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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P63096: Variant p.Asp173Val

Guanine nucleotide-binding protein G(i) subunit alpha-1
Gene: GNAI1
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Variant information Variant position: help 173 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 Aspartate (D) to Valine (V) at position 173 (D173V, p.Asp173Val). 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 acidic (D) to medium size and hydrophobic (V) 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
Variant description: help In NEDHISB. Any additional useful information about the variant.


Sequence information Variant position: help 173 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 AYYLNDLDRIAQPNYIPTQQ D VLRTRVKTTGIVETHFTFKD 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                         AYYLNDLDRIAQPNYIPTQQDVLRTRVKTTGIVETHFTFKD

Mouse                         AYYLNDLDRIAQPNYIPTQQDVLRTRVKTTGIVETHFTFKD

Rat                           AYYLNDLDRIAQPNYIPTQQDVLRTRVKTTGIVETHFTFKD

Bovine                        AYYLNDLDRIAQPNYIPTQQDVLRTRVKTTGIVETHFTFKD

Chicken                       AYYLNDLDRIAQTSYIPTQQDVLRTRVKTTGIVETHFTFKD

Xenopus laevis                AYYLNDLDRIAQNSYIPTQQDVLRTRVKTTGIVETHFTFKD
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
Region 173 – 181 G2 motif
Binding site 181 – 181
Modified residue 178 – 178 ADP-ribosylarginine; by cholera toxin
Helix 171 – 175



Literature citations
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.