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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P30613: Variant p.Gly332Ser

Pyruvate kinase PKLR
Gene: PKLR
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Variant information Variant position: help 332 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 Glycine (G) to Serine (S) at position 332 (G332S, p.Gly332Ser). 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 glycine (G) to small size and polar (S) 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
Variant description: help In PKRD; loss of catalytical activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 332 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 574 The length of the canonical sequence.
Location on the sequence: help SKIENHEGVKRFDEILEVSD G IMVARGDLGIEIPAEKVFLA 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                         SKIENHEGVKRFDEILEVSDGIMVARGDLGIEIPAEKVFLA

                              SKIENHEGVKKFDEILEVSDGIMVARGDLGIEIPAEKVFLA

Mouse                         SKIENHEGVKKFDEILEVSDGIMMARGDLGIEIPAEKVFLA

Rat                           SKIENHEGVKKFDEILEVSDGIMVARGDLGIEIPAEKVFLA
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 – 574 Pyruvate kinase PKLR
Binding site 313 – 313
Binding site 315 – 315
Binding site 338 – 338
Binding site 339 – 339
Binding site 339 – 339
Site 313 – 313 Transition state stabilizer
Beta strand 330 – 336



Literature citations
Structure and function of human erythrocyte pyruvate kinase. Molecular basis of nonspherocytic hemolytic anemia.
Valentini G.; Chiarelli L.R.; Fortin R.; Dolzan M.; Galizzi A.; Abraham D.J.; Wang C.; Bianchi P.; Zanella A.; Mattevi A.;
J. Biol. Chem. 277:23807-23814(2002)
Cited for: X-RAY CRYSTALLOGRAPHY (2.73 ANGSTROMS) OF 47-574 IN COMPLEX WITH SUBSTRATE ANALOG; FRUCTOSE 1,6-BISPHOSPHATE; POTASSIUM IONS AND MANGANESE IONS; FUNCTION; CATALYTIC ACTIVITY; ALLOSTERIC ACTIVATION; ACTIVITY REGULATION; CHARACTERIZATION OF VARIANTS PKRD SER-332; ASP-364; ASN-390; HIS-479; TRP-486; LEU-504 AND TRP-532; CHARACTERIZATION OF VARIANT MET-384; SUBUNIT; Mutations in the pyruvate kinase L gene in patients with hereditary hemolytic anemia.
Lenzner C.; Nuernberg P.; Thiele B.-J.; Reis A.; Brabec V.; Sakalova A.; Jacobasch G.;
Blood 83:2817-2822(1994)
Cited for: VARIANTS PKRD SER-332; SER-336; LYS-354 DEL; ASP-361; THR-392; HIS-498; GLN-510 AND TRP-532; Novel mutations and structural implications in R-type pyruvate kinase-deficient patients from Southern Italy.
Pastore L.; della Morte R.; Frisso G.; Alfinito F.; Vitale D.; Calise R.M.; Ferraro F.; Zagari A.; Rotoli B.; Salvatore F.;
Hum. Mutat. 11:127-134(1998)
Cited for: VARIANTS PKRD SER-332; PRO-337; TRP-486; CYS-498 AND GLN-510;
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.