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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P01308: Variant p.Phe48Ser

Insulin
Gene: INS
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Variant information Variant position: help 48 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 Serine (S) at position 48 (F48S, p.Phe48Ser). 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 small size and polar (S) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -2 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 HPRI; Los-Angeles. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 48 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 110 The length of the canonical sequence.
Location on the sequence: help QHLCGSHLVEALYLVCGERG F FYTPKTRREAEDLQVGQVEL 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                         QHLCGSHLVEALYLVCGERGFFYTPKTRREAEDLQVGQVEL

Gorilla                       QHLCGSHLVEALYLVCGERGFFYTPKTRREAEDLQVGQVEL

                              QHLCGSHLVEALYLVCGERGFFYTPKARREVEDLQVRDVEL

Chimpanzee                    QHLCGSHLVEALYLVCGERGFFYTPKTRREAEDLQVGQVEL

Pig                           QHLCGSHLVEALYLVCGERGFFYTPKARREAENPQAGAVEL

Bovine                        QHLCGSHLVEALYLVCGERGFFYTPKARREVEGPQVGALEL

Rabbit                        QHLCGSHLVEALYLVCGERGFFYTPKSRREVEELQVGQAEL

Goat                          QHLCGSHLVEALYLVCGERGFFYTPKA--------------

Sheep                         QHLCGSHLVEALYLVCGERGFFYTPKARREVEGPQVGALEL

Cat                           QHLCGSHLVEALYLVCGERGFFYTPKARREAEDLQGKDAEL

Horse                         QHLCGSHLVEALYLVCGERGFFYTPKAXXEAEDPQVGEVEL

Chicken                       QHLCGSHLVEALYLVCGERGFFYSPKARRDVEQPLVSS-PL

Zebrafish                     QHLCGSHLVDALYLVCGPTGFFYNPK--RDVE-PLLGFLPP
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
Peptide 25 – 54 Insulin B chain
Disulfide bond 31 – 96 Interchain (between B and A chains)
Disulfide bond 43 – 109 Interchain (between B and A chains)
Beta strand 48 – 50



Literature citations
Studies on mutant human insulin genes: identification and sequence analysis of a gene encoding [SerB24]insulin.
Haneda M.; Chan S.J.; Kwok S.C.M.; Rubenstein A.H.; Steiner D.F.;
Proc. Natl. Acad. Sci. U.S.A. 80:6366-6370(1983)
Cited for: VARIANT HPRI SER-48; Identification of a mutant human insulin predicted to contain a serine-for-phenylalanine substitution.
Shoelson S.; Fickova M.; Haneda M.; Nahum A.; Musso G.; Kaiser E.T.; Rubenstein A.H.; Tager H.;
Proc. Natl. Acad. Sci. U.S.A. 80:7390-7394(1983)
Cited for: VARIANT HPRI SER-48; VARIANT LEU-49; Paradoxical structure and function in a mutant human insulin associated with diabetes mellitus.
Hua Q.-X.; Shoelson S.E.; Inouye K.; Weiss M.A.;
Proc. Natl. Acad. Sci. U.S.A. 90:582-586(1993)
Cited for: STRUCTURE BY NMR OF 90-110 AND 25-54 OF VARIANT HPRI SER-48; DISULFIDE BONDS;
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.