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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9UGI9: Variant p.Arg307Cys

5'-AMP-activated protein kinase subunit gamma-3
Gene: PRKAG3
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Variant information Variant position: help 307 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 Arginine (R) to Cysteine (C) at position 307 (R307C, p.Arg307Cys). 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 medium size and polar (C) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 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

Polymorphism: help Genetic variation in PRKAG3 defines the skeletal muscle glycogen content and metabolism quantitative trait locus (SMGMQTL) [MIM:619030]. Muscle fibers from carriers of variant Trp-225 have approximately 90% more muscle glycogen content than controls and decreased levels of intramuscular triglyceride. Additional information on the polymorphism described.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 307 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 489 The length of the canonical sequence.
Location on the sequence: help ISPNDSLFEAVYTLIKNRIH R LPVLDPVSGNVLHILTHKRL 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                         ISPNDSLFEAVYTLIKNRIHRLPVLDPVSGNVLHILTHKRL

Mouse                         ISPNDSLFEAVYALIKNRIHRLPVLDPVSGTVLYILTHKRL

Pig                           ISPNDSLFEAVYALIKNRIHRLPVLDPVSGAVLHILTHKRL

Bovine                        ISPSDSLFEAVYTLIKNRIHRLPVLDPVSGAVLHILTHKRL

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 1 – 489 5'-AMP-activated protein kinase subunit gamma-3
Domain 280 – 340 CBS 2
Motif 293 – 314 AMPK pseudosubstrate
Binding site 306 – 307
Binding site 306 – 307
Binding site 306 – 307
Binding site 306 – 306
Binding site 307 – 307
Binding site 325 – 325
Binding site 325 – 325
Binding site 325 – 325



Literature citations
Gain-of-function R225W mutation in human AMPKgamma(3) causing increased glycogen and decreased triglyceride in skeletal muscle.
Costford S.R.; Kavaslar N.; Ahituv N.; Chaudhry S.N.; Schackwitz W.S.; Dent R.; Pennacchio L.A.; McPherson R.; Harper M.E.;
PLoS ONE 2:E903-E903(2007)
Cited for: VARIANTS ALA-71; GLN-76; GLY-103; VAL-113; VAL-153; PRO-161; SER-171; SER-180; THR-197; GLN-211; GLN-225; TRP-225; ARG-260; THR-269; CYS-307; GLN-340; TRP-340; MET-446; VAL-482 AND ASN-485; INVOLVEMENT IN SMGMQTL; FUNCTION; CHARACTERIZATION OF VARIANT TRP-225;
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.