Protein:IL7R |
Protein Summary |
 Gene summary |
| Gene name: IL7R | ASpdb.0 ID: 3575 | Gene | Gene symbol | IL7R | Gene ID | 3575 |
| Gene name | interleukin 7 receptor |
| Synonyms | CD127|CDW127|IL-7R-alpha|IL-7Ralpha|IL7RA|IL7Ralpha|ILRA|IMD104|lnc-IL7R|sIL-7R |
| Cytomap | 5p13.2 |
| Type of gene | protein-coding |
| Description | interleukin-7 receptor subunit alphaCD127 antigenIL-7 receptor subunit alphaIL-7R subunit alphainterleukin 7 receptor alpha chainsoluble interleukin-7 receptor |
| Modification date | 20240305 |
| UniProtAcc | P16871 |
| Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | IL7R | GO:0004896 | cytokine receptor activity | 11418668 |
| Gene | IL7R | GO:0005654 | nucleoplasm | - |
| Gene | IL7R | GO:0005829 | cytosol | - |
| Gene | IL7R | GO:0005886 | plasma membrane | - |
| Gene | IL7R | GO:0008284 | positive regulation of cell population proliferation | 11418668 |
| Gene | IL7R | GO:1904894 | positive regulation of receptor signaling pathway via STAT | 11418668 |
AS Summary |
| Information of the canonical protein with experimentally identified structure from PDB (2023). |
| UniProt Acc | File name | PDB ID | Method | Resolution | Chain | Start | End |
| P16871-1 | P16871-1_3up1_A.pdb | 3UP1 | X-ray | 2.15 | A | 32 | 232 |
| ASpdb's canonical and alternatively spliced isoform information. |
| accession_id | gene_name | canonical_id | alternative_id | canonical_length | alternative_length | canonical_start | canonical_end | type | originalSEQ | variationSEQ | alternative_start | alternative_end |
| P16871 | IL7R | P16871-1 | P16871-2 | 459 | 298 | 293 | 459 | Substitution | NLNVSFNPESFLDCQIHRVDDIQARDEVEGFLQDTFPQQLEESEKQRLGGDVQSPNCPSEDVVITPESFGRDSSLTCLAGNVSACDAPILSSSRSLDCRESGKNGPHVYQDLLLSLGTTNSTLPPPFSLQSGILTLNPVAQGQPILTSLGSNQEEAYVTMSSFYQNQ | VSVFGA | 293 | 298 |
| P16871 | IL7R | P16871-1 | P16871-3 | 459 | 261 | 237 | 459 | Substitution | EMDPILLTISILSFFSVALLVILACVLWKKRIKPIVWPSLPDHKKTLEHLCKKPRKNLNVSFNPESFLDCQIHRVDDIQARDEVEGFLQDTFPQQLEESEKQRLGGDVQSPNCPSEDVVITPESFGRDSSLTCLAGNVSACDAPILSSSRSLDCRESGKNGPHVYQDLLLSLGTTNSTLPPPFSLQSGILTLNPVAQGQPILTSLGSNQEEAYVTMSSFYQNQ | LSLSYGPVSPIIRRLWNIFVRNQEK | 237 | 261 |
| P16871 | IL7R | P16871-1 | P16871-4 | 459 | 252 | 237 | 252 | Substitution | EMDPILLTISILSFFS | LSLSYGPVSPIIRQEL | 237 | 252 |
| P16871 | IL7R | P16871-1 | P16871-4 | 459 | 252 | 253 | 459 | Deletion | none | none | 252 | 252 |
| Multiple sequence alignment of our canonical and alternatively spliced IL7R |
| Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of IL7R |
| UniProt-id | ENSG | ENST | ENSP |
| P16871-1 | ENSG00000168685.15 | ENST00000303115.8 | ENSP00000306157.3 |
| P16871-3 | ENSG00000168685.15 | ENST00000506850.5 | ENSP00000421207.1 |
| UniProt-id | NM ID | NP ID |
| P16871-1 | NM_002185.3 | NP_002176.2 |
| Amino acid sequences of our canonical and alternatively spliced IL7R |
| accession_id | Protein sequence |
| P16871-1 | MTILGTTFGMVFSLLQVVSGESGYAQNGDLEDAELDDYSFSCYSQLEVNGSQHSLTCAFEDPDVNITNLEFEICGALVEVKCLNFRKLQE IYFIETKKFLLIGKSNICVKVGEKSLTCKKIDLTTIVKPEAPFDLSVVYREGANDFVVTFNTSHLQKKYVKVLMHDVAYRQEKDENKWTH VNLSSTKLTLLQRKLQPAAMYEIKVRSIPDHYFKGFWSEWSPSYYFRTPEINNSSGEMDPILLTISILSFFSVALLVILACVLWKKRIKP IVWPSLPDHKKTLEHLCKKPRKNLNVSFNPESFLDCQIHRVDDIQARDEVEGFLQDTFPQQLEESEKQRLGGDVQSPNCPSEDVVITPES FGRDSSLTCLAGNVSACDAPILSSSRSLDCRESGKNGPHVYQDLLLSLGTTNSTLPPPFSLQSGILTLNPVAQGQPILTSLGSNQEEAYV |
| P16871-2 | MTILGTTFGMVFSLLQVVSGESGYAQNGDLEDAELDDYSFSCYSQLEVNGSQHSLTCAFEDPDVNITNLEFEICGALVEVKCLNFRKLQE IYFIETKKFLLIGKSNICVKVGEKSLTCKKIDLTTIVKPEAPFDLSVVYREGANDFVVTFNTSHLQKKYVKVLMHDVAYRQEKDENKWTH VNLSSTKLTLLQRKLQPAAMYEIKVRSIPDHYFKGFWSEWSPSYYFRTPEINNSSGEMDPILLTISILSFFSVALLVILACVLWKKRIKP |
| P16871-3 | MTILGTTFGMVFSLLQVVSGESGYAQNGDLEDAELDDYSFSCYSQLEVNGSQHSLTCAFEDPDVNITNLEFEICGALVEVKCLNFRKLQE IYFIETKKFLLIGKSNICVKVGEKSLTCKKIDLTTIVKPEAPFDLSVVYREGANDFVVTFNTSHLQKKYVKVLMHDVAYRQEKDENKWTH |
| P16871-4 | MTILGTTFGMVFSLLQVVSGESGYAQNGDLEDAELDDYSFSCYSQLEVNGSQHSLTCAFEDPDVNITNLEFEICGALVEVKCLNFRKLQE IYFIETKKFLLIGKSNICVKVGEKSLTCKKIDLTTIVKPEAPFDLSVVYREGANDFVVTFNTSHLQKKYVKVLMHDVAYRQEKDENKWTH |
Protein Functional Features |
| Main function of this protein. (from UniProt) |
| IL7R (go to UniProt):P16871 |
| Retention analysis result of protein across 39 protein features of UniProt such as six molecule processing features, 13 region features, four site features, six amino acid modification features, two natural variation features, five experimental info features, and 3 secondary structure features. Here, because of limited space for viewing, we only show the protein feature retention information belong to the 13 regional features. All retention annotation result can be downloaded at * Minus value of BPloci means that the break pointn is located before the CDS. |
| - Retained protein feature among the 13 regional features. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| P16871 | Topological domain | 21 | 239 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=237;End=459 |
| P16871 | Topological domain | 21 | 239 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=237;End=252 |
| P16871 | Transmembrane | 240 | 264 | Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=237;End=459 |
| P16871 | Transmembrane | 240 | 264 | Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=237;End=252 |
| P16871 | Transmembrane | 240 | 264 | Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=253;End=459 |
| P16871 | Topological domain | 265 | 459 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=293;End=459 |
| P16871 | Topological domain | 265 | 459 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=237;End=459 |
| P16871 | Topological domain | 265 | 459 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=253;End=459 |
| P16871 | Motif | 272 | 280 | Note=Box 1 motif | Type=Substitution;Start=237;End=459 |
| P16871 | Motif | 272 | 280 | Note=Box 1 motif | Type=Deletion;Start=253;End=459 |
Gene Isoform Structures and Expression Levels for IL7R |
| Gene structures of our canonical and alternative spliced genes of IL7R * Click on the image to open the UCSC genome browser with custom track showing this image in a new window. |
| Expression levels of gene isoforms across GTEx. |
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| Expression levels of gene isoforms across TCGA. |
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Protein Structures |
| PDB and CIF files of the predicted protein structures * Here we show the 3D structure of the proteins using Mol*. AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Model confidence is shown from the pLDDT values per residue. pLDDT corresponds to the model’s prediction of its score on the local Distance Difference Test. It is a measure of local accuracy (from AlphfaFold website). To color code individual residues, we transformed individual PDB files into CIF format. |
| 3D view using mol* of P16871-1 |
| 3D view using mol* of P16871-2 |
| 3D view using mol* of P16871-3 |
| 3D view using mol* of P16871-4 |
pLDDT Score Distribution |
| pLDDT score distribution of the predicted protein structures from AlphaFold2 * AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. |
| pLDDT distribution across the protein length of P16871-1 |
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| pLDDT distribution across the protein length of P16871-2 |
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| pLDDT distribution across the protein length of P16871-3 |
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| pLDDT distribution across the protein length of P16871-4 |
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Ramachandran Plot of Protein Structures |
| Ramachandran plot of the torsional angles - phi (φ)and psi (ψ) - of the residues (amino acids) contained in this protein peptide. |
| Ramachandran plot of P16871-1 |
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| Ramachandran plot of P16871-2 |
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| Ramachandran plot of P16871-3 |
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| Ramachandran plot of P16871-4 |
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Potential Active Site Information |
| The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite. |
| UniProt-id | Site score | Size | D score | Volume | Exposure | Enclosure | Contact | Phobic | Philic | Balance | Don/Acc | Residues |
| P16871-1 | 0.624 | 30 | 0.49 | 74.774 | 0.577 | 0.632 | 0.887 | 0.063 | 1.24 | 0.051 | 0.629 | 169,170,171,174,177,179,194,195,196,201
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| P16871-2 | 0.723 | 54 | 0.693 | 142.345 | 0.698 | 0.575 | 0.775 | 0.294 | 1.052 | 0.28 | 0.885 | 139,141,144,192,193,195,196,197,228,229,230,231,23 2,235 |
| P16871-3 | 0.573 | 22 | 0.407 | 59.339 | 0.593 | 0.642 | 0.878 | 0.269 | 1.285 | 0.21 | 2.612 | 30,31,33,34,35,38,114,116
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| P16871-4 | 0.587 | 28 | 0.489 | 56.252 | 0.582 | 0.597 | 0.77 | 0.351 | 1.125 | 0.312 | 2.31 | 30,31,33,35,38,114,116
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Protein Structure and Feature Comparision |
| Protein Structure Comparision Using Template Modeling Scores (TM-score). |
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| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Canonical validated structure (PDB)(green) |
| 3D view using mol* of P16871-1_P16871-1_3up1_A.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical validated structure (PDB)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of P16871-1_3up1_A_P16871-2.pdb |
| 3D view using mol* of P16871-1_3up1_A_P16871-3.pdb |
| 3D view using mol* of P16871-1_3up1_A_P16871-4.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of P16871-1_P16871-2.pdb |
| 3D view using mol* of P16871-1_P16871-3.pdb |
| 3D view using mol* of P16871-1_P16871-4.pdb |
| Protein Feature Comparison of the protein sequendary structures among the protiens. |
| ./stats/secondary_structure/figure/P16871-1_vs_P16871-2.png |
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| ./stats/secondary_structure/figure/P16871-1_vs_P16871-3.png |
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| ./stats/secondary_structure/figure/P16871-1_vs_P16871-4.png |
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| Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens. |
| ./stats/relative_asa/P16871-1_vs_P16871-2.png |
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| ./stats/relative_asa/P16871-1_vs_P16871-3.png |
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| ./stats/relative_asa/P16871-1_vs_P16871-4.png |
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Protein-Protein Interaction |
| Interactors from UniProt. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| Interactors from STRING. |
| Gene name | Interactors |
Related Drugs to IL7R |
| Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
Related Diseases to IL7R |
| Previous studies relating to the alternative splicing of IL7R and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
| IL7R | 20226540 | Alternative splicing of interleukin-7 (IL-7) and interleukin-7 receptor alpha (IL-7Ralpha) in peripheral blood from patients with multiple sclerosis (MS). | IL-7 and IL-7Ralpha (IL-7R) form a non-redundant ligand receptor system which plays a crucial role in human T cell immunity. Both IL-7 and IL-7R are multi-exonal genes and exhibit alternative splicing. We measured the relative distribution of IL-7 and IL-7R spliced mRNA from patients with MS and healthy individuals and observed extensive alternative splicing of both genes with marked differences in proportional transcript expression levels. We report here for the first time that the IL-7 transcript, lacking exon 4, and not the full length IL-7 represents the dominant IL-7 RNA transcript in human PBMCs and a novel IL-7R splice variant lacking exons 5, 6 and 7. | D009103 | Multiple Sclerosis |
| IL7R | 21129157 | Rheumatoid arthritis synovial fibroblasts produce a soluble form of the interleukin-7 receptor in response to pro-inflammatory cytokines. | We previously demonstrated that baseline synovial overexpression of the interleukin-7 receptor α-chain (IL-7R) is associated with poor response to tumour necrosis factor (TNF) blockade in rheumatoid arthritis (RA). We found that IL-7R gene expression is induced in fibroblast-like synovial cells (FLS) by the addition of TNF-α, IL-1β and combinations of TNF-α+ IL-1β or TNF-α+ IL-17, thereby suggesting that these cytokines play a role in the resistance to TNF blockade in RA. Because FLS and CD4 T cells also produce a soluble form of IL-7R (sIL-7R), resulting from an alternative splicing of the full-length transcript, we wondered whether expression of sIL-7R is similarly regulated by pro-inflammatory cytokines. We also investigated whether sIL-7R is detectable in the serum of RA patients and associated with response to TNF blockade. RA FLS were cultured in the presence of pro-inflammatory cytokines and sIL-7R concentrations were measured in culture supernatants. Similarly, sIL-7R titres were measured in sera obtained from healthy individuals, early untreated RA patients with active disease and disease-modifying anti-rheumatic drug (DMARD)-resistant RA patients prior to initiation of TNF-blockade. Baseline serum sIL-7R titres were correlated with validated clinical measurements of disease activity. We found that exposure of RA FLS to pro-inflammatory cytokines (TNF-α, IL-1β and combinations of TNF-α and IL-1β or TNF-α and IL-17) induces sIL-7R secretion. Activated CD4 T cells also produce sIL-7R. sIL-7R serum levels are higher in RA patients as compared to controls. In DMARD-resistant patients, high sIL-7R serum concentrations are strongly associated with poor response to TNF-blockade. In conclusion, sIL-7R is induced by pro-inflammatory cytokines in RA FLS. sIL-7R could qualify as a new biomarker of response to therapy in RA. | D001172 | Arthritis, Rheumatoid |
Clinically important variants in IL7R |
| (ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
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