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UniProtKB/Swiss-Prot P30613: Variant p.Gly332Ser

Pyruvate kinase PKLR
Gene: PKLR
Variant information

Variant position:  332
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 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:  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 PKRD; loss of catalytical activity.
Any additional useful information about the variant.

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



Sequence information

Variant position:  332
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  574
The length of the canonical sequence.

Location on the sequence:   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: 
The multiple alignment of the region surrounding the variant against various orthologous sequences.

Human                         SKIENHEGVKRFDEILEVSDGIMVARGDLGIEIPAEKVFLA

                              SKIENHEGVKKFDEILEVSDGIMVARGDLGIEIPAEKVFLA

Mouse                         SKIENHEGVKKFDEILEVSDGIMMARGDLGIEIPAEKVFLA

Rat                           SKIENHEGVKKFDEILEVSDGIMVARGDLGIEIPAEKVFLA

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 1 – 574 Pyruvate kinase PKLR
Metal binding 315 – 315 Manganese
Metal binding 339 – 339 Manganese
Binding site 313 – 313 Substrate; via amide nitrogen
Binding site 338 – 338 Substrate; via amide nitrogen
Binding site 339 – 339 Substrate; via amide nitrogen
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; 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.