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Interleukin-33 (IL-33) (Interleukin-1 family member 11) (IL-1F11) (Nuclear factor from high endothelial venules) (NF-HEV) [Cleaved into: Interleukin-33 (95-270); Interleukin-33 (99-270); Interleukin-33 (109-270)]

 IL33_HUMAN              Reviewed;         270 AA.
O95760; B2R8L1; B4DJ35; B4E1Q9; D3DRI5; E7EAX4; Q2YEJ5;
05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
17-JUN-2020, entry version 150.
RecName: Full=Interleukin-33;
Short=IL-33;
AltName: Full=Interleukin-1 family member 11;
Short=IL-1F11;
AltName: Full=Nuclear factor from high endothelial venules;
Short=NF-HEV;
Contains:
RecName: Full=Interleukin-33 (95-270);
Contains:
RecName: Full=Interleukin-33 (99-270);
Contains:
RecName: Full=Interleukin-33 (109-270);
Flags: Precursor;
Name=IL33; Synonyms=C9orf26, IL1F11, NFHEV;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
TISSUE=Endothelial cell;
PubMed=12819012; DOI=10.1016/s0002-9440(10)63631-0;
Baekkevold E.S., Roussigne M., Yamanaka T., Johansen F.-E., Jahnsen F.L.,
Amalric F., Brandtzaeg P., Erard M., Haraldsen G., Girard J.-P.;
"Molecular characterization of NF-HEV, a nuclear factor preferentially
expressed in human high endothelial venules.";
Am. J. Pathol. 163:69-79(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=10566975; DOI=10.1097/00004647-199911000-00013;
Onda H., Kasuya H., Takakura K., Hori T., Imaizumi T., Takeuchi T.,
Inoue I., Takeda J.;
"Identification of genes differentially expressed in canine vasospastic
cerebral arteries after subarachnoid hemorrhage.";
J. Cereb. Blood Flow Metab. 19:1279-1288(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND PROTEOLYTIC
PROCESSING.
PubMed=16286016; DOI=10.1016/j.immuni.2005.09.015;
Schmitz J., Owyang A., Oldham E., Song Y., Murphy E., McClanahan T.K.,
Zurawski G., Moshrefi M., Qin J., Li X., Gorman D.M., Bazan J.F.,
Kastelein R.A.;
"IL-33, an interleukin-1-like cytokine that signals via the IL-1 receptor-
related protein ST 2 and induces T helper type 2-associated cytokines.";
Immunity 23:479-490(2005).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
PubMed=21454686; DOI=10.1074/jbc.m111.219089;
Hong J., Bae S., Jhun H., Lee S., Choi J., Kang T., Kwak A., Hong K.,
Kim E., Jo S., Kim S.;
"Identification of constitutively active interleukin 33 (IL-33) splice
variant.";
J. Biol. Chem. 286:20078-20086(2011).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
TISSUE=Adrenal gland, and Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
PROTEIN SEQUENCE OF 95-121, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION,
PROTEOLYTIC CLEAVAGE AT PHE-94 AND LEU-108 BY CSTG, AND PROTEOLYTIC
CLEAVAGE AT ILE-98 BY ELANE.
PubMed=22307629; DOI=10.1073/pnas.1115884109;
Lefrancais E., Roga S., Gautier V., Gonzalez-de-Peredo A., Monsarrat B.,
Girard J.P., Cayrol C.;
"IL-33 is processed into mature bioactive forms by neutrophil elastase and
cathepsin G.";
Proc. Natl. Acad. Sci. U.S.A. 109:1673-1678(2012).
[11]
FUNCTION.
PubMed=17853410; DOI=10.1002/eji.200737547;
Komai-Koma M., Xu D., Li Y., McKenzie A.N., McInnes I.B., Liew F.Y.;
"IL-33 is a chemoattractant for human Th2 cells.";
Eur. J. Immunol. 37:2779-2786(2007).
[12]
FUNCTION, SUBCELLULAR LOCATION, AND NUCLEAR TARGETING DOMAIN.
PubMed=17185418; DOI=10.1073/pnas.0606854104;
Carriere V., Roussel L., Ortega N., Lacorre D.A., Americh L., Aguilar L.,
Bouche G., Girard J.P.;
"IL-33, the IL-1-like cytokine ligand for ST2 receptor, is a chromatin-
associated nuclear factor in vivo.";
Proc. Natl. Acad. Sci. U.S.A. 104:282-287(2007).
[13]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=18787100; DOI=10.2353/ajpath.2008.080014;
Kuchler A.M., Pollheimer J., Balogh J., Sponheim J., Manley L.,
Sorensen D.R., De Angelis P.M., Scott H., Haraldsen G.;
"Nuclear interleukin-33 is generally expressed in resting endothelium but
rapidly lost upon angiogenic or proinflammatory activation.";
Am. J. Pathol. 173:1229-1242(2008).
[14]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=18836528; DOI=10.1371/journal.pone.0003331;
Moussion C., Ortega N., Girard J.P.;
"The IL-1-like cytokine IL-33 is constitutively expressed in the nucleus of
endothelial cells and epithelial cells in vivo: a novel 'alarmin'?";
PLoS ONE 3:E3331-E3331(2008).
[15]
PROTEOLYTIC PROCESSING.
PubMed=19596270; DOI=10.1016/j.bbrc.2009.07.018;
Hayakawa M., Hayakawa H., Matsuyama Y., Tamemoto H., Okazaki H.,
Tominaga S.;
"Mature interleukin-33 is produced by calpain-mediated cleavage in vivo.";
Biochem. Biophys. Res. Commun. 387:218-222(2009).
[16]
PROTEOLYTIC PROCESSING.
PubMed=19559631; DOI=10.1016/j.immuni.2009.05.007;
Luthi A.U., Cullen S.P., McNeela E.A., Duriez P.J., Afonina I.S.,
Sheridan C., Brumatti G., Taylor R.C., Kersse K., Vandenabeele P.,
Lavelle E.C., Martin S.J.;
"Suppression of interleukin-33 bioactivity through proteolysis by apoptotic
caspases.";
Immunity 31:84-98(2009).
[17]
PROTEOLYTIC PROCESSING, AND SUBCELLULAR LOCATION.
PubMed=19465481; DOI=10.1074/jbc.m901744200;
Talabot-Ayer D., Lamacchia C., Gabay C., Palmer G.;
"Interleukin-33 is biologically active independently of caspase-1
cleavage.";
J. Biol. Chem. 284:19420-19426(2009).
[18]
PROTEOLYTIC PROCESSING.
PubMed=19439663; DOI=10.1073/pnas.0812690106;
Cayrol C., Girard J.P.;
"The IL-1-like cytokine IL-33 is inactivated after maturation by caspase-
1.";
Proc. Natl. Acad. Sci. U.S.A. 106:9021-9026(2009).
[19]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=21734074; DOI=10.4049/jimmunol.1003080;
Ali S., Mohs A., Thomas M., Klare J., Ross R., Schmitz M.L., Martin M.U.;
"The dual function cytokine IL-33 interacts with the transcription factor
NF-kappaB to dampen NF-kappaB-stimulated gene transcription.";
J. Immunol. 187:1609-1616(2011).
[20]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=22215666; DOI=10.1074/jbc.m111.298703;
Kakkar R., Hei H., Dobner S., Lee R.T.;
"Interleukin 33 as a mechanically responsive cytokine secreted by living
cells.";
J. Biol. Chem. 287:6941-6948(2012).
[21]
INTERACTION WITH H.POLYGYRUS ARI, AND INDUCTION BY H.POLYGYRUS.
PubMed=29045903; DOI=10.1016/j.immuni.2017.09.015;
Osbourn M., Soares D.C., Vacca F., Cohen E.S., Scott I.C., Gregory W.F.,
Smyth D.J., Toivakka M., Kemter A.M., le Bihan T., Wear M., Hoving D.,
Filbey K.J., Hewitson J.P., Henderson H., Gonzalez-Ciscar A., Errington C.,
Vermeren S., Astier A.L., Wallace W.A., Schwarze J., Ivens A.C.,
Maizels R.M., McSorley H.J.;
"HpARI Protein Secreted by a Helminth Parasite Suppresses Interleukin-33.";
Immunity 47:739-751(2017).
[22]
STRUCTURE BY NMR OF 111-270, INTERACTION WITH IL1RL1 AND IL1RAP, AND
SUBUNIT.
PubMed=19836339; DOI=10.1016/j.str.2009.08.009;
Lingel A., Weiss T.M., Niebuhr M., Pan B., Appleton B.A., Wiesmann C.,
Bazan J.F., Fairbrother W.J.;
"Structure of IL-33 and its interaction with the ST2 and IL-1RAcP
receptors--insight into heterotrimeric IL-1 signaling complexes.";
Structure 17:1398-1410(2009).
[23]
X-RAY CRYSTALLOGRAPHY (3.27 ANGSTROMS) OF 112-270 IN COMPLEX WITH
IL1RL1/ST2, AND MUTAGENESIS OF GLU-144; GLU-148; ASP-149; GLU-165 AND
ASP-244.
PubMed=23980170; DOI=10.1073/pnas.1308651110;
Liu X., Hammel M., He Y., Tainer J.A., Jeng U.S., Zhang L., Wang S.,
Wang X.;
"Structural insights into the interaction of IL-33 with its receptors.";
Proc. Natl. Acad. Sci. U.S.A. 110:14918-14923(2013).
-!- FUNCTION: Cytokine that binds to and signals through the IL1RL1/ST2
receptor which in turn activates NF-kappa-B and MAPK signaling pathways
in target cells (PubMed:16286016). Involved in the maturation of Th2
cells inducing the secretion of T-helper type 2-associated cytokines.
Also involved in activation of mast cells, basophils, eosinophils and
natural killer cells. Acts as a chemoattractant for Th2 cells, and may
function as an 'alarmin', that amplifies immune responses during tissue
injury (PubMed:17853410, PubMed:18836528).
{ECO:0000269|PubMed:16286016, ECO:0000269|PubMed:17853410,
ECO:0000269|PubMed:18836528}.
-!- FUNCTION: In quiescent endothelia the uncleaved form is constitutively
and abundantly expressed, and acts as a chromatin-associated nuclear
factor with transcriptional repressor properties, it may sequester
nuclear NF-kappaB/RELA, lowering expression of its targets
(PubMed:21734074). This form is rapidely lost upon angiogenic or
proinflammatory activation (PubMed:18787100).
{ECO:0000269|PubMed:18787100, ECO:0000269|PubMed:21734074}.
-!- SUBUNIT: Forms a 1:1:1 heterotrimeric complex with its primary high-
affinity receptor IL1RL1 and the coreceptor IL1RAP.
{ECO:0000269|PubMed:19836339, ECO:0000269|PubMed:23980170}.
-!- SUBUNIT: (Microbial infection) Interacts (in reduced form) with
H.polygyrus ARI. {ECO:0000269|PubMed:29045903}.
-!- INTERACTION:
O95760; P0C0S8: H2AC17; NbExp=3; IntAct=EBI-724057, EBI-1390628;
O95760; Q01638: IL1RL1; NbExp=2; IntAct=EBI-724057, EBI-993762;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12819012,
ECO:0000269|PubMed:17185418, ECO:0000269|PubMed:18787100,
ECO:0000269|PubMed:18836528, ECO:0000269|PubMed:21734074}. Chromosome
{ECO:0000269|PubMed:17185418}. Cytoplasmic vesicle, secretory vesicle
{ECO:0000269|PubMed:22215666}. Secreted {ECO:0000269|PubMed:19465481}.
Note=Associates with heterochromatin and mitotic chromosomes
(PubMed:17185418).
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=O95760-1; Sequence=Displayed;
Name=2;
IsoId=O95760-2; Sequence=VSP_042728;
Name=3; Synonyms=spIL-33;
IsoId=O95760-3; Sequence=VSP_044948;
Name=4;
IsoId=O95760-4; Sequence=VSP_045440;
-!- TISSUE SPECIFICITY: Expressed at high level in high endothelial venules
found in tonsils, Peyer patches and mesenteric lymph nodes. Almost
undetectable in placenta. {ECO:0000269|PubMed:12819012}.
-!- INDUCTION: By infection with the parasite H.polygyrus.
{ECO:0000269|PubMed:29045903}.
-!- DOMAIN: The homeodomain-like HTH domain mediates nuclear localization
and heterochromatin association.
-!- PTM: The full-length protein can be released from cells and is able to
signal via the IL1RL1/ST2 receptor. However, proteolytic processing by
CSTG/cathepsin G and ELANE/neutrophil elastase produces C-terminal
peptides that are more active than the unprocessed full length protein.
May also be proteolytically processed by calpains (PubMed:19596270).
Proteolytic cleavage mediated by apoptotic caspases including CASP3 and
CASP7 results in IL33 inactivation (PubMed:19559631). In vitro
proteolytic cleavage by CASP1 was reported (PubMed:16286016) but could
not be confirmed in vivo (PubMed:19465481) suggesting that IL33 is
probably not a direct substrate for that caspase.
{ECO:0000269|PubMed:16286016, ECO:0000269|PubMed:19439663,
ECO:0000269|PubMed:19465481, ECO:0000269|PubMed:19559631,
ECO:0000269|PubMed:19596270, ECO:0000269|PubMed:22307629}.
-!- MISCELLANEOUS: [Isoform 3]: Constitutively active. {ECO:0000305}.
-!- SIMILARITY: Belongs to the IL-1 family. Highly divergent.
{ECO:0000305}.
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EMBL; AB024518; BAA75892.1; -; mRNA.
EMBL; AY905581; AAX86998.1; -; mRNA.
EMBL; HQ641439; ADR77828.1; -; mRNA.
EMBL; AK295908; BAG58697.1; -; mRNA.
EMBL; AK303943; BAG64871.1; -; mRNA.
EMBL; AK313414; BAG36208.1; -; mRNA.
EMBL; CR407619; CAG28547.1; -; mRNA.
EMBL; AL353741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471071; EAW58748.1; -; Genomic_DNA.
EMBL; CH471071; EAW58750.1; -; Genomic_DNA.
EMBL; CH471071; EAW58751.1; -; Genomic_DNA.
EMBL; BC047085; AAH47085.1; -; mRNA.
CCDS; CCDS56563.1; -. [O95760-2]
CCDS; CCDS56564.1; -. [O95760-4]
CCDS; CCDS6468.1; -. [O95760-1]
CCDS; CCDS83341.1; -. [O95760-3]
RefSeq; NP_001186569.1; NM_001199640.1. [O95760-2]
RefSeq; NP_001186570.1; NM_001199641.1. [O95760-4]
RefSeq; NP_001300973.1; NM_001314044.1. [O95760-1]
RefSeq; NP_001300974.1; NM_001314045.1. [O95760-1]
RefSeq; NP_001300975.1; NM_001314046.1.
RefSeq; NP_001300976.1; NM_001314047.1.
RefSeq; NP_001300977.1; NM_001314048.1. [O95760-3]
RefSeq; NP_254274.1; NM_033439.3. [O95760-1]
PDB; 2KLL; NMR; -; A=111-270.
PDB; 4KC3; X-ray; 3.27 A; A=112-270.
PDBsum; 2KLL; -.
PDBsum; 4KC3; -.
SMR; O95760; -.
BioGRID; 124776; 7.
DIP; DIP-37862N; -.
IntAct; O95760; 6.
MINT; O95760; -.
STRING; 9606.ENSP00000370842; -.
iPTMnet; O95760; -.
PhosphoSitePlus; O95760; -.
BioMuta; IL33; -.
MassIVE; O95760; -.
PaxDb; O95760; -.
PeptideAtlas; O95760; -.
PRIDE; O95760; -.
ProteomicsDB; 4342; -.
ProteomicsDB; 51036; -. [O95760-1]
ProteomicsDB; 51037; -. [O95760-2]
ABCD; O95760; 1 sequenced antibody.
Antibodypedia; 3362; 1044 antibodies.
Ensembl; ENST00000381434; ENSP00000370842; ENSG00000137033. [O95760-1]
Ensembl; ENST00000417746; ENSP00000394039; ENSG00000137033. [O95760-4]
Ensembl; ENST00000456383; ENSP00000414238; ENSG00000137033. [O95760-2]
Ensembl; ENST00000611532; ENSP00000478858; ENSG00000137033. [O95760-3]
GeneID; 90865; -.
KEGG; hsa:90865; -.
UCSC; uc011lmh.3; human. [O95760-1]
CTD; 90865; -.
DisGeNET; 90865; -.
EuPathDB; HostDB:ENSG00000137033.11; -.
GeneCards; IL33; -.
HGNC; HGNC:16028; IL33.
HPA; ENSG00000137033; Low tissue specificity.
MIM; 608678; gene.
neXtProt; NX_O95760; -.
OpenTargets; ENSG00000137033; -.
PharmGKB; PA162392005; -.
eggNOG; ENOG410J11H; Eukaryota.
eggNOG; ENOG41118MB; LUCA.
GeneTree; ENSGT00390000005185; -.
HOGENOM; CLU_1795771_0_0_1; -.
InParanoid; O95760; -.
KO; K12967; -.
OMA; HRKSSKC; -.
OrthoDB; 1062809at2759; -.
PhylomeDB; O95760; -.
TreeFam; TF338120; -.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-HSA-9014843; Interleukin-33 signaling.
BioGRID-ORCS; 90865; 2 hits in 785 CRISPR screens.
ChiTaRS; IL33; human.
EvolutionaryTrace; O95760; -.
GenomeRNAi; 90865; -.
Pharos; O95760; Tbio.
PRO; PR:O95760; -.
Proteomes; UP000005640; Chromosome 9.
RNAct; O95760; protein.
Bgee; ENSG00000137033; Expressed in left coronary artery and 192 other tissues.
Genevisible; O95760; HS.
GO; GO:0005737; C:cytoplasm; IDA:CACAO.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
GO; GO:0005720; C:nuclear heterochromatin; IDA:CACAO.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:CACAO.
GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
GO; GO:0005125; F:cytokine activity; IDA:BHF-UCL.
GO; GO:0002112; F:interleukin-33 receptor binding; IEA:Ensembl.
GO; GO:0051607; P:defense response to virus; IEA:Ensembl.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0038172; P:interleukin-33-mediated signaling pathway; TAS:Reactome.
GO; GO:0002282; P:microglial cell activation involved in immune response; IEA:Ensembl.
GO; GO:0061518; P:microglial cell proliferation; IEA:Ensembl.
GO; GO:0051025; P:negative regulation of immunoglobulin secretion; IEA:Ensembl.
GO; GO:0032689; P:negative regulation of interferon-gamma production; IEA:Ensembl.
GO; GO:0002686; P:negative regulation of leukocyte migration; IEA:Ensembl.
GO; GO:0002826; P:negative regulation of T-helper 1 type immune response; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:CACAO.
GO; GO:0090197; P:positive regulation of chemokine secretion; IDA:BHF-UCL.
GO; GO:0001819; P:positive regulation of cytokine production; IBA:GO_Central.
GO; GO:0051024; P:positive regulation of immunoglobulin secretion; IEA:Ensembl.
GO; GO:0050729; P:positive regulation of inflammatory response; ISS:BHF-UCL.
GO; GO:0032736; P:positive regulation of interleukin-13 production; IEA:Ensembl.
GO; GO:0032753; P:positive regulation of interleukin-4 production; IEA:Ensembl.
GO; GO:0032754; P:positive regulation of interleukin-5 production; IEA:Ensembl.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
GO; GO:0043032; P:positive regulation of macrophage activation; IDA:BHF-UCL.
GO; GO:0150078; P:positive regulation of neuroinflammatory response; TAS:ARUK-UCL.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
GO; GO:0002830; P:positive regulation of type 2 immune response; IEA:Ensembl.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
InterPro; IPR026145; IL-33.
PANTHER; PTHR21114; PTHR21114; 1.
Pfam; PF15095; IL33; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chromosome; Cytokine;
Cytoplasmic vesicle; Direct protein sequencing; Nucleus; Polymorphism;
Reference proteome; Secreted; Transcription.
CHAIN 1..270
/note="Interleukin-33"
/id="PRO_0000096790"
PROPEP 1..94
/evidence="ECO:0000269|PubMed:22307629"
/id="PRO_0000430083"
CHAIN 95..270
/note="Interleukin-33 (95-270)"
/id="PRO_0000430084"
CHAIN 99..270
/note="Interleukin-33 (99-270)"
/id="PRO_0000430085"
CHAIN 109..270
/note="Interleukin-33 (109-270)"
/id="PRO_0000430086"
REGION 1..65
/note="Homeodomain-like HTH domain"
REGION 66..111
/note="Interaction with RELA"
/evidence="ECO:0000250"
SITE 94..95
/note="Cleavage; by CTSG"
/evidence="ECO:0000269|PubMed:22307629"
SITE 98..99
/note="Cleavage; by ELANE"
/evidence="ECO:0000269|PubMed:22307629"
SITE 108..109
/note="Cleavage; by CTSG"
/evidence="ECO:0000269|PubMed:22307629"
VAR_SEQ 31..157
/note="KSQQKAKEVCPMYFMKLRSGLMIKKEACYFRRETTKRPSLKTGRKHKRHLVL
AACQQQSTVECFAFGISGVQKYTRALHDSSITGISPITEYLASLSTYNDQSITFALEDE
SYEIYVEDLKKDEKKD -> N (in isoform 4)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_045440"
VAR_SEQ 72..113
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|PubMed:21454686"
/id="VSP_044948"
VAR_SEQ 115..156
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_042728"
VARIANT 263
/note="I -> M (in dbSNP:rs16924241)"
/id="VAR_049576"
MUTAGEN 144
/note="E->K: Decreases affinity for IL1RL1."
/evidence="ECO:0000269|PubMed:23980170"
MUTAGEN 148
/note="E->K: 7-fold decrease in affinity for IL1RL1."
/evidence="ECO:0000269|PubMed:23980170"
MUTAGEN 149
/note="D->K: Almost abolishes binding to IL1RL1."
/evidence="ECO:0000269|PubMed:23980170"
MUTAGEN 165
/note="E->K: 8-fold decrease in affinity for IL1RL1."
/evidence="ECO:0000269|PubMed:23980170"
MUTAGEN 244
/note="D->K: Decreases affinity for IL1RL1."
/evidence="ECO:0000269|PubMed:23980170"
CONFLICT 139
/note="E -> G (in Ref. 5; BAG36208)"
/evidence="ECO:0000305"
STRAND 112..115
/evidence="ECO:0000244|PDB:2KLL"
STRAND 119..127
/evidence="ECO:0000244|PDB:4KC3"
TURN 129..131
/evidence="ECO:0000244|PDB:2KLL"
STRAND 133..138
/evidence="ECO:0000244|PDB:4KC3"
STRAND 140..148
/evidence="ECO:0000244|PDB:4KC3"
STRAND 158..169
/evidence="ECO:0000244|PDB:4KC3"
TURN 170..172
/evidence="ECO:0000244|PDB:2KLL"
STRAND 180..189
/evidence="ECO:0000244|PDB:4KC3"
STRAND 193..197
/evidence="ECO:0000244|PDB:4KC3"
TURN 198..201
/evidence="ECO:0000244|PDB:4KC3"
STRAND 202..206
/evidence="ECO:0000244|PDB:4KC3"
HELIX 214..216
/evidence="ECO:0000244|PDB:4KC3"
STRAND 218..224
/evidence="ECO:0000244|PDB:4KC3"
STRAND 228..235
/evidence="ECO:0000244|PDB:4KC3"
STRAND 238..243
/evidence="ECO:0000244|PDB:4KC3"
STRAND 246..251
/evidence="ECO:0000244|PDB:4KC3"
HELIX 261..263
/evidence="ECO:0000244|PDB:2KLL"
STRAND 265..267
/evidence="ECO:0000244|PDB:4KC3"
SEQUENCE 270 AA; 30759 MW; 7C158069196EF636 CRC64;
MKPKMKYSTN KISTAKWKNT ASKALCFKLG KSQQKAKEVC PMYFMKLRSG LMIKKEACYF
RRETTKRPSL KTGRKHKRHL VLAACQQQST VECFAFGISG VQKYTRALHD SSITGISPIT
EYLASLSTYN DQSITFALED ESYEIYVEDL KKDEKKDKVL LSYYESQHPS NESGDGVDGK
MLMVTLSPTK DFWLHANNKE HSVELHKCEK PLPDQAFFVL HNMHSNCVSF ECKTDPGVFI
GVKDNHLALI KVDSSENLCT ENILFKLSET


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WP1909: Signal regulatory protein (SIRP) family interactions
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WP170: Nuclear Receptors
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Related Genes :
[IL33 C9orf26 IL1F11 NFHEV] Interleukin-33 (IL-33) (Interleukin-1 family member 11) (IL-1F11) (Nuclear factor from high endothelial venules) (NF-HEV) [Cleaved into: Interleukin-33 (95-270); Interleukin-33 (99-270); Interleukin-33 (109-270)]
[Il33] Interleukin-33 (IL-33) [Cleaved into: Interleukin-33(102-266); Interleukin-33(109-266)]
[Il1rap] Interleukin-1 receptor accessory protein (IL-1 receptor accessory protein) (IL-1RAcP) (EC 3.2.2.6) (Interleukin-33 receptot beta chain)
[Il1rl1 Ly84 St2 Ste2] Interleukin-1 receptor-like 1 (EC 3.2.2.6) (Interleukin-33 receptor alpha chain) (Lymphocyte antigen 84) (Protein ST2) (Protein T1)
[Il33] Interleukin-33 (IL-33)
[Il1r1 Il-1r1 Il1ra] Interleukin-1 receptor type 1 (IL-1R-1) (IL-1RT-1) (IL-1RT1) (EC 3.2.2.6) (CD121 antigen-like family member A) (Interleukin-1 receptor alpha) (IL-1R-alpha) (Interleukin-1 receptor type I) (p80) (CD antigen CD121a) [Cleaved into: Interleukin-1 receptor type 1, membrane form (mIL-1R1) (mIL-1RI); Interleukin-1 receptor type 1, soluble form (sIL-1R1) (sIL-1RI)]
[NFIL3 E4BP4 IL3BP1] Nuclear factor interleukin-3-regulated protein (E4 promoter-binding protein 4) (Interleukin-3 promoter transcriptional activator) (Interleukin-3-binding protein 1) (Transcriptional activator NF-IL3A)
[IL37 FIL1Z IL1F7 IL1H4 IL1RP1] Interleukin-37 (FIL1 zeta) (IL-1X) (Interleukin-1 family member 7) (IL-1F7) (Interleukin-1 homolog 4) (IL-1H) (IL-1H4) (Interleukin-1 zeta) (IL-1 zeta) (Interleukin-1-related protein) (IL-1RP1) (Interleukin-23) (IL-37)
[IFNLR1 IL28RA LICR2] Interferon lambda receptor 1 (IFN-lambda receptor 1) (IFN-lambda-R1) (Cytokine receptor class-II member 12) (Cytokine receptor family 2 member 12) (CRF2-12) (Interleukin-28 receptor subunit alpha) (IL-28 receptor subunit alpha) (IL-28R-alpha) (IL-28RA) (Likely interleukin or cytokine receptor 2) (LICR2)
[IL1R1 IL1R IL1RA IL1RT1] Interleukin-1 receptor type 1 (IL-1R-1) (IL-1RT-1) (IL-1RT1) (EC 3.2.2.6) (CD121 antigen-like family member A) (Interleukin-1 receptor alpha) (IL-1R-alpha) (Interleukin-1 receptor type I) (p80) (CD antigen CD121a) [Cleaved into: Interleukin-1 receptor type 1, membrane form (mIL-1R1) (mIL-1RI); Interleukin-1 receptor type 1, soluble form (sIL-1R1) (sIL-1RI)]
[IL36RN FIL1D IL1F5 IL1HY1 IL1L1 IL1RP3 UNQ1896/PRO4342] Interleukin-36 receptor antagonist protein (IL-36Ra) (FIL1 delta) (IL-1-related protein 3) (IL-1RP3) (Interleukin-1 HY1) (IL-1HY1) (Interleukin-1 delta) (IL-1 delta) (Interleukin-1 family member 5) (IL-1F5) (Interleukin-1 receptor antagonist homolog 1) (IL-1ra homolog 1) (Interleukin-1-like protein 1) (IL-1L1)
[IL18 IGIF IL1F4] Interleukin-18 (IL-18) (Iboctadekin) (Interferon gamma-inducing factor) (IFN-gamma-inducing factor) (Interleukin-1 gamma) (IL-1 gamma)
[Il1r1 Il1ra] Interleukin-1 receptor type 1 (IL-1R-1) (IL-1RT-1) (IL-1RT1) (EC 3.2.2.6) (CD121 antigen-like family member A) (Interleukin-1 receptor alpha) (IL-1R-alpha) (Interleukin-1 receptor type I) (p80) (CD antigen CD121a) [Cleaved into: Interleukin-1 receptor type 1, membrane form (mIL-1R1) (mIL-1RI); Interleukin-1 receptor type 1, soluble form (sIL-1R1) (sIL-1RI)]
[IL1RAP C3orf13 IL1R3] Interleukin-1 receptor accessory protein (IL-1 receptor accessory protein) (IL-1RAcP) (EC 3.2.2.6) (Interleukin-1 receptor 3) (IL-1R-3) (IL-1R3)
[IL33] Interleukin-33 (IL-33)
[IL36G IL1E IL1F9 IL1H1 IL1RP2 UNQ2456/PRO5737] Interleukin-36 gamma (IL-1-related protein 2) (IL-1RP2) (Interleukin-1 epsilon) (IL-1 epsilon) (Interleukin-1 family member 9) (IL-1F9) (Interleukin-1 homolog 1) (IL-1H1)
[IL36RN Fil1d Il1f5 Il1h3 Il1hy1] Interleukin-36 receptor antagonist protein (IL-36Ra) (Interleukin-1 HY1) (IL-1HY1) (Interleukin-1 delta) (IL-1 delta) (Interleukin-1 family member 5) (IL-1F5) (Interleukin-1 homolog 3) (IL-1H3) (Interleukin-1-like protein 1) (IL-1L1)
[IL1A IL1F1] Interleukin-1 alpha (IL-1 alpha) (Hematopoietin-1)
[IL36B IL1F8 IL1H2] Interleukin-36 beta (FIL1 eta) (Interleukin-1 eta) (IL-1 eta) (Interleukin-1 family member 8) (IL-1F8) (Interleukin-1 homolog 2) (IL-1H2)
[Il36a Fil1e Il1e Il1f6 Il1h1] Interleukin-36 alpha (FIL1 epsilon) (Interleukin-1 epsilon) (IL-1 epsilon) (Interleukin-1 family member 6) (IL-1F6) (Interleukin-1 homolog 1) (IL-1H1)
[IL4R IL4RA 582J2.1] Interleukin-4 receptor subunit alpha (IL-4 receptor subunit alpha) (IL-4R subunit alpha) (IL-4R-alpha) (IL-4RA) (CD antigen CD124) [Cleaved into: Soluble interleukin-4 receptor subunit alpha (Soluble IL-4 receptor subunit alpha) (Soluble IL-4R-alpha) (sIL4Ralpha/prot) (IL-4-binding protein) (IL4-BP)]
[IL36A FIL1E IL1E IL1F6] Interleukin-36 alpha (FIL1 epsilon) (Interleukin-1 epsilon) (IL-1 epsilon) (Interleukin-1 family member 6) (IL-1F6)
[IL18RAP IL1R7] Interleukin-18 receptor accessory protein (IL-18 receptor accessory protein) (IL-18RAcP) (EC 3.2.2.6) (Accessory protein-like) (AcPL) (CD218 antigen-like family member B) (CDw218b) (IL-1R accessory protein-like) (IL-1RAcPL) (Interleukin-1 receptor 7) (IL-1R-7) (IL-1R7) (Interleukin-18 receptor accessory protein-like) (Interleukin-18 receptor beta) (IL-18R-beta) (IL-18Rbeta) (CD antigen CD218b)
[tat] Protein Tat (Transactivating regulatory protein)
[IL1B IL1F2] Interleukin-1 beta (IL-1 beta) (Catabolin)
[IL17RD IL17RLM SEF UNQ6115/PRO20026] Interleukin-17 receptor D (IL-17 receptor D) (IL-17RD) (IL17Rhom) (Interleukin-17 receptor-like protein) (Sef homolog) (hSef)
[Il1a] Interleukin-1 alpha (IL-1 alpha)
[Il1a] Interleukin-1 alpha (IL-1 alpha)
[IL18R1 IL1RRP] Interleukin-18 receptor 1 (IL-18R-1) (IL-18R1) (EC 3.2.2.6) (CD218 antigen-like family member A) (CDw218a) (IL1 receptor-related protein) (IL-1Rrp) (IL1R-rp) (Interleukin-18 receptor alpha) (IL-18R-alpha) (IL-18Ralpha) (CD antigen CD218a)
[Il1rap] Interleukin-1 receptor accessory protein (IL-1 receptor accessory protein) (IL-1RAcP) (EC 3.2.2.6)

Bibliography :
No related Items