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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P20594: Variant p.Gly959Ala

Atrial natriuretic peptide receptor 2
Gene: NPR2
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Variant information Variant position: help 959 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] 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 Glycine (G) to Alanine (A) at position 959 (G959A, p.Gly959Ala). 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 glycine (G) to small size and hydrophobic (A) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 0 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 In AMD1; no effect on subcellular location; changed glycosylation; no effect on C-type natriuretic peptide binding; decreased guanylate cyclase activity. Any additional useful information about the variant.


Sequence information Variant position: help 959 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 1047 The length of the canonical sequence.
Location on the sequence: help DAVSSFRIRHRPHDQLRLRI G VHTGPVCAGVVGLKMPRYCL 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                         DAVSSFRIRHRPHDQLRLRIGVHTGPVCAGVVGLKMPRYCL

Mouse                         DAVSSFRIRHRPHDQLRLRIGVHTGPVCAGVVGLKMPRYCL

Rat                           DAVSSFRIRHRPHDQLRLRIGVHTGPVCAGVVGLKMPRYCL

Bovine                        DAVSSFRIRHRPHDQLRLRIGVHTGPVCAGVVGLKMPRYCL
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 23 – 1047 Atrial natriuretic peptide receptor 2
Topological domain 479 – 1047 Cytoplasmic
Domain 861 – 991 Guanylate cyclase



Literature citations
Mutations in the transmembrane natriuretic peptide receptor NPR-B impair skeletal growth and cause acromesomelic dysplasia, type Maroteaux.
Bartels C.F.; Buekuelmez H.; Padayatti P.; Rhee D.K.; van Ravenswaaij-Arts C.; Pauli R.M.; Mundlos S.; Chitayat D.; Shih L.-Y.; Al-Gazali L.I.; Kant S.; Cole T.; Morton J.; Cormier-Daire V.; Faivre L.; Lees M.; Kirk J.; Mortier G.R.; Leroy J.; Zabel B.; Kim C.A.; Crow Y.; Braverman N.E.; van den Akker F.; Warman M.L.;
Am. J. Hum. Genet. 75:27-34(2004)
Cited for: FUNCTION; VARIANTS AMD1 THR-32; GLY-115; GLU-176; MET-297; CYS-338; THR-409; GLU-413; CYS-708; TRP-776; CYS-957 AND ALA-959; CHARACTERIZATION OF VARIANTS AMD1 GLY-115; MET-297 AND GLU-413; Catalytically active guanylyl cyclase b requires endoplasmic reticulum-mediated glycosylation, and mutations that inhibit this process cause dwarfism.
Dickey D.M.; Edmund A.B.; Otto N.M.; Chaffee T.S.; Robinson J.W.; Potter L.R.;
J. Biol. Chem. 291:11385-11393(2016)
Cited for: CHARACTERIZATION OF VARIANTS AMD1 PHE-658; CYS-708; TRP-776 AND ALA-959; FUNCTION; CATALYTIC ACTIVITY; SUBCELLULAR LOCATION; TOPOLOGY; GLYCOSYLATION; PHOSPHORYLATION; MUTAGENESIS OF ASN-24;
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.