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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P08865: Variant p.Leu58Phe

Small ribosomal subunit protein uS2
Gene: RPSA
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Variant information Variant position: help 58 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 Leucine (L) to Phenylalanine (F) at position 58 (L58F, p.Leu58Phe). 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 medium size and hydrophobic (L) to large size and aromatic (F) 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 ICAS; reduced protein levels. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 58 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 295 The length of the canonical sequence.
Location on the sequence: help IYKRKSDGIYIINLKRTWEK L LLAARAIVAIENPADVSVIS 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                         IYKRKSDGIYIINLKRTWEKLLLAARAIVAIENPADVSVIS

Mouse                         IYKRKSDGIYIINLKRTWEKLLLAARAIVAIENPADVSVIS

Rat                           IYKRKSDGIYIINLKRTWEKLLLAARAIVAIENPADVSVIS

Pig                           IYKRKSDGIYIINLKRTWEKLLLAARAIVAIENPADVSVIS

Bovine                        IYKRKSDGIYIINLKRTWEKLLLAARAIVAIENPADVSVIS

Sheep                         IYKRKSDGIYIINLKRTWEKLLLAARAIVAIENPADVSVIS

Chicken                       IYKRKSDGIYIINLKRTWEKLLLAARAIVAIENPADVSVIS

Xenopus laevis                IYKRKSDGIYIINLKRTWEKLLLAARAIVAIENPADVCVIS

Xenopus tropicalis            IYKRKSDGIYIINLKRTWEKLLLAARAIVAIENPADVCVIS

Zebrafish                     VYKRKSDGVYIINLKKTWEKLLLAARAIVAIENPADVCVIS

Caenorhabditis elegans        VYKRRFDGPNIINVKKTWEKLLLAARAIAAVENPADVVVVS

Drosophila                    VYKRRADGVNILNLGKTWEKLQLAARAIVAIDNPSDIFVIS

Slime mold                    TWKRKDNGHFIINLAKTWEKIQLAARVIVAIENPADISVIS
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 – 295 Small ribosomal subunit protein uS2
Region 54 – 113 Interaction with PPP1R16B
Modified residue 43 – 43 Phosphoserine
Modified residue 52 – 52 N6-acetyllysine
Helix 51 – 66



Literature citations
Ribosomal protein SA haploinsufficiency in humans with isolated congenital asplenia.
Bolze A.; Mahlaoui N.; Byun M.; Turner B.; Trede N.; Ellis S.R.; Abhyankar A.; Itan Y.; Patin E.; Brebner S.; Sackstein P.; Puel A.; Picard C.; Abel L.; Quintana-Murci L.; Faust S.N.; Williams A.P.; Baretto R.; Duddridge M.; Kini U.; Pollard A.J.; Gaud C.; Frange P.; Orbach D.; Emile J.F.; Stephan J.L.; Sorensen R.; Plebani A.; Hammarstrom L.; Conley M.E.; Selleri L.; Casanova J.L.;
Science 340:976-978(2013)
Cited for: INVOLVEMENT IN ICAS; VARIANTS ICAS ASN-54; PHE-58; GLY-180; TRP-180 AND CYS-186; CHARACTERIZATION OF VARIANTS ICAS ASN-54; PHE-58; GLY-180; TRP-180 AND CYS-186; VARIANTS VAL-185; GLY-257 AND THR-278;
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.