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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P63096: Variant p.Gln52Pro

Guanine nucleotide-binding protein G(i) subunit alpha-1
Gene: GNAI1
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Variant information Variant position: help 52 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 Glutamine (Q) to Proline (P) at position 52 (Q52P, p.Gln52Pro). 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 medium size and polar (Q) to medium size and hydrophobic (P) 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 NEDHISB; loss of GTP binding. Any additional useful information about the variant.


Sequence information Variant position: help 52 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 354 The length of the canonical sequence.
Location on the sequence: help REVKLLLLGAGESGKSTIVK Q MKIIHEAGYSEEECKQYKAV 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                         REVKLLLLGAGESGKSTIVKQMKIIHEAGYSEEECKQYKAV

Mouse                         REVKLLLLGAGESGKSTIVKQMKIIHEAGYSEEECKQYKAV

Rat                           REVKLLLLGAGESGKSTIVKQMKIIHEAGYSEEECKQYKAV

Bovine                        REVKLLLLGAGESGKSTIVKQMKIIHEAGYSEEECKQYKAV

Chicken                       REVKLLLLGAGESGKSTIVKQMKIIHEAGYSEEECKQYKAV

Xenopus laevis                REVKLLLLGAGESGKSTIVKQMKIIHEAGYSEEECKQYKAV
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 – 354 Guanine nucleotide-binding protein G(i) subunit alpha-1
Domain 32 – 354 G-alpha
Binding site 47 – 47
Alternative sequence 1 – 52 Missing. In isoform 2.
Mutagenesis 42 – 42 G -> R. Abolishes switch to an activated conformation and dissociation from beta and gamma subunits upon GTP binding. Abolishes interaction with RGS family members.
Helix 46 – 57



Literature citations
Pediatric Encephalopathy: Clinical, Biochemical and Cellular Insights into the Role of Gln52 of GNAO1 and GNAI1 for the Dominant Disease.
Solis G.P.; Kozhanova T.V.; Koval A.; Zhilina S.S.; Mescheryakova T.I.; Abramov A.A.; Ishmuratov E.V.; Bolshakova E.S.; Osipova K.V.; Ayvazyan S.O.; Lebon S.; Kanivets I.V.; Pyankov D.V.; Troccaz S.; Silachev D.N.; Zavadenko N.N.; Prityko A.G.; Katanaev V.L.;
Cells 10:0-0(2021)
Cited for: CHARACTERIZATION OF VARIANT NEDHISB PRO-52;
Variants in GNAI1 cause a syndrome associated with variable features including developmental delay, seizures, and hypotonia.
Muir A.M.; Gardner J.F.; van Jaarsveld R.H.; de Lange I.M.; van der Smagt J.J.; Wilson G.N.; Dubbs H.; Goldberg E.M.; Zitano L.; Bupp C.; Martinez J.; Srour M.; Accogli A.; Alhakeem A.; Meltzer M.; Gropman A.; Brewer C.; Caswell R.C.; Montgomery T.; McKenna C.; McKee S.; Powell C.; Vasudevan P.C.; Brady A.F.; Joss S.; Tysoe C.; Noh G.; Tarnopolsky M.; Brady L.; Zafar M.; Schrier Vergano S.A.; Murray B.; Sawyer L.; Hainline B.E.; Sapp K.; DeMarzo D.; Huismann D.J.; Wentzensen I.M.; Schnur R.E.; Monaghan K.G.; Juusola J.; Rhodes L.; Dobyns W.B.; Lecoquierre F.; Goldenberg A.; Polster T.; Axer-Schaefer S.; Platzer K.; Kloeckner C.; Hoffman T.L.; MacArthur D.G.; O'Leary M.C.; VanNoy G.E.; England E.; Varghese V.C.; Mefford H.C.;
Genet. Med. 23:881-887(2021)
Cited for: VARIANTS NEDHISB ARG-40; CYS-40; ASP-45; ILE-48; LYS-48; PRO-52; SER-75 DEL; GLN-172 DEL; VAL-173; 186-GLU--PHE-189 DEL; TYR-224; ARG-270; ASN-270; PRO-326 AND GLU-332; INVOLVEMENT IN NEDHISB;
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.