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P35557

- HXK4_HUMAN

UniProt

P35557 - HXK4_HUMAN

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Protein

Glucokinase

Gene

GCK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiP35557.
CleanExiHS_GCK.
ExpressionAtlasiP35557. baseline.
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.
GeneTreeiENSGT00390000017159.
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

        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
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]
ENST00000616242; ENSP00000482149; ENSG00000106633. [P35557-3]
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 ]
ENST00000616242 ; ENSP00000482149 ; ENSG00000106633 . [P35557-3 ]
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.
GeneTreei ENSGT00390000017159.
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

Bgeei P35557.
CleanExi HS_GCK.
ExpressionAtlasi P35557. baseline.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 162 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