6 [UniParc].

Checksum: 41E23E686642323B
Show »

FASTA73983,100
Isoform 7 [UniParc].

Checksum: 07CC5FACF3EB7236
Show »

FASTA40946,068

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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]"Expression of NALP1 in cerebellar granule neurons stimulates apoptosis."
Liu F., Lo C.F., Ning X., Kajkowski E.M., Jin M., Chiriac C., Gonzales C., Naureckiene S., Lock Y.-W., Pong K., Zaleska M.M., Jacobsen J.S., Silverman S., Ozenberger B.A.
Cell. Signal. 16:1013-1021(2004) [PubMed] [Europe PMC] [Abstract]
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]"Novel role of PKR in inflammasome activation and HMGB1 release."
Lu B., Nakamura T., Inouye K., Li J., Tang Y., Lundbaeck P., Valdes-Ferrer S.I., Olofsson P.S., Kalb T., Roth J., Zou Y., Erlandsson-Harris H., Yang H., Ting J.P., Wang H., Andersson U., Antoine D.J., Chavan S.S., Hotamisligil G.S., Tracey K.J.
Nature 488:670-674(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EIF2AK2.
[17]"Whole exome sequencing identifies a mutation for a novel form of corneal intraepithelial dyskeratosis."
Soler V.J., Tran-Viet K.N., Galiacy S.D., Limviphuvadh V., Klemm T.P., St Germain E., Fournie P.R., Guillaud C., Maurer-Stroh S., Hawthorne F., Suarez C., Kantelip B., Afshari N.A., Creveaux I., Luo X., Meng W., Calvas P., Cassagne M. expand/collapse author list , Arne J.L., Rozen S.G., Malecaze F., Young T.L.
J. Med. Genet. 50:246-254(2013) [PubMed] [Europe PMC] [Abstract]
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]"NALP1 in vitiligo-associated multiple autoimmune disease."
Jin Y., Mailloux C.M., Gowan K., Riccardi S.L., LaBerge G., Bennett D.C., Fain P.R., Spritz R.A.
N. Engl. J. Med. 356:1216-1225(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS42244.1. [Q9C000-4]
CCDS42245.1. [Q9C000-2]
CCDS42246.1. [Q9C000-1]
CCDS58508.1. [Q9C000-3]
PIRT17255.
RefSeqNP_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]
UniGeneHs.652273.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PN5NMR-A1-93[»]
3KATX-ray3.10A1371-1467[»]
4IFPX-ray1.99A/B/C1379-1462[»]
4IM6X-ray1.65A791-990[»]
DisProtDP00554.
ProteinModelPortalQ9C000.
SMRQ9C000. Positions 1-93, 325-350, 763-1035, 1379-1462.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116529. 5 interactions.
DIPDIP-38407N.
IntActQ9C000. 9 interactions.
MINTMINT-150191.

Chemistry

BindingDBQ9C000.
ChEMBLCHEMBL1741214.
GuidetoPHARMACOLOGY1768.

Protein family/group databases

MEROPSS79.002.

PTM databases

PhosphoSiteQ9C000.

Polymorphism databases

DMDM17380146.

Proteomic databases

PaxDbQ9C000.
PRIDEQ9C000.

Protocols and materials databases

DNASU22861.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262467; ENSP00000262467; ENSG00000091592.
ENST00000269280; ENSP00000269280; ENSG00000091592. [Q9C000-2]
ENST00000345221; ENSP00000324366; ENSG00000091592. [Q9C000-2]
ENST00000354411; ENSP00000346390; ENSG00000091592. [Q9C000-4]
ENST00000544378; ENSP00000442029; ENSG00000091592.
ENST00000572272; ENSP00000460475; ENSG00000091592. [Q9C000-1]
ENST00000577119; ENSP00000460216; ENSG00000091592. [Q9C000-3]
GeneID22861.
KEGGhsa:22861.
UCSCuc002gch.4. human. [Q9C000-2]
uc002gci.3. human. [Q9C000-1]
uc002gcj.3. human. [Q9C000-4]
uc002gcl.3. human. [Q9C000-3]

Organism-specific databases

CTD22861.
GeneCardsGC17M005407.
HGNCHGNC:14374. NLRP1.
HPACAB009189.
MIM193200. phenotype.
606579. phenotype.
606636. gene.
615225. phenotype.
neXtProtNX_Q9C000.
Orphanet352662. Corneal intraepithelial dyskeratosis with palmoplantar hyperkeratosis and laryngeal dyskeratosis.
3435. Vitiligo.
247871. Vitiligo-associated autoimmune disease.
PharmGKBPA162397797.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG146295.
HOGENOMHOG000230509.
HOVERGENHBG052573.
InParanoidQ9C000.
KOK12798.
OMAHPHLIME.
OrthoDBEOG7P5T07.
PhylomeDBQ9C000.
TreeFamTF340267.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressQ9C000.
BgeeQ9C000.
CleanExHS_NLRP1.
GenevestigatorQ9C000.

Family and domain databases

Gene3D1.10.533.10. 2 hits.
InterProIPR001315. 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]
PfamPF00619. CARD. 1 hit.
PF13553. FIIND. 1 hit.
PF02758. PYRIN. 1 hit.
[Graphical view]
PRINTSPR00364. DISEASERSIST.
SUPFAMSSF47986. SSF47986. 2 hits.
SSF52540. SSF52540. 2 hits.
PROSITEPS50209. CARD. 1 hit.
PS50824. DAPIN. 1 hit.
PS51450. LRR. 3 hits.
PS50837. NACHT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNLRP1. human.
EvolutionaryTraceQ9C000.
GeneWikiNLRP1.
GenomeRNAi22861.
NextBio35533902.
PROQ9C000.
SOURCESearch...

Entry information

Entry nameNALP1_HUMAN
AccessionPrimary (citable) accession number: Q9C000
Secondary accession number(s): E9PE50 expand/collapse secondary AC list , I6L9D9, Q9BZZ8, Q9BZZ9, Q9H5Z7, Q9H5Z8, Q9HAV8, Q9UFT4, Q9Y2E0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 152 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM