| UniProt ID | IL36B_HUMAN | |
|---|---|---|
| UniProt AC | Q9NZH7 | |
| Protein Name | Interleukin-36 beta | |
| Gene Name | IL36B | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 164 | |
| Subcellular Localization | Secreted . | |
| Protein Description | Cytokine that binds to and signals through the IL1RL2/IL-36R receptor which in turn activates NF-kappa-B and MAPK signaling pathways in target cells linked to a pro-inflammatory response. Part of the IL-36 signaling system that is thought to be present in epithelial barriers and to take part in local inflammatory response; similar to the IL-1 system with which it shares the coreceptor IL1RAP. Stimulates production of interleukin-6 and interleukin-8 in synovial fibrobasts, articular chondrocytes and mature adipocytes. Induces expression of a number of antimicrobial peptides including beta-defensins 4 and 103 as well as a number of matrix metalloproteases. Seems to be involved in skin inflammatory response by acting on keratinocytes, dendritic cells and indirectly on T-cells to drive tissue infiltration, cell maturation and cell proliferation. In cultured keratinocytes induces the expression of macrophage, T-cell, and neutrophil chemokines, such as CCL3, CCL4, CCL5, CCL2, CCL17, CCL22, CL20, CCL5, CCL2, CCL17, CCL22, CXCL8, CCL20 and CXCL1, and the production of proinflammatory cytokines such as TNF-alpha, IL-8 and IL-6.. | |
| Protein Sequence | MNPQREAAPKSYAIRDSRQMVWVLSGNSLIAAPLSRSIKPVTLHLIACRDTEFSDKEKGNMVYLGIKGKDLCLFCAEIQGKPTLQLKLQGSQDNIGKDTCWKLVGIHTCINLDVRESCFMGTLDQWGIGVGRKKWKSSFQHHHLRKKDKDFSSMRTNIGMPGRM | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 11 | Phosphorylation | QREAAPKSYAIRDSR CHHCCCCCEEEECCC | 20.81 | 25002506 | |
| 12 | Phosphorylation | REAAPKSYAIRDSRQ HHCCCCCEEEECCCE | 16.51 | 25002506 | |
| 17 | Phosphorylation | KSYAIRDSRQMVWVL CCEEEECCCEEEEEE | 17.98 | 22210691 | |
| 25 | Phosphorylation | RQMVWVLSGNSLIAA CEEEEEEECCCEEEE | 26.72 | 24043423 | |
| 28 | Phosphorylation | VWVLSGNSLIAAPLS EEEEECCCEEEECCC | 25.36 | 24043423 | |
| 35 | Phosphorylation | SLIAAPLSRSIKPVT CEEEECCCCCCCCEE | 23.95 | 24043423 | |
| 37 | Phosphorylation | IAAPLSRSIKPVTLH EEECCCCCCCCEEEE | 31.43 | 24043423 | |
| 51 | Phosphorylation | HLIACRDTEFSDKEK EEEEEECCCCCCCCC | 21.41 | 29038488 | |
| 83 | Phosphorylation | AEIQGKPTLQLKLQG EEECCCCEEEEEEEC | 30.53 | 19413330 | |
| 83 (in isoform 2) | Phosphorylation | - | 30.53 | 19413330 | |
| 95 (in isoform 2) | Phosphorylation | - | 11.04 | - | |
| 153 | Phosphorylation | KKDKDFSSMRTNIGM HHCCCHHHHCCCCCC | 16.57 | 30631047 | |
| 156 | Phosphorylation | KDFSSMRTNIGMPGR CCHHHHCCCCCCCCC | 23.65 | 30631047 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of IL36B_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of IL36B_HUMAN !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of IL36B_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of IL36B_HUMAN !! | ||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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