Sequence information
Variant position: 201 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 394 The length of the canonical sequence.
Location on the sequence:
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: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human KIDVIKQADYVPSDQDLLRCR VLTSGIFETKFQVDKVNFHM
Mouse KIDVIKQADYVPSDQDLLRCR VLTSGIFETKFQVDKVNFHM
Rat KIDVIKQADYVPSDQDLLRCR VLTSGIFETKFQVDKVNFHM
Bovine KIDVIKQDDYVPSDQDLLRCR VLTSGIFETKFQVDKVNFHM
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
2 – 394
Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
Domain
39 – 394
G-alpha
Nucleotide binding
197 – 204
GTP
Region
196 – 204
G2 motif
Metal binding
204 – 204
Magnesium
Modified residue
201 – 201
ADP-ribosylarginine; by cholera toxin
Literature citations
Identification of a mutation in the gene encoding the alpha subunit of the stimulatory G protein of adenylyl cyclase in McCune-Albright syndrome.
Schwindinger W.F.; Francomano C.A.; Levine M.A.;
Proc. Natl. Acad. Sci. U.S.A. 89:5152-5156(1992)
Cited for: VARIANT MAS HIS-201;
Activating mutations of the stimulatory G protein in the McCune-Albright syndrome.
Weinstein L.S.; Shenker A.; Gejman P.V.; Merino M.J.; Friedman E.; Spiegel A.M.;
N. Engl. J. Med. 325:1688-1695(1991)
Cited for: VARIANTS MAS CYS-201 AND HIS-201;
GTPase inhibiting mutations activate the alpha chain of Gs and stimulate adenylyl cyclase in human pituitary tumours.
Landis C.A.; Masters S.B.; Spada A.; Pace A.M.; Bourne H.R.; Vallar L.;
Nature 340:692-696(1989)
Cited for: VARIANTS SOMATOTROPHINOMA CYS-201; HIS-201 AND ARG-227;
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.