Variant position: 223 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 VNDTVATMISCYYEDHQCEV GMIVGTGCNACYMEEMQNVEL
Mouse VNDTVATMISCYYEDRQCEV GMIVGTGCNACYMEEMQNVEL
Rat VNDTVATMISCYYEDRQCEV GMIVGTGCNACYMEEMQNVEL
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
228 – 228 ATP
231 – 231 Substrate
211 – 211 I -> F. Increased glucokinase activity based on measure of catalytic efficiency. Increased affinity for glucose.
214 – 214 Y -> A. Increased glucokinase activity based on measure of catalytic efficiency. Increased affinity for glucose. No effect on affinity for ATP.
215 – 215 Y -> A. Increased glucokinase activity based on measure of catalytic efficiency. Increased affinity for glucose. Loss of inhibition by GCKR. No effect on affinity for ATP.
220 – 237
Identification of novel and recurrent glucokinase mutations in Belgian and Luxembourg maturity onset diabetes of the young patients.
Vits L.; Beckers D.; Craen M.; de Beaufort C.; Vanfleteren E.; Dahan K.; Nollet A.; Vanhaverbeke G.; Imschoot S.V.; Bourguignon J.P.; Beauloye V.; Storm K.; Massa G.; Giri M.; Nobels F.; De Schepper J.; Rooman R.; Van den Bruel A.; Mathieu C.; Wuyts W.;
Clin. Genet. 70:355-359(2006)
Cited for: VARIANTS MODY2 TRP-36; TYR-129; LEU-152; VAL-188; TRP-191; ARG-202; SER-223; MET-226; HIS-231; PHE-315; THR-378; PHE-434; TRP-441 AND GLN-447;
Mutations in GCK and HNF-1alpha explain the majority of cases with clinical diagnosis of MODY in Spain.
Estalella I.; Rica I.; Perez de Nanclares G.; Bilbao J.R.; Vazquez J.A.; San Pedro J.I.; Busturia M.A.; Castano L.;
Clin. Endocrinol. (Oxf.) 67:538-546(2007)
Cited for: VARIANTS MODY2 GLU-16; ASN-19; PRO-20; TRP-36; SER-43; SER-44; 61-TYR--GLN-465 DEL; SER-61; LYS-70; ARG-72; PRO-77; GLU-78; ASP-80; ILE-82; HIS-108; PRO-116; LEU-182; 186-ARG--GLN-465 DEL; TYR-187; TRP-191; LEU-200; THR-202; MET-206; MET-209; SER-223; ARG-224; SER-227; MET-228; ARG-233; 234-TYR--GLN-465 DEL; GLY-252; ALA-255; LYS-256; ARG-261; LYS-265; LYS-298; TRP-308; HIS-377; VAL-379; LEU-383; 399-GLU--GLN-465 DEL; PHE-411; PRO-416; GLU-420 AND TRP-441;
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.