| UniProt ID | IL2RA_HUMAN | |
|---|---|---|
| UniProt AC | P01589 | |
| Protein Name | Interleukin-2 receptor subunit alpha | |
| Gene Name | IL2RA | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 272 | |
| Subcellular Localization |
Membrane Single-pass type I membrane protein. |
|
| Protein Description | Receptor for interleukin-2. The receptor is involved in the regulation of immune tolerance by controlling regulatory T cells (TREGs) activity. TREGs suppress the activation and expansion of autoreactive T-cells.. | |
| Protein Sequence | MDSYLLMWGLLTFIMVPGCQAELCDDDPPEIPHATFKAMAYKEGTMLNCECKRGFRRIKSGSLYMLCTGNSSHSSWDNQCQCTSSATRNTTKQVTPQPEEQKERKTTEMQSPMQPVDQASLPGHCREPPPWENEATERIYHFVVGQMVYYQCVQGYRALHRGPAESVCKMTHGKTRWTQPQLICTGEMETSQFPGEEKPQASPEGRPESETSCLVTTTDFQIQTEMAATMETSIFTTEYQVAVAGCVFLLISVLLLSGLTWQRRQRKSRRTI | |
| 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 |
|---|---|---|---|---|---|
| 70 | N-linked_Glycosylation | LYMLCTGNSSHSSWD EEEEEECCCCCCCCC | 23.37 | 3134887 | |
| 89 | N-linked_Glycosylation | CTSSATRNTTKQVTP ECCCCCCCCCCCCCC | 47.98 | 3134887 | |
| 218 | O-linked_Glycosylation | TSCLVTTTDFQIQTE CEEEEEECCHHHHHH | 26.00 | 3264879 | |
| 224 | O-linked_Glycosylation | TTDFQIQTEMAATME ECCHHHHHHHHHHCC | 29.38 | 3264879 | |
| 229 | O-linked_Glycosylation | IQTEMAATMETSIFT HHHHHHHHCCCCCCC | 13.15 | 3264879 | |
| 236 | O-linked_Glycosylation | TMETSIFTTEYQVAV HCCCCCCCCHHHHHH | 19.63 | 3264879 | |
| 237 | O-linked_Glycosylation | METSIFTTEYQVAVA CCCCCCCCHHHHHHH | 23.19 | 3264879 | |
| 268 | Phosphorylation | WQRRQRKSRRTI--- HHHHHHHHCCCC--- | 29.23 | 2941417 | |
| 271 | Phosphorylation | RQRKSRRTI------ HHHHHCCCC------ | 29.90 | 2941417 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 268 | S | Phosphorylation | Kinase | PRKCA | P17252 | GPS |
| 268 | S | Phosphorylation | Kinase | PKC-FAMILY | - | GPS |
| 268 | S | Phosphorylation | Kinase | PKC_GROUP | - | PhosphoELM |
| 271 | T | Phosphorylation | Kinase | PRKCA | P17252 | GPS |
| 271 | T | Phosphorylation | Kinase | PKC-FAMILY | - | GPS |
| 271 | T | Phosphorylation | Kinase | PKC_GROUP | - | PhosphoELM |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of IL2RA_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 IL2RA_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| IL2RA_HUMAN | IL2RA | physical | 11886175 | |
| HGS_HUMAN | HGS | physical | 24134837 |
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| H00006 | Hairy-cell leukemia | |||||
| H00080 | Systemic lupus erythematosus | |||||
| H00091 | T-B+Severe combined immunodeficiencies (SCIDs), including the following eight diseases: X-linked SCI | |||||
| H00408 | Type I diabetes mellitus | |||||
| OMIM Disease | ||||||
| 601942 | Diabetes mellitus, insulin-dependent, 10 (IDDM10) | |||||
| Kegg Drug | ||||||
| D00748 | Aldesleukin (USAN/INN); Interleukin-2; Proleukin (TN) | |||||
| D02743 | Celmoleukin (genetical recombination) (JP16); Celmoleukin (INN); Celeuk (TN) | |||||
| D02749 | Teceleukin (genetical recombination) (JP16); Teceleukin (USAN); Imunace (TN) | |||||
| D03058 | Basiliximab (genetical recombination) (JAN); Basiliximab (USAN/INN); Simulect (TN) | |||||
| D03639 | Daclizumab (USAN/INN); Zenapax (TN) | |||||
| D03682 | Denileukin diftitox (USAN/INN); Ontak (TN) | |||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| N-linked Glycosylation | |
| Reference | PubMed |
| "Structural analysis of recombinant soluble human interleukin-2receptor. Primary structure, assignment of disulfide bonds and coreIL-2 binding structure."; Miedel M.C., Hulmes J.D., Weber D.V., Bailon P., Pan Y.C.; Biochem. Biophys. Res. Commun. 154:372-379(1988). Cited for: DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-70; ASN-89; THR-218;THR-224; THR-229 AND THR-237. | |
| O-linked Glycosylation | |
| Reference | PubMed |
| "Structural analysis of recombinant soluble human interleukin-2receptor. Primary structure, assignment of disulfide bonds and coreIL-2 binding structure."; Miedel M.C., Hulmes J.D., Weber D.V., Bailon P., Pan Y.C.; Biochem. Biophys. Res. Commun. 154:372-379(1988). Cited for: DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-70; ASN-89; THR-218;THR-224; THR-229 AND THR-237. | |
