Sequence information
Variant position: 401 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 427 The length of the canonical sequence.
Location on the sequence:
VGGASSLENTVDLHISNSHP
L SLTSDQYKAYLQDLVEGMDF
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: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human VGGASSLEN-TVDLHISNSHPL SLTSDQYKAYLQDLVEGMDF
Mouse EGGASSLK--TVDLHISNSQPI SLTSDQYKAYLQDLVEDMD
Pig DGGASSLEN-TVDLHISNSHPL SLTSDQYKACLRDLVEDMD
Bovine QGGASSLEN-TVDLHISNSDPL SLTPDQYMACLQDLAEDMD
Chicken RGGASSLNSGNVSLQLSDSFNL FELIEQYHMQTD-------
Sequence annotation in neighborhood: 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.
Type Positions Description
Chain
1 – 427
Interferon regulatory factor 3
Region
141 – 427
Mediates interaction with ZDHHC11
Modified residue
385 – 385
Phosphoserine
Modified residue
386 – 386
Phosphoserine; by TBK1
Modified residue
396 – 396
Phosphoserine; by IKKE and TBK1
Modified residue
398 – 398
Phosphoserine
Modified residue
404 – 404
Phosphothreonine
Alternative sequence
105 – 427
Missing. In isoform 5.
Alternative sequence
328 – 427
DLITFTEGSGRSPRYALWFCVGESWPQDQPWTKRLVMVKVVPTCLRALVEMARVGGASSLENTVDLHISNSHPLSLTSDQYKAYLQDLVEGMDFQGPGES -> GSWAPRSDYLHGRKRTLTTLCPLVLCGGVMAPGPAVDQEARDGQGCAHVPQGLGRNGPGRGCLLPGEYCGPAHFQQPPTLPHLRPVQGLPAGLGGGHGFPGPWGELSPRSSWCASNPPVPHHLNQ. In isoform 4.
Mutagenesis
385 – 385
S -> ADE. Complete loss of viral infection induced phosphorylation.
Mutagenesis
386 – 386
S -> ADE. Complete loss of viral infection induced phosphorylation.
Mutagenesis
386 – 386
S -> E. Phosphomimetic mutant; interacts with CREBBP; when associated with E-396.
Mutagenesis
396 – 405
SNSHPLSLTS -> ANAHPLALAA. Complete loss of viral infection induced phosphorylation.
Mutagenesis
396 – 405
SNSHPLSLTS -> DNDHPLDLDD. Acts as a constitutively activated IRF3.
Mutagenesis
396 – 396
S -> E. Phosphomimetic mutant; interacts with CREBBP; when associated with E-386.
Beta strand
401 – 404
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 GLU-49 DEL; 145-GLY--GLU-200 DEL; LYS-146; GLN-227; GLN-285 AND VAL-401; CHARACTERIZATION OF VARIANTS GLU-49 DEL; 145-GLY--GLU-200 DEL; LYS-146; GLN-227; GLN-285 AND VAL-401; 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.