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O95760 (IL33_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length270 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 vesiclesecretory 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 processTranscription
   Cellular componentChromosome
Cytoplasmic vesicle
Nucleus
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionCytokine
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnegative regulation of T-helper 1 type immune response

Inferred from electronic annotation. Source: Ensembl

negative regulation of immunoglobulin secretion

Inferred from electronic annotation. Source: Ensembl

negative regulation of interferon-gamma production

Inferred from electronic annotation. Source: Ensembl

negative regulation of leukocyte migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of chemokine secretion

Inferred from direct assay PubMed 19841166. Source: BHF-UCL

positive regulation of immunoglobulin secretion

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

positive regulation of interleukin-4 production

Inferred from electronic annotation. Source: Ensembl

positive regulation of interleukin-5 production

Inferred from electronic annotation. Source: Ensembl

positive regulation of interleukin-6 production

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentchromosome

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_functioncytokine activity

Inferred from direct assay PubMed 19841166. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.3PubMed 18688256. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HIST1H2AMP0C0S83EBI-724057,EBI-1390628
IL1RL1Q016382EBI-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 111111
PRO_0000248845
Chain112 – 270159Interleukin-33
PRO_0000096790

Regions

Region1 – 6565Homeodomain-like HTH domain
Region66 – 11146Interaction with RELA By similarity

Natural variations

Alternative sequence31 – 157127KSQQK…DEKKD → N in isoform 4.
VSP_045440
Alternative sequence72 – 11342Missing in isoform 3.
VSP_044948
Alternative sequence115 – 15642Missing in isoform 2.
VSP_042728
Natural variant2631I → M.
Corresponds to variant rs16924241 [ dbSNP | Ensembl ].
VAR_049576

Experimental info

Mutagenesis1441E → K: Decreases affinity for IL1RL1. Ref.21
Mutagenesis1481E → K: 7-fold decrease in affinity for IL1RL1. Ref.21
Mutagenesis1491D → K: Almost abolishes binding to IL1RL1. Ref.21
Mutagenesis1651E → K: 8-fold decrease in affinity for IL1RL1. Ref.21
Mutagenesis2441D → K: Decreases affinity for IL1RL1. Ref.21
Sequence conflict1391E → G in BAG36208. Ref.5

Secondary structure

.................................. 270
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 7C158069196EF636

FASTA27030,759
        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 

« Hide

Isoform 2 [UniParc].

Checksum: D48B2E3078CFA6C8
Show »

FASTA22825,930
Isoform 3 (spIL-33) [UniParc].

Checksum: A982BD564D8FEC0E
Show »

FASTA22826,104
Isoform 4 [UniParc].

Checksum: 1B73431981DFFF46
Show »

FASTA14416,250

References

« Hide '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. expand/collapse author list , 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; 2 AND 4).
Tissue: Adrenal gland and 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. expand/collapse author list , 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. expand/collapse author list , 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.
[21]"Structural insights into the interaction of IL-33 with its receptors."
Liu X., Hammel M., He Y., Tainer J.A., Jeng U.S., Zhang L., Wang S., Wang X.
Proc. Natl. Acad. Sci. U.S.A. 110:14918-14923(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.27 ANGSTROMS) OF 112-270 IN COMPLEX WITH IL1RL1/ST2, MUTAGENESIS OF GLU-144; GLU-148; ASP-149; GLU-165 AND ASP-244.
+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.
AK313414 mRNA. Translation: BAG36208.1.
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.
CCDSCCDS56563.1. [O95760-2]
CCDS56564.1. [O95760-4]
CCDS6468.1. [O95760-1]
RefSeqNP_001186569.1. NM_001199640.1. [O95760-2]
NP_001186570.1. NM_001199641.1. [O95760-4]
NP_254274.1. NM_033439.3. [O95760-1]
XP_005251683.1. XM_005251626.2. [O95760-1]
XP_005251684.1. XM_005251627.1. [O95760-1]
UniGeneHs.731660.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KLLNMR-A111-270[»]
4KC3X-ray3.27A112-270[»]
ProteinModelPortalO95760.
SMRO95760. Positions 111-270.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124776. 3 interactions.
DIPDIP-37862N.
IntActO95760. 4 interactions.
MINTMINT-1423224.
STRING9606.ENSP00000370842.

PTM databases

PhosphoSiteO95760.

Proteomic databases

PaxDbO95760.
PRIDEO95760.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000381434; ENSP00000370842; ENSG00000137033. [O95760-1]
ENST00000417746; ENSP00000394039; ENSG00000137033. [O95760-4]
ENST00000456383; ENSP00000414238; ENSG00000137033. [O95760-2]
GeneID90865.
KEGGhsa:90865.
UCSCuc003zjt.3. human. [O95760-1]
uc011lmg.2. human. [O95760-2]
uc011lmh.2. human.

Organism-specific databases

CTD90865.
GeneCardsGC09P006206.
HGNCHGNC:16028. IL33.
HPACAB007057.
HPA024426.
MIM608678. gene.
neXtProtNX_O95760.
PharmGKBPA162392005.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG41297.
HOGENOMHOG000070215.
HOVERGENHBG081791.
InParanoidO95760.
KOK12967.
OMADPGVFIG.
OrthoDBEOG7TQV1R.
PhylomeDBO95760.
TreeFamTF338120.

Gene expression databases

BgeeO95760.
CleanExHS_IL33.
GenevestigatorO95760.

Family and domain databases

InterProIPR026145. IL-33.
[Graphical view]
PANTHERPTHR21114. PTHR21114. 1 hit.
PfamPF15095. IL33. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO95760.
GenomeRNAi90865.
NextBio35467794.
PROO95760.
SOURCESearch...

Entry information

Entry nameIL33_HUMAN
AccessionPrimary (citable) accession number: O95760
Secondary accession number(s): B2R8L1 expand/collapse secondary AC list , B4DJ35, B4E1Q9, D3DRI5, E7EAX4, Q2YEJ5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: May 1, 1999
Last modified: July 9, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM