| UniProt ID | IL2_HUMAN | |
|---|---|---|
| UniProt AC | P60568 | |
| Protein Name | Interleukin-2 | |
| Gene Name | IL2 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 153 | |
| Subcellular Localization | Secreted. | |
| Protein Description | Produced by T-cells in response to antigenic or mitogenic stimulation, this protein is required for T-cell proliferation and other activities crucial to regulation of the immune response. Can stimulate B-cells, monocytes, lymphokine-activated killer cells, natural killer cells, and glioma cells.. | |
| Protein Sequence | MYRMQLLSCIALSLALVTNSAPTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKKATELKHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNRWITFCQSIISTLT | |
| 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 |
|---|---|---|---|---|---|
| 8 | Phosphorylation | MYRMQLLSCIALSLA CHHHHHHHHHHHHHH | 16.45 | - | |
| 23 | O-linked_Glycosylation | LVTNSAPTSSSTKKT HHHCCCCCCCCCCHH | 40.74 | 2793860 | |
| 23 | O-linked_Glycosylation | LVTNSAPTSSSTKKT HHHCCCCCCCCCCHH | 40.74 | 2793860 | |
| 23 | Sulfoxidation | LVTNSAPTSSSTKKT HHHCCCCCCCCCCHH | 40.74 | 2598316 | |
| 39 | Sulfoxidation | LQLEHLLLDLQMILN HHHHHHHHHHHHHHH | 8.54 | 2598316 | |
| 46 | Sulfoxidation | LDLQMILNGINNYKN HHHHHHHHCHHCCCC | 38.07 | 11697473 | |
| 65 | Phosphorylation | RMLTFKFYMPKKATE EEEEEEECCCCCHHH | 17.07 | - | |
| 104 | Sulfoxidation | NFHLRPRDLISNINV CCCCCHHHHHHCEEE | 51.54 | 2598316 |
| 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 IL2_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of IL2_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 IL2_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of IL2_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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| O-linked Glycosylation | |
| Reference | PubMed |
| "Expression of human interleukin-2 in recombinant baby hamster kidney,Ltk-, and Chinese hamster ovary cells. Structure of O-linkedcarbohydrate chains and their location within the polypeptide."; Conradt H.S., Nimtz M., Dittmar K.E.J., Lindenmaier W., Hoppe J.,Hauser H.; J. Biol. Chem. 264:17368-17373(1989). Cited for: GLYCOSYLATION AT THR-23. | |
| "Amino acid sequence and post-translational modification of humaninterleukin 2."; Robb R.J., Kutny R.M., Panico M., Morris H.R., Chowdhry V.; Proc. Natl. Acad. Sci. U.S.A. 81:6486-6490(1984). Cited for: PROTEIN SEQUENCE OF 21-153, DISULFIDE BOND, AND GLYCOSYLATION ATTHR-23. | |
