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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P00367: Variant p.His507Tyr

Glutamate dehydrogenase 1, mitochondrial
Gene: GLUD1
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Variant information Variant position: help 507 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 Histidine (H) to Tyrosine (Y) at position 507 (H507Y, p.His507Tyr). 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 (H) to large size and aromatic (Y) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 2 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 HHF6; abolishes inhibition by ATP; no effect on activation by ADP; Strongly reduces inhibition by GTP. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 507 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 558 The length of the canonical sequence.
Location on the sequence: help IVPTAEFQDRISGASEKDIV H SGLAYTMERSARQIMRTAMK 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                         IVPTAEFQDRISGASEKDIVHSGLAYTMERSARQIMRTAMK

Mouse                         VVPTAEFQDRISGASEKDIVHSGLAYTMERSARQIMRTAMK

Rat                           VVPTAEFQDRISGASEKDIVHSGLAYTMERSARQIMRTAMK

Pig                           IVPTAEFQDRISGASEKDIVHSGLAYTMERSARQIMRTAMK

Bovine                        IVPTAEFQDRISGASEKDIVHSGLAYTMERSARQIMRTAMK

Drosophila                    VTPSESFQKRISGASEKDIVHSGLDYTMERSARAIMKTAMK

Slime mold                    IH----------GADEIDIVRSGLEDTMQNACAETRKTANE
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 54 – 558 Glutamate dehydrogenase 1, mitochondrial
Binding site 516 – 516
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
Modified residue 527 – 527 N6-acetyllysine; alternate
Modified residue 527 – 527 N6-malonyllysine; alternate
Modified residue 527 – 527 N6-succinyllysine; alternate
Mutagenesis 501 – 501 S -> A. Reduces activity and inhibition by GTP.
Mutagenesis 516 – 516 R -> A. Abolishes activation by ADP.
Helix 502 – 527



Literature citations
Structures of bovine glutamate dehydrogenase complexes elucidate the mechanism of purine regulation.
Smith T.J.; Peterson P.E.; Schmidt T.; Fang J.; Stanley C.A.;
J. Mol. Biol. 307:707-720(2001)
Cited for: CHARACTERIZATION OF VARIANT TYR-507; ACTIVITY REGULATION; FUNCTION; CATALYTIC ACTIVITY; Expression, purification and characterization of human glutamate dehydrogenase (GDH) allosteric regulatory mutations.
Fang J.; Hsu B.Y.L.; MacMullen C.M.; Poncz M.; Smith T.J.; Stanley C.A.;
Biochem. J. 363:81-87(2002)
Cited for: MUTAGENESIS OF SER-501 AND ARG-516; CHARACTERIZATION OF VARIANT TYR-507; ALLOSTERIC REGULATION; 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.