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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P17181: Variant p.Glu515Lys

Interferon alpha/beta receptor 1
Gene: IFNAR1
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Variant information Variant position: help 515 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LB/B The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance

Residue change: help From Glutamate (E) to Lysine (K) at position 515 (E515K, p.Glu515Lys). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties: help Change from medium size and acidic (E) to large size and basic (K) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 1 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page

Variant description: help No effect on activation of STAT1 upon IFNA2 or IFNG binding. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 515 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 557 The length of the canonical sequence.
Location on the sequence: help SEEQIEKCFIIENISTIATV E ETNQTDEDHKKYSSQTSQDS The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: help The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human                         SEEQIEKCFIIENISTIATVEETNQTDEDHKKYSSQTSQDS

Mouse                         AEEHTERCFIIENTDTVA-VEVKHAPEEDLRKYSSQTSQDS

Pig                           SEEQTEICFIVENTNTITTIEETDQIDDNHSRCSSQTNRDS

Bovine                        SEEQTERCFIIENASIITEIEETDEIDEVHKKYSSQTSQDS

Sheep                         SEEQTERCFIIENASIITEIEETNEVAEVHEEYNSQASQDS

Sequence annotation in neighborhood: help The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
  • Type: the type of sequence feature.
  • Positions: endpoints of the sequence feature.
  • Description: contains additional information about the feature.
TypePositionsDescription
Chain 28 – 557 Interferon alpha/beta receptor 1
Topological domain 458 – 557 Cytoplasmic
Modified residue 495 – 495 Phosphoserine
Modified residue 535 – 535 Phosphoserine
Cross 501 – 501 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross 525 – 525 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross 526 – 526 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Alternative sequence 435 – 557 Missing. In isoform 2.
Mutagenesis 500 – 500 E -> A. Impairs interaction with TYK2.
Mutagenesis 501 – 501 K -> R. Mildly reduces ubiquitination. Nearly abolishes ubiquitination and subsequent degradation; when associated with 525-R-R-526.
Mutagenesis 535 – 535 S -> A. Abolishes interaction with FBXW11 and decreases ubiquitination.
Mutagenesis 535 – 535 S -> A. Abolishes phosphorylation at this site and interaction with SHMT2.



Literature citations
Inborn errors of type I IFN immunity in patients with life-threatening COVID-19.
Zhang Q.; Bastard P.; Liu Z.; Le Pen J.; Moncada-Velez M.; Chen J.; Ogishi M.; Sabli I.K.D.; Hodeib S.; Korol C.; Rosain J.; Bilguvar K.; Ye J.; Bolze A.; Bigio B.; Yang R.; Arias A.A.; Zhou Q.; Zhang Y.; Onodi F.; Korniotis S.; Karpf L.; Philippot Q.; Chbihi M.; Bonnet-Madin L.; Dorgham K.; Smith N.; Schneider W.M.; Razooky B.S.; Hoffmann H.H.; Michailidis E.; Moens L.; Han J.E.; Lorenzo L.; Bizien L.; Meade P.; Neehus A.L.; Ugurbil A.C.; Corneau A.; Kerner G.; Zhang P.; Rapaport F.; Seeleuthner Y.; Manry J.; Masson C.; Schmitt Y.; Schlueter A.; Le Voyer T.; Khan T.; Li J.; Fellay J.; Roussel L.; Shahrooei M.; Alosaimi M.F.; Mansouri D.; Al-Saud H.; Al-Mulla F.; Almourfi F.; Al-Muhsen S.Z.; Alsohime F.; Al Turki S.; Hasanato R.; van de Beek D.; Biondi A.; Bettini L.R.; D'Angio' M.; Bonfanti P.; Imberti L.; Sottini A.; Paghera S.; Quiros-Roldan E.; Rossi C.; Oler A.J.; Tompkins M.F.; Alba C.; Vandernoot I.; Goffard J.C.; Smits G.; Migeotte I.; Haerynck F.; Soler-Palacin P.; Martin-Nalda A.; Colobran R.; Morange P.E.; Keles S.; Coelkesen F.; Ozcelik T.; Yasar K.K.; Senoglu S.; Karabela S.N.; Rodriguez-Gallego C.; Novelli G.; Hraiech S.; Tandjaoui-Lambiotte Y.; Duval X.; Laouenan C.; Snow A.L.; Dalgard C.L.; Milner J.D.; Vinh D.C.; Mogensen T.H.; Marr N.; Spaan A.N.; Boisson B.; Boisson-Dupuis S.; Bustamante J.; Puel A.; Ciancanelli M.J.; Meyts I.; Maniatis T.; Soumelis V.; Amara A.; Nussenzweig M.; Garcia-Sastre A.; Krammer F.; Pujol A.; Duffy D.; Lifton R.P.; Zhang S.Y.; Gorochov G.; Beziat V.; Jouanguy E.; Sancho-Shimizu V.; Rice C.M.; Abel L.; Notarangelo L.D.; Cobat A.; Su H.C.; Casanova J.L.;
Science 370:0-0(2020)
Cited for: VARIANTS VAL-24; ARG-57; CYS-73; HIS-80; ALA-83; SER-88; MET-169; VAL-183; CYS-306; ILE-307; PRO-335 DEL; LEU-386; ARG-422; THR-424 AND LYS-515; CHARACTERIZATION OF VARIANTS VAL-24; ARG-57; CYS-73; HIS-80; ALA-83; SER-88; MET-169; VAL-183; CYS-306; ILE-307; PRO-335 DEL; LEU-386; ARG-422; THR-424 AND LYS-515; FUNCTION;
Disclaimer: Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.