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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P30613: Variant p.Arg486Trp

Pyruvate kinase PKLR
Gene: PKLR
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Variant information Variant position: help 486 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 Arginine (R) to Tryptophan (W) at position 486 (R486W, p.Arg486Trp). 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 (R) to large size and aromatic (W) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 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; no conformational change. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 486 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 CCAAAIIVLTTTGRSAQLLS R YRPRAAVIAVTRSAQAARQV 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                         CCAAAIIVLTTTGRSAQLLSRYRPRAAVIAVTRSAQAARQV

                              CCAAAIIVLTKTGRSAQLLSRYRPRAAVIAVTRSAQAARQA

Mouse                         CCAAAIIVLTKTGRSAQLLSRYRPRAAVIAVTRSAQAARQV

Rat                           CCAAAIIVLTKTGRSAQLLSQYRPRAAVIAVTRSAQAARQV

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



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; Analysis of pyruvate kinase-deficiency mutations that produce nonspherocytic hemolytic anemia.
Baronciani L.; Beutler E.;
Proc. Natl. Acad. Sci. U.S.A. 90:4324-4327(1993)
Cited for: VARIANTS PKRD ASP-134; PRO-155; HIS-359; TRP-486; VAL-495 AND GLN-510; Molecular characterization of the PK-LR gene in pyruvate kinase deficient Spanish patients.
Zarza R.; Alvarez R.; Pujades A.; Nomdedeu B.; Carrera A.; Estella J.; Remacha A.; Sanchez J.M.; Morey M.; Cortes T.; Perez Lungmus G.; Bureo E.; Vives Corrons J.L.;
Br. J. Haematol. 103:377-382(1998)
Cited for: VARIANTS PKRD GLN-172; GLN-337; HIS-339; THR-357; ILE-408; THR-431; TRP-486 AND GLN-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.