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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P00492: Variant p.Phe74Leu

Hypoxanthine-guanine phosphoribosyltransferase
Gene: HPRT1
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Variant information Variant position: help 74 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 Phenylalanine (F) to Leucine (L) at position 74 (F74L, p.Phe74Leu). 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 aromatic (F) to medium size and hydrophobic (L) 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 LNS; Flint/RJK 892/DW/Perth/1522, Japan. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 74 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 218 The length of the canonical sequence.
Location on the sequence: help MKEMGGHHIVALCVLKGGYK F FADLLDYIKALNRNSDRSIP 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                         MKEM-GGHHIVALCVLKGGYKFFADLLDYIKALNRNSDRSIP

                              MKEM-GGHHIVALCVLKGGYKFFADLLDYIKALNRNSDGSI

Chimpanzee                    MKEM-GGHHIVALCVLKGGYKFFADLLDYIKALNRNSDRSI

Mouse                         MKEM-GGHHIVALCVLKGGYKFFADLLDYIKALNRNSDRSI

Rat                           MKEM-GGHHIVALCVLKGGYKFFADLLDYIKALNRNSDRSI

Pig                           MKEM-GGHHIVALCVLKGGYKFFADLLDYIKALNRNSDRSI

Bovine                        MKEM-GGHHIVALCVLKGGYKFFADLLDYIKALNRNSDKSI

Chicken                       MKGM-GGHHIVALCVLKGGYKFFADLLDYIKALNRNSDKSI

Slime mold                    TQDYKDSKNLVLVGILKGSFVFMSDLVRSIHLPNTN-----

Baker's yeast                 IIAI-GG----------GGFIPARILRTFLKEPGVPTIRIF

Fission yeast                 IIAI-GG----------GGFIPARILRTFLKKKGSKNIPIQ
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 – 218 Hypoxanthine-guanine phosphoribosyltransferase
Binding site 69 – 69
Mutagenesis 69 – 69 K -> A. Reduced affinity for hypoxanthine, phosphoribosylpyrophosphate and IMP. Reduced catalytic activity.
Helix 72 – 87



Literature citations
Genetic basis of hypoxanthine guanine phosphoribosyltransferase deficiency in a patient with the Lesch-Nyhan syndrome (HPRTFlint).
Davidson B.L.; Pashmforoush M.; Kelly W.N.; Palella T.D.;
Gene 63:331-336(1988)
Cited for: VARIANT LNS FLINT LEU-74; Multiplex DNA deletion detection and exon sequencing of the hypoxanthine phosphoribosyltransferase gene in Lesch-Nyhan families.
Gibbs R.A.; Nguyen P.N.; Edwards A.; Civitello A.B.; Caskey C.T.;
Genomics 7:235-244(1990)
Cited for: VARIANTS LNS RJK LYS-45; LEU-74; ASP-130; SER-131; LYS-143; SER-161; TYR-177; ASN-194; VAL-199; ASP-204 AND TYR-206; Determination of the mutations responsible for the Lesch-Nyhan syndrome in 17 subjects.
Tarle S.A.; Davidson B.L.; Wu V.C.; Zidar F.J.; Seegmiller J.E.; Kelley W.N.; Palella T.D.;
Genomics 10:499-501(1991)
Cited for: VARIANTS LNS TYR-28 DEL; VAL-50; GLU-70; LEU-74; THR-183 AND ARG-204; Molecular analysis of two enzyme genes, HPRT1 and PRPS1, causing X-linked inborn errors of purine metabolism.
Yamada Y.; Yamada K.; Nomura N.; Yamano A.; Kimura R.; Tomida S.; Naiki M.; Wakamatsu N.;
Nucleosides Nucleotides Nucleic Acids 29:291-294(2010)
Cited for: VARIANTS LNS TYR-44 AND LEU-74;
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.