P35225 · IL13_HUMAN
- ProteinInterleukin-13
- GeneIL13
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids146 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Cytokine that plays important roles in allergic inflammation and immune response to parasite infection (PubMed:8096327, PubMed:8097324).
Synergizes with IL2 in regulating interferon-gamma synthesis (PubMed:8096327).
Stimulates B-cell proliferation, and activation of eosinophils, basophils, and mast cells (PubMed:7903680, PubMed:8759755).
Plays an important role in controlling IL33 activity by modulating the production of transmembrane and soluble forms of interleukin-1 receptor-like 1/IL1RL1 (By similarity).
Displays the capacity to antagonize Th1-driven proinflammatory immune response and downregulates synthesis of many proinflammatory cytokines including IL1, IL6, IL10, IL12 and TNF-alpha through a mechanism that partially involves suppression of NF-kappa-B (By similarity).
Functions also on nonhematopoietic cells, including endothelial cells where it induces vascular cell adhesion protein 1/VCAM1, which is important in the recruitment of eosinophils (PubMed:8639787).
Exerts its biological effects through its receptors which comprises the IL4R chain and the IL13RA1 chain, to activate JAK1 and TYK2, leading to the activation of STAT6 (PubMed:9013879).
Aside from IL13RA1, another receptor IL13RA2 acts as a high affinity decoy for IL13 and mediates internalization and depletion of extracellular IL13 (PubMed:21622864).
Synergizes with IL2 in regulating interferon-gamma synthesis (PubMed:8096327).
Stimulates B-cell proliferation, and activation of eosinophils, basophils, and mast cells (PubMed:7903680, PubMed:8759755).
Plays an important role in controlling IL33 activity by modulating the production of transmembrane and soluble forms of interleukin-1 receptor-like 1/IL1RL1 (By similarity).
Displays the capacity to antagonize Th1-driven proinflammatory immune response and downregulates synthesis of many proinflammatory cytokines including IL1, IL6, IL10, IL12 and TNF-alpha through a mechanism that partially involves suppression of NF-kappa-B (By similarity).
Functions also on nonhematopoietic cells, including endothelial cells where it induces vascular cell adhesion protein 1/VCAM1, which is important in the recruitment of eosinophils (PubMed:8639787).
Exerts its biological effects through its receptors which comprises the IL4R chain and the IL13RA1 chain, to activate JAK1 and TYK2, leading to the activation of STAT6 (PubMed:9013879).
Aside from IL13RA1, another receptor IL13RA2 acts as a high affinity decoy for IL13 and mediates internalization and depletion of extracellular IL13 (PubMed:21622864).
GO annotations
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameInterleukin-13
- Short namesIL-13
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP35225
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Allergic rhinitis (ALRH)
- Note
- DescriptionA common disease with complex inheritance characterized by mucosal inflammation caused by allergen exposure.
- See alsoMIM:607154
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_010037 | 144 | probable protective factor against ALRH; may be associated with decreased risk for asthma development; at homozygosity may be associated with lower levels of serum total IgE in some allergic rhinitis patients; dbSNP:rs20541 | |||
Sequence: Q → R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 154 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-24 | |||||
Sequence: MHPLLNPLLLALGLMALLLTTVIA | ||||||
Chain | PRO_0000015547 | 25-146 | Interleukin-13 | |||
Sequence: LTCLGGFASPGPVPPSTALRELIEELVNITQNQKAPLCNGSMVWSINLTAGMYCAALESLINVSGCSAIEKTQRMLSGFCPHKVSAGQFSSLHVRDTKIEVAQFVKDLLLHLKKLFREGQFN | ||||||
Glycosylation | 52 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 62↔90 | |||||
Sequence: CNGSMVWSINLTAGMYCAALESLINVSGC | ||||||
Glycosylation | 63 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 71 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 78↔104 | |||||
Sequence: CAALESLINVSGCSAIEKTQRMLSGFC | ||||||
Glycosylation | 86 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with IL13RA2.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P35225 | IL13RA1 P78552 | 7 | EBI-1647828, EBI-1391535 | |
BINARY | P35225 | IL13RA2 Q14627 | 9 | EBI-1647828, EBI-4320063 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length146
- Mass (Da)15,788
- Last updated2024-01-24 v3
- ChecksumBE2D441CF913D129
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 1 | in Ref. 2; CAA48824 | ||||
Sequence: M → R | ||||||
Sequence conflict | 26 | in Ref. 9; no nucleotide entry | ||||
Sequence: T → A | ||||||
Sequence conflict | 32 | in Ref. 9; no nucleotide entry | ||||
Sequence: A → D | ||||||
Sequence conflict | 51 | in Ref. 9; no nucleotide entry | ||||
Sequence: V → S | ||||||
Sequence conflict | 56 | in Ref. 9; no nucleotide entry | ||||
Sequence: N → T | ||||||
Sequence conflict | 59 | in Ref. 3; AAA83738 | ||||
Sequence: A → R | ||||||
Sequence conflict | 101 | in Ref. 8; AAC03535 | ||||
Sequence: S → G | ||||||
Sequence conflict | 112 | in Ref. 3; AAA83738 | ||||
Sequence: Missing |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X69079 EMBL· GenBank· DDBJ | CAA48823.1 EMBL· GenBank· DDBJ | mRNA | ||
X69079 EMBL· GenBank· DDBJ | CAA48824.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
L06801 EMBL· GenBank· DDBJ | AAA36107.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
U10307 EMBL· GenBank· DDBJ | AAA83738.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
U31120 EMBL· GenBank· DDBJ | AAB01681.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
AF377331 EMBL· GenBank· DDBJ | AAK53823.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
AC004039 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC096139 EMBL· GenBank· DDBJ | AAH96139.1 EMBL· GenBank· DDBJ | mRNA | ||
AF043334 EMBL· GenBank· DDBJ | AAC03535.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |