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:
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 KIDVIKQADYVPSDQDLLRC RVLTSGIFETKFQVDKVNFHM
Mouse KIDVIKQADYVPSDQDLLRC RVLTSGIFETKFQVDKVNFHM
Rat KIDVIKQADYVPSDQDLLRC RVLTSGIFETKFQVDKVNFHM
Bovine KIDVIKQDDYVPSDQDLLRC RVLTSGIFETKFQVDKVNFHM
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
2 – 394 Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
39 – 394 G-alpha
197 – 204 GTP
196 – 204 G2 motif
204 – 204 Magnesium
201 – 201 ADP-ribosylarginine; by cholera toxin
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.;
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;
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.