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P35557

- HXK4_HUMAN

UniProt

P35557 - HXK4_HUMAN

Protein

Glucokinase

Gene

GCK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      Previous versions | rss
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    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.

    Catalytic activityi

    ATP + D-glucose = ADP + D-glucose 6-phosphate.

    Enzyme 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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei104 – 1041ATPSequence Analysis
    Binding sitei228 – 2281ATPBy similarity
    Binding sitei231 – 2311Substrate
    Binding sitei256 – 2561Substrate
    Binding sitei290 – 2901Substrate

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi78 – 836ATPBy similarity
    Nucleotide bindingi295 – 2962ATPBy similarity
    Nucleotide bindingi332 – 3365ATPBy similarity
    Nucleotide bindingi411 – 4155ATPBy similarity

    GO - Molecular functioni

    1. ADP binding Source: Ensembl
    2. ATP binding Source: UniProtKB
    3. glucokinase activity Source: UniProtKB
    4. glucose binding Source: UniProtKB
    5. magnesium ion binding Source: Ensembl
    6. protein binding Source: UniProtKB

    GO - Biological processi

    1. calcium ion import Source: Ensembl
    2. carbohydrate metabolic process Source: Reactome
    3. cellular glucose homeostasis Source: RefGenome
    4. cellular response to glucose starvation Source: Ensembl
    5. cellular response to insulin stimulus Source: BHF-UCL
    6. cellular response to leptin stimulus Source: BHF-UCL
    7. detection of glucose Source: UniProtKB
    8. endocrine pancreas development Source: Reactome
    9. fructose 2,6-bisphosphate metabolic process Source: Ensembl
    10. glucose homeostasis Source: UniProtKB
    11. glucose metabolic process Source: Ensembl
    12. glucose transport Source: Reactome
    13. glycogen biosynthetic process Source: Ensembl
    14. glycolytic process Source: UniProtKB-KW
    15. hexose transport Source: Reactome
    16. NADP metabolic process Source: Ensembl
    17. negative regulation of epinephrine secretion Source: Ensembl
    18. negative regulation of gluconeogenesis Source: UniProtKB
    19. positive regulation of cytosolic calcium ion concentration Source: Ensembl
    20. positive regulation of glycogen biosynthetic process Source: UniProtKB
    21. positive regulation of glycolytic process Source: Ensembl
    22. positive regulation of insulin secretion Source: UniProtKB
    23. positive regulation of phosphorylation Source: Ensembl
    24. regulation of glucose transport Source: Reactome
    25. regulation of glycolytic process Source: BHF-UCL
    26. regulation of insulin secretion Source: BHF-UCL
    27. regulation of potassium ion transport Source: Ensembl
    28. second-messenger-mediated signaling Source: Ensembl
    29. small molecule metabolic process Source: Reactome
    30. transmembrane transport Source: Reactome

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS02935-MONOMER.
    ReactomeiREACT_13819. Regulation of gene expression in beta cells.
    REACT_212. Glucose transport.
    REACT_6804. Regulation of Glucokinase by Glucokinase Regulatory Protein.
    SABIO-RKP35557.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glucokinase (EC:2.7.1.2)
    Alternative name(s):
    Hexokinase type IV
    Short name:
    HK IV
    Hexokinase-4
    Short name:
    HK4
    Hexokinase-D
    Gene namesi
    Name:GCK
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:4195. GCK.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication
    Note: Under low glucose concentrations, GCK associates with GKRP and the inactive complex is recruited to the hepatocyte nucleus.

    GO - Cellular componenti

    1. cell cortex Source: Ensembl
    2. cytosol Source: Reactome
    3. mitochondrion Source: Ensembl
    4. nucleoplasm Source: Reactome
    5. secretory granule Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Maturity-onset diabetes of the young 2 (MODY2) [MIM:125851]: A 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.12 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti36 – 361R → W in MODY2. 1 Publication
    VAR_010584
    Natural varianti53 – 531A → S in MODY2.
    VAR_010585
    Natural varianti70 – 701E → K in MODY2; large increase in Km for glucose. 1 Publication
    VAR_003693
    Natural varianti80 – 801G → A in MODY2.
    VAR_003694
    Natural varianti80 – 801G → S in MODY2. 1 Publication
    VAR_003695
    Natural varianti108 – 1081Y → H in MODY2. 1 Publication
    VAR_010586
    Natural varianti110 – 1101I → T in MODY2. 1 Publication
    VAR_012352
    Natural varianti119 – 1191A → D in MODY2. 1 Publication
    VAR_012353
    Natural varianti131 – 1311S → P in MODY2; significant increase in the Km and in the affinity for ATP. 2 Publications
    VAR_003697
    Natural varianti137 – 1371H → R in MODY2.
    VAR_010587
    Natural varianti150 – 1501F → S in MODY2. 1 Publication
    VAR_010588
    Natural varianti164 – 1641L → P in MODY2. 1 Publication
    VAR_012350
    Natural varianti168 – 1681T → P in MODY2.
    VAR_010589
    Natural varianti175 – 1751G → R in MODY2.
    VAR_003698
    Natural varianti182 – 1821V → M in MODY2.
    VAR_003699
    Natural varianti188 – 1881A → T in MODY2; large increase in Km for glucose. 1 Publication
    VAR_003700
    Natural varianti203 – 2031V → A in MODY2.
    VAR_003701
    Natural varianti209 – 2091T → M in MODY2. 1 Publication
    VAR_010590
    Natural varianti210 – 2101M → K in MODY2. 1 Publication
    VAR_012351
    Natural varianti210 – 2101M → T in MODY2.
    VAR_010591
    Natural varianti213 – 2131C → R in MODY2.
    VAR_010592
    Natural varianti221 – 2211E → K in MODY2. 1 Publication
    VAR_003702
    Natural varianti226 – 2261V → M in MODY2.
    VAR_003703
    Natural varianti227 – 2271G → C in MODY2. 1 Publication
    VAR_003704
    Natural varianti228 – 2281T → M in MODY2. 2 Publications
    VAR_003705
    Natural varianti256 – 2561E → K in MODY2.
    VAR_003706
    Natural varianti257 – 2571W → R in MODY2; almost complete loss of activity. 1 Publication
    VAR_003707
    Natural varianti259 – 2591A → T in MODY2. 1 Publication
    VAR_010593
    Natural varianti261 – 2611G → E in MODY2. 1 Publication
    VAR_010594
    Natural varianti261 – 2611G → R in MODY2. 2 Publications
    VAR_003708
    Natural varianti279 – 2791E → Q in MODY2.
    Corresponds to variant rs104894005 [ dbSNP | Ensembl ].
    VAR_003709
    Natural varianti299 – 2991G → R in MODY2. 2 Publications
    VAR_003710
    Natural varianti300 – 3001E → K in MODY2.
    VAR_003712
    Natural varianti300 – 3001E → Q in MODY2.
    VAR_003711
    Natural varianti309 – 3091L → P in MODY2.
    VAR_003713
    Natural varianti336 – 3361S → L in MODY2.
    VAR_010595
    Natural varianti367 – 3671V → M in MODY2.
    VAR_010596
    Natural varianti382 – 3821C → Y in MODY2. 1 Publication
    VAR_010597
    Natural varianti384 – 3841A → T in MODY2. 1 Publication
    VAR_010598
    Natural varianti385 – 3851G → V in MODY2. 1 Publication
    VAR_012354
    Natural varianti392 – 3921R → C in MODY2. 1 Publication
    VAR_010599
    Natural varianti414 – 4141K → E in MODY2; large increase in Km for glucose. 1 Publication
    VAR_003714
    Familial hyperinsulinemic hypoglycemia 3 (HHF3) [MIM:602485]: Most common cause of persistent hypoglycemia in infancy. Unless early and aggressive intervention is undertaken, brain damage from recurrent episodes of hypoglycemia may occur.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti455 – 4551V → M in HHF3. 1 Publication
    VAR_003715

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi177 – 1771E → K: Small change in activity.
    Mutagenesisi256 – 2561E → A: Inactive enzyme.
    Mutagenesisi414 – 4141K → A: Small change in activity.

    Keywords - Diseasei

    Diabetes mellitus, Disease mutation

    Organism-specific databases

    MIMi125851. phenotype.
    602485. phenotype.
    606391. phenotype.
    Orphaneti79299. Hyperinsulinism due to glucokinase deficiency.
    552. MODY syndrome.
    99885. Permanent neonatal diabetes mellitus.
    PharmGKBiPA28610.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 465465GlucokinasePRO_0000197593Add
    BLAST

    Proteomic databases

    PaxDbiP35557.
    PRIDEiP35557.

    PTM databases

    PhosphoSiteiP35557.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiP35557.
    BgeeiP35557.
    CleanExiHS_GCK.
    GenevestigatoriP35557.

    Organism-specific databases

    HPAiHPA007034.
    HPA007093.

    Interactioni

    Subunit structurei

    Monomer.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GCKRQ143972EBI-709928,EBI-709948
    PFKFB1P161182EBI-709928,EBI-709807

    Protein-protein interaction databases

    BioGridi108915. 4 interactions.
    IntActiP35557. 5 interactions.
    STRINGi9606.ENSP00000223366.

    Structurei

    Secondary structure

    1
    465
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi12 – 209
    Helixi21 – 233
    Helixi27 – 4519
    Turni47 – 526
    Beta strandi58 – 658
    Turni66 – 683
    Beta strandi72 – 9221
    Beta strandi95 – 973
    Beta strandi99 – 10911
    Helixi112 – 1154
    Beta strandi116 – 1183
    Helixi119 – 13618
    Beta strandi140 – 1423
    Beta strandi145 – 1506
    Beta strandi154 – 1585
    Beta strandi161 – 1644
    Helixi181 – 19212
    Beta strandi198 – 2036
    Helixi205 – 21410
    Beta strandi220 – 23718
    Helixi238 – 2403
    Beta strandi248 – 2547
    Helixi257 – 2593
    Turni260 – 2634
    Beta strandi264 – 2663
    Helixi267 – 2693
    Helixi272 – 2809
    Beta strandi281 – 2833
    Helixi288 – 2914
    Helixi295 – 31117
    Helixi316 – 3183
    Turni322 – 3254
    Helixi332 – 3398
    Beta strandi340 – 3423
    Beta strandi343 – 3453
    Helixi346 – 3549
    Helixi361 – 39636
    Beta strandi400 – 40910
    Helixi411 – 4155
    Beta strandi416 – 4183
    Helixi419 – 43012
    Beta strandi434 – 4407
    Helixi444 – 45613
    Turni457 – 4593

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GLKmodel-A1-465[»]
    1V4SX-ray2.30A16-465[»]
    1V4TX-ray3.40A16-465[»]
    3A0IX-ray2.20X16-465[»]
    3F9MX-ray1.50A12-465[»]
    3FGUX-ray2.15A12-465[»]
    3FR0X-ray2.70A16-465[»]
    3GOIX-ray2.52A16-465[»]
    3H1VX-ray2.11X16-465[»]
    3ID8X-ray2.40A12-465[»]
    3IDHX-ray2.14A12-465[»]
    3IMXX-ray2.00A16-465[»]
    3QICX-ray2.20A12-465[»]
    3S41X-ray2.18A12-465[»]
    3VEVX-ray1.80A12-465[»]
    3VEYX-ray2.25A16-465[»]
    3VF6X-ray1.86A12-465[»]
    4DCHX-ray1.79A1-465[»]
    4DHYX-ray2.38A12-465[»]
    4ISEX-ray1.78A16-465[»]
    4ISFX-ray2.09A16-465[»]
    4ISGX-ray2.64A16-465[»]
    4IWVX-ray2.10A16-465[»]
    4IXCX-ray2.00A16-465[»]
    4L3QX-ray2.70A16-465[»]
    4LC9X-ray3.40B3-465[»]
    4MLEX-ray2.60A16-465[»]
    4MLHX-ray2.90A16-465[»]
    ProteinModelPortaliP35557.
    SMRiP35557. Positions 16-460.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP35557.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini12 – 217206Hexokinase type-1Add
    BLAST
    Domaini219 – 458240Hexokinase type-2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni151 – 1522Substrate binding
    Regioni168 – 1692Substrate binding
    Regioni204 – 2052Substrate binding

    Sequence similaritiesi

    Belongs to the hexokinase family.Curated
    Contains 1 hexokinase type-1 domain.Curated
    Contains 1 hexokinase type-2 domain.Curated

    Phylogenomic databases

    eggNOGiCOG5026.
    HOGENOMiHOG000162670.
    HOVERGENiHBG000142.
    InParanoidiP35557.
    KOiK12407.
    OMAiEDHQCEV.
    PhylomeDBiP35557.
    TreeFamiTF314238.

    Family and domain databases

    InterProiIPR001312. Hexokinase.
    IPR022673. Hexokinase_C.
    IPR019807. Hexokinase_CS.
    IPR022672. Hexokinase_N.
    [Graphical view]
    PANTHERiPTHR19443. PTHR19443. 1 hit.
    PfamiPF00349. Hexokinase_1. 1 hit.
    PF03727. Hexokinase_2. 1 hit.
    [Graphical view]
    PRINTSiPR00475. HEXOKINASE.
    PROSITEiPS00378. HEXOKINASES. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    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

    MLDDRARMEA AKKEKVEQIL AEFQLQEEDL KKVMRRMQKE MDRGLRLETH    50
    EEASVKMLPT YVRSTPEGSE VGDFLSLDLG GTNFRVMLVK VGEGEEGQWS 100
    VKTKHQMYSI PEDAMTGTAE MLFDYISECI SDFLDKHQMK HKKLPLGFTF 150
    SFPVRHEDID KGILLNWTKG FKASGAEGNN VVGLLRDAIK RRGDFEMDVV 200
    AMVNDTVATM ISCYYEDHQC EVGMIVGTGC NACYMEEMQN VELVEGDEGR 250
    MCVNTEWGAF GDSGELDEFL LEYDRLVDES SANPGQQLYE KLIGGKYMGE 300
    LVRLVLLRLV DENLLFHGEA SEQLRTRGAF ETRFVSQVES DTGDRKQIYN 350
    ILSTLGLRPS TTDCDIVRRA CESVSTRAAH MCSAGLAGVI NRMRESRSED 400
    VMRITVGVDG SVYKLHPSFK ERFHASVRRL TPSCEITFIE SEEGSGRGAA 450
    LVSAVACKKA CMLGQ 465
    Length:465
    Mass (Da):52,191
    Last modified:June 1, 1994 - v1
    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

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti4 – 41D → N.1 Publication
    VAR_003692
    Natural varianti11 – 111A → T.1 Publication
    Corresponds to variant rs116093166 [ dbSNP | Ensembl ].
    VAR_010583
    Natural varianti36 – 361R → W in MODY2. 1 Publication
    VAR_010584
    Natural varianti53 – 531A → S in MODY2.
    VAR_010585
    Natural varianti70 – 701E → K in MODY2; large increase in Km for glucose. 1 Publication
    VAR_003693
    Natural varianti80 – 801G → A in MODY2.
    VAR_003694
    Natural varianti80 – 801G → S in MODY2. 1 Publication
    VAR_003695
    Natural varianti107 – 1071M → T.2 Publications
    VAR_003696
    Natural varianti108 – 1081Y → H in MODY2. 1 Publication
    VAR_010586
    Natural varianti110 – 1101I → T in MODY2. 1 Publication
    VAR_012352
    Natural varianti119 – 1191A → D in MODY2. 1 Publication
    VAR_012353
    Natural varianti131 – 1311S → P in MODY2; significant increase in the Km and in the affinity for ATP. 2 Publications
    VAR_003697
    Natural varianti137 – 1371H → R in MODY2.
    VAR_010587
    Natural varianti150 – 1501F → S in MODY2. 1 Publication
    VAR_010588
    Natural varianti164 – 1641L → P in MODY2. 1 Publication
    VAR_012350
    Natural varianti168 – 1681T → P in MODY2.
    VAR_010589
    Natural varianti175 – 1751G → R in MODY2.
    VAR_003698
    Natural varianti182 – 1821V → M in MODY2.
    VAR_003699
    Natural varianti188 – 1881A → T in MODY2; large increase in Km for glucose. 1 Publication
    VAR_003700
    Natural varianti203 – 2031V → A in MODY2.
    VAR_003701
    Natural varianti209 – 2091T → M in MODY2. 1 Publication
    VAR_010590
    Natural varianti210 – 2101M → K in MODY2. 1 Publication
    VAR_012351
    Natural varianti210 – 2101M → T in MODY2.
    VAR_010591
    Natural varianti213 – 2131C → R in MODY2.
    VAR_010592
    Natural varianti221 – 2211E → K in MODY2. 1 Publication
    VAR_003702
    Natural varianti226 – 2261V → M in MODY2.
    VAR_003703
    Natural varianti227 – 2271G → C in MODY2. 1 Publication
    VAR_003704
    Natural varianti228 – 2281T → M in MODY2. 2 Publications
    VAR_003705
    Natural varianti256 – 2561E → K in MODY2.
    VAR_003706
    Natural varianti257 – 2571W → R in MODY2; almost complete loss of activity. 1 Publication
    VAR_003707
    Natural varianti259 – 2591A → T in MODY2. 1 Publication
    VAR_010593
    Natural varianti261 – 2611G → E in MODY2. 1 Publication
    VAR_010594
    Natural varianti261 – 2611G → R in MODY2. 2 Publications
    VAR_003708
    Natural varianti279 – 2791E → Q in MODY2.
    Corresponds to variant rs104894005 [ dbSNP | Ensembl ].
    VAR_003709
    Natural varianti299 – 2991G → R in MODY2. 2 Publications
    VAR_003710
    Natural varianti300 – 3001E → K in MODY2.
    VAR_003712
    Natural varianti300 – 3001E → Q in MODY2.
    VAR_003711
    Natural varianti309 – 3091L → P in MODY2.
    VAR_003713
    Natural varianti336 – 3361S → L in MODY2.
    VAR_010595
    Natural varianti342 – 3421T → P.1 Publication
    VAR_066615
    Natural varianti367 – 3671V → M in MODY2.
    VAR_010596
    Natural varianti382 – 3821C → Y in MODY2. 1 Publication
    VAR_010597
    Natural varianti384 – 3841A → T in MODY2. 1 Publication
    VAR_010598
    Natural varianti385 – 3851G → V in MODY2. 1 Publication
    VAR_012354
    Natural varianti392 – 3921R → C in MODY2. 1 Publication
    VAR_010599
    Natural varianti414 – 4141K → E in MODY2; large increase in Km for glucose. 1 Publication
    VAR_003714
    Natural varianti455 – 4551V → M in HHF3. 1 Publication
    VAR_003715

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1515MLDDR…AKKEK → MAMDVTRSQAQTALTL in isoform 2. 1 PublicationVSP_002074Add
    BLAST
    Alternative sequencei1 – 1515MLDDR…AKKEK → MPRPRSQLPQPNSQ in isoform 3. CuratedVSP_002075Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M88011 mRNA. Translation: AAA51824.1.
    M69051 mRNA. Translation: AAB59563.1. Sequence problems.
    M90298 Genomic DNA. Translation: AAA67541.1. Different termination.
    M90298 Genomic DNA. Translation: AAA67542.1. Different termination.
    M90299 mRNA. Translation: AAA52562.1.
    AF041022
    , AF041012, AF041015, AF041016, AF041017, AF041018, AF041019, AF041020, AF041021 Genomic DNA. Translation: AAB97680.1.
    AF041022
    , AF041013, AF041015, AF041016, AF041017, AF041018, AF041019, AF041020, AF041021 Genomic DNA. Translation: AAB97681.1.
    AF041022
    , AF041014, AF041015, AF041016, AF041017, AF041018, AF041019, AF041020, AF041021 Genomic DNA. Translation: AAB97682.1.
    AK122876 mRNA. Translation: BAG53774.1.
    CH236960 Genomic DNA. Translation: EAL23765.1.
    CH236960 Genomic DNA. Translation: EAL23766.1.
    CH471128 Genomic DNA. Translation: EAW61114.1.
    CH471128 Genomic DNA. Translation: EAW61116.1.
    BC001890 mRNA. Translation: AAH01890.1.
    CCDSiCCDS5479.1. [P35557-1]
    CCDS5480.1. [P35557-2]
    CCDS5481.1. [P35557-3]
    PIRiA46157.
    B46157.
    C46157.
    RefSeqiNP_000153.1. NM_000162.3. [P35557-1]
    NP_277042.1. NM_033507.1. [P35557-2]
    NP_277043.1. NM_033508.1. [P35557-3]
    UniGeneiHs.1270.

    Genome annotation databases

    EnsembliENST00000345378; ENSP00000223366; ENSG00000106633. [P35557-2]
    ENST00000395796; ENSP00000379142; ENSG00000106633. [P35557-3]
    ENST00000403799; ENSP00000384247; ENSG00000106633. [P35557-1]
    GeneIDi2645.
    KEGGihsa:2645.
    UCSCiuc003tkj.1. human. [P35557-3]
    uc003tkk.1. human. [P35557-2]
    uc003tkl.2. human. [P35557-1]

    Polymorphism databases

    DMDMi547696.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Glucokinase entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M88011 mRNA. Translation: AAA51824.1 .
    M69051 mRNA. Translation: AAB59563.1 . Sequence problems.
    M90298 Genomic DNA. Translation: AAA67541.1 . Different termination.
    M90298 Genomic DNA. Translation: AAA67542.1 . Different termination.
    M90299 mRNA. Translation: AAA52562.1 .
    AF041022
    , AF041012 , AF041015 , AF041016 , AF041017 , AF041018 , AF041019 , AF041020 , AF041021 Genomic DNA. Translation: AAB97680.1 .
    AF041022
    , AF041013 , AF041015 , AF041016 , AF041017 , AF041018 , AF041019 , AF041020 , AF041021 Genomic DNA. Translation: AAB97681.1 .
    AF041022
    , AF041014 , AF041015 , AF041016 , AF041017 , AF041018 , AF041019 , AF041020 , AF041021 Genomic DNA. Translation: AAB97682.1 .
    AK122876 mRNA. Translation: BAG53774.1 .
    CH236960 Genomic DNA. Translation: EAL23765.1 .
    CH236960 Genomic DNA. Translation: EAL23766.1 .
    CH471128 Genomic DNA. Translation: EAW61114.1 .
    CH471128 Genomic DNA. Translation: EAW61116.1 .
    BC001890 mRNA. Translation: AAH01890.1 .
    CCDSi CCDS5479.1. [P35557-1 ]
    CCDS5480.1. [P35557-2 ]
    CCDS5481.1. [P35557-3 ]
    PIRi A46157.
    B46157.
    C46157.
    RefSeqi NP_000153.1. NM_000162.3. [P35557-1 ]
    NP_277042.1. NM_033507.1. [P35557-2 ]
    NP_277043.1. NM_033508.1. [P35557-3 ]
    UniGenei Hs.1270.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GLK model - A 1-465 [» ]
    1V4S X-ray 2.30 A 16-465 [» ]
    1V4T X-ray 3.40 A 16-465 [» ]
    3A0I X-ray 2.20 X 16-465 [» ]
    3F9M X-ray 1.50 A 12-465 [» ]
    3FGU X-ray 2.15 A 12-465 [» ]
    3FR0 X-ray 2.70 A 16-465 [» ]
    3GOI X-ray 2.52 A 16-465 [» ]
    3H1V X-ray 2.11 X 16-465 [» ]
    3ID8 X-ray 2.40 A 12-465 [» ]
    3IDH X-ray 2.14 A 12-465 [» ]
    3IMX X-ray 2.00 A 16-465 [» ]
    3QIC X-ray 2.20 A 12-465 [» ]
    3S41 X-ray 2.18 A 12-465 [» ]
    3VEV X-ray 1.80 A 12-465 [» ]
    3VEY X-ray 2.25 A 16-465 [» ]
    3VF6 X-ray 1.86 A 12-465 [» ]
    4DCH X-ray 1.79 A 1-465 [» ]
    4DHY X-ray 2.38 A 12-465 [» ]
    4ISE X-ray 1.78 A 16-465 [» ]
    4ISF X-ray 2.09 A 16-465 [» ]
    4ISG X-ray 2.64 A 16-465 [» ]
    4IWV X-ray 2.10 A 16-465 [» ]
    4IXC X-ray 2.00 A 16-465 [» ]
    4L3Q X-ray 2.70 A 16-465 [» ]
    4LC9 X-ray 3.40 B 3-465 [» ]
    4MLE X-ray 2.60 A 16-465 [» ]
    4MLH X-ray 2.90 A 16-465 [» ]
    ProteinModelPortali P35557.
    SMRi P35557. Positions 16-460.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108915. 4 interactions.
    IntActi P35557. 5 interactions.
    STRINGi 9606.ENSP00000223366.

    Chemistry

    BindingDBi P35557.
    ChEMBLi CHEMBL3820.

    PTM databases

    PhosphoSitei P35557.

    Polymorphism databases

    DMDMi 547696.

    Proteomic databases

    PaxDbi P35557.
    PRIDEi P35557.

    Protocols and materials databases

    DNASUi 2645.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000345378 ; ENSP00000223366 ; ENSG00000106633 . [P35557-2 ]
    ENST00000395796 ; ENSP00000379142 ; ENSG00000106633 . [P35557-3 ]
    ENST00000403799 ; ENSP00000384247 ; ENSG00000106633 . [P35557-1 ]
    GeneIDi 2645.
    KEGGi hsa:2645.
    UCSCi uc003tkj.1. human. [P35557-3 ]
    uc003tkk.1. human. [P35557-2 ]
    uc003tkl.2. human. [P35557-1 ]

    Organism-specific databases

    CTDi 2645.
    GeneCardsi GC07M044183.
    GeneReviewsi GCK.
    HGNCi HGNC:4195. GCK.
    HPAi HPA007034.
    HPA007093.
    MIMi 125851. phenotype.
    138079. gene.
    602485. phenotype.
    606391. phenotype.
    neXtProti NX_P35557.
    Orphaneti 79299. Hyperinsulinism due to glucokinase deficiency.
    552. MODY syndrome.
    99885. Permanent neonatal diabetes mellitus.
    PharmGKBi PA28610.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5026.
    HOGENOMi HOG000162670.
    HOVERGENi HBG000142.
    InParanoidi P35557.
    KOi K12407.
    OMAi EDHQCEV.
    PhylomeDBi P35557.
    TreeFami TF314238.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS02935-MONOMER.
    Reactomei REACT_13819. Regulation of gene expression in beta cells.
    REACT_212. Glucose transport.
    REACT_6804. Regulation of Glucokinase by Glucokinase Regulatory Protein.
    SABIO-RK P35557.

    Miscellaneous databases

    EvolutionaryTracei P35557.
    GeneWikii Glucokinase.
    GenomeRNAii 2645.
    NextBioi 10434.
    PROi P35557.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P35557.
    Bgeei P35557.
    CleanExi HS_GCK.
    Genevestigatori P35557.

    Family and domain databases

    InterProi IPR001312. Hexokinase.
    IPR022673. Hexokinase_C.
    IPR019807. Hexokinase_CS.
    IPR022672. Hexokinase_N.
    [Graphical view ]
    PANTHERi PTHR19443. PTHR19443. 1 hit.
    Pfami PF00349. Hexokinase_1. 1 hit.
    PF03727. Hexokinase_2. 1 hit.
    [Graphical view ]
    PRINTSi PR00475. HEXOKINASE.
    PROSITEi PS00378. HEXOKINASES. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human glucokinase gene: isolation, structural characterization, and identification of a microsatellite repeat polymorphism."
      Tanizawa Y., Matsutani A., Chiu K.C., Permutt M.A.
      Mol. Endocrinol. 6:1070-1081(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Human liver glucokinase gene: cloning and sequence determination of two alternatively spliced cDNAs."
      Tanizawa Y., Koranyi L.I., Welling C.M., Permutt M.A.
      Proc. Natl. Acad. Sci. U.S.A. 88:7294-7297(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT THR-107.
    3. "Human pancreatic beta-cell glucokinase: cDNA sequence and localization of the polymorphic gene to chromosome 7, band p13."
      Nishi S., Stoffel M., Xiang K.S., Shows T.B., Bell G.I., Takeda J.
      Diabetologia 35:743-747(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Pancreas.
    4. "Human islet glucokinase gene. Isolation and sequence analysis of full-length cDNA."
      Koranyi L.I., Tanizawa Y., Welling C.M., Rabin D.U., Permutt M.A.
      Diabetes 41:807-811(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Pancreas.
    5. "Human glucokinase gene: isolation, characterization, and identification of two missense mutations linked to early-onset non-insulin-dependent (type 2) diabetes mellitus."
      Stoffel M., Froguel P., Takeda J., Zouali H., Vionnet N., Nishi S., Weber I.T., Harrison R.W., Pilkis S.J., Lesage S., Vaxillaire M., Velho G., Sun F., Iris F., Passa P., Cohen D., Bell G.I.
      Proc. Natl. Acad. Sci. U.S.A. 89:7698-7702(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS MODY2 MET-228 AND ARG-261.
      Tissue: Placenta.
    6. "Structure of the human glucokinase gene and identification of a missense mutation in a Japanese patient with early-onset non-insulin-dependent diabetes mellitus."
      Sakura H., Eto K., Kadowaki H., Simokawa K., Ueno H., Koda N., Fukushima Y., Akanuma Y., Yazaki Y., Kadowaki T.
      J. Clin. Endocrinol. Metab. 75:1571-1573(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-107, VARIANT MODY2 ARG-261.
    7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Liver.
    8. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Lung.
    11. "Glucokinase regulatory protein is essential for the proper subcellular localisation of liver glucokinase."
      de la Iglesia N., Veiga-da-Cunha M., Van Schaftingen E., Guinovart J.J., Ferrer J.C.
      FEBS Lett. 456:332-338(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, SUBCELLULAR LOCATION.
    12. "Molecular model of human beta-cell glucokinase built by analogy to the crystal structure of yeast hexokinase B."
      St Charles R., Harrison R.W., Bell G.I., Pilkis S.J., Weber I.T.
      Diabetes 43:784-791(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING.
    13. "Structural basis for allosteric regulation of the monomeric allosteric enzyme human glucokinase."
      Kamata K., Mitsuya M., Nishimura T., Eiki J., Nagata Y.
      Structure 12:429-438(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 16-465 OF APOPROTEIN AND IN COMPLEX WITH GLUCOSE, SUBUNIT, ENZYME REGULATION.
    14. "Discovery of novel 3,6-disubstituted 2-pyridinecarboxamide derivatives as GK activators."
      Mitsuya M., Kamata K., Bamba M., Watanabe H., Sasaki Y., Sasaki K., Ohyama S., Hosaka H., Nagata Y., Eiki J., Nishimura T.
      Bioorg. Med. Chem. Lett. 19:2718-2721(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 16-465 IN COMPLEX WITH SYNTHETIC ALLOSTERIC ACTIVATOR.
    15. "Structural basis for regulation of human glucokinase by glucokinase regulatory protein."
      Beck T., Miller B.G.
      Biochemistry 52:6232-6239(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 3-465 IN COMPLEX WITH RAT GKRP.
    16. "Missense glucokinase mutation in maturity-onset diabetes of the young and mutation screening in late-onset diabetes."
      Stoffel M., Patel P., Lo Y.-M.D., Hattersley A.T., Lucassen A.M., Page R., Bell J.I., Bell G.I., Turner R.C., Wainscoat J.S.
      Nat. Genet. 2:153-156(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MODY2 ARG-299.
    17. "Glucokinase gene variants in the common form of NIDDM."
      Chiu K.C., Tanizawa Y., Permutt M.A.
      Diabetes 42:579-582(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT THR-11.
    18. "Identification of glucokinase mutations in subjects with gestational diabetes mellitus."
      Stoffel M., Bell K.L., Blackburn C.L., Powell K.L., Seo T.S., Takeda J., Vionnet N., Xiang K.-S., Gidh-Jain M., Pilkis S.J., Ober C., Bell G.I.
      Diabetes 42:937-940(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MODY2 PRO-131.
    19. "Structure/function studies of human beta-cell glucokinase. Enzymatic properties of a sequence polymorphism, mutations associated with diabetes, and other site-directed mutants."
      Takeda J., Gidh-Jain M., Xu L.Z., Froguel P., Velho G., Vaxillaire M., Cohen D., Shimada F., Makino H., Nishi S., Stoffel M., Vionnet N., St Charles R., Harrison R.W., Weber I.T., Bell G.I., Pilkis S.J.
      J. Biol. Chem. 268:15200-15204(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ASN-4, VARIANTS MODY2 LYS-70; PRO-131; THR-188; ARG-257 AND GLU-414.
    20. "Glucokinase mutations associated with non-insulin-dependent (type 2) diabetes mellitus have decreased enzymatic activity: implications for structure/function relationships."
      Gidh-Jain M., Takeda J., Xu L.Z., Lange A.J., Vionnet N., Stoffel M., Froguel P., Velho G., Sun D., Cohen D., Patel P., Lo Y.-M.D., Hattersley A.T., Luthman H., Wedell A., St Charles R., Harrison R.W., Weber I.T., Bell G.I., Pilkis S.J.
      Proc. Natl. Acad. Sci. U.S.A. 90:1932-1936(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANTS MODY2.
    21. "Six mutations in the glucokinase gene identified in MODY by using a nonradioactive sensitive screening technique."
      Hager J., Blanche H., Sun F., Vionnet N., Vaxillaire M., Poller W., Cohen D., Czernichow P., Velho G., Robert J.-J., Cohen N., Froguel P.
      Diabetes 43:730-733(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS MODY2 TRP-36; MET-209 AND GLU-261.
    22. "Identification of 14 new glucokinase mutations and description of the clinical profile of 42 MODY-2 families."
      Velho G., Blanche H., Vaxillaire M., Bellanne-Chantelot C., Pardini V.C., Timsit J., Passa P., Deschamps I., Robert J.-J., Weber I.T., Marotta D., Pilkis S.J., Lipkind G.M., Bell G.I., Froguel P.
      Diabetologia 40:217-224(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS MODY2.
    23. "Three novel missense mutations in the glucokinase gene (G80S; E221K; G227C) in Italian subjects with maturity-onset diabetes of the young (MODY)."
      Guazzini B., Gaffi D., Mainieri D., Multari G., Cordera R., Bertolini S., Pozza G., Meschi F., Barbetti F.
      Hum. Mutat. 12:136-136(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS MODY2 SER-80; LYS-221 AND CYS-227.
    24. "Mutations in the glucokinase gene of the fetus result in reduced birth weight."
      Hattersley A.T., Beards F., Ballantyne E., Appleton M., Harvey R., Ellard S.
      Nat. Genet. 19:268-270(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS MODY2 HIS-108; SER-150; THR-259; ARG-299; TYR-382; THR-384 AND CYS-392.
    25. Cited for: VARIANT HHF3 MET-455.
    26. "Molecular genetics of diabetes mellitus in Chinese subjects: identification of mutations in glucokinase and hepatocyte nuclear factor-1alpha genes in patients with early-onset type 2 diabetes mellitus/MODY."
      Ng M.C.Y., Cockburn B.N., Lindner T.H., Yeung V.T.F., Chow C.-C., So W.-Y., Li J.K.Y., Lo Y.M.D., Lee Z.S.K., Cockram C.S., Critchley J.A.J.H., Bell G.I., Chan J.C.N.
      Diabet. Med. 16:956-963(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS MODY2 THR-110; ASP-119 AND VAL-385.
    27. "Identification of glucokinase mutation in subjects with post-renal transplantation diabetes mellitus."
      Nam J.H., Lee H.C., Kim Y.H., Cha B.S., Song Y.D., Lim S.K., Kim K.R., Huh K.B.
      Diabetes Res. Clin. Pract. 50:169-176(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MODY2 PRO-164.
    28. Cited for: VARIANTS MODY2 LYS-210 AND MET-228.
    29. "The previously reported T342P GCK missense variant is not a pathogenic mutation causing MODY."
      Steele A.M., Tribble N.D., Caswell R., Wensley K.J., Hattersley A.T., Gloyn A.L., Ellard S.
      Diabetologia 54:2202-2205(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PRO-342.

    Entry informationi

    Entry nameiHXK4_HUMAN
    AccessioniPrimary (citable) accession number: P35557
    Secondary accession number(s): A4D2J2, A4D2J3, Q05810
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 161 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

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

    Keywords - Technical termi

    3D-structure, Allosteric enzyme, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3