Sequence information
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:
CLNVILWLGFWAVQLNVCLS
R IYLAAHFPHQVVAGVLSGIA
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 CLNVILWLGFWAVQLNVCLSR IYLAAHFPHQVVAGVLSGIA
Mouse CLNVILWLGFWAVQLNVCLSR IYLAAHFPHQVVAGVLSGIA
Rat CLNVVLWLGYWAVQLNVCLSR IYLAAHFPHQVVAGVLSGIA
Bovine CLNVMLWLGFWVVQLNVCLSR IYLAAHFPHQVVAGVLSGIA
Cat CLNVILWLGFWAVQLNVCLSR IYLAAHFPHQVVAGVLSGIA
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
1 – 357
Glucose-6-phosphatase catalytic subunit 1
Topological domain
169 – 179
Lumenal
Active site
176 – 176
Nucleophile
Binding site
170 – 170
Substrate
Alternative sequence
115 – 175
SPSGHAMGTAGVYYVMVTSTLSIFQGKIKPTYRFRCLNVILWLGFWAVQLNVCLSRIYLAA -> KDKADLQISVLECHFVVGILGCAAECLSVTNLPCCSFSSSSCCWSPVRHCCCRNFQPHPQH. In isoform 2.
Mutagenesis
176 – 176
H -> AIKMNSR. Loss of glucose-6-phosphatase activity.
Mutagenesis
179 – 179
H -> A. Loss of glucose-6-phosphatase activity.
Literature citations
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; CATALYTIC ACTIVITY; FUNCTION;
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;
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.