Variant position: 207 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 556 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 FTINESTIIDSPRFSHRGIL IDTSRHYLPVKIILKTLDAMA
Mouse FTINESSIADSPRFPHRGIL IDTSRHFLPVKTILKTLDAMA
Rat FTINESTIADSPRFPHRGIL IDTSRHYLPVKTIFKTLDAMA
Pig FTVNESEIIDFPRFPHRGIL IDTGRHFLSVKTIFKTLDAMA
Cat FTVNESDIIDSPRFPHRGIL IDTARHFLPVKSILKTLDAMA
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
122 – 556 Beta-hexosaminidase subunit beta
122 – 311 Beta-hexosaminidase subunit beta chain B
190 – 190 N-linked (GlcNAc...) asparagine
211 – 211 R -> K. Does not affect the native conformation of the isozyme A. Does not affect hydrolysis of GM2 ganglioside by the isozyme A.
201 – 212
Molecular basis of an adult form of beta-hexosaminidase B deficiency with motor neuron disease.
Banerjee P.; Siciliano L.; Oliveri D.; McCabe N.R.; Boyers M.J.; Horwitz A.L.; Li S.-C.; Dawson G.;
Biochem. Biophys. Res. Commun. 181:108-115(1991)
Cited for: VARIANT GM2G2 SER-456; VARIANT VAL-207;
Significance of two point mutations present in each HEXB allele of patients with adult GM2 gangliosidosis (Sandhoff disease) homozygosity for the Ile207-->Val substitution is not associated with a clinical or biochemical phenotype.
Redonnet-Vernhet I.; Mahuran D.J.; Salvayre R.; Dubas F.; Levade T.;
Biochim. Biophys. Acta 1317:127-133(1996)
Cited for: VARIANT GM2G2 GLN-505; VARIANT VAL-207;
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