Variant position: 54 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 128 The length of the canonical sequence.
Location on the sequence:
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: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human SESVPGVYCLCVLYHGYIYT YRVSQTETGSWSAETAPGVHK
Rhesus macaque SESVPGVYCLCVLYHGYIYT YRVSQTETGSWSAETAPGVHK
Mouse SESVPGVYCLCVLYQGYIYT YRVSQTETGSWSAETAPGVHK
Rat SESVPGVYCLCVLYQGYIYT YRVSQTETGSWSAETAPGVHK
Pig SESVPGVYCLCVLYQGYIYT YRVSHTETGSWIADTAPGVHK
Bovine SESVPGVYCLCVLYQGYIYT YRVSQTETGSWSAETAPGVHK
Sequence annotation in neighborhood: 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.
Type Positions Description
1 – 128 SH2 domain-containing protein 1A
6 – 104 SH2
40 – 128 VYCLCVLYHGYIYTYRVSQTETGSWSAETAPGVHKRYFRKIKNLISAFQKPDQGIVIPLQYPVEKKSSARSTQGTTGIREDPDVCLKAP -> ITVTFIHTECPRQKQVLGVLSISEARSRHCNTSAVSS. In isoform E.
47 – 128 YHGYIYTYRVSQTETGSWSAETAPGVHKRYFRKIKNLISAFQKPDQGIVIPLQYPVEKKSSARSTQGTTGIREDPDVCLKAP -> QHLGYIKDISGK. In isoform C.
47 – 128 YHGYIYTYRVSQTETGSWSAETAPGVHKRYFRKIKNLISAFQKPDQGIVIPLQYPVEKKSSARSTQGTTGIREDPDVCLKAP -> ISEARSRHCNTSAVSS. In isoform F.
50 – 58
Correlation of mutations of the SH2D1A gene and Epstein-Barr virus infection with clinical phenotype and outcome in X-linked lymphoproliferative disease.
Sumegi J.; Huang D.; Lanyi A.; Davis J.D.; Seemayer T.A.; Maeda A.; Klein G.; Seri M.; Wakiguchi H.; Purtilo D.T.; Gross T.G.;
Cited for: VARIANTS XLP1 CYS-7; ARG-28; PRO-31; TRP-42; ILE-53; CYS-54; SER-87; PRO-99 AND GLY-102;
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.;
Cited for: CHARACTERIZATION OF VARIANTS XLP1 PRO-31; CYS-54; LEU-55 AND SER-87;
Missense mutations in SH2D1A identified in patients with X-linked lymphoproliferative disease differentially affect the expression and function of SAP.
Hare N.J.; Ma C.S.; Alvaro F.; Nichols K.E.; Tangye S.G.;
Int. Immunol. 18:1055-1065(2006)
Cited for: VARIANTS XLP1 CYS-54; THR-84 AND SER-87; CHARACTERIZATION OF VARIANTS XLP1 CYS-54; THR-84 AND SER-87;
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.