Protein:IFNAR1 |
Protein Summary |
Gene summary |
| Gene name: IFNAR1 | ASpdb.0 ID: 3454 | Gene | Gene symbol | IFNAR1 | Gene ID | 3454 |
| Gene name | interferon alpha and beta receptor subunit 1 |
| Synonyms | AVP|IFN-alpha-REC|IFNAR|IFNBR|IFRC|IMD106 |
| Cytomap | 21q22.11 |
| Type of gene | protein-coding |
| Description | interferon alpha/beta receptor 1CRF2-1IFN-R-1IFN-alpha/beta receptor 1IFNalpha/beta receptor 1alpha-type antiviral proteinbeta-type antiviral proteincytokine receptor class-II member 1cytokine receptor family 2 member 1interferon (alpha, beta and |
| Modification date | 20240411 |
| UniProtAcc | P17181 |
Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | IFNAR1 | GO:0004905 | type I interferon receptor activity | 7665574|7813427|21854986 |
| Gene | IFNAR1 | GO:0005886 | plasma membrane | 14532120 |
| Gene | IFNAR1 | GO:0007259 | cell surface receptor signaling pathway via JAK-STAT | 7526154|7657660|7813427|8605876 |
| Gene | IFNAR1 | GO:0008269 | JAK pathway signal transduction adaptor activity | 8605876 |
| Gene | IFNAR1 | GO:0035458 | cellular response to interferon-beta | 7813427 |
| Gene | IFNAR1 | GO:0060337 | type I interferon-mediated signaling pathway | 7665574|21854986 |
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 |
| P17181-1 | P17181-1_3se4_A.pdb | 3SE4 | X-ray | 3.5 | A | 33 | 329 |
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 |
| P17181 | IFNAR1 | P17181-1 | P17181-2 | 557 | 434 | 428 | 434 | Substitution | KTKPGNT | NISLNSH | 428 | 434 |
| P17181 | IFNAR1 | P17181-1 | P17181-2 | 557 | 434 | 435 | 557 | Deletion | none | none | 434 | 434 |
| P17181 | IFNAR1 | P17181-1 | P17181-3 | 557 | 496 | 414 | 421 | Deletion | none | none | 413 | 413 |
| P17181 | IFNAR1 | P17181-1 | P17181-3 | 557 | 496 | 428 | 480 | Deletion | none | none | 419 | 419 |
| P17181 | IFNAR1 | P17181-1 | P17181-4 | 557 | 488 | 1 | 69 | Deletion | none | none | 0 | 0 |
Multiple sequence alignment of our canonical and alternatively spliced IFNAR1 |
Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of IFNAR1 |
| UniProt-id | ENSG | ENST | ENSP |
| P17181-1 | ENSG00000142166.15 | ENST00000270139.8 | ENSP00000270139.3 |
| P17181-1 | ENSG00000142166.15 | ENST00000703515.1 | ENSP00000515348.1 |
| P17181-1 | ENSG00000142166.15 | ENST00000703556.1 | ENSP00000515372.1 |
| P17181-4 | ENSG00000142166.15 | ENST00000652450.2 | ENSP00000498654.1 |
| P17181-4 | ENSG00000142166.15 | ENST00000700080.1 | ENSP00000514785.1 |
| UniProt-id | NM ID | NP ID |
| P17181-1 | NM_000629.2 | NP_000620.2 |
Amino acid sequences of our canonical and alternatively spliced IFNAR1 |
| accession_id | Protein sequence |
| P17181-1 | MMVVLLGATTLVLVAVAPWVLSAAAGGKNLKSPQKVEVDIIDDNFILRWNRSDESVGNVTFSFDYQKTGMDNWIKLSGCQNITSTKCNFS SLKLNVYEEIKLRIRAEKENTSSWYEVDSFTPFRKAQIGPPEVHLEAEDKAIVIHISPGTKDSVMWALDGLSFTYSLVIWKNSSGVEERI ENIYSRHKIYKLSPETTYCLKVKAALLTSWKIGVYSPVHCIKTTVENELPPPENIEVSVQNQNYVLKWDYTYANMTFQVQWLHAFLKRNP GNHLYKWKQIPDCENVKTTQCVFPQNVFQKGIYLLRVQASDGNNTSFWSEEIKFDTEIQAFLLPPVFNIRSLSDSFHIYIGAPKQSGNTP VIQDYPLIYEIIFWENTSNAERKIIEKKTDVTVPNLKPLTVYCVKARAHTMDEKLNKSSVFSDAVCEKTKPGNTSKIWLIVGICIALFAL PFVIYAAKVFLRCINYVFFPSLKPSSSIDEYFSEQPLKNLLLSTSEEQIEKCFIIENISTIATVEETNQTDEDHKKYSSQTSQDSGNYSN |
| P17181-2 | MMVVLLGATTLVLVAVAPWVLSAAAGGKNLKSPQKVEVDIIDDNFILRWNRSDESVGNVTFSFDYQKTGMDNWIKLSGCQNITSTKCNFS SLKLNVYEEIKLRIRAEKENTSSWYEVDSFTPFRKAQIGPPEVHLEAEDKAIVIHISPGTKDSVMWALDGLSFTYSLVIWKNSSGVEERI ENIYSRHKIYKLSPETTYCLKVKAALLTSWKIGVYSPVHCIKTTVENELPPPENIEVSVQNQNYVLKWDYTYANMTFQVQWLHAFLKRNP GNHLYKWKQIPDCENVKTTQCVFPQNVFQKGIYLLRVQASDGNNTSFWSEEIKFDTEIQAFLLPPVFNIRSLSDSFHIYIGAPKQSGNTP |
| P17181-3 | MMVVLLGATTLVLVAVAPWVLSAAAGGKNLKSPQKVEVDIIDDNFILRWNRSDESVGNVTFSFDYQKTGMDNWIKLSGCQNITSTKCNFS SLKLNVYEEIKLRIRAEKENTSSWYEVDSFTPFRKAQIGPPEVHLEAEDKAIVIHISPGTKDSVMWALDGLSFTYSLVIWKNSSGVEERI ENIYSRHKIYKLSPETTYCLKVKAALLTSWKIGVYSPVHCIKTTVENELPPPENIEVSVQNQNYVLKWDYTYANMTFQVQWLHAFLKRNP GNHLYKWKQIPDCENVKTTQCVFPQNVFQKGIYLLRVQASDGNNTSFWSEEIKFDTEIQAFLLPPVFNIRSLSDSFHIYIGAPKQSGNTP VIQDYPLIYEIIFWENTSNAERKIIEKKTDVTVPNLKPLTVYCVKARAHTMDESDAVCEYFSEQPLKNLLLSTSEEQIEKCFIIENISTI |
| P17181-4 | MDNWIKLSGCQNITSTKCNFSSLKLNVYEEIKLRIRAEKENTSSWYEVDSFTPFRKAQIGPPEVHLEAEDKAIVIHISPGTKDSVMWALD GLSFTYSLVIWKNSSGVEERIENIYSRHKIYKLSPETTYCLKVKAALLTSWKIGVYSPVHCIKTTVENELPPPENIEVSVQNQNYVLKWD YTYANMTFQVQWLHAFLKRNPGNHLYKWKQIPDCENVKTTQCVFPQNVFQKGIYLLRVQASDGNNTSFWSEEIKFDTEIQAFLLPPVFNI RSLSDSFHIYIGAPKQSGNTPVIQDYPLIYEIIFWENTSNAERKIIEKKTDVTVPNLKPLTVYCVKARAHTMDEKLNKSSVFSDAVCEKT KPGNTSKIWLIVGICIALFALPFVIYAAKVFLRCINYVFFPSLKPSSSIDEYFSEQPLKNLLLSTSEEQIEKCFIIENISTIATVEETNQ |
Protein Functional Features |
Main function of this protein. (from UniProt) |
| IFNAR1 (go to UniProt):P17181 |
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 |
| P17181 | Topological domain | 28 | 436 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=428;End=434 |
| P17181 | Topological domain | 28 | 436 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=435;End=557 |
| P17181 | Topological domain | 28 | 436 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=414;End=421 |
| P17181 | Topological domain | 28 | 436 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=428;End=480 |
| P17181 | Topological domain | 28 | 436 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=1;End=69 |
| P17181 | Transmembrane | 437 | 457 | Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=435;End=557 |
| P17181 | Transmembrane | 437 | 457 | Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=428;End=480 |
| P17181 | Topological domain | 458 | 557 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=435;End=557 |
| P17181 | Topological domain | 458 | 557 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=428;End=480 |
| P17181 | Domain | 32 | 126 | Note=Fibronectin type-III 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316 | Type=Deletion;Start=1;End=69 |
| P17181 | Domain | 331 | 432 | Note=Fibronectin type-III 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316 | Type=Substitution;Start=428;End=434 |
| P17181 | Domain | 331 | 432 | Note=Fibronectin type-III 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316 | Type=Deletion;Start=414;End=421 |
| P17181 | Domain | 331 | 432 | Note=Fibronectin type-III 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316 | Type=Deletion;Start=428;End=480 |
| P17181 | Region | 491 | 500 | Note=Important for interaction with TYK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24704786;Dbxref=PMID:24704786 | Type=Deletion;Start=435;End=557 |
| P17181 | Region | 516 | 557 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=435;End=557 |
| P17181 | Compositional bias | 540 | 557 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=435;End=557 |
Gene Isoform Structures and Expression Levels for IFNAR1 |
Gene structures of our canonical and alternative spliced genes of IFNAR1* 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. |
Expression levels of gene isoforms across TCGA. |
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 P17181-1 |
| 3D view using mol* of P17181-2 |
| 3D view using mol* of P17181-3 |
| 3D view using mol* of P17181-4 |
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. |
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 P17181-1 |
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| Ramachandran plot of P17181-2 |
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| Ramachandran plot of P17181-3 |
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| Ramachandran plot of P17181-4 |
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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 |
| P17181-1 | 0.998 | 106 | 1.035 | 406.455 | 0.677 | 0.662 | 0.807 | 0.34 | 0.927 | 0.367 | 0.853 | 239,240,241,242,244,295,296,298,300,326,327,328,33 0,331,332,333,353,355,361,362,363,364,365,367,408, 412,414,415,419 |
| P17181-2 | 0.902 | 75 | 0.903 | 124.852 | 0.516 | 0.679 | 0.928 | 0.557 | 0.977 | 0.571 | 0.576 | 138,139,140,141,188,190,191,230,231,232,233,234,23 5,317,318,319,320,322 |
| P17181-3 | 1.01 | 489 | 1.036 | 1602.153 | 0.567 | 0.697 | 0.914 | 0.493 | 0.987 | 0.499 | 1.139 | 138,139,140,141,188,190,191,226,227,229,230,231,23 2,233,234,235,236,237,238,239,240,241,242,244,245, 247,248,249,250,251,295,298,300,302,316,317,318,31 9,320,322,323,324,325,326,327,328,329,330,331,332, 333,334,335,337,352,353,354,355,357,359,360,361,36 2,363,364,365,367,372,405,406,407,408,409,410,411, 412,428,429,430,431,432,434,435,436,437,438 |
| P17181-4 | 1.041 | 313 | 1.102 | 675.024 | 0.55 | 0.675 | 0.835 | 0.92 | 0.745 | 1.235 | 0.652 | 2,3,4,5,6,7,10,11,12,13,15,16,18,19,20,21,23,25,29 ,31,32,33,34,35,36,37,38,45,48,51,53,56,57,58,59,6 0,61,62,79,80,81,84,85,86,87,94,96,135 |
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 P17181-1_P17181-1_3se4_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 P17181-1_3se4_A_P17181-2.pdb |
| 3D view using mol* of P17181-1_3se4_A_P17181-3.pdb |
| 3D view using mol* of P17181-1_3se4_A_P17181-4.pdb |
Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of P17181-1_P17181-2.pdb |
| 3D view using mol* of P17181-1_P17181-3.pdb |
| 3D view using mol* of P17181-1_P17181-4.pdb |
Protein Feature Comparison of the protein sequendary structures among the protiens. |
| ./stats/secondary_structure/figure/P17181-1_vs_P17181-2.png |
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| ./stats/secondary_structure/figure/P17181-1_vs_P17181-3.png |
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| ./stats/secondary_structure/figure/P17181-1_vs_P17181-4.png |
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Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens. |
| ./stats/relative_asa/P17181-1_vs_P17181-2.png |
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| ./stats/relative_asa/P17181-1_vs_P17181-3.png |
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| ./stats/relative_asa/P17181-1_vs_P17181-4.png |
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Protein-Protein Interaction |
Interactors from UniProt. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| P17181 | Region | 491 | 500 | Note=Important for interaction with TYK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24704786;Dbxref=PMID:24704786 | Type=Deletion;Start=435;End=557 |
Interactors from STRING. |
| Gene name | Interactors |
Related Drugs to IFNAR1 |
Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
| P17181 | IFNAR1 | DB00011 | Interferon alfa-n1 | approved, investigational | agonist |
| P17181 | IFNAR1 | DB00034 | Interferon alfa-2a | approved, investigational | |
| P17181 | IFNAR1 | DB00022 | Peginterferon alfa-2b | approved | agonist |
| P17181 | IFNAR1 | DB09122 | Peginterferon beta-1a | approved | activator, downregulator |
| P17181 | IFNAR1 | DB15119 | Ropeginterferon alfa-2b | approved, investigational | binder |
| P17181 | IFNAR1 | DB14999 | Human interferon beta | approved, investigational | binder |
| P17181 | IFNAR1 | DB05258 | Interferon alfa | investigational | |
| P17181 | IFNAR1 | DB00068 | Interferon beta-1b | approved | agonist |
| P17181 | IFNAR1 | DB00018 | Interferon alfa-n3 | approved, investigational | agonist |
| P17181 | IFNAR1 | DB00060 | Interferon beta-1a | approved, investigational | agonist |
| P17181 | IFNAR1 | DB00008 | Peginterferon alfa-2a | approved, investigational | agonist |
| P17181 | IFNAR1 | DB00105 | Interferon alfa-2b | approved | binder |
| P17181 | IFNAR1 | DB00069 | Interferon alfacon-1 | approved, investigational | binder |
| P17181 | IFNAR1 | DB11976 | Anifrolumab | approved, investigational | inhibitor |
| P17181 | IFNAR1 | DB05472 | Human interferon omega-1 | investigational |
Related Diseases to IFNAR1 |
Previous studies relating to the alternative splicing of IFNAR1 and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
| IFNAR1 | 7665574 | Cloning and expression of a long form of the beta subunit of the interferon alpha beta receptor that is required for signaling. | The interferon alpha beta receptor (IFN alpha R) or type I IFN-R is formed by a 110-kDa alpha subunit or IFNAR and by a beta subunit, which has short and long forms (molecular masses of 55 and 95-100 kDa, respectively). In this report, we demonstrate that the IFN alpha/beta R cDNA recently cloned corresponds to the 55-kDa or short form of the beta subunit, while the 95-100-kDa species reported here corresponds to a longer form of the IFN alpha/beta R cDNA that is probably produced by alternative splicing of the same gene. Stable transfection of the alpha subunit with either form of the beta subunit results in the expression of low and high affinity receptors, while expression of either form of the beta subunit alone only produces low affinity receptors. More important, only expression of the alpha and long form of the human beta subunits in mouse L-929 cells reconstitutes the activation of the Jak kinases and the Stat factors, as well as the antiviral response to human type I IFNs. | D009101 | Multiple Myeloma |
Clinically important variants in IFNAR1 |
(ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
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