Variant position: 170 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 357 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 CLNVILWLGFWAVQLNVCLS RIYLAAHFPHQVVAGVLSGIA
Mouse CLNVILWLGFWAVQLNVCLS RIYLAAHFPHQVVAGVLSGIA
Rat CLNVVLWLGYWAVQLNVCLS RIYLAAHFPHQVVAGVLSGIA
Bovine CLNVMLWLGFWVVQLNVCLS RIYLAAHFPHQVVAGVLSGIA
Cat CLNVILWLGFWAVQLNVCLS RIYLAAHFPHQVVAGVLSGIA
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 – 357 Glucose-6-phosphatase
169 – 179 Lumenal
176 – 176 Nucleophile
170 – 170 Substrate
115 – 175 SPSGHAMGTAGVYYVMVTSTLSIFQGKIKPTYRFRCLNVILWLGFWAVQLNVCLSRIYLAA -> KDKADLQISVLECHFVVGILGCAAECLSVTNLPCCSFSSSSCCWSPVRHCCCRNFQPHPQH. In isoform 2.
176 – 176 H -> A. Loss of catalytic activity.
179 – 179 H -> A. Loss of catalytic activity.
The catalytic center of glucose-6-phosphatase. HIS176 is the nucleophile forming the phosphohistidine-enzyme intermediate during catalysis.
Ghosh A.; Shieh J.-J.; Pan C.-J.; Sun M.-S.; Chou J.Y.;
J. Biol. Chem. 277:32837-32842(2002)
Cited for: ACTIVE SITES; MUTAGENESIS OF HIS-9; HIS-52; HIS-119; HIS-176; HIS-179; HIS-197; HIS-252; HIS-307 AND HIS-353; CHARACTERIZATION OF VARIANTS ASN-76; CYS-83 AND GLN-170;
Molecular aspects of glycogen storage disease type Ia in Turkish patients: a novel mutation in the glucose-6-phosphatase gene.
Huener G.; Podskarbi T.; Schuetz M.; Baykal T.; Sarbat G.; Shin Y.S.; Demirkol M.;
J. Inherit. Metab. Dis. 21:445-446(1998)
Cited for: VARIANTS GSD1A CYS-83; GLN-170 AND TRP-270;
Glycogen storage disease type I: diagnosis and phenotype/genotype correlation.
Matern D.; Seydewitz H.H.; Bali D.; Lang C.; Chen Y.-T.;
Eur. J. Pediatr. 161:S10-S19(2002)
Cited for: VARIANTS GSD1A ARG-20; VAL-38; PRO-65; ARG-68; ARG-77; ARG-81; CYS-83; HIS-83; LYS-110; LEU-113; LEU-156; GLN-170; CYS-177; SER-178; ARG-188; SER-188; ARG-236; PRO-265; VAL-270; PHE-327 DEL AND ARG-345;
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.