Variant position: 442 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 465 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 RFHASVRRLTPSCEITFIES EEGSGRGAALVSAVACKKACM
Mouse RFHASVRRLTPNCEITFIES EEGSGRGAALVSAVACKKACM
Rat RFHASVRRLTPNCEITFIES EEGSGRGAALVSAVACKKACM
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 – 465 Hexokinase-4
10 – 454 Hexokinase
204 – 443 Hexokinase large subdomain
453 – 453 S -> A. Increased glucokinase activity based on measure of catalytic efficiency. Increased affinity for glucose.
Opposite clinical phenotypes of glucokinase disease: Description of a novel activating mutation and contiguous inactivating mutations in human glucokinase (GCK) gene.
Barbetti F.; Cobo-Vuilleumier N.; Dionisi-Vici C.; Toni S.; Ciampalini P.; Massa O.; Rodriguez-Bada P.; Colombo C.; Lenzi L.; Garcia-Gimeno M.A.; Bermudez-Silva F.J.; Rodriguez de Fonseca F.; Banin P.; Aledo J.C.; Baixeras E.; Sanz P.; Cuesta-Munoz A.L.;
Mol. Endocrinol. 23:1983-1989(2009)
Cited for: VARIANT MODY2 TRP-441; CHARACTERIZATION OF VARIANT MODY2 TRP-441; VARIANT HHF3 LYS-442; CHARACTERIZATION OF VARIANT HHF3 LYS-442;
Heterogeneity in phenotype of hyperinsulinism caused by activating glucokinase mutations: a novel mutation and its functional characterization.
Martinez R.; Gutierrez-Nogues A.; Fernandez-Ramos C.; Velayos T.; Vela A.; Navas M.A.; Castano L.;
Clin. Endocrinol. (Oxf.) 86:778-783(2017)
Cited for: VARIANTS HHF3 ILE-65; LEU-91; CYS-99 AND LYS-442; CHARACTERIZATION OF VARIANT HHF3 CYS-99;
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.