Search results for IL22

Showing 19 results out of 43

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Protein (4 results from a total of 4)

Identifier: R-HSA-448460
Species: Homo sapiens
Compartment: extracellular region
Primary external reference: UniProt: IL22: Q9GZX6
Identifier: R-HSA-448489
Species: Homo sapiens
Compartment: plasma membrane
Primary external reference: UniProt: Q8N6P7
Identifier: R-HSA-448432
Species: Homo sapiens
Compartment: extracellular region
Primary external reference: UniProt: IL22RA2: Q969J5
Identifier: R-HSA-8987198
Species: Homo sapiens
Compartment: plasma membrane
Primary external reference: UniProt: IL22RA1: Q8N6P7

Reaction (7 results from a total of 21)

Identifier: R-HSA-448741
Species: Homo sapiens
Compartment: extracellular region, plasma membrane
Interleukin-22 receptor subunit alpha-2 (IL22RA2), also known as Interleukin-22 binding protein (IL22BP), is a soluble receptor that binds Interleukin-22 (IL22) within the extracellular region, preventing IL22 from binding to the functional membrane-associated IL22 receptor (Xu et al. 2001, De Moura et al. 2009, Dumoutier et al. 2001, Kotenko et al. 2001). This may play a regulatory role in inflammation.
Identifier: R-HSA-448480
Species: Homo sapiens
Compartment: extracellular region, plasma membrane, cytosol
Temporal models suggest that the first event in IL22 receptor formation is binding of Interleukin-22 (IL22) to IL22RA1), which pre associates with JAK1 (Li et al. 2004, Jones et al. 2008, Xie et al. 2000, Xu et al. 2001).
The Interleukin-22 receptor consists of IL22RA1 and Interleukin-10 receptor subunit beta (IL10RB), which is also a component of the receptors for Interleukin-10 (IL10), Interleukin-22 (IL22), Interleukin-26 (IL26), Interleukin-28 (IL28), and Interferon lambda-1 (IFNL1).
Identifier: R-HSA-8854645
Species: Homo sapiens
Compartment: extracellular region, plasma membrane, cytosol
Temporal models suggest that binding of Interleukin‑22 (IL22) to Interleukin‑22 receptor subunit alpha 1 (IL22RA1) creates a surface that is bound by the extracellular region of Interleukin‑10 receptor beta chain (IL10RB) (Li et al. 2004, Bleicher et al. 2008).
Identifier: R-HSA-8986995
Species: Homo sapiens
Compartment: cytosol, extracellular region, plasma membrane
Interleukin-22 receptor subunit alpha-1 (IL22RA1) is phosphorylated within the receptor complex, which consists of Interleukin-22 (IL22), IL22RA1 associated with phosphorylated Tyrosine protein kinase JAK1 (JAK1) and Interleukin-10 receptor subunit beta (IL10RB) associated with phosphorylated non-receptor tyrosine-protein kinase TYK2 (TYK2). IL22 stimulated IL22RA1 tyrosine phosphorylation and recruitment of Tyrosine protein phosphatase non receptor type 11 (PTPN11, SHP2). PTPN11 binding was abolished by mutation of Tyrosines-251 and 301 (Meng et al. 2010).
This is a black-box event because it is not clear which kinase is responsible for IL22RA1 phosphorylation.
Identifier: R-HSA-8987042
Species: Homo sapiens
Compartment: plasma membrane, cytosol, extracellular region
Inferred from rat, mouse, human :Tyrosine protein kinase JAK1 (JAK1) and Non-receptor tyrosine-protein kinase TYK2 (TYK2) are believed to be phosphorylated after Interleukin-22 interacts with its receptor. The receptor is a complex formed by Interleukin-22 receptor subunit alpha-1 (IL22RA1), JAK1, Interleukin-10 receptor subunit beta (IL10RB) and TYK2 (Lejeune et al. 2002, Sabat et al. 2014). This is a black-box event because the JAK1/TYK2 coordinates phosphorylated after IL22 stimulus are unknown.
Identifier: R-HSA-8987070
Species: Homo sapiens
Compartment: cytosol, extracellular region, plasma membrane
Signal transducer and activator of transcription 3 (STAT3) is phosphorylated by the Interleukin-22 (IL22) receptor complex (Lejeune et al. 2002, Dumoutier et al. 2009, Lindemanns et al. 2015), which consists of IL22, phosphorylated Interleukin-22 receptor subunit alpha-1 (IL22RA1), phosphorylated Tyrosine-protein kinase JAK1 (JAK1), Interleukin-10 receptor subunit beta (IL10RB), phosphorylated Non-receptor tyrosine-protein kinase TYK2 (TYK2) and STAT3 (Meng et al. 2010, Sestito et al. 2011).
Identifier: R-HSA-8987014
Species: Homo sapiens
Compartment: cytosol, plasma membrane, extracellular region
Signal transducer and activator of transcription 3 (STAT3) is believed to bind the Interleukin-22 (IL22) receptor complex, which consists of IL22, phosphorylated Interleukin-22 receptor subunit alpha-1 (IL22RA1), phosphorylated Tyrosine-protein kinase JAK1 (JAK1), Interleukin-10 receptor subunit beta (IL10RB), phosphorylated Non-receptor tyrosine-protein kinase TYK2 (TYK2) and Tyrosine-protein phosphatase non-receptor type 11 (PTPN11 or SHP2) (Meng et al. 2010, Sestito et al. 2011). STAT3 has been reported to pre-associate with IL22RA in the absence of phosphorylated receptor tyrosines (Dumoutier et al. 2009).
This is a black box event because STAT3 binding is represented here as a post-receptor phosphorylation event, inferred from the consensus on interleukin receptor JAK-STAT signaling (Li et al. 2008, Santos et al. 2011).

Complex (7 results from a total of 17)

Identifier: R-HSA-448738
Species: Homo sapiens
Compartment: extracellular region
Identifier: R-HSA-8854697
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-448411
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-8987249
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-8987001
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-8987122
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-8987108
Species: Homo sapiens
Compartment: plasma membrane

Pathway (1 results from a total of 1)

Identifier: R-HSA-8854691
Species: Homo sapiens
The interleukin 20 (IL20) subfamily comprises IL19, IL20, IL22, IL24 and IL26. They are members of the larger IL10 family, but have been grouped together based on their usage of common receptor subunits and similarities in their target cell profiles and biological functions. Members of the IL20 subfamily facilitate the communication between leukocytes and epithelial cells, thereby enhancing innate defence mechanisms and tissue repair processes at epithelial surfaces. Much of the understanding of this group of cytokines is based on IL22, which is the most studied member (Rutz et al. 2014, Akdis M et al. 2016, Longsdon et al. 2012).
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