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Protein

Glucokinase

Gene

GCK

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the initial step in utilization of glucose by the beta-cell and liver at physiological glucose concentration. Glucokinase has a high Km for glucose, and so it is effective only when glucose is abundant. The role of GCK is to provide G6P for the synthesis of glycogen. Pancreatic glucokinase plays an important role in modulating insulin secretion. Hepatic glucokinase helps to facilitate the uptake and conversion of glucose by acting as an insulin-sensitive determinant of hepatic glucose usage.7 Publications

Miscellaneous

In vertebrates there are four major glucose-phosphorylating isoenzymes, designated hexokinase I, II, III and IV (glucokinase).

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

The use of alternative promoters apparently enables the type IV hexokinase gene to be regulated by insulin in the liver and glucose in the beta cell. This may constitute an important feedback loop for maintaining glucose homeostasis. Subject to allosteric regulation. Low glucose and high fructose-6-phosphate triggers association with the inhibitor GKRP followed by sequestration in the nucleus.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei104ATPSequence analysis1
Binding sitei228ATPBy similarity1
Binding sitei231Substrate1
Binding sitei256Substrate1
Binding sitei290Substrate1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi78 – 83ATPBy similarity6
Nucleotide bindingi295 – 296ATPBy similarity2
Nucleotide bindingi332 – 336ATPBy similarity5
Nucleotide bindingi411 – 415ATPBy similarity5

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • fructokinase activity Source: GO_Central
  • glucokinase activity Source: UniProtKB
  • glucose binding Source: UniProtKB
  • mannokinase activity Source: GO_Central

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAllosteric enzyme, Kinase, Transferase
Biological processGlycolysis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
MetaCyc:HS02935-MONOMER

BRENDA Comprehensive Enzyme Information System

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BRENDAi
2.7.1.1 2681
2.7.1.2 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-170822 Regulation of Glucokinase by Glucokinase Regulatory Protein
R-HSA-210745 Regulation of gene expression in beta cells
R-HSA-5619073 Defective GCK causes maturity-onset diabetes of the young 2 (MODY2)
R-HSA-5619107 Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC)
R-HSA-70171 Glycolysis

SABIO-RK: Biochemical Reaction Kinetics Database

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SABIO-RKi
P35557

SIGNOR Signaling Network Open Resource

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SIGNORi
P35557

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Glucokinase (EC:2.7.1.27 Publications)
Alternative name(s):
Hexokinase type IV
Short name:
HK IV
Hexokinase-4
Short name:
HK4
Hexokinase-D
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:GCK
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 7

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000106633.15

Human Gene Nomenclature Database

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HGNCi
HGNC:4195 GCK

Online Mendelian Inheritance in Man (OMIM)

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MIMi
138079 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P35557

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Maturity-onset diabetes of the young 2 (MODY2)19 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of diabetes that is characterized by an autosomal dominant mode of inheritance, onset in childhood or early adulthood (usually before 25 years of age), a primary defect in insulin secretion and frequent insulin-independence at the beginning of the disease.
See also OMIM:125851
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_07943016V → E in MODY2. 1 Publication1
Natural variantiVAR_07943119I → N in MODY2. 1 Publication1
Natural variantiVAR_07943220L → P in MODY2. 1 Publication1
Natural variantiVAR_01058436R → W in MODY2. 3 PublicationsCorresponds to variant dbSNP:rs762263694EnsemblClinVar.1
Natural variantiVAR_07522043R → H in MODY2; unknown pathological significance; no change in glucokinase activity. 1 PublicationCorresponds to variant dbSNP:rs764232985EnsemblClinVar.1
Natural variantiVAR_07943543R → S in MODY2. 1 Publication1
Natural variantiVAR_07943644G → S in MODY2. 1 PublicationCorresponds to variant dbSNP:rs267601516Ensembl.1
Natural variantiVAR_01058553A → S in MODY2. 1
Natural variantiVAR_07943861 – 465Missing in MODY2. 1 PublicationAdd BLAST405
Natural variantiVAR_07943961Y → S in MODY2; decreased glucokinase activity; decreased affinity for glucose; increased affinity for ATP. 2 Publications1
Natural variantiVAR_07522168G → D in MODY2; unknown pathological significance; mildly increases glucokinase activity. 1 PublicationCorresponds to variant dbSNP:rs373418736Ensembl.1
Natural variantiVAR_00369370E → K in MODY2; decreased affinity for glucose. 2 Publications1
Natural variantiVAR_07944177L → P in MODY2. 1 Publication1
Natural variantiVAR_07944278D → E in MODY2. 1 Publication1
Natural variantiVAR_00369480G → A in MODY2. 1
Natural variantiVAR_07944380G → D in MODY2. 1 Publication1
Natural variantiVAR_00369580G → S in MODY2. 1 Publication1
Natural variantiVAR_07944482T → I in MODY2. 1 Publication1
Natural variantiVAR_010586108Y → H in MODY2. 2 Publications1
Natural variantiVAR_012352110I → T in MODY2. 1 PublicationCorresponds to variant dbSNP:rs1338970607Ensembl.1
Natural variantiVAR_079445116T → P in MODY2. 1 Publication1
Natural variantiVAR_012353119A → D in MODY2. 1 PublicationCorresponds to variant dbSNP:rs1176659689Ensembl.1
Natural variantiVAR_078246129C → Y in MODY2. 1 Publication1
Natural variantiVAR_003697131S → P in MODY2; decreased affinity for glucose. 2 PublicationsCorresponds to variant dbSNP:rs104894010EnsemblClinVar.1
Natural variantiVAR_010587137H → R in MODY2. 1
Natural variantiVAR_010588150F → S in MODY2. 1 PublicationCorresponds to variant dbSNP:rs193922297EnsemblClinVar.1
Natural variantiVAR_078247152F → L in MODY2; unknown pathological significance. 1 Publication1
Natural variantiVAR_079447160D → N in MODY2; no effect on stability; decreased glucokinase activity; decreased affinity for glucose. 1 Publication1
Natural variantiVAR_010589168T → P in MODY2. 1
Natural variantiVAR_003698175G → R in MODY2. Corresponds to variant dbSNP:rs587780344EnsemblClinVar.1
Natural variantiVAR_079450182V → L in MODY2; decreased glucokinase activity; decreased affinity for glucose; increased affinity for ATP. 2 Publications1
Natural variantiVAR_003699182V → M in MODY2. Corresponds to variant dbSNP:rs587780345EnsemblClinVar.1
Natural variantiVAR_079452187D → Y in MODY2. 1 Publication1
Natural variantiVAR_003700188A → T in MODY2; decreased affinity for glucose. 1 PublicationCorresponds to variant dbSNP:rs751279776Ensembl.1
Natural variantiVAR_078248188A → V in MODY2. 1 PublicationCorresponds to variant dbSNP:rs193922307EnsemblClinVar.1
Natural variantiVAR_078249191R → W in MODY2. 2 PublicationsCorresponds to variant dbSNP:rs1085307455Ensembl.1
Natural variantiVAR_079453200V → L in MODY2. 1 Publication1
Natural variantiVAR_078250202M → R in MODY2. 1 Publication1
Natural variantiVAR_079454202M → T in MODY2. 1 PublicationCorresponds to variant dbSNP:rs193922311EnsemblClinVar.1
Natural variantiVAR_003701203V → A in MODY2. 1
Natural variantiVAR_079455206T → M in MODY2. 1 PublicationCorresponds to variant dbSNP:rs1441649062Ensembl.1
Natural variantiVAR_010590209T → M in MODY2. 2 Publications1
Natural variantiVAR_010591210M → T in MODY2. 1
Natural variantiVAR_010592213C → R in MODY2. 1
Natural variantiVAR_075222217D → N in MODY2; associated in cis with R-261 in some patients; mildly increased glucokinase activity; loss of glucokinase activity when associated with R-261. 1 PublicationCorresponds to variant dbSNP:rs147065275Ensembl.1
Natural variantiVAR_003702221E → K in MODY2. 1 PublicationCorresponds to variant dbSNP:rs193922317EnsemblClinVar.1
Natural variantiVAR_078251223G → S in MODY2. 2 Publications1
Natural variantiVAR_079457224M → R in MODY2. 1 Publication1
Natural variantiVAR_075223225I → M in MODY2; associated in cis with K-248; highly decreased glucokinase activity; loss of glucokinase activity when associated with K-248. 1 Publication1
Natural variantiVAR_003703226V → M in MODY2; no effect on stability; decreased glucokinase activity; decreased affinity for glucose. 2 PublicationsCorresponds to variant dbSNP:rs148311934EnsemblClinVar.1
Natural variantiVAR_003704227G → C in MODY2. 1 Publication1
Natural variantiVAR_079458227G → S in MODY2. 1 Publication1
Natural variantiVAR_078252231N → H in MODY2; unknown pathological significance. 1 Publication1
Natural variantiVAR_079459233C → R in MODY2; loss of glucokinase activity; loss of affinity for glucose; loss of affinity for ATP. 2 Publications1
Natural variantiVAR_079460234 – 465Missing in MODY2. 1 PublicationAdd BLAST232
Natural variantiVAR_075224248E → K in MODY2; associated in cis with M-225; highly decreased glucokinase activity; loss of glucokinase activity when associated with M-225. 1 PublicationCorresponds to variant dbSNP:rs759421263Ensembl.1
Natural variantiVAR_079461252C → G in MODY2. 1 Publication1
Natural variantiVAR_079462255T → A in MODY2. 1 Publication1
Natural variantiVAR_003706256E → K in MODY2. 1 PublicationCorresponds to variant dbSNP:rs769268803EnsemblClinVar.1
Natural variantiVAR_003707257W → R in MODY2; almost complete loss of glucokinase activity. 1 Publication1
Natural variantiVAR_010593259A → T in MODY2. 1 PublicationCorresponds to variant dbSNP:rs1375656631Ensembl.1
Natural variantiVAR_010594261G → E in MODY2. 1 Publication1
Natural variantiVAR_079463265E → K in MODY2; decreased glucokinase activity; decreased affinity for glucose; no effect on affinity for ATP. 2 Publications1
Natural variantiVAR_003709279E → Q in MODY2. Corresponds to variant dbSNP:rs104894005EnsemblClinVar.1
Natural variantiVAR_079464298M → K in MODY2. 1 Publication1
Natural variantiVAR_003710299G → R in MODY2. 2 PublicationsCorresponds to variant dbSNP:rs104894009EnsemblClinVar.1
Natural variantiVAR_003712300E → K in MODY2. Corresponds to variant dbSNP:rs1255911887Ensembl.1
Natural variantiVAR_003711300E → Q in MODY2. 1
Natural variantiVAR_079465308R → W in MODY2. 1 Publication1
Natural variantiVAR_003713309L → P in MODY2. 1
Natural variantiVAR_078253315L → F in MODY2; unknown pathological significance. 1 Publication1
Natural variantiVAR_010595336S → L in MODY2. 1
Natural variantiVAR_010596367V → M in MODY2. Corresponds to variant dbSNP:rs1057521092Ensembl.1
Natural variantiVAR_079466377R → H in MODY2. 1 PublicationCorresponds to variant dbSNP:rs193922264EnsemblClinVar.1
Natural variantiVAR_078254378A → T in MODY2. 1 PublicationCorresponds to variant dbSNP:rs104894016EnsemblClinVar.1
Natural variantiVAR_079467379A → V in MODY2; decreased glucokinase activity; decreased affinity for glucose; decreased affinity for ATP. 2 Publications1
Natural variantiVAR_010597382C → Y in MODY2. 1 Publication1
Natural variantiVAR_079468383S → L in MODY2. 1 PublicationCorresponds to variant dbSNP:rs777870079Ensembl.1
Natural variantiVAR_010598384A → T in MODY2. 1 PublicationCorresponds to variant dbSNP:rs1376620210Ensembl.1
Natural variantiVAR_012354385G → V in MODY2. 1 Publication1
Natural variantiVAR_010599392R → C in MODY2. 1 PublicationCorresponds to variant dbSNP:rs1167124132Ensembl.1
Natural variantiVAR_079471399 – 465Missing in MODY2. 1 PublicationAdd BLAST67
Natural variantiVAR_079472411S → F in MODY2. 1 Publication1
Natural variantiVAR_003714414K → E in MODY2; decreased affinity for glucose. 1 PublicationCorresponds to variant dbSNP:rs193922272EnsemblClinVar.1
Natural variantiVAR_079473416H → P in MODY2. 1 Publication1
Natural variantiVAR_079474420K → E in MODY2; no effect on glucokinase activity; decreased affinity for glucose; no effect on affinity for ATP. 2 Publications1
Natural variantiVAR_078255434C → F in MODY2; unknown pathological significance. 1 Publication1
Natural variantiVAR_078256441S → W in MODY2; decreased affinity for glucose. 3 Publications1
Natural variantiVAR_078258447R → Q in MODY2. 1 PublicationCorresponds to variant dbSNP:rs1131691416Ensembl.1
Familial hyperinsulinemic hypoglycemia 3 (HHF3)8 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionMost common cause of persistent hypoglycemia in infancy. Unless early and aggressive intervention is undertaken, brain damage from recurrent episodes of hypoglycemia may occur.
See also OMIM:602485
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07824365T → I in HHF3; increased glucokinase activity based on measure of catalytic efficiency; increased affinity for glucose; loss of inhibition by GKRP; unchanged affinity for ATP. 3 Publications1
Natural variantiVAR_07824491V → L in HHF3; increased glucokinase activity; increased affinity for glucose. 2 Publications1
Natural variantiVAR_07824599W → C in HHF3; increased glucokinase activity; increased affinity for glucose; increased affinity for ATP. 1 Publication1
Natural variantiVAR_079456214Y → C in HHF3; increased glucokinase activity based on measure of catalytic efficiency; increased affinity for glucose; decreased inhibition by GKRP. 2 PublicationsCorresponds to variant dbSNP:rs104894015EnsemblClinVar.1
Natural variantiVAR_078257442E → K in HHF3; increased affinity for glucose. 2 PublicationsCorresponds to variant dbSNP:rs758737171EnsemblClinVar.1
Natural variantiVAR_003715455V → M in HHF3; increased glucokinase activity based on measure of catalytic efficiency; increased affinity for glucose; decreased inhibition by GKRP; no effect on affinity for ATP. 2 PublicationsCorresponds to variant dbSNP:rs104894012EnsemblClinVar.1
Natural variantiVAR_079477456A → V in HHF3; increased glucokinase activity based on measure of catalytic efficiency; increased affinity for glucose; loss of inhibition by GKRP; no effect on affinity for ATP. 2 PublicationsCorresponds to variant dbSNP:rs104894014EnsemblClinVar.1
Diabetes mellitus, non-insulin-dependent (NIDDM)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to the body's own insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels.
See also OMIM:125853
Diabetes mellitus, permanent neonatal (PNDM)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare form of diabetes distinct from childhood-onset autoimmune diabetes mellitus type 1. It is characterized by insulin-requiring hyperglycemia that is diagnosed within the first months of life. Permanent neonatal diabetes requires lifelong therapy.
See also OMIM:606176
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07943340E → K in PNDM; decreased stability; decreased glucokinase activity; decreased affinity for glucose. 1 PublicationCorresponds to variant dbSNP:rs794727236EnsemblClinVar.1
Natural variantiVAR_07943443R → C in PNDM; decreased stability; decreased glucokinase activity; no effect on affinity for glucose. 1 PublicationCorresponds to variant dbSNP:rs1486280029Ensembl.1
Natural variantiVAR_07943750H → D in PNDM; loss of stability; loss of glucokinase activity; decreased affinity for glucose. 1 Publication1
Natural variantiVAR_079446151S → T in PNDM. 1 Publication1
Natural variantiVAR_079448168T → A in PNDM; decreased glucokinase activity; decreased affinity for glucose. 1 Publication1
Natural variantiVAR_079449169K → R in PNDM. 1 Publication1
Natural variantiVAR_079469393M → T in PNDM; decreased stability; increased glucokinase activity; no effect on affinity for glucose. 1 Publication1
Natural variantiVAR_079470397R → L in PNDM; decreased stability; increased glucokinase activity; no effect on affinity for glucose. 1 PublicationCorresponds to variant dbSNP:rs193929375EnsemblClinVar.1
Natural variantiVAR_079475441S → L in PNDM; decreased stability; decreased glucokinase activity; no effect on affinity for glucose. 1 PublicationCorresponds to variant dbSNP:rs1286804191Ensembl.1
Natural variantiVAR_079476449A → T in PNDM; decreased stability; increased glucokinase activity; increased affinity for glucose. 1 PublicationCorresponds to variant dbSNP:rs193922282EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi64S → P: Increased glucokinase activity based on measure of catalytic efficiency. Increased affinity for glucose. 1 Publication1
Mutagenesisi177E → K: Small change in glucokinase activity. 1 Publication1
Mutagenesisi197M → V: Increased glucokinase activity based on measure of catalytic efficiency. Increased affinity for glucose. 1 Publication1
Mutagenesisi211I → F: Increased glucokinase activity based on measure of catalytic efficiency. Increased affinity for glucose. 1 Publication1
Mutagenesisi214Y → A: Increased glucokinase activity based on measure of catalytic efficiency. Increased affinity for glucose. No effect on affinity for ATP. 1 Publication1
Mutagenesisi215Y → A: Increased glucokinase activity based on measure of catalytic efficiency. Increased affinity for glucose. Loss of inhibition by GKRP. No effect on affinity for ATP. 1 Publication1
Mutagenesisi256E → A: Inactive enzyme with no glucokinase activity. 1 Publication1
Mutagenesisi414K → A: Small change in glucokinase activity. 1 Publication1
Mutagenesisi453S → A: Increased glucokinase activity based on measure of catalytic efficiency. Increased affinity for glucose. 1 Publication1

Keywords - Diseasei

Diabetes mellitus, Disease mutation

Organism-specific databases

DisGeNET

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DisGeNETi
2645

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
GCK

MalaCards human disease database

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MalaCardsi
GCK
MIMi125851 phenotype
125853 phenotype
602485 phenotype
606176 phenotype
606391 phenotype

Open Targets

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OpenTargetsi
ENSG00000106633

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
79299 Hyperinsulinism due to glucokinase deficiency
552 MODY
99885 Permanent neonatal diabetes mellitus

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA28610

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL3820

Drug and drug target database

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DrugBanki
DB02379 Beta-D-Glucose

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
2798

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
GCK

Domain mapping of disease mutations (DMDM)

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DMDMi
547696

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001975931 – 465GlucokinaseAdd BLAST465

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P35557

PeptideAtlas

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PeptideAtlasi
P35557

PRoteomics IDEntifications database

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PRIDEi
P35557

ProteomicsDB human proteome resource

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ProteomicsDBi
55084
55085 [P35557-2]
55086 [P35557-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P35557

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P35557

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Isoform 1 is expressed in pancreas. Isoform 2 and isoform 3 is expressed in liver.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000106633 Expressed in 96 organ(s), highest expression level in liver

CleanEx database of gene expression profiles

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CleanExi
HS_GCK

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P35557 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P35557 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA007034
HPA007093

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer (PubMed:15016359, PubMed:19362831, PubMed:23957911). Interacts with MIDN; the interaction occurs preferentially at low glucose levels and results in inhibition of GCK activity (PubMed:24187134).4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
108915, 10 interactors

Protein interaction database and analysis system

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IntActi
P35557, 6 interactors

STRING: functional protein association networks

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STRINGi
9606.ENSP00000223366

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P35557

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1465
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P35557

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P35557

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P35557

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini10 – 454HexokinasePROSITE-ProRule annotationAdd BLAST445

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni67 – 203Hexokinase small subdomainPROSITE-ProRule annotationAdd BLAST137
Regioni151 – 152Substrate binding2
Regioni168 – 169Substrate binding2
Regioni204 – 443Hexokinase large subdomainPROSITE-ProRule annotationAdd BLAST240
Regioni204 – 205Substrate binding2

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the hexokinase family.PROSITE-ProRule annotationCurated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1369 Eukaryota
COG5026 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000153555

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000162670

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG000142

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P35557

KEGG Orthology (KO)

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KOi
K12407

Identification of Orthologs from Complete Genome Data

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OMAi
ASHYVNP

Database of Orthologous Groups

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OrthoDBi
EOG091G08MD

Database for complete collections of gene phylogenies

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PhylomeDBi
P35557

TreeFam database of animal gene trees

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TreeFami
TF314238

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR039073 GCK_chordate
IPR001312 Hexokinase
IPR019807 Hexokinase_BS
IPR022673 Hexokinase_C
IPR022672 Hexokinase_N

The PANTHER Classification System

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PANTHERi
PTHR19443 PTHR19443, 1 hit
PTHR19443:SF3 PTHR19443:SF3, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00349 Hexokinase_1, 1 hit
PF03727 Hexokinase_2, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00378 HEXOKINASE_1, 1 hit
PS51748 HEXOKINASE_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P35557-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MLDDRARMEA AKKEKVEQIL AEFQLQEEDL KKVMRRMQKE MDRGLRLETH
60 70 80 90 100
EEASVKMLPT YVRSTPEGSE VGDFLSLDLG GTNFRVMLVK VGEGEEGQWS
110 120 130 140 150
VKTKHQMYSI PEDAMTGTAE MLFDYISECI SDFLDKHQMK HKKLPLGFTF
160 170 180 190 200
SFPVRHEDID KGILLNWTKG FKASGAEGNN VVGLLRDAIK RRGDFEMDVV
210 220 230 240 250
AMVNDTVATM ISCYYEDHQC EVGMIVGTGC NACYMEEMQN VELVEGDEGR
260 270 280 290 300
MCVNTEWGAF GDSGELDEFL LEYDRLVDES SANPGQQLYE KLIGGKYMGE
310 320 330 340 350
LVRLVLLRLV DENLLFHGEA SEQLRTRGAF ETRFVSQVES DTGDRKQIYN
360 370 380 390 400
ILSTLGLRPS TTDCDIVRRA CESVSTRAAH MCSAGLAGVI NRMRESRSED
410 420 430 440 450
VMRITVGVDG SVYKLHPSFK ERFHASVRRL TPSCEITFIE SEEGSGRGAA
460
LVSAVACKKA CMLGQ
Length:465
Mass (Da):52,191
Last modified:June 1, 1994 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i094D4A2F78096724
GO
Isoform 2 (identifier: P35557-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MLDDRARMEAAKKEK → MAMDVTRSQAQTALTL

Show »
Length:466
Mass (Da):52,136
Checksum:iA44B768452105627
GO
Isoform 3 (identifier: P35557-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MLDDRARMEAAKKEK → MPRPRSQLPQPNSQ

Show »
Length:464
Mass (Da):52,035
Checksum:i5FA1020BBF98A4E9
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
C9JQD1C9JQD1_HUMAN
Phosphotransferase
GCK
448Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H7BXV0H7BXV0_HUMAN
Phosphotransferase
GCK
149Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0036924D → N1 PublicationCorresponds to variant dbSNP:rs202091228Ensembl.1
Natural variantiVAR_01058311A → T1 PublicationCorresponds to variant dbSNP:rs116093166EnsemblClinVar.1
Natural variantiVAR_07943016V → E in MODY2. 1 Publication1
Natural variantiVAR_07943119I → N in MODY2. 1 Publication1
Natural variantiVAR_07943220L → P in MODY2. 1 Publication1
Natural variantiVAR_01058436R → W in MODY2. 3 PublicationsCorresponds to variant dbSNP:rs762263694EnsemblClinVar.1
Natural variantiVAR_07943340E → K in PNDM; decreased stability; decreased glucokinase activity; decreased affinity for glucose. 1 PublicationCorresponds to variant dbSNP:rs794727236EnsemblClinVar.1
Natural variantiVAR_07943443R → C in PNDM; decreased stability; decreased glucokinase activity; no effect on affinity for glucose. 1 PublicationCorresponds to variant dbSNP:rs1486280029Ensembl.1
Natural variantiVAR_07522043R → H in MODY2; unknown pathological significance; no change in glucokinase activity. 1 PublicationCorresponds to variant dbSNP:rs764232985EnsemblClinVar.1
Natural variantiVAR_07943543R → S in MODY2. 1 Publication1
Natural variantiVAR_07943644G → S in MODY2. 1 PublicationCorresponds to variant dbSNP:rs267601516Ensembl.1
Natural variantiVAR_07943750H → D in PNDM; loss of stability; loss of glucokinase activity; decreased affinity for glucose. 1 Publication1
Natural variantiVAR_01058553A → S in MODY2. 1
Natural variantiVAR_07943861 – 465Missing in MODY2. 1 PublicationAdd BLAST405
Natural variantiVAR_07943961Y → S in MODY2; decreased glucokinase activity; decreased affinity for glucose; increased affinity for ATP. 2 Publications1
Natural variantiVAR_07824365T → I in HHF3; increased glucokinase activity based on measure of catalytic efficiency; increased affinity for glucose; loss of inhibition by GKRP; unchanged affinity for ATP. 3 Publications1
Natural variantiVAR_07522168G → D in MODY2; unknown pathological significance; mildly increases glucokinase activity. 1 PublicationCorresponds to variant dbSNP:rs373418736Ensembl.1
Natural variantiVAR_00369370E → K in MODY2; decreased affinity for glucose. 2 Publications1
Natural variantiVAR_07944072G → R in MODY2 and PNDM; decreased stability; no effect on glucokinase activity; no effect on affinity for glucose. 2 PublicationsCorresponds to variant dbSNP:rs193922289EnsemblClinVar.1
Natural variantiVAR_07944177L → P in MODY2. 1 Publication1
Natural variantiVAR_07944278D → E in MODY2. 1 Publication1
Natural variantiVAR_00369480G → A in MODY2. 1
Natural variantiVAR_07944380G → D in MODY2. 1 Publication1
Natural variantiVAR_00369580G → S in MODY2. 1 Publication1
Natural variantiVAR_07944482T → I in MODY2. 1 Publication1
Natural variantiVAR_07824491V → L in HHF3; increased glucokinase activity; increased affinity for glucose. 2 Publications1
Natural variantiVAR_07824599W → C in HHF3; increased glucokinase activity; increased affinity for glucose; increased affinity for ATP. 1 Publication1
Natural variantiVAR_003696107M → T2 Publications1
Natural variantiVAR_010586108Y → H in MODY2. 2 Publications1
Natural variantiVAR_012352110I → T in MODY2. 1 PublicationCorresponds to variant dbSNP:rs1338970607Ensembl.1
Natural variantiVAR_079445116T → P in MODY2. 1 Publication1
Natural variantiVAR_012353119A → D in MODY2. 1 PublicationCorresponds to variant dbSNP:rs1176659689Ensembl.1
Natural variantiVAR_078246129C → Y in MODY2. 1 Publication1
Natural variantiVAR_003697131S → P in MODY2; decreased affinity for glucose. 2 PublicationsCorresponds to variant dbSNP:rs104894010EnsemblClinVar.1
Natural variantiVAR_010587137H → R in MODY2. 1
Natural variantiVAR_010588150F → S in MODY2. 1 PublicationCorresponds to variant dbSNP:rs193922297EnsemblClinVar.1
Natural variantiVAR_079446151S → T in PNDM. 1 Publication1
Natural variantiVAR_078247152F → L in MODY2; unknown pathological significance. 1 Publication1
Natural variantiVAR_079447160D → N in MODY2; no effect on stability; decreased glucokinase activity; decreased affinity for glucose. 1 Publication1
Natural variantiVAR_012350164L → P in MODY2 and PNDM. 2 Publications1
Natural variantiVAR_079448168T → A in PNDM; decreased glucokinase activity; decreased affinity for glucose. 1 Publication1
Natural variantiVAR_010589168T → P in MODY2. 1
Natural variantiVAR_079449169K → R in PNDM. 1 Publication1
Natural variantiVAR_003698175G → R in MODY2. Corresponds to variant dbSNP:rs587780344EnsemblClinVar.1
Natural variantiVAR_079450182V → L in MODY2; decreased glucokinase activity; decreased affinity for glucose; increased affinity for ATP. 2 Publications1
Natural variantiVAR_003699182V → M in MODY2. Corresponds to variant dbSNP:rs587780345EnsemblClinVar.1
Natural variantiVAR_079451186 – 465Missing in MODY2 and NIDDM. 2 PublicationsAdd BLAST280
Natural variantiVAR_079452187D → Y in MODY2. 1 Publication1
Natural variantiVAR_003700188A → T in MODY2; decreased affinity for glucose. 1 PublicationCorresponds to variant dbSNP:rs751279776Ensembl.1
Natural variantiVAR_078248188A → V in MODY2. 1 PublicationCorresponds to variant dbSNP:rs193922307EnsemblClinVar.1
Natural variantiVAR_078249191R → W in MODY2. 2 PublicationsCorresponds to variant dbSNP:rs1085307455Ensembl.1
Natural variantiVAR_079453200V → L in MODY2. 1 Publication1
Natural variantiVAR_078250202M → R in MODY2. 1 Publication1
Natural variantiVAR_079454202M → T in MODY2. 1 PublicationCorresponds to variant dbSNP:rs193922311EnsemblClinVar.1
Natural variantiVAR_003701203V → A in MODY2. 1
Natural variantiVAR_079455206T → M in MODY2. 1 PublicationCorresponds to variant dbSNP:rs1441649062Ensembl.1
Natural variantiVAR_010590209T → M in MODY2. 2 Publications1
Natural variantiVAR_012351210M → K in MODY2 and PNDM. 1 PublicationCorresponds to variant dbSNP:rs80356654EnsemblClinVar.1
Natural variantiVAR_010591210M → T in MODY2. 1
Natural variantiVAR_010592213C → R in MODY2. 1
Natural variantiVAR_079456214Y → C in HHF3; increased glucokinase activity based on measure of catalytic efficiency; increased affinity for glucose; decreased inhibition by GKRP. 2 PublicationsCorresponds to variant dbSNP:rs104894015EnsemblClinVar.1
Natural variantiVAR_075222217D → N in MODY2; associated in cis with R-261 in some patients; mildly increased glucokinase activity; loss of glucokinase activity when associated with R-261. 1 PublicationCorresponds to variant dbSNP:rs147065275Ensembl.1
Natural variantiVAR_003702221E → K in MODY2. 1 PublicationCorresponds to variant dbSNP:rs193922317EnsemblClinVar.1
Natural variantiVAR_078251223G → S in MODY2. 2 Publications1
Natural variantiVAR_079457224M → R in MODY2. 1 Publication1
Natural variantiVAR_075223225I → M in MODY2; associated in cis with K-248; highly decreased glucokinase activity; loss of glucokinase activity when associated with K-248. 1 Publication1
Natural variantiVAR_003703226V → M in MODY2; no effect on stability; decreased glucokinase activity; decreased affinity for glucose. 2 PublicationsCorresponds to variant dbSNP:rs148311934EnsemblClinVar.1
Natural variantiVAR_003704227G → C in MODY2. 1 Publication1
Natural variantiVAR_079458227G → S in MODY2. 1 Publication1
Natural variantiVAR_003705228T → M in MODY2 and PNDM. 3 PublicationsCorresponds to variant dbSNP:rs80356655Ensembl