Variant position: 122 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 IKQFPVTCETGPGSPSGHAM GTAGVYYVMVTSTLSIFQGKI
Mouse IKQFPVTCETGPGSPSGHAM GAAGVYYVMVTSTLAIFRGKK
Rat IKQFPVTCETGPGSPSGHAM GTAGVYYVMVTSTLAIFRGKK
Bovine IKQFPVTCETGPGSPSGHAM GTAGVYYVMVTSTLSIFRGKK
Cat IKQFPVTCETGPGSPSGHAM GTAGVYYVMVTSTLSMFRGKK
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
118 – 138 Helical
119 – 119 Proton donor
115 – 175 SPSGHAMGTAGVYYVMVTSTLSIFQGKIKPTYRFRCLNVILWLGFWAVQLNVCLSRIYLAA -> KDKADLQISVLECHFVVGILGCAAECLSVTNLPCCSFSSSSCCWSPVRHCCCRNFQPHPQH. In isoform 2.
119 – 119 H -> A. Loss of catalytic activity.
Glycogen storage disease type Ia: molecular diagnosis of 51 Japanese patients and characterization of splicing mutations by analysis of ectopically transcribed mRNA from lymphoblastoid cells.
Akanuma J.; Nishigaki T.; Fujii K.; Matsubara Y.; Inui K.; Takahashi K.; Kure S.; Suzuki Y.; Ohura T.; Miyabayashi S.; Ogawa E.; Iinuma K.; Okada S.; Narisawa K.;
Am. J. Med. Genet. 91:107-112(2000)
Cited for: VARIANTS GSD1A HIS-83; ASP-122; PRO-179 AND LEU-257;
Mutation spectrum of the glucose-6-phosphatase gene and its implication in molecular diagnosis of Korean patients with glycogen storage disease type Ia.
Ki C.S.; Han S.H.; Kim H.J.; Lee S.G.; Kim E.J.; Kim J.W.; Choe Y.H.; Seo J.K.; Chang Y.J.; Park J.Y.;
Clin. Genet. 65:487-489(2004)
Cited for: VARIANTS GSD1A ASP-122; ALA-178 AND ILE-255;
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.