Variant position: 384 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:
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 GKPVVCATQMLESMITKPRP TRAETSDVANAVLDGADCIML
Mouse GKPVVCATQMLESMITKARP TRAETSDVANAVLDGADCIML
Rat GKPVVCATQMLESMITKARP TRAETSDVANAVLDGADCIML
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.
Type Positions Description
1 – 574 Pyruvate kinase PKLR
371 – 371 Substrate
cDNA cloning of human R-type pyruvate kinase and identification of a single amino acid substitution (Thr384-->Met) affecting enzymatic stability in a pyruvate kinase variant (PK Tokyo) associated with hereditary hemolytic anemia.
Kanno H.; Fujii H.; Hirono A.; Miwa S.;
Proc. Natl. Acad. Sci. U.S.A. 88:8218-8221(1991)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; VARIANT PKRD MET-384;
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;
Point mutations in the L-type pyruvate kinase gene of two children with hemolytic anemia caused by pyruvate kinase deficiency.
Neubauer B.; Lakomek M.; Winkler H.; Parke M.; Hofferbert S.; Schroter W.;
Cited for: VARIANTS PKRD CYS-163 AND MET-384;
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