O95760 (IL33_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Interleukin-33
Short name=IL-33

Alternative name(s):
Interleukin-1 family member 11
Short name=IL-1F11
Nuclear factor from high endothelial venules
Short name=NF-HEV

Gene names

Name:	IL33
Synonyms:	C9orf26, IL1F11, NFHEV

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	270 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Cytokine that binds to and signals through IL1RL1/ST2 and its stimulation recruits MYD88, IRAK1, IRAK4, and TRAF6, followed by phosphorylation of MAPK3/ERK1 and/or MAPK1/ERK2, MAPK14, and MAPK8. Induces T-helper type 2-associated cytokines. Acts as a chemoattractant tor Th2 cells, and may function as an "alarmin", that amplifies immune responses during tissue injury. Ref.3 Ref.10 Ref.11 Ref.12 Ref.13 Ref.17 Ref.18 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. This form is rapidely lost upon angiogenic or proinflammatory activation. Ref.3 Ref.10 Ref.11 Ref.12 Ref.13 Ref.17 Ref.18
Subunit structure	Forms a 1:1:1 heterotrimeric complex with its primary high-affinity receptor IL1RL1 and the coreceptor IL1RAP. Ref.20
Subcellular location	Nucleus. Chromosome. Cytoplasmic vesicle › secretory vesicle. Secreted. Note: Associates with heterochromatin and mitotic chromosomes. Translocation from the nucleus occurs upon biomechanical strain, depends on an intact microtubule network, and is ATP-dependent. Ref.1 Ref.3 Ref.11 Ref.12 Ref.13 Ref.17 Ref.18
Tissue specificity	Expressed at high level in high endothelial venules found in tonsils, Peyer patches and mesenteric lymph nodes. Almost undetectable in placenta.
Domain	The homeodomain-like HTH domain mediates nuclear localization and heterochromatin association. Ref.11
Post-translational modification	Proteolytically converted to a mature form by CASP1 in vitro and calpains in vivo. Caspase-mediated proteolysis, once thought to activate IL33, rather acts as a switch to dampen its activity. Cathepsin G and elastase can cleave IL33 and generate highly active forms in activated neutrophils (IL-33(95-270), IL-33(99-270) and IL-33(109-270)). Proteolysis is not strictly required for biological activity.
Sequence similarities	Belongs to the IL-1 family. Highly divergent.

Ontologies

Keywords
Biological process	Transcription
Cellular component	Chromosome Cytoplasmic vesicle Nucleus Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Cytokine
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of T-helper 1 type immune response Inferred from electronic annotation. Source: Compara negative regulation of immunoglobulin secretion Inferred from electronic annotation. Source: Compara negative regulation of interferon-gamma production Inferred from electronic annotation. Source: Compara negative regulation of leukocyte migration Inferred from electronic annotation. Source: Compara positive regulation of chemokine secretion Inferred from direct assay PubMed 19841166. Source: BHF-UCL positive regulation of immunoglobulin secretion Inferred from electronic annotation. Source: Compara positive regulation of inflammatory response Inferred from sequence or structural similarity PubMed 19841166. Source: BHF-UCL positive regulation of interleukin-13 production Inferred from electronic annotation. Source: Compara positive regulation of interleukin-4 production Inferred from electronic annotation. Source: Compara positive regulation of interleukin-5 production Inferred from electronic annotation. Source: Compara positive regulation of interleukin-6 production Inferred from electronic annotation. Source: Compara positive regulation of macrophage activation Inferred from direct assay PubMed 19841166. Source: BHF-UCL positive regulation of transcription from RNA polymerase II promoter Inferred from sequence or structural similarity PubMed 19841166. Source: BHF-UCL positive regulation of type 2 immune response Inferred from electronic annotation. Source: Compara transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	chromosome Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular space Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell transport vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cytokine activity Inferred from direct assay PubMed 19841166. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
IL1RL1	Q01638	2	EBI-724057,EBI-993762

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O95760-1)

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

Isoform 2 (identifier: O95760-2)

The sequence of this isoform differs from the canonical sequence as follows:
     115-156: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: O95760-3)

Also known as: spIL-33;

The sequence of this isoform differs from the canonical sequence as follows:
     72-113: Missing.

Note: Constitutively active.

Isoform 4 (identifier: O95760-4)

The sequence of this isoform differs from the canonical sequence as follows:
     31-157: KSQQKAKEVC...EDLKKDEKKD → N

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – 111

111

PRO_0000248845

Chain

112 – 270

159

Interleukin-33

PRO_0000096790

Regions

Region

1 – 65

65

Homeodomain-like HTH domain

Region

66 – 111

46

Interaction with RELA By similarity

Natural variations

Alternative sequence

31 – 157

127

KSQQK…DEKKD → N in isoform 4.

VSP_045440

Alternative sequence

72 – 113

42

Missing in isoform 3.

VSP_044948

Alternative sequence

115 – 156

42

Missing in isoform 2.

VSP_042728

Natural variant

263

1

I → M.
Corresponds to variant rs16924241 [ dbSNP | Ensembl ].

VAR_049576

Secondary structure

1

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270

Helix Strand Turn

Details...

Beta strand

112 – 115

4

Beta strand

118 – 128

11

Turn

129 – 131

3

Beta strand

132 – 138

7

Beta strand

143 – 149

7

Beta strand

159 – 165

7

Turn

170 – 172

3

Beta strand

182 – 197

16

Turn

198 – 201

4

Beta strand

202 – 207

6

Turn

214 – 216

3

Beta strand

218 – 222

5

Beta strand

224 – 226

3

Beta strand

228 – 235

8

Beta strand

238 – 251

14

Helix

261 – 263

3

Beta strand

265 – 268

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 7C158069196EF636	FASTA	270	30,759
	10 20 30 40 50 60 MKPKMKYSTN KISTAKWKNT ASKALCFKLG KSQQKAKEVC PMYFMKLRSG LMIKKEACYF 70 80 90 100 110 120 RRETTKRPSL KTGRKHKRHL VLAACQQQST VECFAFGISG VQKYTRALHD SSITGISPIT 130 140 150 160 170 180 EYLASLSTYN DQSITFALED ESYEIYVEDL KKDEKKDKVL LSYYESQHPS NESGDGVDGK 190 200 210 220 230 240 MLMVTLSPTK DFWLHANNKE HSVELHKCEK PLPDQAFFVL HNMHSNCVSF ECKTDPGVFI 250 260 270 GVKDNHLALI KVDSSENLCT ENILFKLSET
	Isoform 2 [UniParc]. Checksum: D48B2E3078CFA6C8	FASTA	228	25,930
	10 20 30 40 50 60 MKPKMKYSTN KISTAKWKNT ASKALCFKLG KSQQKAKEVC PMYFMKLRSG LMIKKEACYF 70 80 90 100 110 120 RRETTKRPSL KTGRKHKRHL VLAACQQQST VECFAFGISG VQKYTRALHD SSITDKVLLS 130 140 150 160 170 180 YYESQHPSNE SGDGVDGKML MVTLSPTKDF WLHANNKEHS VELHKCEKPL PDQAFFVLHN 190 200 210 220 MHSNCVSFEC KTDPGVFIGV KDNHLALIKV DSSENLCTEN ILFKLSET
	Isoform 3 (spIL-33) [UniParc]. Checksum: A982BD564D8FEC0E	FASTA	228	26,104
	10 20 30 40 50 60 MKPKMKYSTN KISTAKWKNT ASKALCFKLG KSQQKAKEVC PMYFMKLRSG LMIKKEACYF 70 80 90 100 110 120 RRETTKRPSL KTGISPITEY LASLSTYNDQ SITFALEDES YEIYVEDLKK DEKKDKVLLS 130 140 150 160 170 180 YYESQHPSNE SGDGVDGKML MVTLSPTKDF WLHANNKEHS VELHKCEKPL PDQAFFVLHN 190 200 210 220 MHSNCVSFEC KTDPGVFIGV KDNHLALIKV DSSENLCTEN ILFKLSET
	Isoform 4 [UniParc]. Checksum: 1B73431981DFFF46	FASTA	144	16,250
	10 20 30 40 50 60 MKPKMKYSTN KISTAKWKNT ASKALCFKLG NKVLLSYYES QHPSNESGDG VDGKMLMVTL 70 80 90 100 110 120 SPTKDFWLHA NNKEHSVELH KCEKPLPDQA FFVLHNMHSN CVSFECKTDP GVFIGVKDNH 130 140 LALIKVDSSE NLCTENILFK LSET

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular characterization of NF-HEV, a nuclear factor preferentially expressed in human high endothelial venules." Baekkevold E.S., Roussigne M., Yamanaka T., Johansen F.-E., Jahnsen F.L., Amalric F., Brandtzaeg P., Erard M., Haraldsen G., Girard J.-P. Am. J. Pathol. 163:69-79(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION, SUBCELLULAR LOCATION. Tissue: Endothelial cell.
[2]	"Identification of genes differentially expressed in canine vasospastic cerebral arteries after subarachnoid hemorrhage." Onda H., Kasuya H., Takakura K., Hori T., Imaizumi T., Takeuchi T., Inoue I., Takeda J. J. Cereb. Blood Flow Metab. 19:1279-1288(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"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." 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. Immunity 23:479-490(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, FUNCTION.
[4]	"Identification of constitutively active interleukin 33 (IL-33) splice variant." Hong J., Bae S., Jhun H., Lee S., Choi J., Kang T., Kwak A., Hong K., Kim E., Jo S., Kim S. J. Biol. Chem. 286:20078-20086(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[5]	"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 2 AND 4). Tissue: Trachea.
[6]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[7]	"DNA sequence and analysis of human chromosome 9." 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. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"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 1). Tissue: Brain.
[10]	"IL-33 is a chemoattractant for human Th2 cells." Komai-Koma M., Xu D., Li Y., McKenzie A.N., McInnes I.B., Liew F.Y. Eur. J. Immunol. 37:2779-2786(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"IL-33, the IL-1-like cytokine ligand for ST2 receptor, is a chromatin-associated nuclear factor in vivo." Carriere V., Roussel L., Ortega N., Lacorre D.A., Americh L., Aguilar L., Bouche G., Girard J.P. Proc. Natl. Acad. Sci. U.S.A. 104:282-287(2007) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, FUNCTION, NUCLEAR TARGETING DOMAIN.
[12]	"Nuclear interleukin-33 is generally expressed in resting endothelium but rapidly lost upon angiogenic or proinflammatory activation." Kuchler A.M., Pollheimer J., Balogh J., Sponheim J., Manley L., Sorensen D.R., De Angelis P.M., Scott H., Haraldsen G. Am. J. Pathol. 173:1229-1242(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[13]	"The IL-1-like cytokine IL-33 is constitutively expressed in the nucleus of endothelial cells and epithelial cells in vivo: a novel 'alarmin'?" Moussion C., Ortega N., Girard J.P. PLoS ONE 3:E3331-E3331(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[14]	"Mature interleukin-33 is produced by calpain-mediated cleavage in vivo." Hayakawa M., Hayakawa H., Matsuyama Y., Tamemoto H., Okazaki H., Tominaga S. Biochem. Biophys. Res. Commun. 387:218-222(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEOLYTIC PROCESSING.
[15]	"Suppression of interleukin-33 bioactivity through proteolysis by apoptotic caspases." 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. Immunity 31:84-98(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEOLYTIC PROCESSING.
[16]	"The IL-1-like cytokine IL-33 is inactivated after maturation by caspase-1." Cayrol C., Girard J.P. Proc. Natl. Acad. Sci. U.S.A. 106:9021-9026(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEOLYTIC PROCESSING.
[17]	"The dual function cytokine IL-33 interacts with the transcription factor NF-kappaB to dampen NF-kappaB-stimulated gene transcription." Ali S., Mohs A., Thomas M., Klare J., Ross R., Schmitz M.L., Martin M.U. J. Immunol. 187:1609-1616(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[18]	"Interleukin 33 as a mechanically responsive cytokine secreted by living cells." Kakkar R., Hei H., Dobner S., Lee R.T. J. Biol. Chem. 287:6941-6948(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[19]	"IL-33 is processed into mature bioactive forms by neutrophil elastase and cathepsin G." Lefrancais E., Roga S., Gautier V., Gonzalez-de-Peredo A., Monsarrat B., Girard J.P., Cayrol C. Proc. Natl. Acad. Sci. U.S.A. 109:1673-1678(2012) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEOLYTIC PROCESSING.
[20]	"Structure of IL-33 and its interaction with the ST2 and IL-1RAcP receptors--insight into heterotrimeric IL-1 signaling complexes." Lingel A., Weiss T.M., Niebuhr M., Pan B., Appleton B.A., Wiesmann C., Bazan J.F., Fairbrother W.J. Structure 17:1398-1410(2009) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 111-270, INTERACTION WITH IL1RL1 AND IL1RAP, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB024518 mRNA. Translation: BAA75892.1.
AY905581 mRNA. Translation: AAX86998.1.
HQ641439 mRNA. Translation: ADR77828.1.
AK295908 mRNA. Translation: BAG58697.1.
AK303943 mRNA. Translation: BAG64871.1.
CR407619 mRNA. Translation: CAG28547.1.
AL353741 Genomic DNA. Translation: CAI16003.1.
CH471071 Genomic DNA. Translation: EAW58748.1.
CH471071 Genomic DNA. Translation: EAW58750.1.
CH471071 Genomic DNA. Translation: EAW58751.1.
BC047085 mRNA. Translation: AAH47085.1.

IPI

IPI00027628.
IPI00908682.
IPI00981232.

RefSeq

NP_001186569.1. NM_001199640.1.
NP_001186570.1. NM_001199641.1.
NP_254274.1. NM_033439.3.

UniGene

Hs.731660.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2KLL	NMR	-	A	111-270	[»]

ProteinModelPortal

O95760.

ModBase

Search...

Protein-protein interaction databases

IntAct

O95760. 2 interactions.

MINT

MINT-1423224.

STRING

9606.ENSP00000370842.

PTM databases

PhosphoSite

O95760.

Proteomic databases

PaxDb

O95760.

PRIDE

O95760.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000381434; ENSP00000370842; ENSG00000137033.
ENST00000417746; ENSP00000394039; ENSG00000137033.
ENST00000456383; ENSP00000414238; ENSG00000137033.

GeneID

90865.

KEGG

hsa:90865.

UCSC

uc003zjt.3. human.

Organism-specific databases

CTD

90865.

GeneCards

GC09P006206.

HGNC

HGNC:16028. IL33.

HPA

CAB007057.
HPA024426.

MIM

608678. gene.

neXtProt

NX_O95760.

PharmGKB

PA162392005.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG41297.

HOGENOM

HOG000070215.

HOVERGEN

HBG081791.

InParanoid

O95760.

KO

K12967.

OMA

PKMKYST.

OrthoDB

EOG4FXR8C.

PhylomeDB

O95760.

Gene expression databases

ArrayExpress

O95760.

Bgee

O95760.

CleanEx

HS_IL33.

Genevestigator

O95760.

GermOnline

ENSG00000137033. Homo sapiens.

Family and domain databases

InterPro

IPR026145. IL33.
[Graphical view]

PANTHER

PTHR21114. PTHR21114. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

O95760.

GenomeRNAi

90865.

NextBio

35499393.

SOURCE

Search...

Entry information

Entry name

IL33_HUMAN

Accession

Primary (citable) accession number: O95760
Secondary accession number(s): B4DJ35 , B4E1Q9, D3DRI5, E7EAX4, Q2YEJ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2005
Last sequence update:	May 1, 1999
Last modified:	May 1, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.