ASpdb: an integrative knowledgebase of human protein isoforms from experimental and AI-predicted structures
ASpdb Logo

Home

Download

Statistics

Examples

Help

Contact

Terms of Use

Center for Computational Systems Medicine
leaf

Protein Summary

leaf

AS Summary

leaf

Protein Functional Features

leaf

Gene Isoform Structures and Expression Levels

leaf

Protein Structures

leaf

pLDDT Score Distribution

leaf

Ramachandran Plot of Protein Structures

leaf

Potential Active Site Information

leaf

Protein Structure and Feature Comparision

leaf

Protein-Protein Interaction

leaf

Related Drugs

leaf

Related Diseases

leaf

Clinically Important Variants

Protein:IFNAR1

Protein Summary

check button Gene summary
Gene name: IFNAR1
ASpdb.0 ID: 3454
Gene
Gene symbol

IFNAR1

Gene ID

3454

Gene nameinterferon alpha and beta receptor subunit 1
SynonymsAVP|IFN-alpha-REC|IFNAR|IFNBR|IFRC|IMD106
Cytomap

21q22.11

Type of geneprotein-coding
Descriptioninterferon 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 date20240411
UniProtAcc

P17181


check button Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez
PartnerGeneGO IDGO termPubMed ID
GeneIFNAR1

GO:0004905

type I interferon receptor activity

7665574|7813427|21854986

GeneIFNAR1

GO:0005886

plasma membrane

14532120

GeneIFNAR1

GO:0007259

cell surface receptor signaling pathway via JAK-STAT

7526154|7657660|7813427|8605876

GeneIFNAR1

GO:0008269

JAK pathway signal transduction adaptor activity

8605876

GeneIFNAR1

GO:0035458

cellular response to interferon-beta

7813427

GeneIFNAR1

GO:0060337

type I interferon-mediated signaling pathway

7665574|21854986



AS Summary

check button Information of the canonical protein with experimentally identified structure from PDB (2023).
UniProt AccFile namePDB IDMethodResolutionChainStartEnd
P17181-1P17181-1_3se4_A.pdb3SE4X-ray3.5A33329

check button ASpdb's canonical and alternatively spliced isoform information.
accession_idgene_namecanonical_idalternative_idcanonical_lengthalternative_lengthcanonical_startcanonical_endtypeoriginalSEQvariationSEQalternative_startalternative_end
P17181IFNAR1P17181-1P17181-2557434428434SubstitutionKTKPGNTNISLNSH428434
P17181IFNAR1P17181-1P17181-2557434435557Deletionnonenone434434
P17181IFNAR1P17181-1P17181-3557496414421Deletionnonenone413413
P17181IFNAR1P17181-1P17181-3557496428480Deletionnonenone419419
P17181IFNAR1P17181-1P17181-4557488169Deletionnonenone00

check buttonMultiple sequence alignment of our canonical and alternatively spliced IFNAR1

check button Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of IFNAR1
UniProt-idENSGENSTENSP
P17181-1ENSG00000142166.15ENST00000270139.8ENSP00000270139.3
P17181-1ENSG00000142166.15ENST00000703515.1ENSP00000515348.1
P17181-1ENSG00000142166.15ENST00000703556.1ENSP00000515372.1
P17181-4ENSG00000142166.15ENST00000652450.2ENSP00000498654.1
P17181-4ENSG00000142166.15ENST00000700080.1ENSP00000514785.1

UniProt-idNM IDNP ID
P17181-1NM_000629.2NP_000620.2

check buttonAmino acid sequences of our canonical and alternatively spliced IFNAR1
accession_idProtein sequence
P17181-1MMVVLLGATTLVLVAVAPWVLSAAAGGKNLKSPQKVEVDIIDDNFILRWNRSDESVGNVTFSFDYQKTGMDNWIKLSGCQNITSTKCNFS
SLKLNVYEEIKLRIRAEKENTSSWYEVDSFTPFRKAQIGPPEVHLEAEDKAIVIHISPGTKDSVMWALDGLSFTYSLVIWKNSSGVEERI
ENIYSRHKIYKLSPETTYCLKVKAALLTSWKIGVYSPVHCIKTTVENELPPPENIEVSVQNQNYVLKWDYTYANMTFQVQWLHAFLKRNP
GNHLYKWKQIPDCENVKTTQCVFPQNVFQKGIYLLRVQASDGNNTSFWSEEIKFDTEIQAFLLPPVFNIRSLSDSFHIYIGAPKQSGNTP
VIQDYPLIYEIIFWENTSNAERKIIEKKTDVTVPNLKPLTVYCVKARAHTMDEKLNKSSVFSDAVCEKTKPGNTSKIWLIVGICIALFAL
PFVIYAAKVFLRCINYVFFPSLKPSSSIDEYFSEQPLKNLLLSTSEEQIEKCFIIENISTIATVEETNQTDEDHKKYSSQTSQDSGNYSN
P17181-2MMVVLLGATTLVLVAVAPWVLSAAAGGKNLKSPQKVEVDIIDDNFILRWNRSDESVGNVTFSFDYQKTGMDNWIKLSGCQNITSTKCNFS
SLKLNVYEEIKLRIRAEKENTSSWYEVDSFTPFRKAQIGPPEVHLEAEDKAIVIHISPGTKDSVMWALDGLSFTYSLVIWKNSSGVEERI
ENIYSRHKIYKLSPETTYCLKVKAALLTSWKIGVYSPVHCIKTTVENELPPPENIEVSVQNQNYVLKWDYTYANMTFQVQWLHAFLKRNP
GNHLYKWKQIPDCENVKTTQCVFPQNVFQKGIYLLRVQASDGNNTSFWSEEIKFDTEIQAFLLPPVFNIRSLSDSFHIYIGAPKQSGNTP
P17181-3MMVVLLGATTLVLVAVAPWVLSAAAGGKNLKSPQKVEVDIIDDNFILRWNRSDESVGNVTFSFDYQKTGMDNWIKLSGCQNITSTKCNFS
SLKLNVYEEIKLRIRAEKENTSSWYEVDSFTPFRKAQIGPPEVHLEAEDKAIVIHISPGTKDSVMWALDGLSFTYSLVIWKNSSGVEERI
ENIYSRHKIYKLSPETTYCLKVKAALLTSWKIGVYSPVHCIKTTVENELPPPENIEVSVQNQNYVLKWDYTYANMTFQVQWLHAFLKRNP
GNHLYKWKQIPDCENVKTTQCVFPQNVFQKGIYLLRVQASDGNNTSFWSEEIKFDTEIQAFLLPPVFNIRSLSDSFHIYIGAPKQSGNTP
VIQDYPLIYEIIFWENTSNAERKIIEKKTDVTVPNLKPLTVYCVKARAHTMDESDAVCEYFSEQPLKNLLLSTSEEQIEKCFIIENISTI
P17181-4MDNWIKLSGCQNITSTKCNFSSLKLNVYEEIKLRIRAEKENTSSWYEVDSFTPFRKAQIGPPEVHLEAEDKAIVIHISPGTKDSVMWALD
GLSFTYSLVIWKNSSGVEERIENIYSRHKIYKLSPETTYCLKVKAALLTSWKIGVYSPVHCIKTTVENELPPPENIEVSVQNQNYVLKWD
YTYANMTFQVQWLHAFLKRNPGNHLYKWKQIPDCENVKTTQCVFPQNVFQKGIYLLRVQASDGNNTSFWSEEIKFDTEIQAFLLPPVFNI
RSLSDSFHIYIGAPKQSGNTPVIQDYPLIYEIIFWENTSNAERKIIEKKTDVTVPNLKPLTVYCVKARAHTMDEKLNKSSVFSDAVCEKT
KPGNTSKIWLIVGICIALFALPFVIYAAKVFLRCINYVFFPSLKPSSSIDEYFSEQPLKNLLLSTSEEQIEKCFIIENISTIATVEETNQ

Protein Functional Features

check buttonMain function of this protein. (from UniProt)
IFNAR1 (go to UniProt):P17181

check buttonRetention 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

download page

* Minus value of BPloci means that the break pointn is located before the CDS.
- Retained protein feature among the 13 regional features.
Accession_idSubsectionStartEndFuncitonal featureSplicing information
P17181Topological domain28436Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Substitution;Start=428;End=434
P17181Topological domain28436Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=435;End=557
P17181Topological domain28436Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=414;End=421
P17181Topological domain28436Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=428;End=480
P17181Topological domain28436Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=1;End=69
P17181Transmembrane437457Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=435;End=557
P17181Transmembrane437457Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=428;End=480
P17181Topological domain458557Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=435;End=557
P17181Topological domain458557Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=428;End=480
P17181Domain32126Note=Fibronectin type-III 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316Type=Deletion;Start=1;End=69
P17181Domain331432Note=Fibronectin type-III 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316Type=Substitution;Start=428;End=434
P17181Domain331432Note=Fibronectin type-III 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316Type=Deletion;Start=414;End=421
P17181Domain331432Note=Fibronectin type-III 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316Type=Deletion;Start=428;End=480
P17181Region491500Note=Important for interaction with TYK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24704786;Dbxref=PMID:24704786Type=Deletion;Start=435;End=557
P17181Region516557Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=435;End=557
P17181Compositional bias540557Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=435;End=557


Gene Isoform Structures and Expression Levels for IFNAR1

check buttonGene 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.
gene isoform structure of IFNAR1

check button Expression levels of gene isoforms across GTEx.
gtex expression

check button Expression levels of gene isoforms across TCGA.
tcga expression


Protein Structures

check button 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

check button 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 P17181-1
all structure
pLDDT distribution across the protein length of P17181-2
all structure
pLDDT distribution across the protein length of P17181-3
all structure
pLDDT distribution across the protein length of P17181-4
all structure


Ramachandran Plot of Protein Structures


check button 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
all structure
Ramachandran plot of P17181-2
all structure
Ramachandran plot of P17181-3
all structure
Ramachandran plot of P17181-4
all structure

Potential Active Site Information


check button The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite.
UniProt-idSite scoreSizeD scoreVolumeExposureEnclosureContactPhobicPhilicBalanceDon/AccResidues
P17181-10.9981061.035406.4550.6770.6620.8070.340.9270.3670.853239,240,241,242,244,295,296,298,300,326,327,328,33
0,331,332,333,353,355,361,362,363,364,365,367,408,
412,414,415,419
P17181-20.902750.903124.8520.5160.6790.9280.5570.9770.5710.576138,139,140,141,188,190,191,230,231,232,233,234,23
5,317,318,319,320,322
P17181-31.014891.0361602.1530.5670.6970.9140.4930.9870.4991.139138,139,140,141,188,190,191,226,227,229,230,231,23
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
P17181-41.0413131.102675.0240.550.6750.8350.920.7451.2350.6522,3,4,5,6,7,10,11,12,13,15,16,18,19,20,21,23,25,29
,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


check button Protein Structure Comparision Using Template Modeling Scores (TM-score).
all structure

check button 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

check button 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

check button 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

check button Protein Feature Comparison of the protein sequendary structures among the protiens.
./stats/secondary_structure/figure/P17181-1_vs_P17181-2.png
all structure<
./stats/secondary_structure/figure/P17181-1_vs_P17181-3.png
all structure<
./stats/secondary_structure/figure/P17181-1_vs_P17181-4.png
all structure<

check button Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens.
./stats/relative_asa/P17181-1_vs_P17181-2.png
all structure<
./stats/relative_asa/P17181-1_vs_P17181-3.png
all structure<
./stats/relative_asa/P17181-1_vs_P17181-4.png
all structure<


Protein-Protein Interaction


check button Interactors from UniProt.
Accession_idSubsectionStartEndFuncitonal featureSplicing information
P17181Region491500Note=Important for interaction with TYK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24704786;Dbxref=PMID:24704786Type=Deletion;Start=435;End=557


check button Interactors from STRING.
Gene nameInteractors


Related Drugs to IFNAR1


check button Drugs targeting this gene/protein.
(DrugBank)
UniProt accessionGene nameDrugBank IDDrug nameDrug groupActions
P17181IFNAR1DB00011Interferon alfa-n1approved, investigationalagonist
P17181IFNAR1DB00034Interferon alfa-2aapproved, investigational
P17181IFNAR1DB00022Peginterferon alfa-2bapprovedagonist
P17181IFNAR1DB09122Peginterferon beta-1aapprovedactivator, downregulator
P17181IFNAR1DB15119Ropeginterferon alfa-2bapproved, investigationalbinder
P17181IFNAR1DB14999Human interferon betaapproved, investigationalbinder
P17181IFNAR1DB05258Interferon alfainvestigational
P17181IFNAR1DB00068Interferon beta-1bapprovedagonist
P17181IFNAR1DB00018Interferon alfa-n3approved, investigationalagonist
P17181IFNAR1DB00060Interferon beta-1aapproved, investigationalagonist
P17181IFNAR1DB00008Peginterferon alfa-2aapproved, investigationalagonist
P17181IFNAR1DB00105Interferon alfa-2bapprovedbinder
P17181IFNAR1DB00069Interferon alfacon-1approved, investigationalbinder
P17181IFNAR1DB11976Anifrolumabapproved, investigationalinhibitor
P17181IFNAR1DB05472Human interferon omega-1investigational

Related Diseases to IFNAR1


check button Previous studies relating to the alternative splicing of IFNAR1 and disease information from the MeSH term (PubMed)
GenePMIDTitleAbstractMeSH IDMeSH term
IFNAR17665574Cloning 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.D009101Multiple Myeloma


Clinically important variants in IFNAR1


check button (ClinVar, 04/20/2024)
accession_iduniprot_idgene_nameTypeVariantClinical_significance