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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P63092: Variant p.Arg201Ser

Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
Gene: GNAS
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Variant information Variant position: help 201 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 Arginine (R) to Serine (S) at position 201 (R201S, p.Arg201Ser). 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 large size and basic (R) to small size and polar (S) 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 In AIMAH1; also found in pituitary tumor and polyostotic fibrous dysplasia. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 201 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 394 The length of the canonical sequence.
Location on the sequence: help KIDVIKQADYVPSDQDLLRC R VLTSGIFETKFQVDKVNFHM 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                         KIDVIKQADYVPSDQDLLRCRVLTSGIFETKFQVDKVNFHM

Mouse                         KIDVIKQADYVPSDQDLLRCRVLTSGIFETKFQVDKVNFHM

Rat                           KIDVIKQADYVPSDQDLLRCRVLTSGIFETKFQVDKVNFHM

Bovine                        KIDVIKQDDYVPSDQDLLRCRVLTSGIFETKFQVDKVNFHM
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 2 – 394 Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
Domain 39 – 394 G-alpha
Region 196 – 204 G2 motif
Binding site 197 – 204
Binding site 204 – 204
Modified residue 201 – 201 ADP-ribosylarginine; by cholera toxin



Literature citations
Characteristics of gsp-positive growth hormone-secreting pituitary tumors in Korean acromegalic patients.
Yang I.; Park S.; Ryu M.; Woo J.; Kim S.; Kim J.; Kim Y.; Choi Y.;
Eur. J. Endocrinol. 134:720-726(1996)
Cited for: VARIANT PITUITARY TUMOR SER-201; Polymerase chain reaction-based technique for the selective enrichment and analysis of mosaic arg201 mutations in G alpha s from patients with fibrous dysplasia of bone.
Candeliere G.A.; Roughley P.J.; Glorieux F.H.;
Bone 21:201-206(1997)
Cited for: VARIANT POLYOSTOTIC FIBROUS DYSPLASIA SER-201; Cushing's syndrome secondary to adrenocorticotropin-independent macronodular adrenocortical hyperplasia due to activating mutations of GNAS1 gene.
Fragoso M.C.B.V.; Domenice S.; Latronico A.C.; Martin R.M.; Pereira M.A.A.; Zerbini M.C.N.; Lucon A.M.; Mendonca B.B.;
J. Clin. Endocrinol. Metab. 88:2147-2151(2003)
Cited for: VARIANTS AIMAH1 HIS-201 AND SER-201;
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.