| UniProt ID | I18BP_HUMAN | |
|---|---|---|
| UniProt AC | O95998 | |
| Protein Name | Interleukin-18-binding protein | |
| Gene Name | IL18BP | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 194 | |
| Subcellular Localization | Secreted . | |
| Protein Description | Isoform A binds to IL-18 and inhibits its activity. Functions as an inhibitor of the early TH1 cytokine response.. | |
| Protein Sequence | MTMRHNWTPDLSPLWVLLLCAHVVTLLVRATPVSQTTTAATASVRSTKDPCPSQPPVFPAAKQCPALEVTWPEVEVPLNGTLSLSCVACSRFPNFSILYWLGNGSFIEHLPGRLWEGSTSRERGSTGTQLCKALVLEQLTPALHSTNFSCVLVDPEQVVQRHVVLAQLWAGLRATLPPTQEALPSSHSSPQQQG | |
| 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 |
|---|---|---|---|---|---|
| 31 | Phosphorylation | VTLLVRATPVSQTTT HHHHHHCCCCCCCCC | 17.41 | - | |
| 34 | Phosphorylation | LVRATPVSQTTTAAT HHHCCCCCCCCCCEE | 24.02 | - | |
| 46 | O-linked_Glycosylation | AATASVRSTKDPCPS CEECCCCCCCCCCCC | 37.34 | 55828249 | |
| 47 | O-linked_Glycosylation | ATASVRSTKDPCPSQ EECCCCCCCCCCCCC | 28.98 | 55828253 | |
| 53 | O-linked_Glycosylation | STKDPCPSQPPVFPA CCCCCCCCCCCCCCH | 63.13 | 55828257 | |
| 79 | N-linked_Glycosylation | PEVEVPLNGTLSLSC CEEEEECCCEEEEEE | 35.02 | UniProtKB CARBOHYD | |
| 94 | N-linked_Glycosylation | VACSRFPNFSILYWL EECCCCCCEEEEEEE | 40.35 | UniProtKB CARBOHYD | |
| 99 (in isoform 3) | Phosphorylation | - | 9.27 | - | |
| 100 (in isoform 3) | Phosphorylation | - | 8.37 | - | |
| 103 | N-linked_Glycosylation | SILYWLGNGSFIEHL EEEEEECCCCHHHHC | 40.54 | 22171320 | |
| 120 | Phosphorylation | RLWEGSTSRERGSTG CCCCCCCCCCCCCHH | 33.56 | 29759185 | |
| 147 | N-linked_Glycosylation | TPALHSTNFSCVLVD CHHHHCCCCCEEEEC | 29.83 | 22171320 | |
| 147 (in isoform 4) | Phosphorylation | - | 29.83 | - | |
| 148 (in isoform 4) | Phosphorylation | - | 6.41 | - |
| 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 I18BP_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of I18BP_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 I18BP_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of I18BP_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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| N-linked Glycosylation | |
| Reference | PubMed |
| "Human urinary glycoproteomics; attachment site specific analysis ofN-and O-linked glycosylations by CID and ECD."; Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.; Mol. Cell. Proteomics 0:0-0(2011). Cited for: GLYCOSYLATION AT SER-53; ASN-103 AND ASN-147, STRUCTURE OFCARBOHYDRATES, AND MASS SPECTROMETRY. | |
| O-linked Glycosylation | |
| Reference | PubMed |
| "Human urinary glycoproteomics; attachment site specific analysis ofN-and O-linked glycosylations by CID and ECD."; Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.; Mol. Cell. Proteomics 0:0-0(2011). Cited for: GLYCOSYLATION AT SER-53; ASN-103 AND ASN-147, STRUCTURE OFCARBOHYDRATES, AND MASS SPECTROMETRY. | |
