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Q9NX02

- NALP2_HUMAN

UniProt

Q9NX02 - NALP2_HUMAN

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Protein

NACHT, LRR and PYD domains-containing protein 2

Gene

NLRP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Suppresses TNF- and CD40-induced NFKB1 activity at the level of the IKK complex, by inhibiting NFKBIA degradation induced by TNF. When associated with PYCARD, activates CASP1, leading to the secretion of mature proinflammatory cytokine IL1B. May be a component of the inflammasome, a protein complex which also includes PYCARD, CARD8 and CASP1 and whose function would be the activation of proinflammatory caspases.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi213 – 2208ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. Pyrin domain binding Source: HGNC

GO - Biological processi

  1. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: HGNC
  2. positive regulation of interleukin-1 beta secretion Source: HGNC
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
NACHT, LRR and PYD domains-containing protein 2
Alternative name(s):
Nucleotide-binding site protein 1
PYRIN domain and NACHT domain-containing protein 1
PYRIN-containing APAF1-like protein 2
Gene namesi
Name:NLRP2
Synonyms:NALP2, NBS1, PAN1, PYPAF2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:22948. NLRP2.

Subcellular locationi

Cytoplasm 2 Publications

GO - Cellular componenti

  1. cytoplasm Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162397946.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10621062NACHT, LRR and PYD domains-containing protein 2PRO_0000080888Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei671 – 6711Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9NX02.
PaxDbiQ9NX02.
PeptideAtlasiQ9NX02.
PRIDEiQ9NX02.

PTM databases

PhosphoSiteiQ9NX02.

Expressioni

Tissue specificityi

Expressed at high levels in lung, placenta and thymus and at lower levels in ovary, intestine and brain.1 Publication

Inductioni

By interferons and bacterial lipopolysaccharides (LPS).1 Publication

Gene expression databases

BgeeiQ9NX02.
CleanExiHS_NLRP2.
ExpressionAtlasiQ9NX02. baseline and differential.
GenevestigatoriQ9NX02.

Organism-specific databases

HPAiHPA020765.
HPA048863.

Interactioni

Subunit structurei

Interacts with CHUK, IKBKB, IKBKG and MEFV, as well as with full-length PYCARD and with the DAPIN domain of NAPL1, but not the full-length protein.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PYDC2Q56P426EBI-6374482,EBI-6374418

Protein-protein interaction databases

BioGridi120787. 10 interactions.
DIPiDIP-42460N.
IntActiQ9NX02. 1 interaction.
MINTiMINT-5006655.
STRINGi9606.ENSP00000263437.

Structurei

3D structure databases

ProteinModelPortaliQ9NX02.
SMRiQ9NX02. Positions 2-94, 205-230, 701-1043.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9494DAPINPROSITE-ProRule annotationAdd
BLAST
Domaini207 – 526320NACHTPROSITE-ProRule annotationAdd
BLAST
Repeati812 – 83221LRR 1Add
BLAST
Repeati841 – 86121LRR 2Add
BLAST
Repeati869 – 88921LRR 3Add
BLAST
Repeati898 – 91821LRR 4Add
BLAST
Repeati926 – 94621LRR 5Add
BLAST
Repeati955 – 97622LRR 6Add
BLAST
Repeati983 – 100321LRR 7Add
BLAST
Repeati1010 – 103324LRR 8Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi518 – 5236Poly-Glu

Domaini

The DAPIN domain is necessary and sufficient for suppression of NFKB1 activation induced by TNF and for inducing IL1B secretion in collaboration with caspase-1. It is involved in interaction with PYCARD.
When isolated, the NACHT domain is involved in interaction with CARD8. This interaction is not detected for the full-length protein, maybe due to autoinhibition, this inhibition might by relieved by an inducible change in protein folding.

Sequence similaritiesi

Belongs to the NLRP family.Curated
Contains 1 DAPIN domain.PROSITE-ProRule annotation
Contains 8 LRR (leucine-rich) repeats.Curated
Contains 1 NACHT domain.PROSITE-ProRule annotation

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiNOG146691.
GeneTreeiENSGT00760000118770.
HOVERGENiHBG103856.
InParanoidiQ9NX02.
OMAiELLRCDI.
PhylomeDBiQ9NX02.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR004020. DAPIN.
IPR011029. DEATH-like_dom.
IPR007111. NACHT_NTPase.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF02758. PYRIN. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEiPS50824. DAPIN. 1 hit.
PS50837. NACHT. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NX02-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVSSAQMGFN LQALLEQLSQ DELSKFKYLI TTFSLAHELQ KIPHKEVDKA
60 70 80 90 100
DGKQLVEILT THCDSYWVEM ASLQVFEKMH RMDLSERAKD EVREAALKSF
110 120 130 140 150
NKRKPLSLGI TRKERPPLDV DEMLERFKTE AQAFTETKGN VICLGKEVFK
160 170 180 190 200
GKKPDKDNRC RYILKTKFRE MWKSWPGDSK EVQVMAERYK MLIPFSNPRV
210 220 230 240 250
LPGPFSYTVV LYGPAGLGKT TLAQKLMLDW AEDNLIHKFK YAFYLSCREL
260 270 280 290 300
SRLGPCSFAE LVFRDWPELQ DDIPHILAQA RKILFVIDGF DELGAAPGAL
310 320 330 340 350
IEDICGDWEK KKPVPVLLGS LLNRVMLPKA ALLVTTRPRA LRDLRILAEE
360 370 380 390 400
PIYIRVEGFL EEDRRAYFLR HFGDEDQAMR AFELMRSNAA LFQLGSAPAV
410 420 430 440 450
CWIVCTTLKL QMEKGEDPVP TCLTRTGLFL RFLCSRFPQG AQLRGALRTL
460 470 480 490 500
SLLAAQGLWA QTSVLHREDL ERLGVQESDL RLFLDGDILR QDRVSKGCYS
510 520 530 540 550
FIHLSFQQFL TALFYTLEKE EEEDRDGHTW DIGDVQKLLS GVERLRNPDL
560 570 580 590 600
IQAGYYSFGL ANEKRAKELE ATFGCRMSPD IKQELLRCDI SCKGGHSTVT
610 620 630 640 650
DLQELLGCLY ESQEEELVKE VMAQFKEISL HLNAVDVVPS SFCVKHCRNL
660 670 680 690 700
QKMSLQVIKE NLPENVTASE SDAEVERSQD DQHMLPFWTD LCSIFGSNKD
710 720 730 740 750
LMGLAINDSF LSASLVRILC EQIASDTCHL QRVVFKNISP ADAHRNLCLA
760 770 780 790 800
LRGHKTVTYL TLQGNDQDDM FPALCEVLRH PECNLRYLGL VSCSATTQQW
810 820 830 840 850
ADLSLALEVN QSLTCVNLSD NELLDEGAKL LYTTLRHPKC FLQRLSLENC
860 870 880 890 900
HLTEANCKDL AAVLVVSREL THLCLAKNPI GNTGVKFLCE GLRYPECKLQ
910 920 930 940 950
TLVLWNCDIT SDGCCDLTKL LQEKSSLLCL DLGLNHIGVK GMKFLCEALR
960 970 980 990 1000
KPLCNLRCLW LWGCSIPPFS CEDLCSALSC NQSLVTLDLG QNPLGSSGVK
1010 1020 1030 1040 1050
MLFETLTCSS GTLRTLRLKI DDFNDELNKL LEEIEEKNPQ LIIDTEKHHP
1060
WAERPSSHDF MI
Length:1,062
Mass (Da):120,515
Last modified:October 1, 2000 - v1
Checksum:i4DBB0F6E9C2BC8A7
GO
Isoform 2 (identifier: Q9NX02-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     133-154: Missing.

Show »
Length:1,040
Mass (Da):118,138
Checksum:i0FF49C18762CEDB4
GO
Isoform 3 (identifier: Q9NX02-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     847-1062: Missing.

Note: No experimental confirmation available. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Show »
Length:846
Mass (Da):96,383
Checksum:i22DD3265062DC0CB
GO
Isoform 4 (identifier: Q9NX02-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     109-132: Missing.

Note: No experimental confirmation available.

Show »
Length:1,038
Mass (Da):117,674
Checksum:iAA066954D53827F2
GO
Isoform 5 (identifier: Q9NX02-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     47-69: Missing.

Note: No experimental confirmation available.

Show »
Length:1,039
Mass (Da):117,883
Checksum:iB55EABADF1A74126
GO

Sequence cautioni

The sequence BAD92537.1 differs from that shown. Reason: Erroneous prediction of the initiator methionine.
The sequence BAD92537.1 differs from that shown. Reason: Frameshift at position 769.
The sequence AAG15253.1 differs from that shown. Reason: Erroneous initiation.
The sequence BAA91377.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 11M → V in AAG15253. (PubMed:11270363)Curated
Sequence conflicti35 – 351L → P in AAG15253. (PubMed:11270363)Curated
Sequence conflicti46 – 461E → G in BAG64129. (PubMed:14702039)Curated
Sequence conflicti58 – 581I → V in AAH39269. (PubMed:15489334)Curated
Sequence conflicti175 – 1751W → C in BAD96973. 1 PublicationCurated
Sequence conflicti175 – 1751W → C in BAD96989. 1 PublicationCurated
Sequence conflicti216 – 2161G → S in BAG64129. (PubMed:14702039)Curated
Sequence conflicti304 – 3041I → S in BAB15293. (PubMed:14702039)Curated
Sequence conflicti980 – 9801Missing in AAG15253. (PubMed:11270363)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti221 – 2211T → M.
Corresponds to variant rs17699678 [ dbSNP | Ensembl ].
VAR_053616
Natural varianti302 – 3021E → Q.
Corresponds to variant rs3745904 [ dbSNP | Ensembl ].
VAR_053617
Natural varianti364 – 3641R → K.1 Publication
Corresponds to variant rs4306647 [ dbSNP | Ensembl ].
VAR_025011
Natural varianti516 – 5161T → A.1 Publication
Corresponds to variant rs61735082 [ dbSNP | Ensembl ].
VAR_068977
Natural varianti522 – 5221E → G.1 Publication
Corresponds to variant rs61735083 [ dbSNP | Ensembl ].
VAR_068978
Natural varianti529 – 5291T → A.2 Publications
Corresponds to variant rs34804158 [ dbSNP | Ensembl ].
VAR_068979
Natural varianti884 – 8841G → R.
Corresponds to variant rs59779270 [ dbSNP | Ensembl ].
VAR_062140
Natural varianti1052 – 10521A → E.1 Publication
Corresponds to variant rs1043673 [ dbSNP | Ensembl ].
VAR_020006

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei47 – 6923Missing in isoform 5. 1 PublicationVSP_044898Add
BLAST
Alternative sequencei109 – 13224Missing in isoform 4. 1 PublicationVSP_017085Add
BLAST
Alternative sequencei133 – 15422Missing in isoform 2. 1 PublicationVSP_005522Add
BLAST
Alternative sequencei847 – 1062216Missing in isoform 3. 1 PublicationVSP_017086Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF298547 mRNA. Translation: AAG15253.1. Different initiation.
AF310106 mRNA. Translation: AAG30289.1.
AF464764 mRNA. Translation: AAL69962.1.
AK000517 mRNA. Translation: BAA91223.1.
AK000784 mRNA. Translation: BAA91377.1. Different initiation.
AK025952 mRNA. Translation: BAB15293.1.
AK302989 mRNA. Translation: BAG64129.1.
AB209300 mRNA. Translation: BAD92537.1. Sequence problems.
AK223253 mRNA. Translation: BAD96973.1.
AK223269 mRNA. Translation: BAD96989.1.
AC011476 Genomic DNA. No translation available.
BC001039 mRNA. Translation: AAH01039.1.
BC003592 mRNA. Translation: AAH03592.1.
BC039269 mRNA. Translation: AAH39269.1.
CCDSiCCDS12913.1. [Q9NX02-1]
CCDS54318.1. [Q9NX02-5]
CCDS54319.1. [Q9NX02-2]
RefSeqiNP_001167552.1. NM_001174081.1. [Q9NX02-1]
NP_001167553.1. NM_001174082.1. [Q9NX02-2]
NP_001167554.1. NM_001174083.1. [Q9NX02-5]
NP_060322.1. NM_017852.3. [Q9NX02-1]
UniGeneiHs.369279.

Genome annotation databases

EnsembliENST00000339757; ENSP00000344074; ENSG00000022556. [Q9NX02-2]
ENST00000391721; ENSP00000375601; ENSG00000022556. [Q9NX02-4]
ENST00000427260; ENSP00000402474; ENSG00000022556. [Q9NX02-5]
ENST00000448584; ENSP00000409370; ENSG00000022556. [Q9NX02-1]
ENST00000537859; ENSP00000440601; ENSG00000022556. [Q9NX02-2]
ENST00000543010; ENSP00000445135; ENSG00000022556. [Q9NX02-1]
ENST00000613062; ENSP00000483281; ENSG00000273992. [Q9NX02-1]
ENST00000613485; ENSP00000484351; ENSG00000273992. [Q9NX02-2]
ENST00000615173; ENSP00000482889; ENSG00000273992. [Q9NX02-1]
ENST00000618731; ENSP00000478787; ENSG00000273992. [Q9NX02-2]
ENST00000621057; ENSP00000484382; ENSG00000273992. [Q9NX02-4]
ENST00000622773; ENSP00000484759; ENSG00000273992. [Q9NX02-5]
GeneIDi55655.
KEGGihsa:55655.
UCSCiuc002qij.3. human. [Q9NX02-1]
uc010esn.3. human. [Q9NX02-4]
uc010esp.3. human. [Q9NX02-2]

Polymorphism databases

DMDMi17380148.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF298547 mRNA. Translation: AAG15253.1 . Different initiation.
AF310106 mRNA. Translation: AAG30289.1 .
AF464764 mRNA. Translation: AAL69962.1 .
AK000517 mRNA. Translation: BAA91223.1 .
AK000784 mRNA. Translation: BAA91377.1 . Different initiation.
AK025952 mRNA. Translation: BAB15293.1 .
AK302989 mRNA. Translation: BAG64129.1 .
AB209300 mRNA. Translation: BAD92537.1 . Sequence problems.
AK223253 mRNA. Translation: BAD96973.1 .
AK223269 mRNA. Translation: BAD96989.1 .
AC011476 Genomic DNA. No translation available.
BC001039 mRNA. Translation: AAH01039.1 .
BC003592 mRNA. Translation: AAH03592.1 .
BC039269 mRNA. Translation: AAH39269.1 .
CCDSi CCDS12913.1. [Q9NX02-1 ]
CCDS54318.1. [Q9NX02-5 ]
CCDS54319.1. [Q9NX02-2 ]
RefSeqi NP_001167552.1. NM_001174081.1. [Q9NX02-1 ]
NP_001167553.1. NM_001174082.1. [Q9NX02-2 ]
NP_001167554.1. NM_001174083.1. [Q9NX02-5 ]
NP_060322.1. NM_017852.3. [Q9NX02-1 ]
UniGenei Hs.369279.

3D structure databases

ProteinModelPortali Q9NX02.
SMRi Q9NX02. Positions 2-94, 205-230, 701-1043.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120787. 10 interactions.
DIPi DIP-42460N.
IntActi Q9NX02. 1 interaction.
MINTi MINT-5006655.
STRINGi 9606.ENSP00000263437.

PTM databases

PhosphoSitei Q9NX02.

Polymorphism databases

DMDMi 17380148.

Proteomic databases

MaxQBi Q9NX02.
PaxDbi Q9NX02.
PeptideAtlasi Q9NX02.
PRIDEi Q9NX02.

Protocols and materials databases

DNASUi 55655.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000339757 ; ENSP00000344074 ; ENSG00000022556 . [Q9NX02-2 ]
ENST00000391721 ; ENSP00000375601 ; ENSG00000022556 . [Q9NX02-4 ]
ENST00000427260 ; ENSP00000402474 ; ENSG00000022556 . [Q9NX02-5 ]
ENST00000448584 ; ENSP00000409370 ; ENSG00000022556 . [Q9NX02-1 ]
ENST00000537859 ; ENSP00000440601 ; ENSG00000022556 . [Q9NX02-2 ]
ENST00000543010 ; ENSP00000445135 ; ENSG00000022556 . [Q9NX02-1 ]
ENST00000613062 ; ENSP00000483281 ; ENSG00000273992 . [Q9NX02-1 ]
ENST00000613485 ; ENSP00000484351 ; ENSG00000273992 . [Q9NX02-2 ]
ENST00000615173 ; ENSP00000482889 ; ENSG00000273992 . [Q9NX02-1 ]
ENST00000618731 ; ENSP00000478787 ; ENSG00000273992 . [Q9NX02-2 ]
ENST00000621057 ; ENSP00000484382 ; ENSG00000273992 . [Q9NX02-4 ]
ENST00000622773 ; ENSP00000484759 ; ENSG00000273992 . [Q9NX02-5 ]
GeneIDi 55655.
KEGGi hsa:55655.
UCSCi uc002qij.3. human. [Q9NX02-1 ]
uc010esn.3. human. [Q9NX02-4 ]
uc010esp.3. human. [Q9NX02-2 ]

Organism-specific databases

CTDi 55655.
GeneCardsi GC19P055476.
HGNCi HGNC:22948. NLRP2.
HPAi HPA020765.
HPA048863.
MIMi 609364. gene.
neXtProti NX_Q9NX02.
PharmGKBi PA162397946.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG146691.
GeneTreei ENSGT00760000118770.
HOVERGENi HBG103856.
InParanoidi Q9NX02.
OMAi ELLRCDI.
PhylomeDBi Q9NX02.

Miscellaneous databases

GeneWikii NLRP2.
GenomeRNAii 55655.
NextBioi 60371.
PROi Q9NX02.
SOURCEi Search...

Gene expression databases

Bgeei Q9NX02.
CleanExi HS_NLRP2.
ExpressionAtlasi Q9NX02. baseline and differential.
Genevestigatori Q9NX02.

Family and domain databases

Gene3Di 1.10.533.10. 1 hit.
3.40.50.300. 1 hit.
InterProi IPR004020. DAPIN.
IPR011029. DEATH-like_dom.
IPR007111. NACHT_NTPase.
IPR027417. P-loop_NTPase.
[Graphical view ]
Pfami PF02758. PYRIN. 1 hit.
[Graphical view ]
SUPFAMi SSF47986. SSF47986. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEi PS50824. DAPIN. 1 hit.
PS50837. NACHT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« 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), VARIANT LYS-364.
  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 1).
  3. "PYPAF7, a novel PYRIN-containing Apaf1-like protein that regulates activation of NF-kappa B and caspase-1-dependent cytokine processing."
    Wang L., Manji G.A., Grenier J.M., Al-Garawi A., Merriam S., Lora J.M., Geddes B.J., Briskin M., DiStefano P.S., Bertin J.
    J. Biol. Chem. 277:29874-29880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "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 1 AND 5), VARIANTS ALA-516; GLY-522 AND ALA-529.
    Tissue: Colon, Kidney epithelium and Testis.
  5. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), VARIANT ALA-529.
    Tissue: Brain and Gastric mucosa.
  6. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), VARIANT GLU-1052.
    Tissue: Lung, Placenta and Testis.
  8. "NALP3 forms an IL-1beta-processing inflammasome with increased activity in Muckle-Wells autoinflammatory disorder."
    Agostini L., Martinon F., Burns K., McDermott M.F., Hawkins P.N., Tschopp J.
    Immunity 20:319-325(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PYCARD AND CARD8, SUBCELLULAR LOCATION.
  9. "PAN1/NALP2/PYPAF2, an inducible inflammatory mediator that regulates NF-kappaB and caspase-1 activation in macrophages."
    Bruey J.-M., Bruey-Sedano N., Newman R., Chandler S., Stehlik C., Reed J.C.
    J. Biol. Chem. 279:51897-51907(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CHUK; IKBKB; IKBKG AND PYCARD, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
  10. "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.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-671, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNALP2_HUMAN
AccessioniPrimary (citable) accession number: Q9NX02
Secondary accession number(s): B4DZL7
, I3L0G4, Q53FL5, Q59G09, Q8IXT0, Q9BVN5, Q9H6G6, Q9HAV9, Q9NWK3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: October 1, 2000
Last modified: October 29, 2014
This is version 143 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3