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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P08865: Variant p.Arg180Gly

Small ribosomal subunit protein uS2
Gene: RPSA
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Variant information Variant position: help 180 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 Arginine (R) to Glycine (G) at position 180 (R180G, p.Arg180Gly). 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 basic (R) to glycine (G) 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 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 180 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 AIPCNNKGAHSVGLMWWMLA R EVLRMRGTISREHPWEVMPD 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                         AIPCNNKGAHSVGLMWWMLAREVLRMRGTISREHPW-----EVMPD

Mouse                         AIPCNNKGAHSVGLMWWMLAREVLRMRGTISREHPW-----

Rat                           AIPCNNKGAHSVGLMWWMLAREVLRMRGTISREHPW-----

Pig                           AIPCNNKGAHSVGLMWWMLAREVLRMRGTISREHPW-----

Bovine                        AIPCNNKGAHSVGLMWWMLAREVLRMRGTISREHPW-----

Sheep                         AIPCNNKGAHSVGLMWWMLAREVLRMRGTISREHPW-----

Chicken                       AIPCNNKGAHSVGLMWWMLAREVLRMRGTISREHPW-----

Xenopus laevis                AIPCNNKGAHSVGLMWWMLAREVLRMRGTISREHPW-----

Xenopus tropicalis            AIPCNNKGAHSVGLMWWMLAREVLRMRGTISREHPW-----

Zebrafish                     AIPCNNKGPHSVGLMWWMLAREVLRMRGTISREHPW-----

Caenorhabditis elegans        GVPCNNKGERSIGLMWWMLAREILILRGKISRQTGFVLEGK

Drosophila                    AIPCNNKSAHSIGLMWWLLAREVLRLRGTISRSVEW-----

Slime mold                    AIPCNNRGKNSIALMFWLLAREVLYLRGTIPRNTTW-----

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 161 – 180 Laminin-binding
Helix 168 – 185



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.