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UniProtKB/Swiss-Prot P00367: Variant p.Gly499Ser

Glutamate dehydrogenase 1, mitochondrial
Gene: GLUD1
Variant information

Variant position:  499
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  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:  From Glycine (G) to Serine (S) at position 499 (G499S, p.Gly499Ser).
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:  Change from glycine (G) to small size and polar (S)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  0
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:  In HHF6.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  499
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  558
The length of the canonical sequence.

Location on the sequence:   GKHGGTIPIVPTAEFQDRIS  G ASEKDIVHSGLAYTMERSAR
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                         GKHGGTIPIVPTAEFQDRISGASEKDIVHSGLAYTMERSAR

Mouse                         GKHGGTIPVVPTAEFQDRISGASEKDIVHSGLAYTMERSAR

Rat                           GKHGGTIPVVPTAEFQDRISGASEKDIVHSGLAYTMERSAR

Pig                           GKHGGTIPIVPTAEFQDRISGASEKDIVHSGLAYTMERSAR

Bovine                        GKHGGTIPIVPTAEFQDRISGASEKDIVHSGLAYTMERSAR

Drosophila                    GRVGGRIPVTPSESFQKRISGASEKDIVHSGLDYTMERSAR

Slime mold                    SEAERSL----------IIHGADEIDIVRSGLEDTMQNACA

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.

TypePositionsDescription
Chain 54 – 558 Glutamate dehydrogenase 1, mitochondrial
Binding site 516 – 516 ADP
Modified residue 480 – 480 N6-acetyllysine; alternate
Modified residue 480 – 480 N6-succinyllysine; alternate
Modified residue 503 – 503 N6-acetyllysine; alternate
Modified residue 503 – 503 N6-malonyllysine; alternate
Modified residue 503 – 503 N6-succinyllysine; alternate
Modified residue 512 – 512 Phosphotyrosine
Mutagenesis 501 – 501 S -> A. Reduces activity and inhibition by GTP.
Mutagenesis 516 – 516 R -> A. Abolishes activation by ADP.


Literature citations

Hyperinsulinism and hyperammonemia in infants with regulatory mutations of the glutamate dehydrogenase gene.
Stanley C.A.; Lieu Y.K.; Hsu B.Y.L.; Burlina A.B.; Greenberg C.R.; Hopwood N.J.; Perlman K.; Rich B.H.; Zammarchi E.; Poncz M.;
N. Engl. J. Med. 338:1352-1357(1998)
Cited for: VARIANTS HHF6 LEU-498; SER-499; ASP-499; PRO-501 AND TYR-507; CHARACTERIZATION OF VARIANT TYR-507; FUNCTION; ACTIVITY REGULATION;

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.