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O95760

- IL33_HUMAN

UniProt

O95760 - IL33_HUMAN

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Protein
Interleukin-33
Gene
IL33, C9orf26, IL1F11, NFHEV
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 (1 Publication). 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 (1 Publication, 1 Publication).
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 (1 Publication). This form is rapidely lost upon angiogenic or proinflammatory activation (1 Publication).7 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei94 – 952Cleavage by CTSG
Sitei98 – 992Cleavage by ELANE
Sitei108 – 1092Cleavage by CTSG

GO - Molecular functioni

  1. cytokine activity Source: BHF-UCL
  2. protein binding Source: IntAct

GO - Biological processi

  1. negative regulation of T-helper 1 type immune response Source: Ensembl
  2. negative regulation of immunoglobulin secretion Source: Ensembl
  3. negative regulation of interferon-gamma production Source: Ensembl
  4. negative regulation of leukocyte migration Source: Ensembl
  5. positive regulation of chemokine secretion Source: BHF-UCL
  6. positive regulation of immunoglobulin secretion Source: Ensembl
  7. positive regulation of inflammatory response Source: BHF-UCL
  8. positive regulation of interleukin-13 production Source: Ensembl
  9. positive regulation of interleukin-4 production Source: Ensembl
  10. positive regulation of interleukin-5 production Source: Ensembl
  11. positive regulation of interleukin-6 production Source: Ensembl
  12. positive regulation of macrophage activation Source: BHF-UCL
  13. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  14. positive regulation of type 2 immune response Source: Ensembl
  15. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Cytokine

Keywords - Biological processi

Transcription

Names & Taxonomyi

Protein namesi
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
Cleaved into the following 3 chains:
Gene namesi
Name:IL33
Synonyms:C9orf26, IL1F11, NFHEV
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:16028. IL33.

Subcellular locationi

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.7 Publications

GO - Cellular componenti

  1. chromosome Source: UniProtKB-SubCell
  2. extracellular space Source: UniProtKB-KW
  3. nucleus Source: UniProtKB-SubCell
  4. transport vesicle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasmic vesicle, Nucleus, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi144 – 1441E → K: Decreases affinity for IL1RL1. 1 Publication
Mutagenesisi148 – 1481E → K: 7-fold decrease in affinity for IL1RL1. 1 Publication
Mutagenesisi149 – 1491D → K: Almost abolishes binding to IL1RL1. 1 Publication
Mutagenesisi165 – 1651E → K: 8-fold decrease in affinity for IL1RL1. 1 Publication
Mutagenesisi244 – 2441D → K: Decreases affinity for IL1RL1. 1 Publication

Organism-specific databases

PharmGKBiPA162392005.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 270270Interleukin-33
PRO_0000096790Add
BLAST
Propeptidei1 – 9494
PRO_0000430083Add
BLAST
Chaini95 – 270176Interleukin-33 (95-270)
PRO_0000430084Add
BLAST
Chaini99 – 270172Interleukin-33 (99-270)
PRO_0000430085Add
BLAST
Chaini109 – 270162Interleukin-33 (109-270)
PRO_0000430086Add
BLAST

Post-translational modificationi

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 (1 Publication). Proteolytic cleavage mediated by apoptotic caspases including CASP3 and CASP7 results in IL33 inactivation (1 Publication). In vitro proteolytic cleavage by CASP1 was reported (1 Publication) but could not be confirmed in vivo (1 Publication) suggesting that IL33 is probably not a direct substrate for that caspase.

Proteomic databases

PaxDbiO95760.
PRIDEiO95760.

PTM databases

PhosphoSiteiO95760.

Expressioni

Tissue specificityi

Expressed at high level in high endothelial venules found in tonsils, Peyer patches and mesenteric lymph nodes. Almost undetectable in placenta.

Gene expression databases

BgeeiO95760.
CleanExiHS_IL33.
GenevestigatoriO95760.

Organism-specific databases

HPAiCAB007057.
HPA024426.

Interactioni

Subunit structurei

Forms a 1:1:1 heterotrimeric complex with its primary high-affinity receptor IL1RL1 and the coreceptor IL1RAP.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
HIST1H2AMP0C0S83EBI-724057,EBI-1390628
IL1RL1Q016382EBI-724057,EBI-993762

Protein-protein interaction databases

BioGridi124776. 3 interactions.
DIPiDIP-37862N.
IntActiO95760. 4 interactions.
MINTiMINT-1423224.
STRINGi9606.ENSP00000370842.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi112 – 1154
Beta strandi119 – 1279
Turni129 – 1313
Beta strandi133 – 1386
Beta strandi140 – 1489
Beta strandi158 – 16912
Turni170 – 1723
Beta strandi180 – 18910
Beta strandi193 – 1975
Turni198 – 2014
Beta strandi202 – 2065
Helixi214 – 2163
Beta strandi218 – 2247
Beta strandi228 – 2358
Beta strandi238 – 2436
Beta strandi246 – 2516
Helixi261 – 2633
Beta strandi265 – 2673

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KLLNMR-A111-270[»]
4KC3X-ray3.27A112-270[»]
ProteinModelPortaliO95760.
SMRiO95760. Positions 111-270.

Miscellaneous databases

EvolutionaryTraceiO95760.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 6565Homeodomain-like HTH domain
Add
BLAST
Regioni66 – 11146Interaction with RELA By similarity
Add
BLAST

Domaini

The homeodomain-like HTH domain mediates nuclear localization and heterochromatin association.1 Publication

Sequence similaritiesi

Belongs to the IL-1 family. Highly divergent.

Phylogenomic databases

eggNOGiNOG41297.
HOGENOMiHOG000070215.
HOVERGENiHBG081791.
InParanoidiO95760.
KOiK12967.
OMAiDPGVFIG.
OrthoDBiEOG7TQV1R.
PhylomeDBiO95760.
TreeFamiTF338120.

Family and domain databases

InterProiIPR026145. IL-33.
[Graphical view]
PANTHERiPTHR21114. PTHR21114. 1 hit.
PfamiPF15095. IL33. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O95760-1) [UniParc]FASTAAdd to Basket

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

« Hide

MKPKMKYSTN KISTAKWKNT ASKALCFKLG KSQQKAKEVC PMYFMKLRSG    50
LMIKKEACYF RRETTKRPSL KTGRKHKRHL VLAACQQQST VECFAFGISG 100
VQKYTRALHD SSITGISPIT EYLASLSTYN DQSITFALED ESYEIYVEDL 150
KKDEKKDKVL LSYYESQHPS NESGDGVDGK MLMVTLSPTK DFWLHANNKE 200
HSVELHKCEK PLPDQAFFVL HNMHSNCVSF ECKTDPGVFI GVKDNHLALI 250
KVDSSENLCT ENILFKLSET 270
Length:270
Mass (Da):30,759
Last modified:May 1, 1999 - v1
Checksum:i7C158069196EF636
GO
Isoform 2 (identifier: O95760-2) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:228
Mass (Da):25,930
Checksum:iD48B2E3078CFA6C8
GO
Isoform 3 (identifier: O95760-3) [UniParc]FASTAAdd to Basket

Also known as: spIL-33

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

Note: Constitutively active.

Show »
Length:228
Mass (Da):26,104
Checksum:iA982BD564D8FEC0E
GO
Isoform 4 (identifier: O95760-4) [UniParc]FASTAAdd to Basket

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

Show »
Length:144
Mass (Da):16,250
Checksum:i1B73431981DFFF46
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti263 – 2631I → M.
Corresponds to variant rs16924241 [ dbSNP | Ensembl ].
VAR_049576

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei31 – 157127KSQQK…DEKKD → N in isoform 4.
VSP_045440Add
BLAST
Alternative sequencei72 – 11342Missing in isoform 3.
VSP_044948Add
BLAST
Alternative sequencei115 – 15642Missing in isoform 2.
VSP_042728Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti139 – 1391E → G in BAG36208. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS56563.1. [O95760-2]
CCDS56564.1. [O95760-4]
CCDS6468.1. [O95760-1]
RefSeqiNP_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]
UniGeneiHs.731660.

Genome annotation databases

EnsembliENST00000381434; ENSP00000370842; ENSG00000137033. [O95760-1]
ENST00000417746; ENSP00000394039; ENSG00000137033. [O95760-4]
ENST00000456383; ENSP00000414238; ENSG00000137033. [O95760-2]
GeneIDi90865.
KEGGihsa:90865.
UCSCiuc003zjt.3. human. [O95760-1]
uc011lmg.2. human. [O95760-2]
uc011lmh.2. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS56563.1. [O95760-2 ]
CCDS56564.1. [O95760-4 ]
CCDS6468.1. [O95760-1 ]
RefSeqi NP_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 ]
UniGenei Hs.731660.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2KLL NMR - A 111-270 [» ]
4KC3 X-ray 3.27 A 112-270 [» ]
ProteinModelPortali O95760.
SMRi O95760. Positions 111-270.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 124776. 3 interactions.
DIPi DIP-37862N.
IntActi O95760. 4 interactions.
MINTi MINT-1423224.
STRINGi 9606.ENSP00000370842.

PTM databases

PhosphoSitei O95760.

Proteomic databases

PaxDbi O95760.
PRIDEi O95760.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000381434 ; ENSP00000370842 ; ENSG00000137033 . [O95760-1 ]
ENST00000417746 ; ENSP00000394039 ; ENSG00000137033 . [O95760-4 ]
ENST00000456383 ; ENSP00000414238 ; ENSG00000137033 . [O95760-2 ]
GeneIDi 90865.
KEGGi hsa:90865.
UCSCi uc003zjt.3. human. [O95760-1 ]
uc011lmg.2. human. [O95760-2 ]
uc011lmh.2. human.

Organism-specific databases

CTDi 90865.
GeneCardsi GC09P006206.
HGNCi HGNC:16028. IL33.
HPAi CAB007057.
HPA024426.
MIMi 608678. gene.
neXtProti NX_O95760.
PharmGKBi PA162392005.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG41297.
HOGENOMi HOG000070215.
HOVERGENi HBG081791.
InParanoidi O95760.
KOi K12967.
OMAi DPGVFIG.
OrthoDBi EOG7TQV1R.
PhylomeDBi O95760.
TreeFami TF338120.

Miscellaneous databases

EvolutionaryTracei O95760.
GenomeRNAii 90865.
NextBioi 35467794.
PROi O95760.
SOURCEi Search...

Gene expression databases

Bgeei O95760.
CleanExi HS_IL33.
Genevestigatori O95760.

Family and domain databases

InterProi IPR026145. IL-33.
[Graphical view ]
PANTHERi PTHR21114. PTHR21114. 1 hit.
Pfami PF15095. IL33. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    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), FUNCTION, SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING.
  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 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.
    , 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. 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 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: PROTEIN SEQUENCE OF 95-121, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, PROTEOLYTIC PROCESSING, CLEAVAGE AT PHE-94 AND LEU-108 BY CSTG, CLEAVAGE AT ILE-98 BY ELANE.
  11. Cited for: FUNCTION.
  12. "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: FUNCTION, SUBCELLULAR LOCATION, NUCLEAR TARGETING DOMAIN.
  13. "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.
  14. "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.
  15. "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.
  16. Cited for: PROTEOLYTIC PROCESSING.
  17. "Interleukin-33 is biologically active independently of caspase-1 cleavage."
    Talabot-Ayer D., Lamacchia C., Gabay C., Palmer G.
    J. Biol. Chem. 284:19420-19426(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION.
  18. "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.
  19. "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.
  20. "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.
  21. "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.
  22. "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.

Entry informationi

Entry nameiIL33_HUMAN
AccessioniPrimary (citable) accession number: O95760
Secondary accession number(s): B2R8L1
, B4DJ35, B4E1Q9, D3DRI5, E7EAX4, Q2YEJ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: May 1, 1999
Last modified: September 3, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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