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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9BUM1: Variant p.Met116Lys

Glucose-6-phosphatase 3
Gene: G6PC3
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Variant information Variant position: help 116 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 Methionine (M) to Lysine (K) at position 116 (M116K, p.Met116Lys). 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 hydrophobic (M) to large size and basic (K) 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 SCN4; the patient also carries mutation Thr-166 in ELANE; complete loss of activity. Any additional useful information about the variant.


Sequence information Variant position: help 116 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 346 The length of the canonical sequence.
Location on the sequence: help QVHQFPSSCETGPGSPSGHC M ITGAALWPIMTALSSQVATR 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                         QVHQFPSSCETGPGSPSGHCMITGAALWPIMTALSSQVATR

Mouse                         QIHQFPSSCETGPGSPSGHCMITGAALWPVMTAISSQVASR

Rat                           QIHQFPSSCETGPGSPSGHCMITGAALWPVMIAISSQVASQ

Bovine                        QVHQFPSSCETGPGSPSGHCMITGAALWPIMTAVSSQMATR

Zebrafish                     EVQQFQSTCESGPGSPSGHAMVTSAVWWVIISSLASFSQAY
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 – 346 Glucose-6-phosphatase 3
Transmembrane 115 – 135 Helical
Active site 114 – 114 Proton donor
Mutagenesis 114 – 114 H -> A. Loss of catalytic activity.



Literature citations
Digenic mutations in severe congenital neutropenia.
Germeshausen M.; Zeidler C.; Stuhrmann M.; Lanciotti M.; Ballmaier M.; Welte K.;
Haematologica 95:1207-1210(2010)
Cited for: VARIANTS SCN4 LYS-116; GLN-189 AND ARG-260; Extended spectrum of human glucose-6-phosphatase catalytic subunit 3 deficiency: novel genotypes and phenotypic variability in severe congenital neutropenia.
Boztug K.; Rosenberg P.S.; Dorda M.; Banka S.; Moulton T.; Curtin J.; Rezaei N.; Corns J.; Innis J.W.; Avci Z.; Tran H.C.; Pellier I.; Pierani P.; Fruge R.; Parvaneh N.; Mamishi S.; Mody R.; Darbyshire P.; Motwani J.; Murray J.; Buchanan G.R.; Newman W.G.; Alter B.P.; Boxer L.A.; Donadieu J.; Welte K.; Klein C.;
J. Pediatr. 160:679-683(2012)
Cited for: VARIANTS SCN4 LEU-44; LYS-116; ILE-139; GLN-161; HIS-253; ARG-260 AND ASP-260; Functional analysis of mutations in a severe congenital neutropenia syndrome caused by glucose-6-phosphatase-beta deficiency.
Lin S.R.; Pan C.J.; Mansfield B.C.; Chou J.Y.;
Mol. Genet. Metab. 114:41-45(2015)
Cited for: CHARACTERIZATION OF VARIANTS SCN4 LEU-44; SER-44; ILE-116; LYS-116; THR-116; VAL-116; ARG-118; ILE-139; PRO-154; GLN-161; PRO-185; GLN-189; ARG-208; HIS-253; ARG-260 AND ASP-260;
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.