Sequence information
Variant position: 517 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 631 The length of the canonical sequence.
Location on the sequence:
YRVYQIDGNYSGSSHVVLDH
E TYILNLTQANIPGAIPHWQL
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 YRVYQIDGNYSGSSHVVLDHE TYILNLTQANIPGAIPHWQL
Mouse YRVYQIDGNYPGSSHVVLDHE TYILNLTQANAAGGTPSWKR
Bovine YRVYQIDGNYSGSSHVVLDHE TYIMNLTEANEPGATPHWYL
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
Chain
47 – 631
Sphingomyelin phosphodiesterase
Modified residue
510 – 510
Phosphoserine; by PKC/PRKCD
Glycosylation
505 – 505
N-linked (GlcNAc...) asparagine
Glycosylation
522 – 522
N-linked (GlcNAc...) asparagine
Mutagenesis
505 – 505
N -> G. Loss of sphingomyelin phosphodiesterase activity. Loss of secretion.
Mutagenesis
510 – 510
S -> A. Abolishes constitutive secretion and decreases secretion in response to IL1B. No effect on lysosomal targeting. No effect on sphingomyelin phosphodiesterase activity. No effect on endolysosome location. Abolishes phosphorylation by PRKCD.
Mutagenesis
522 – 522
N -> G. Loss of sphingomyelin phosphodiesterase activity. Loss of secretion.
Beta strand
513 – 520
Literature citations
The demographics and distribution of type B Niemann-Pick disease: novel mutations lead to new genotype/phenotype correlations.
Simonaro C.M.; Desnick R.J.; McGovern M.M.; Wasserstein M.P.; Schuchman E.H.;
Am. J. Hum. Genet. 71:1413-1419(2002)
Cited for: VARIANTS NPDB VAL-51; TRP-94; PRO-139; ARG-159; PRO-198; CYS-202; MET-227; CYS-230; ASP-234; SER-247; ARG-250; HIS-291; ALA-325; ARG-332; ASP-359; HIS-378; LEU-378; PRO-381; VAL-415; TYR-423; ARG-433; PRO-434; CYS-437; VAL-454; ASP-458; TRP-476; LEU-477; LEU-482; ASN-490; SER-496; CYS-498; GLN-516; VAL-517; ARG-535; PRO-551; ASN-578; HIS-602 AND PRO-602; VARIANT VAL-487;
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.