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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P08865: Variant p.Thr54Asn

Small ribosomal subunit protein uS2
Gene: RPSA
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Variant information Variant position: help 54 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 Threonine (T) to Asparagine (N) at position 54 (T54N, p.Thr54Asn). 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 Similar physico-chemical property. Both residues are medium size and polar. 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 54 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 MEQYIYKRKSDGIYIINLKR T WEKLLLAARAIVAIENPADV 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                         MEQYIYKRKSDGIYIINLKRTWEKLLLAARAIVAIENPADV

Mouse                         MEQYIYKRKSDGIYIINLKRTWEKLLLAARAIVAIENPADV

Rat                           MEQYIYKRKSDGIYIINLKRTWEKLLLAARAIVAIENPADV

Pig                           MEQYIYKRKSDGIYIINLKRTWEKLLLAARAIVAIENPADV

Bovine                        MEQYIYKRKSDGIYIINLKRTWEKLLLAARAIVAIENPADV

Sheep                         MEQYIYKRKSDGIYIINLKRTWEKLLLAARAIVAIENPADV

Chicken                       MEQYIYKRKSDGIYIINLKRTWEKLLLAARAIVAIENPADV

Xenopus laevis                MEQYIYKRKSDGIYIINLKRTWEKLLLAARAIVAIENPADV

Xenopus tropicalis            MEQYIYKRKSDGIYIINLKRTWEKLLLAARAIVAIENPADV

Zebrafish                     MEQYVYKRKSDGVYIINLKKTWEKLLLAARAIVAIENPADV

Caenorhabditis elegans        MQQYVYKRRFDGPNIINVKKTWEKLLLAARAIAAVENPADV

Drosophila                    MEQYVYKRRADGVNILNLGKTWEKLQLAARAIVAIDNPSDI

Slime mold                    MESYTWKRKDNGHFIINLAKTWEKIQLAARVIVAIENPADI
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.