Variant position: 182 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 879 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 QVPPDCPPLVQKGECHVNFV RKEQCSFSWDWGPSFPTQGIW
Mouse RVPPECPPVEQKGECHVNFI RKAQCSFSWDWGPSFPSQGIW
Rat RVPPECPPVEQKGECHVNFI RKEQCSFSWDWGPSFPSQGIW
Bovine WVPPNCPPPVQDGECHVNFI RKMQCSFGWDWGPSFPTQGIW
Goat WVPPNCPPPVQDGECHVNFI RKMQCSFGWDWGPSFPTQGIW
Caenorhabditis elegans SLPPDCNPDIYHGECHQNFI RKAQYSFAWDWGPSFPTVGIP
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
18 – 879 Beta-mannosidase
Molecular analysis in two beta-mannosidosis patients: description of a new adult case.
Gort L.; Duque J.; Fabeiro J.M.; Zulaica A.; Coll M.J.; Chabas A.;
Mol. Genet. Metab. 89:398-400(2006)
Cited for: VARIANTS MANSB TRP-182; GLU-392 AND 466-TRP--TYR-879 DEL; CATALYTIC ACTIVITY;
Identification of two novel beta-mannosidosis-associated sequence variants: biochemical analysis of beta-mannosidase (MANBA) missense mutations.
Riise Stensland H.M.; Persichetti E.; Sorriso C.; Hansen G.M.; Bibi L.; Paciotti S.; Balducci C.; Beccari T.;
Mol. Genet. Metab. 94:476-480(2008)
Cited for: VARIANT MANSB PRO-505; CHARACTERIZATION OF VARIANTS MANSB TRP-182; GLU-392 AND PRO-505; CHARACTERIZATION OF VARIANT ILE-253; CATALYTIC ACTIVITY; MUTAGENESIS OF ARG-638; ARG-641 AND LEU-749;
The structure of mammalian beta-mannosidase provides insight into beta-mannosidosis and nystagmus.
Gytz H.; Liang J.; Liang Y.; Gorelik A.; Illes K.; Nagar B.;
FEBS J. 286:1319-1331(2019)
Cited for: CHARACTERIZATION OF VARIANTS MANSB TRP-182; GLU-392; 466-TRP--TYR-879 DEL AND PRO-505; FUNCTION; CATALYTIC ACTIVITY; PATHWAY; BIOPHYSICOCHEMICAL PROPERTIES;
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.