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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9BYF1: Variant p.Lys26Arg

Angiotensin-converting enzyme 2
Gene: ACE2
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Variant information Variant position: help 26 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 Lysine (K) to Arginine (R) at position 26 (K26R, p.Lys26Arg). 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 Similar physico-chemical property. Both residues are large size and basic. The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 2 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

Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 26 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 805 The length of the canonical sequence.
Location on the sequence: help WLLLSLVAVTAAQSTIEEQA K TFLDKFNHEAEDLFYQSSLA 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                         WLLLSLVAVTAAQSTIEEQAKTFLDKFNHEAEDLFYQSSLA

Mouse                         WLLLSLVAVTTAQSLTEENAKTFLNNFNQEAEDLSYQSSLA

Rat                           WLLLSLVAVATAQSLIEEKAESFLNKFNQEAEDLSYQSSLA

Bovine                        WLLLSLVAVTAAQSTTEEQAKTFLEKFNHEAEDLSYQSSLA

Cat                           WLLLSFAALTAAQSTTEELAKTFLEKFNHEAEELSYQSSLA

Baker's yeast                 WYINPSGFAKDTQDEE-------YVQHHDNVNPTIPPP---

Fission yeast                 ---LSYLSSSSQKS---------FESFRQEESPACNHS---

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 18 – 805 Angiotensin-converting enzyme 2
Chain 18 – 708 Processed angiotensin-converting enzyme 2
Topological domain 18 – 740 Extracellular
Domain 19 – 607 Peptidase M2
Alternative sequence 1 – 356 MSSSSWLLLSLVAVTAAQSTIEEQAKTFLDKFNHEAEDLFYQSSLASWNYNTNITEENVQNMNNAGDKWSAFLKEQSTLAQMYPLQEIQNLTVKLQLQALQQNGSSVLSEDKSKRLNTILNTMSTIYSTGKVCNPDNPQECLLLEPGLNEIMANSLDYNERLWAWESWRSEVGKQLRPLYEEYVVLKNEMARANHYEDYGDYWRGDYEVNGVDGYDYSRGQLIEDVEHTFEEIKPLYEHLHAYVRAKLMNAYPSYISPIGCLPAHLLGDMWGRFWTNLYSLTVPFGQKPNIDVTDAMVDQAWDAQRIFKEAEKFFVSVGLPNMTQGFWENSMLTDPGNVQKAVCHPTAWDLGKGDF -> MREAGWDKGG. In isoform 2.
Mutagenesis 19 – 19 S -> P. Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein.
Mutagenesis 24 – 26 QAK -> KAE. Slightly inhibits interaction with SARS-CoV spike glycoprotein.
Mutagenesis 24 – 24 Q -> T. Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein.
Mutagenesis 25 – 25 A -> V. Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein.
Mutagenesis 27 – 27 T -> Y. Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. In sACE2.v2.2; increases interaction with RBD domain of SARS-CoV-2 spike protein; when associated with Y-330 and L-386.
Mutagenesis 29 – 29 L -> F. Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein.
Mutagenesis 31 – 31 K -> D. Abolishes interaction with SARS-CoV spike glycoprotein.
Mutagenesis 31 – 31 K -> Y. Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein.
Mutagenesis 33 – 33 N -> D. Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein.
Mutagenesis 34 – 34 H -> A. Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein.
Mutagenesis 37 – 37 E -> A. No effect on interaction with SARS-CoV spike glycoprotein.
Mutagenesis 38 – 38 D -> A. No effect on interaction with SARS-CoV spike glycoprotein.
Mutagenesis 39 – 39 L -> R. Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein.
Mutagenesis 40 – 40 F -> D. Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein.
Mutagenesis 41 – 41 Y -> A. Strongly inhibits interaction with SARS-CoV spike glycoprotein.
Mutagenesis 41 – 41 Y -> R. Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein.
Mutagenesis 42 – 42 Q -> L. Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein.
Helix 23 – 52



Literature citations
Submission
SeattleSNPs variation discovery resource;
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANT ARG-26; Genetic variability of human angiotensin-converting enzyme 2 (hACE2) among various ethnic populations.
Li Q.; Cao Z.; Rahman P.;
Mol. Genet. Genomic Med. 0:0-0(2020)
Cited for: VARIANTS ARG-26; VAL-468; SER-638 AND ASP-720;
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.