NALP2_HUMAN
ID NALP2_HUMAN Reviewed; 1062 AA.
AC Q9NX02; B4DZL7; I3L0G4; Q53FL5; Q59G09; Q8IXT0; Q9BVN5; Q9H6G6; Q9HAV9;
AC Q9NWK3;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=NACHT, LRR and PYD domains-containing protein 2;
DE AltName: Full=Nucleotide-binding site protein 1;
DE AltName: Full=PYRIN domain and NACHT domain-containing protein 1;
DE AltName: Full=PYRIN-containing APAF1-like protein 2;
GN Name=NLRP2; Synonyms=NALP2, NBS1, PAN1, PYPAF2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT LYS-364.
RX PubMed=11270363; DOI=10.1038/sj.cdd.4400774;
RA Bertin J., DiStefano P.S.;
RT "The PYRIN domain: a novel motif found in apoptosis and inflammation
RT proteins.";
RL Cell Death Differ. 7:1273-1274(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=11250163; DOI=10.1016/s0960-9822(01)00056-2;
RA Martinon F., Hofmann K., Tschopp J.;
RT "The pyrin domain: a possible member of the death domain-fold family
RT implicated in apoptosis and inflammation.";
RL Curr. Biol. 11:R118-R120(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=12019269; DOI=10.1074/jbc.m203915200;
RA Wang L., Manji G.A., Grenier J.M., Al-Garawi A., Merriam S., Lora J.M.,
RA Geddes B.J., Briskin M., DiStefano P.S., Bertin J.;
RT "PYPAF7, a novel PYRIN-containing Apaf1-like protein that regulates
RT activation of NF-kappa B and caspase-1-dependent cytokine processing.";
RL J. Biol. Chem. 277:29874-29880(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5), AND VARIANTS
RP ALA-516; GLY-522 AND ALA-529.
RC TISSUE=Colon, Kidney epithelium, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND VARIANT
RP ALA-529.
RC TISSUE=Brain, and Gastric mucosa;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP GLU-1052.
RC TISSUE=Lung, Placenta, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP INTERACTION WITH PYCARD AND CARD8, AND SUBCELLULAR LOCATION.
RX PubMed=15030775; DOI=10.1016/s1074-7613(04)00046-9;
RA Agostini L., Martinon F., Burns K., McDermott M.F., Hawkins P.N.,
RA Tschopp J.;
RT "NALP3 forms an IL-1beta-processing inflammasome with increased activity in
RT Muckle-Wells autoinflammatory disorder.";
RL Immunity 20:319-325(2004).
RN [9]
RP FUNCTION, INTERACTION WITH CHUK; IKBKB; IKBKG AND PYCARD, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15456791; DOI=10.1074/jbc.m406741200;
RA Bruey J.-M., Bruey-Sedano N., Newman R., Chandler S., Stehlik C.,
RA Reed J.C.;
RT "PAN1/NALP2/PYPAF2, an inducible inflammatory mediator that regulates NF-
RT kappaB and caspase-1 activation in macrophages.";
RL J. Biol. Chem. 279:51897-51907(2004).
RN [10]
RP INTERACTION WITH MEFV.
RX PubMed=17431422; DOI=10.1038/sj.cdd.4402142;
RA Papin S., Cuenin S., Agostini L., Martinon F., Werner S., Beer H.D.,
RA Grutter C., Grutter M., Tschopp J.;
RT "The SPRY domain of Pyrin, mutated in familial Mediterranean fever
RT patients, interacts with inflammasome components and inhibits proIL-1beta
RT processing.";
RL Cell Death Differ. 14:1457-1466(2007).
RN [11]
RP INTERACTION WITH PYDC2.
RX PubMed=17178784; DOI=10.1128/iai.01315-06;
RA Dorfleutner A., Bryan N.B., Talbott S.J., Funya K.N., Rellick S.L.,
RA Reed J.C., Shi X., Rojanasakul Y., Flynn D.C., Stehlik C.;
RT "Cellular pyrin domain-only protein 2 is a candidate regulator of
RT inflammasome activation.";
RL Infect. Immun. 75:1484-1492(2007).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-671, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-671, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP TISSUE SPECIFICITY, AND VARIANTS CYS-175; MET-221; SER-258; VAL-616;
RP ASP-848; 654-SER--ILE-1062 DEL AND 752-ARG--ILE-1062 DEL.
RX PubMed=30877238; DOI=10.1136/jmedgenet-2018-105936;
RA Mu J., Wang W., Chen B., Wu L., Li B., Mao X., Zhang Z., Fu J., Kuang Y.,
RA Sun X., Li Q., Jin L., He L., Sang Q., Wang L.;
RT "Mutations in NLRP2 and NLRP5 cause female infertility characterised by
RT early embryonic arrest.";
RL J. Med. Genet. 56:471-480(2019).
RN [16]
RP VARIANT 115-ARG--ILE-1062 DEL.
RX PubMed=33020905; DOI=10.1111/cge.13858;
RA Zheng W., Hu H., Dai J., Zhang S., Gu Y., Dai C., Guo J., Xu X., Li Y.,
RA Zhang S., Hu L., Gong F., Lu G., Lin G.;
RT "Expanding the genetic and phenotypic spectrum of the subcortical maternal
RT complex genes in recurrent preimplantation embryonic arrest.";
RL Clin. Genet. 99:286-291(2021).
CC -!- FUNCTION: Suppresses TNF- and CD40-induced NFKB1 activity at the level
CC of the IKK complex, by inhibiting NFKBIA degradation induced by TNF.
CC When associated with PYCARD, activates CASP1, leading to the secretion
CC of mature pro-inflammatory cytokine IL1B. May be a component of the
CC inflammasome, a protein complex which also includes PYCARD, CARD8 and
CC CASP1 and whose function would be the activation of pro-inflammatory
CC caspases. {ECO:0000269|PubMed:15456791}.
CC -!- SUBUNIT: Interacts with CHUK (PubMed:15456791). Interacts with IKBKB
CC (PubMed:15456791). Interacts with IKBKG (PubMed:15456791). Interacts
CC with MEFV (PubMed:17431422). Interacts with PYCARD (PubMed:15030775,
CC PubMed:15456791). Interacts (via pyrin domain) with PYDC2
CC (PubMed:17178784). Interacts with CARD8 (PubMed:15030775).
CC {ECO:0000269|PubMed:15030775, ECO:0000269|PubMed:15456791,
CC ECO:0000269|PubMed:17178784, ECO:0000269|PubMed:17431422}.
CC -!- INTERACTION:
CC Q9NX02; Q56P42: PYDC2; NbExp=6; IntAct=EBI-6374482, EBI-6374418;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15030775,
CC ECO:0000269|PubMed:15456791}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9NX02-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NX02-2; Sequence=VSP_005522;
CC Name=3;
CC IsoId=Q9NX02-3; Sequence=VSP_017086;
CC Name=4;
CC IsoId=Q9NX02-4; Sequence=VSP_017085;
CC Name=5;
CC IsoId=Q9NX02-5; Sequence=VSP_044898;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in lung, placenta and
CC thymus and at lower levels in ovary, intestine and brain
CC (PubMed:15456791). Highly abundant in oocytes and early embryos,
CC however poorly expressed in somatic tissues such as brain, kidney,
CC liver and spinal cord (PubMed:30877238). {ECO:0000269|PubMed:15456791,
CC ECO:0000269|PubMed:30877238}.
CC -!- INDUCTION: By interferons and bacterial lipopolysaccharides (LPS).
CC {ECO:0000269|PubMed:15456791}.
CC -!- DOMAIN: When isolated, the NACHT domain is involved in interaction with
CC CARD8. This interaction is not detected for the full-length protein,
CC maybe due to autoinhibition, this inhibition might by relieved by an
CC inducible change in protein folding.
CC -!- DOMAIN: The pyrin domain is necessary and sufficient for suppression of
CC NFKB1 activation induced by TNF and for inducing IL1B secretion in
CC collaboration with caspase-1. It is involved in interaction with
CC PYCARD.
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the NLRP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG15253.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA91377.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAD92537.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD92537.1; Type=Miscellaneous discrepancy; Note=Erroneous prediction of the initiator methionine.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF298547; AAG15253.1; ALT_INIT; mRNA.
DR EMBL; AF310106; AAG30289.1; -; mRNA.
DR EMBL; AF464764; AAL69962.1; -; mRNA.
DR EMBL; AK000517; BAA91223.1; -; mRNA.
DR EMBL; AK000784; BAA91377.1; ALT_INIT; mRNA.
DR EMBL; AK025952; BAB15293.1; -; mRNA.
DR EMBL; AK302989; BAG64129.1; -; mRNA.
DR EMBL; AB209300; BAD92537.1; ALT_SEQ; mRNA.
DR EMBL; AK223253; BAD96973.1; -; mRNA.
DR EMBL; AK223269; BAD96989.1; -; mRNA.
DR EMBL; AC011476; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001039; AAH01039.1; -; mRNA.
DR EMBL; BC003592; AAH03592.1; -; mRNA.
DR EMBL; BC039269; AAH39269.1; -; mRNA.
DR CCDS; CCDS12913.1; -. [Q9NX02-1]
DR CCDS; CCDS54318.1; -. [Q9NX02-5]
DR CCDS; CCDS54319.1; -. [Q9NX02-2]
DR RefSeq; NP_001167552.1; NM_001174081.2. [Q9NX02-1]
DR RefSeq; NP_001167553.1; NM_001174082.2. [Q9NX02-2]
DR RefSeq; NP_001167554.1; NM_001174083.1. [Q9NX02-5]
DR RefSeq; NP_001334932.1; NM_001348003.1.
DR RefSeq; NP_060322.1; NM_017852.4. [Q9NX02-1]
DR AlphaFoldDB; Q9NX02; -.
DR SMR; Q9NX02; -.
DR BioGRID; 120787; 53.
DR CORUM; Q9NX02; -.
DR DIP; DIP-42460N; -.
DR IntAct; Q9NX02; 13.
DR MINT; Q9NX02; -.
DR STRING; 9606.ENSP00000445135; -.
DR iPTMnet; Q9NX02; -.
DR PhosphoSitePlus; Q9NX02; -.
DR BioMuta; NLRP2; -.
DR DMDM; 17380148; -.
DR EPD; Q9NX02; -.
DR jPOST; Q9NX02; -.
DR MassIVE; Q9NX02; -.
DR MaxQB; Q9NX02; -.
DR PaxDb; Q9NX02; -.
DR PeptideAtlas; Q9NX02; -.
DR PRIDE; Q9NX02; -.
DR ProteomicsDB; 46351; -.
DR ProteomicsDB; 83009; -. [Q9NX02-1]
DR ProteomicsDB; 83010; -. [Q9NX02-2]
DR ProteomicsDB; 83011; -. [Q9NX02-3]
DR ProteomicsDB; 83012; -. [Q9NX02-4]
DR Antibodypedia; 19479; 314 antibodies from 39 providers.
DR DNASU; 55655; -.
DR Ensembl; ENST00000339757.11; ENSP00000344074.7; ENSG00000022556.16. [Q9NX02-2]
DR Ensembl; ENST00000391721.8; ENSP00000375601.4; ENSG00000022556.16. [Q9NX02-4]
DR Ensembl; ENST00000427260.6; ENSP00000402474.2; ENSG00000022556.16. [Q9NX02-5]
DR Ensembl; ENST00000448584.7; ENSP00000409370.2; ENSG00000022556.16. [Q9NX02-1]
DR Ensembl; ENST00000537859.5; ENSP00000440601.1; ENSG00000022556.16. [Q9NX02-2]
DR Ensembl; ENST00000543010.5; ENSP00000445135.1; ENSG00000022556.16. [Q9NX02-1]
DR Ensembl; ENST00000611410.4; ENSP00000479220.1; ENSG00000275843.4. [Q9NX02-1]
DR Ensembl; ENST00000611642.1; ENSP00000484150.1; ENSG00000275082.4. [Q9NX02-5]
DR Ensembl; ENST00000611676.4; ENSP00000481999.1; ENSG00000275399.4. [Q9NX02-2]
DR Ensembl; ENST00000611679.4; ENSP00000484354.1; ENSG00000278682.4. [Q9NX02-1]
DR Ensembl; ENST00000611772.4; ENSP00000479109.1; ENSG00000278682.4. [Q9NX02-1]
DR Ensembl; ENST00000613062.4; ENSP00000483281.1; ENSG00000273992.4. [Q9NX02-1]
DR Ensembl; ENST00000613485.4; ENSP00000484351.1; ENSG00000273992.4. [Q9NX02-2]
DR Ensembl; ENST00000613825.4; ENSP00000483963.1; ENSG00000274638.4. [Q9NX02-1]
DR Ensembl; ENST00000613851.1; ENSP00000482628.1; ENSG00000278789.4. [Q9NX02-5]
DR Ensembl; ENST00000615173.1; ENSP00000482889.1; ENSG00000273992.4. [Q9NX02-1]
DR Ensembl; ENST00000615391.4; ENSP00000481851.1; ENSG00000275399.4. [Q9NX02-1]
DR Ensembl; ENST00000615521.4; ENSP00000479352.1; ENSG00000275399.4. [Q9NX02-1]
DR Ensembl; ENST00000616040.4; ENSP00000478876.1; ENSG00000278789.4. [Q9NX02-1]
DR Ensembl; ENST00000616903.1; ENSP00000482355.1; ENSG00000275399.4. [Q9NX02-5]
DR Ensembl; ENST00000616919.4; ENSP00000481564.1; ENSG00000278789.4. [Q9NX02-2]
DR Ensembl; ENST00000618018.4; ENSP00000483886.1; ENSG00000275843.4. [Q9NX02-2]
DR Ensembl; ENST00000618694.1; ENSP00000482465.1; ENSG00000275843.4. [Q9NX02-5]
DR Ensembl; ENST00000618731.4; ENSP00000478787.1; ENSG00000273992.4. [Q9NX02-2]
DR Ensembl; ENST00000618789.1; ENSP00000478318.1; ENSG00000275796.4. [Q9NX02-5]
DR Ensembl; ENST00000618943.1; ENSP00000482309.1; ENSG00000274638.4. [Q9NX02-5]
DR Ensembl; ENST00000619281.4; ENSP00000478265.1; ENSG00000278789.4. [Q9NX02-1]
DR Ensembl; ENST00000619454.4; ENSP00000483528.1; ENSG00000274638.4. [Q9NX02-1]
DR Ensembl; ENST00000619664.4; ENSP00000478774.1; ENSG00000275796.4. [Q9NX02-1]
DR Ensembl; ENST00000619885.4; ENSP00000483389.1; ENSG00000278682.4. [Q9NX02-2]
DR Ensembl; ENST00000621057.4; ENSP00000484382.1; ENSG00000273992.4. [Q9NX02-4]
DR Ensembl; ENST00000621200.4; ENSP00000479783.1; ENSG00000275082.4. [Q9NX02-1]
DR Ensembl; ENST00000621239.4; ENSP00000479713.1; ENSG00000275082.4. [Q9NX02-1]
DR Ensembl; ENST00000621594.4; ENSP00000478450.1; ENSG00000275843.4. [Q9NX02-1]
DR Ensembl; ENST00000622042.4; ENSP00000482253.1; ENSG00000275796.4. [Q9NX02-1]
DR Ensembl; ENST00000622216.4; ENSP00000482044.1; ENSG00000275082.4. [Q9NX02-2]
DR Ensembl; ENST00000622444.1; ENSP00000482065.1; ENSG00000278682.4. [Q9NX02-5]
DR Ensembl; ENST00000622600.4; ENSP00000482727.1; ENSG00000274638.4. [Q9NX02-2]
DR Ensembl; ENST00000622773.4; ENSP00000484759.1; ENSG00000273992.4. [Q9NX02-5]
DR Ensembl; ENST00000622864.4; ENSP00000477726.1; ENSG00000275796.4. [Q9NX02-2]
DR GeneID; 55655; -.
DR KEGG; hsa:55655; -.
DR MANE-Select; ENST00000448584.7; ENSP00000409370.2; NM_017852.5; NP_060322.1.
DR UCSC; uc002qij.4; human. [Q9NX02-1]
DR CTD; 55655; -.
DR DisGeNET; 55655; -.
DR GeneCards; NLRP2; -.
DR HGNC; HGNC:22948; NLRP2.
DR HPA; ENSG00000022556; Low tissue specificity.
DR MIM; 609364; gene.
DR neXtProt; NX_Q9NX02; -.
DR OpenTargets; ENSG00000022556; -.
DR PharmGKB; PA162397946; -.
DR VEuPathDB; HostDB:ENSG00000022556; -.
DR eggNOG; ENOG502S92U; Eukaryota.
DR GeneTree; ENSGT00940000161714; -.
DR HOGENOM; CLU_002274_2_1_1; -.
DR InParanoid; Q9NX02; -.
DR OMA; GNDQNNM; -.
DR OrthoDB; 155336at2759; -.
DR PhylomeDB; Q9NX02; -.
DR PathwayCommons; Q9NX02; -.
DR SignaLink; Q9NX02; -.
DR BioGRID-ORCS; 55655; 18 hits in 1072 CRISPR screens.
DR ChiTaRS; NLRP2; human.
DR GeneWiki; NLRP2; -.
DR GenomeRNAi; 55655; -.
DR Pharos; Q9NX02; Tbio.
DR PRO; PR:Q9NX02; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9NX02; protein.
DR Bgee; ENSG00000022556; Expressed in placenta and 99 other tissues.
DR ExpressionAtlas; Q9NX02; baseline and differential.
DR Genevisible; Q9NX02; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0032090; F:Pyrin domain binding; IPI:HGNC-UCL.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IGI:UniProtKB.
DR GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:HGNC-UCL.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IDA:HGNC-UCL.
DR GO; GO:0050727; P:regulation of inflammatory response; IBA:GO_Central.
DR Gene3D; 1.10.533.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR004020; DAPIN.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR007111; NACHT_NTPase.
DR InterPro; IPR041267; NLRP_HD2.
DR InterPro; IPR041075; NOD2_WH.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF13516; LRR_6; 4.
DR Pfam; PF05729; NACHT; 1.
DR Pfam; PF17776; NLRC4_HD2; 1.
DR Pfam; PF17779; NOD2_WH; 1.
DR Pfam; PF02758; PYRIN; 1.
DR SMART; SM01289; PYRIN; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50824; DAPIN; 1.
DR PROSITE; PS50837; NACHT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; ATP-binding; Cytoplasm; Immunity;
KW Inflammatory response; Innate immunity; Leucine-rich repeat;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1062
FT /note="NACHT, LRR and PYD domains-containing protein 2"
FT /id="PRO_0000080888"
FT DOMAIN 1..94
FT /note="Pyrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00061"
FT DOMAIN 207..526
FT /note="NACHT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00136"
FT REPEAT 812..832
FT /note="LRR 1"
FT REPEAT 841..861
FT /note="LRR 2"
FT REPEAT 869..889
FT /note="LRR 3"
FT REPEAT 898..918
FT /note="LRR 4"
FT REPEAT 926..946
FT /note="LRR 5"
FT REPEAT 955..976
FT /note="LRR 6"
FT REPEAT 983..1003
FT /note="LRR 7"
FT REPEAT 1010..1033
FT /note="LRR 8"
FT BINDING 213..220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00136"
FT MOD_RES 671
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 47..69
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044898"
FT VAR_SEQ 109..132
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_017085"
FT VAR_SEQ 133..154
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11270363"
FT /id="VSP_005522"
FT VAR_SEQ 847..1062
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017086"
FT VARIANT 115..1062
FT /note="Missing (found in patients with female infertility;
FT unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:33020905"
FT /id="VAR_084172"
FT VARIANT 175
FT /note="W -> C (found in patients with female infertility;
FT unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:30877238"
FT /id="VAR_084586"
FT VARIANT 221
FT /note="T -> M (found in patients with female infertility;
FT unknown pathological significance; dbSNP:rs17699678)"
FT /evidence="ECO:0000269|PubMed:30877238"
FT /id="VAR_053616"
FT VARIANT 258
FT /note="F -> S (found in patients with female infertility;
FT unknown pathological significance; dbSNP:rs1194295774)"
FT /evidence="ECO:0000269|PubMed:30877238"
FT /id="VAR_084587"
FT VARIANT 302
FT /note="E -> Q (in dbSNP:rs3745904)"
FT /id="VAR_053617"
FT VARIANT 364
FT /note="R -> K (in dbSNP:rs4306647)"
FT /evidence="ECO:0000269|PubMed:11270363"
FT /id="VAR_025011"
FT VARIANT 516
FT /note="T -> A (in dbSNP:rs61735082)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_068977"
FT VARIANT 522
FT /note="E -> G (in dbSNP:rs61735083)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_068978"
FT VARIANT 529
FT /note="T -> A (in dbSNP:rs34804158)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.5"
FT /id="VAR_068979"
FT VARIANT 616
FT /note="E -> V (found in patients with female infertility;
FT unknown pathological significance; dbSNP:rs1471763280)"
FT /evidence="ECO:0000269|PubMed:30877238"
FT /id="VAR_084588"
FT VARIANT 654..1062
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:30877238"
FT /id="VAR_084589"
FT VARIANT 752..1062
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:30877238"
FT /id="VAR_084590"
FT VARIANT 848
FT /note="E -> D (found in patients with female infertility;
FT unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:30877238"
FT /id="VAR_084591"
FT VARIANT 884
FT /note="G -> R (in dbSNP:rs59779270)"
FT /id="VAR_062140"
FT VARIANT 1052
FT /note="A -> E (in dbSNP:rs1043673)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_020006"
FT CONFLICT 1
FT /note="M -> V (in Ref. 1; AAG15253)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="L -> P (in Ref. 1; AAG15253)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="E -> G (in Ref. 4; BAG64129)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="I -> V (in Ref. 7; AAH39269)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="W -> C (in Ref. 5; BAD96973/BAD96989)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="G -> S (in Ref. 4; BAG64129)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="I -> S (in Ref. 4; BAB15293)"
FT /evidence="ECO:0000305"
FT CONFLICT 980
FT /note="Missing (in Ref. 1; AAG15253)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1062 AA; 120515 MW; 4DBB0F6E9C2BC8A7 CRC64;
MVSSAQMGFN LQALLEQLSQ DELSKFKYLI TTFSLAHELQ KIPHKEVDKA DGKQLVEILT
THCDSYWVEM ASLQVFEKMH RMDLSERAKD EVREAALKSF NKRKPLSLGI TRKERPPLDV
DEMLERFKTE AQAFTETKGN VICLGKEVFK GKKPDKDNRC RYILKTKFRE MWKSWPGDSK
EVQVMAERYK MLIPFSNPRV LPGPFSYTVV LYGPAGLGKT TLAQKLMLDW AEDNLIHKFK
YAFYLSCREL SRLGPCSFAE LVFRDWPELQ DDIPHILAQA RKILFVIDGF DELGAAPGAL
IEDICGDWEK KKPVPVLLGS LLNRVMLPKA ALLVTTRPRA LRDLRILAEE PIYIRVEGFL
EEDRRAYFLR HFGDEDQAMR AFELMRSNAA LFQLGSAPAV CWIVCTTLKL QMEKGEDPVP
TCLTRTGLFL RFLCSRFPQG AQLRGALRTL SLLAAQGLWA QTSVLHREDL ERLGVQESDL
RLFLDGDILR QDRVSKGCYS FIHLSFQQFL TALFYTLEKE EEEDRDGHTW DIGDVQKLLS
GVERLRNPDL IQAGYYSFGL ANEKRAKELE ATFGCRMSPD IKQELLRCDI SCKGGHSTVT
DLQELLGCLY ESQEEELVKE VMAQFKEISL HLNAVDVVPS SFCVKHCRNL QKMSLQVIKE
NLPENVTASE SDAEVERSQD DQHMLPFWTD LCSIFGSNKD LMGLAINDSF LSASLVRILC
EQIASDTCHL QRVVFKNISP ADAHRNLCLA LRGHKTVTYL TLQGNDQDDM FPALCEVLRH
PECNLRYLGL VSCSATTQQW ADLSLALEVN QSLTCVNLSD NELLDEGAKL LYTTLRHPKC
FLQRLSLENC HLTEANCKDL AAVLVVSREL THLCLAKNPI GNTGVKFLCE GLRYPECKLQ
TLVLWNCDIT SDGCCDLTKL LQEKSSLLCL DLGLNHIGVK GMKFLCEALR KPLCNLRCLW
LWGCSIPPFS CEDLCSALSC NQSLVTLDLG QNPLGSSGVK MLFETLTCSS GTLRTLRLKI
DDFNDELNKL LEEIEEKNPQ LIIDTEKHHP WAERPSSHDF MI
