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Q9C000

- NALP1_HUMAN

UniProt

Q9C000 - NALP1_HUMAN

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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

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 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
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_75927. The NLRP1 inflammasome.

Protein family/group databases

MEROPSiS79.A03.

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
Complete GO annotation...

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. 1 Publication

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

BgeeiQ9C000.
CleanExiHS_NLRP1.
ExpressionAtlasiQ9C000. baseline and differential.
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. 7 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 – 157Combined sources
Helixi18 – 3114Combined sources
Helixi50 – 6011Combined sources
Helixi63 – 7715Combined sources
Helixi80 – 856Combined sources
Beta strandi88 – 914Combined sources
Helixi794 – 80411Combined sources
Beta strandi812 – 8143Combined sources
Helixi822 – 83312Combined sources
Beta strandi840 – 8434Combined sources
Helixi851 – 86212Combined sources
Beta strandi869 – 8713Combined sources
Helixi878 – 88912Combined sources
Beta strandi898 – 9003Combined sources
Helixi908 – 9103Combined sources
Helixi911 – 92010Combined sources
Beta strandi926 – 9283Combined sources
Beta strandi931 – 9333Combined sources
Helixi935 – 94612Combined sources
Beta strandi955 – 9573Combined sources
Helixi965 – 97713Combined sources
Beta strandi982 – 9843Combined sources
Helixi1381 – 13844Combined sources
Helixi1386 – 13927Combined sources
Helixi1396 – 14038Combined sources
Turni1405 – 14073Combined sources
Helixi1410 – 14178Combined sources
Beta strandi1419 – 14213Combined sources
Helixi1422 – 143312Combined sources
Helixi1438 – 145114Combined sources
Helixi1453 – 146210Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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, 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.
GeneTreeiENSGT00770000120466.
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.
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]
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

        10         20         30         40         50
MAGGAWGRLA CYLEFLKKEE LKEFQLLLAN KAHSRSSSGE TPAQPEKTSG
60 70 80 90 100
MEVASYLVAQ YGEQRAWDLA LHTWEQMGLR SLCAQAQEGA GHSPSFPYSP
110 120 130 140 150
SEPHLGSPSQ PTSTAVLMPW IHELPAGCTQ GSERRVLRQL PDTSGRRWRE
160 170 180 190 200
ISASLLYQAL PSSPDHESPS QESPNAPTST AVLGSWGSPP QPSLAPREQE
210 220 230 240 250
APGTQWPLDE TSGIYYTEIR EREREKSEKG RPPWAAVVGT PPQAHTSLQP
260 270 280 290 300
HHHPWEPSVR ESLCSTWPWK NEDFNQKFTQ LLLLQRPHPR SQDPLVKRSW
310 320 330 340 350
PDYVEENRGH LIEIRDLFGP GLDTQEPRIV ILQGAAGIGK STLARQVKEA
360 370 380 390 400
WGRGQLYGDR FQHVFYFSCR ELAQSKVVSL AELIGKDGTA TPAPIRQILS
410 420 430 440 450
RPERLLFILD GVDEPGWVLQ EPSSELCLHW SQPQPADALL GSLLGKTILP
460 470 480 490 500
EASFLITART TALQNLIPSL EQARWVEVLG FSESSRKEYF YRYFTDERQA
510 520 530 540 550
IRAFRLVKSN KELWALCLVP WVSWLACTCL MQQMKRKEKL TLTSKTTTTL
560 570 580 590 600
CLHYLAQALQ AQPLGPQLRD LCSLAAEGIW QKKTLFSPDD LRKHGLDGAI
610 620 630 640 650
ISTFLKMGIL QEHPIPLSYS FIHLCFQEFF AAMSYVLEDE KGRGKHSNCI
660 670 680 690 700
IDLEKTLEAY GIHGLFGAST TRFLLGLLSD EGEREMENIF HCRLSQGRNL
710 720 730 740 750
MQWVPSLQLL LQPHSLESLH CLYETRNKTF LTQVMAHFEE MGMCVETDME
760 770 780 790 800
LLVCTFCIKF SRHVKKLQLI EGRQHRSTWS PTMVVLFRWV PVTDAYWQIL
810 820 830 840 850
FSVLKVTRNL KELDLSGNSL SHSAVKSLCK TLRRPRCLLE TLRLAGCGLT
860 870 880 890 900
AEDCKDLAFG LRANQTLTEL DLSFNVLTDA GAKHLCQRLR QPSCKLQRLQ
910 920 930 940 950
LVSCGLTSDC CQDLASVLSA SPSLKELDLQ QNNLDDVGVR LLCEGLRHPA
960 970 980 990 1000
CKLIRLGLDQ TTLSDEMRQE LRALEQEKPQ LLIFSRRKPS VMTPTEGLDT
1010 1020 1030 1040 1050
GEMSNSTSSL KRQRLGSERA ASHVAQANLK LLDVSKIFPI AEIAEESSPE
1060 1070 1080 1090 1100
VVPVELLCVP SPASQGDLHT KPLGTDDDFW GPTGPVATEV VDKEKNLYRV
1110 1120 1130 1140 1150
HFPVAGSYRW PNTGLCFVMR EAVTVEIEFC VWDQFLGEIN PQHSWMVAGP
1160 1170 1180 1190 1200
LLDIKAEPGA VEAVHLPHFV ALQGGHVDTS LFQMAHFKEE GMLLEKPARV
1210 1220 1230 1240 1250
ELHHIVLENP SFSPLGVLLK MIHNALRFIP VTSVVLLYHR VHPEEVTFHL
1260 1270 1280 1290 1300
YLIPSDCSIR KAIDDLEMKF QFVRIHKPPP LTPLYMGCRY TVSGSGSGML
1310 1320 1330 1340 1350
EILPKELELC YRSPGEDQLF SEFYVGHLGS GIRLQVKDKK DETLVWEALV
1360 1370 1380 1390 1400
KPGDLMPATT LIPPARIAVP SPLDAPQLLH FVDQYREQLI ARVTSVEVVL
1410 1420 1430 1440 1450
DKLHGQVLSQ EQYERVLAEN TRPSQMRKLF SLSQSWDRKC KDGLYQALKE
1460 1470
THPHLIMELW EKGSKKGLLP LSS
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 BAA76770.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAB15469.1 differs from that shown. Reason: Frameshift at position 1241. Curated

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:
EMBLi
GenBanki
DDBJi
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]
ENST00000613500; ENSP00000483359; ENSG00000091592. [Q9C000-5]
ENST00000617618; ENSP00000478516; ENSG00000091592. [Q9C000-1]
ENST00000619223; ENSP00000484692; ENSG00000091592. [Q9C000-4]
GeneIDi22861.
KEGGihsa:22861.
UCSCiuc002gcg.1. human.
uc002gch.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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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, 763-1035, 1379-1462.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116529. 7 interactions.
DIPi DIP-38407N.
IntActi Q9C000. 9 interactions.
MINTi MINT-150191.

Chemistry

BindingDBi Q9C000.
ChEMBLi CHEMBL1741214.
GuidetoPHARMACOLOGYi 1768.

Protein family/group databases

MEROPSi S79.A03.

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 ]
ENST00000613500 ; ENSP00000483359 ; ENSG00000091592 . [Q9C000-5 ]
ENST00000617618 ; ENSP00000478516 ; ENSG00000091592 . [Q9C000-1 ]
ENST00000619223 ; ENSP00000484692 ; ENSG00000091592 . [Q9C000-4 ]
GeneIDi 22861.
KEGGi hsa:22861.
UCSCi uc002gcg.1. human.
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.
GeneTreei ENSGT00770000120466.
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

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

Gene expression databases

Bgeei Q9C000.
CleanExi HS_NLRP1.
ExpressionAtlasi Q9C000. baseline and differential.
Genevestigatori Q9C000.

Family and domain databases

Gene3Di 1.10.533.10. 2 hits.
InterProi IPR001315. CARD.
IPR004020. DAPIN.
IPR011029. DEATH-like_dom.
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 ]
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 156 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