Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P04406: Variant p.Lys251Asn

Glyceraldehyde-3-phosphate dehydrogenase
Gene: GAPDH
Feedback?
Variant information Variant position: help 251 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LB/B 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 Lysine (K) to Asparagine (N) at position 251 (K251N, p.Lys251Asn). 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 large size and basic (K) to medium size and polar (N) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 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

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


Sequence information Variant position: help 251 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 335 The length of the canonical sequence.
Location on the sequence: help MAFRVPTANVSVVDLTCRLE K PAKYDDIKKVVKQASEGPLK 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.
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 – 335 Glyceraldehyde-3-phosphate dehydrogenase
Binding site 234 – 234
Modified residue 237 – 237 Phosphothreonine
Modified residue 241 – 241 Phosphoserine
Modified residue 247 – 247 S-(2-succinyl)cysteine
Modified residue 247 – 247 S-nitrosocysteine
Modified residue 254 – 254 N6-acetyllysine
Modified residue 260 – 260 N6,N6-dimethyllysine
Modified residue 263 – 263 N6,N6-dimethyllysine
Mutagenesis 241 – 241 S -> A. Does not affect glycosylation by C.rodentium protein NleB.
Mutagenesis 245 – 245 L -> M. Inhibits S-nitrosylation of Cys-247; when associated with M-250.
Mutagenesis 246 – 246 T -> A. Does not affect glycosylation by C.rodentium protein NleB.
Mutagenesis 247 – 247 C -> S. Markedly reduced glycolytic activity; when associated with S-152 and S-156. Forms free radical-induced aggregates, but to a lesser extent than wild-type protein; when associated with S-156 and S-247.
Mutagenesis 250 – 250 E -> M. Inhibits S-nitrosylation of Cys-247; when associated with M-245.
Beta strand 241 – 251



Literature citations
No reference for the current variant in UniProtKB/Swiss-Prot.
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.