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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O60880: Variant p.Arg55Leu

SH2 domain-containing protein 1A
Gene: SH2D1A
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Variant information Variant position: help 55 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 Leucine (L) at position 55 (R55L, p.Arg55Leu). 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 medium size and hydrophobic (L) 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 XLP1; reduced affinity for SLAMF1 and FYN. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 55 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 128 The length of the canonical sequence.
Location on the sequence: help ESVPGVYCLCVLYHGYIYTY R VSQTETGSWSAETAPGVHKR 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                         ESVPGVYCLCVLYHGYIYTYRVSQTETGSWSAETAPGVHKR

Rhesus macaque                ESVPGVYCLCVLYHGYIYTYRVSQTETGSWSAETAPGVHKR

Mouse                         ESVPGVYCLCVLYQGYIYTYRVSQTETGSWSAETAPGVHKR

Rat                           ESVPGVYCLCVLYQGYIYTYRVSQTETGSWSAETAPGVHKR

Pig                           ESVPGVYCLCVLYQGYIYTYRVSHTETGSWIADTAPGVHKR

Bovine                        ESVPGVYCLCVLYQGYIYTYRVSQTETGSWSAETAPGVHKR
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 1 – 128 SH2 domain-containing protein 1A
Domain 6 – 104 SH2
Alternative sequence 40 – 128 VYCLCVLYHGYIYTYRVSQTETGSWSAETAPGVHKRYFRKIKNLISAFQKPDQGIVIPLQYPVEKKSSARSTQGTTGIREDPDVCLKAP -> ITVTFIHTECPRQKQVLGVLSISEARSRHCNTSAVSS. In isoform E.
Alternative sequence 47 – 128 YHGYIYTYRVSQTETGSWSAETAPGVHKRYFRKIKNLISAFQKPDQGIVIPLQYPVEKKSSARSTQGTTGIREDPDVCLKAP -> QHLGYIKDISGK. In isoform C.
Alternative sequence 47 – 128 YHGYIYTYRVSQTETGSWSAETAPGVHKRYFRKIKNLISAFQKPDQGIVIPLQYPVEKKSSARSTQGTTGIREDPDVCLKAP -> ISEARSRHCNTSAVSS. In isoform F.
Beta strand 50 – 58



Literature citations
Defective NK cell activation in X-linked lymphoproliferative disease.
Benoit L.; Wang X.; Pabst H.F.; Dutz J.; Tan R.;
J. Immunol. 165:3549-3553(2000)
Cited for: VARIANT XLP1 LEU-55; Disease-causing SAP mutants are defective in ligand binding and protein folding.
Li C.; Iosef C.; Jia C.Y.H.; Gkourasas T.; Han V.K.M.; Li S.-C.;
Biochemistry 42:14885-14892(2003)
Cited for: CHARACTERIZATION OF VARIANTS XLP1 PRO-31; CYS-54; LEU-55 AND SER-87;
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.