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P52789

- HXK2_HUMAN

UniProt

P52789 - HXK2_HUMAN

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Protein

Hexokinase-2

Gene

HK2

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

Functioni

Catalytic activityi

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

Enzyme regulationi

Hexokinase is an allosteric enzyme inhibited by its product Glc-6-P.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei30 – 301ATP 1By similarity
Binding sitei209 – 2091Glucose-6-phosphate 11 Publication
Binding sitei232 – 2321Glucose-6-phosphate 11 Publication
Binding sitei235 – 2351Substrate 1
Binding sitei260 – 2601Substrate 1
Binding sitei449 – 4491Glucose-6-phosphate 11 Publication
Binding sitei558 – 5581ATPSequence Analysis
Binding sitei657 – 6571Glucose-6-phosphate 21 Publication
Binding sitei680 – 6801ATP 2By similarity
Binding sitei680 – 6801Glucose-6-phosphate 21 Publication
Binding sitei708 – 7081Substrate 2
Binding sitei897 – 8971Glucose-6-phosphate 21 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi84 – 896ATP 1Sequence Analysis
Nucleotide bindingi425 – 4262ATP 1By similarity
Nucleotide bindingi532 – 5376ATP 2By similarity
Nucleotide bindingi747 – 7482ATP 2By similarity
Nucleotide bindingi784 – 7885ATP 2By similarity
Nucleotide bindingi863 – 8675ATP 2By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. fructokinase activity Source: RefGenome
  3. glucokinase activity Source: RefGenome
  4. glucose binding Source: Ensembl
  5. hexokinase activity Source: ProtInc
  6. mannokinase activity Source: RefGenome

GO - Biological processi

  1. apoptotic mitochondrial changes Source: MGI
  2. carbohydrate metabolic process Source: Reactome
  3. cellular glucose homeostasis Source: RefGenome
  4. glucose 6-phosphate metabolic process Source: GOC
  5. glucose metabolic process Source: Ensembl
  6. glucose transport Source: Reactome
  7. glycolytic process Source: RefGenome
  8. hexose transport Source: Reactome
  9. lactation Source: Ensembl
  10. regulation of glucose import Source: Ensembl
  11. small molecule metabolic process Source: Reactome
  12. 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:HS08399-MONOMER.
ReactomeiREACT_212. Glucose transport.
SABIO-RKP52789.
UniPathwayiUPA00242.

Names & Taxonomyi

Protein namesi
Recommended name:
Hexokinase-2 (EC:2.7.1.1)
Alternative name(s):
Hexokinase type II
Short name:
HK II
Muscle form hexokinase
Gene namesi
Name:HK2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:4923. HK2.

Subcellular locationi

Mitochondrion outer membrane By similarity
Note: Its hydrophobic N-terminal sequence may be involved in membrane binding.By similarity

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. membrane Source: UniProtKB
  3. mitochondrial outer membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29301.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 917917Hexokinase-2PRO_0000197587Add
BLAST

Proteomic databases

MaxQBiP52789.
PaxDbiP52789.
PeptideAtlasiP52789.
PRIDEiP52789.

PTM databases

PhosphoSiteiP52789.

Expressioni

Tissue specificityi

Predominant hexokinase isozyme expressed in insulin-responsive tissues such as skeletal muscle.

Gene expression databases

BgeeiP52789.
CleanExiHS_HK2.
ExpressionAtlasiP52789. baseline and differential.
GenevestigatoriP52789.

Organism-specific databases

HPAiHPA028587.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi109346. 24 interactions.
DIPiDIP-50110N.
IntActiP52789. 4 interactions.
MINTiMINT-1461614.
STRINGi9606.ENSP00000290573.

Structurei

Secondary structure

1
917
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi19 – 257Combined sources
Helixi27 – 293Combined sources
Helixi33 – 5119Combined sources
Turni53 – 553Combined sources
Helixi56 – 583Combined sources
Beta strandi78 – 9720Combined sources
Beta strandi106 – 1127Combined sources
Helixi116 – 1194Combined sources
Helixi123 – 14119Combined sources
Beta strandi148 – 1547Combined sources
Helixi185 – 19410Combined sources
Beta strandi201 – 2077Combined sources
Helixi209 – 21810Combined sources
Beta strandi224 – 24118Combined sources
Helixi242 – 2443Combined sources
Beta strandi252 – 2587Combined sources
Helixi261 – 2633Combined sources
Turni264 – 2674Combined sources
Turni269 – 2735Combined sources
Helixi276 – 2838Combined sources
Beta strandi285 – 2873Combined sources
Helixi292 – 2954Combined sources
Turni299 – 3013Combined sources
Helixi302 – 31514Combined sources
Helixi320 – 3223Combined sources
Helixi326 – 3294Combined sources
Helixi336 – 3449Combined sources
Beta strandi345 – 3473Combined sources
Helixi348 – 35811Combined sources
Helixi365 – 40137Combined sources
Beta strandi404 – 41310Combined sources
Helixi415 – 4195Combined sources
Beta strandi420 – 4223Combined sources
Helixi423 – 43412Combined sources
Beta strandi438 – 4447Combined sources
Helixi449 – 47426Combined sources
Helixi475 – 4773Combined sources
Helixi481 – 49919Combined sources
Helixi501 – 5044Combined sources
Beta strandi527 – 53610Combined sources
Beta strandi539 – 5457Combined sources
Beta strandi553 – 5597Combined sources
Helixi564 – 5685Combined sources
Helixi571 – 58818Combined sources
Beta strandi597 – 6026Combined sources
Beta strandi606 – 6105Combined sources
Beta strandi613 – 6164Combined sources
Helixi633 – 64210Combined sources
Beta strandi650 – 6556Combined sources
Helixi657 – 66610Combined sources
Beta strandi672 – 68918Combined sources
Turni690 – 6923Combined sources
Beta strandi699 – 7068Combined sources
Helixi709 – 7113Combined sources
Turni712 – 7154Combined sources
Turni717 – 7215Combined sources
Helixi724 – 7318Combined sources
Beta strandi733 – 7353Combined sources
Helixi742 – 7443Combined sources
Turni747 – 7493Combined sources
Helixi750 – 76314Combined sources
Helixi768 – 7703Combined sources
Turni774 – 7763Combined sources
Helixi785 – 7884Combined sources
Turni789 – 7913Combined sources
Helixi797 – 80610Combined sources
Helixi813 – 84836Combined sources
Beta strandi852 – 86110Combined sources
Helixi863 – 8675Combined sources
Helixi871 – 88212Combined sources
Beta strandi886 – 8927Combined sources
Helixi897 – 91115Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NZTX-ray2.45A/B17-916[»]
ProteinModelPortaliP52789.
SMRiP52789. Positions 17-913.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52789.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 221205Hexokinase type-1 1Add
BLAST
Domaini223 – 462240Hexokinase type-2 1Add
BLAST
Domaini465 – 669205Hexokinase type-1 2Add
BLAST
Domaini671 – 910240Hexokinase type-2 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 1212HydrophobicAdd
BLAST
Regioni13 – 475463RegulatoryAdd
BLAST
Regioni84 – 885Glucose-6-phosphate 1 binding
Regioni155 – 1562Substrate 1 binding
Regioni172 – 1732Substrate 1 binding
Regioni208 – 2092Substrate 1 binding
Regioni291 – 2944Substrate 1 binding
Regioni413 – 4153Glucose-6-phosphate 1 binding
Regioni476 – 917442CatalyticAdd
BLAST
Regioni532 – 5365Glucose-6-phosphate 2 binding
Regioni603 – 6042Substrate 2 binding
Regioni620 – 6212Substrate 2 binding
Regioni656 – 6572Substrate 2 binding
Regioni682 – 6832Substrate 2 binding
Regioni739 – 7424Substrate 2 binding
Regioni861 – 8633Glucose-6-phosphate 2 binding

Domaini

The N- and C-terminal halves of this hexokinase show extensive sequence similarity to each other. The catalytic activity is associated with the C-terminus while regulatory function is associated with the N-terminus. Each domain can bind a single glucose and Gluc-6-P molecule.

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5026.
GeneTreeiENSGT00390000017159.
HOGENOMiHOG000162671.
HOVERGENiHBG005020.
InParanoidiP52789.
KOiK00844.
OMAiHHLGLES.
OrthoDBiEOG7S21X5.
PhylomeDBiP52789.
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. 2 hits.
PF03727. Hexokinase_2. 2 hits.
[Graphical view]
PRINTSiPR00475. HEXOKINASE.
PROSITEiPS00378. HEXOKINASES. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P52789-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIASHLLAYF FTELNHDQVQ KVDQYLYHMR LSDETLLEIS KRFRKEMEKG
60 70 80 90 100
LGATTHPTAA VKMLPTFVRS TPDGTEHGEF LALDLGGTNF RVLWVKVTDN
110 120 130 140 150
GLQKVEMENQ IYAIPEDIMR GSGTQLFDHI AECLANFMDK LQIKDKKLPL
160 170 180 190 200
GFTFSFPCHQ TKLDESFLVS WTKGFKSSGV EGRDVVALIR KAIQRRGDFD
210 220 230 240 250
IDIVAVVNDT VGTMMTCGYD DHNCEIGLIV GTGSNACYME EMRHIDMVEG
260 270 280 290 300
DEGRMCINME WGAFGDDGSL NDIRTEFDQE IDMGSLNPGK QLFEKMISGM
310 320 330 340 350
YMGELVRLIL VKMAKEELLF GGKLSPELLN TGRFETKDIS DIEGEKDGIR
360 370 380 390 400
KAREVLMRLG LDPTQEDCVA THRICQIVST RSASLCAATL AAVLQRIKEN
410 420 430 440 450
KGEERLRSTI GVDGSVYKKH PHFAKRLHKT VRRLVPGCDV RFLRSEDGSG
460 470 480 490 500
KGAAMVTAVA YRLADQHRAR QKTLEHLQLS HDQLLEVKRR MKVEMERGLS
510 520 530 540 550
KETHASAPVK MLPTYVCATP DGTEKGDFLA LDLGGTNFRV LLVRVRNGKW
560 570 580 590 600
GGVEMHNKIY AIPQEVMHGT GDELFDHIVQ CIADFLEYMG MKGVSLPLGF
610 620 630 640 650
TFSFPCQQNS LDESILLKWT KGFKASGCEG EDVVTLLKEA IHRREEFDLD
660 670 680 690 700
VVAVVNDTVG TMMTCGFEDP HCEVGLIVGT GSNACYMEEM RNVELVEGEE
710 720 730 740 750
GRMCVNMEWG AFGDNGCLDD FRTEFDVAVD ELSLNPGKQR FEKMISGMYL
760 770 780 790 800
GEIVRNILID FTKRGLLFRG RISERLKTRG IFETKFLSQI ESDCLALLQV
810 820 830 840 850
RAILQHLGLE STCDDSIIVK EVCTVVARRA AQLCGAGMAA VVDRIRENRG
860 870 880 890 900
LDALKVTVGV DGTLYKLHPH FAKVMHETVK DLAPKCDVSF LQSEDGSGKG
910
AALITAVACR IREAGQR
Length:917
Mass (Da):102,380
Last modified:December 7, 2004 - v2
Checksum:iF17CE1938CF13880
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti803 – 8031I → T in CAA86511. (PubMed:8250948)Curated
Sequence conflicti870 – 8701Missing in CAA86476. (PubMed:8786021)Curated

Polymorphismi

Although found in NIDDM patients, genetic variations of HK2 do not contribute to the disease.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti142 – 1421Q → H Does not affect activity. 4 Publications
Corresponds to variant rs2229621 [ dbSNP | Ensembl ].
VAR_003691
Natural varianti148 – 1481L → F.1 Publication
VAR_010577
Natural varianti274 – 2741R → C.1 Publication
Corresponds to variant rs28363006 [ dbSNP | Ensembl ].
VAR_020504
Natural varianti314 – 3141A → P.1 Publication
Corresponds to variant rs28363015 [ dbSNP | Ensembl ].
VAR_020505
Natural varianti314 – 3141A → V.1 Publication
VAR_010578
Natural varianti331 – 3311T → I.1 Publication
Corresponds to variant rs28363016 [ dbSNP | Ensembl ].
VAR_020506
Natural varianti353 – 3531R → C.1 Publication
Corresponds to variant rs61748096 [ dbSNP | Ensembl ].
VAR_010579
Natural varianti387 – 3871A → S.1 Publication
Corresponds to variant rs28363029 [ dbSNP | Ensembl ].
VAR_020507
Natural varianti497 – 4971R → Q.1 Publication
Corresponds to variant rs2229625 [ dbSNP | Ensembl ].
VAR_010580
Natural varianti775 – 7751R → Q.1 Publication
Corresponds to variant rs185927605 [ dbSNP | Ensembl ].
VAR_010581
Natural varianti801 – 8011R → Q.1 Publication
Corresponds to variant rs28363057 [ dbSNP | Ensembl ].
VAR_020508
Natural varianti844 – 8441R → K.2 Publications
Corresponds to variant rs2229629 [ dbSNP | Ensembl ].
VAR_010582
Natural varianti881 – 8811D → N.1 Publication
Corresponds to variant rs28363065 [ dbSNP | Ensembl ].
VAR_020509

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46376 mRNA. Translation: CAA86511.1.
Z46354
, Z46355, Z46604, Z46356, Z46357, Z46358, Z46359, Z46360, Z46361, Z46362, Z46363, Z46364, Z46365, Z46366, Z46367, Z46368, Z46369 Genomic DNA. Translation: CAA86476.2.
AF148513 mRNA. Translation: AAD30174.1.
AY623118 Genomic DNA. Translation: AAT38114.1.
CH471053 Genomic DNA. Translation: EAW99601.1.
CH471053 Genomic DNA. Translation: EAW99602.1.
BC021116 mRNA. Translation: AAH21116.1.
BC064369 mRNA. Translation: AAH64369.1.
D25412 Genomic DNA. Translation: BAA04999.1.
CCDSiCCDS1956.1.
PIRiS48809. JC2025.
RefSeqiNP_000180.2. NM_000189.4.
UniGeneiHs.406266.
Hs.591588.

Genome annotation databases

EnsembliENST00000290573; ENSP00000290573; ENSG00000159399.
GeneIDi3099.
KEGGihsa:3099.
UCSCiuc002snd.3. human.

Polymorphism databases

DMDMi56405344.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Wikipedia

Hexokinase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46376 mRNA. Translation: CAA86511.1 .
Z46354
, Z46355 , Z46604 , Z46356 , Z46357 , Z46358 , Z46359 , Z46360 , Z46361 , Z46362 , Z46363 , Z46364 , Z46365 , Z46366 , Z46367 , Z46368 , Z46369 Genomic DNA. Translation: CAA86476.2 .
AF148513 mRNA. Translation: AAD30174.1 .
AY623118 Genomic DNA. Translation: AAT38114.1 .
CH471053 Genomic DNA. Translation: EAW99601.1 .
CH471053 Genomic DNA. Translation: EAW99602.1 .
BC021116 mRNA. Translation: AAH21116.1 .
BC064369 mRNA. Translation: AAH64369.1 .
D25412 Genomic DNA. Translation: BAA04999.1 .
CCDSi CCDS1956.1.
PIRi S48809. JC2025.
RefSeqi NP_000180.2. NM_000189.4.
UniGenei Hs.406266.
Hs.591588.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2NZT X-ray 2.45 A/B 17-916 [» ]
ProteinModelPortali P52789.
SMRi P52789. Positions 17-913.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109346. 24 interactions.
DIPi DIP-50110N.
IntActi P52789. 4 interactions.
MINTi MINT-1461614.
STRINGi 9606.ENSP00000290573.

Chemistry

ChEMBLi CHEMBL2640.

PTM databases

PhosphoSitei P52789.

Polymorphism databases

DMDMi 56405344.

Proteomic databases

MaxQBi P52789.
PaxDbi P52789.
PeptideAtlasi P52789.
PRIDEi P52789.

Protocols and materials databases

DNASUi 3099.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000290573 ; ENSP00000290573 ; ENSG00000159399 .
GeneIDi 3099.
KEGGi hsa:3099.
UCSCi uc002snd.3. human.

Organism-specific databases

CTDi 3099.
GeneCardsi GC02P075059.
H-InvDB HIX0030207.
HGNCi HGNC:4923. HK2.
HPAi HPA028587.
MIMi 601125. gene.
neXtProti NX_P52789.
PharmGKBi PA29301.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5026.
GeneTreei ENSGT00390000017159.
HOGENOMi HOG000162671.
HOVERGENi HBG005020.
InParanoidi P52789.
KOi K00844.
OMAi HHLGLES.
OrthoDBi EOG7S21X5.
PhylomeDBi P52789.
TreeFami TF314238.

Enzyme and pathway databases

UniPathwayi UPA00242 .
BioCyci MetaCyc:HS08399-MONOMER.
Reactomei REACT_212. Glucose transport.
SABIO-RK P52789.

Miscellaneous databases

ChiTaRSi HK2. human.
EvolutionaryTracei P52789.
GeneWikii HK2.
GenomeRNAii 3099.
NextBioi 12305.
PROi P52789.
SOURCEi Search...

Gene expression databases

Bgeei P52789.
CleanExi HS_HK2.
ExpressionAtlasi P52789. baseline and differential.
Genevestigatori P52789.

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. 2 hits.
PF03727. Hexokinase_2. 2 hits.
[Graphical view ]
PRINTSi PR00475. HEXOKINASE.
PROSITEi PS00378. HEXOKINASES. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human hexokinase II: sequence and homology to other hexokinases."
    Deeb S.S., Malkki M., Laakso M.
    Biochem. Biophys. Res. Commun. 197:68-74(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Skeletal muscle.
  2. "Human hexokinase II gene: exon-intron organization, mutation screening in NIDDM, and its relationship to muscle hexokinase activity."
    Lehto M., Huang X., Davis E.M., Le Beau M.M., Laurila E., Eriksson K.F., Bell G.I., Groop L.C.
    Diabetologia 38:1466-1474(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT HIS-142.
    Tissue: Blood, Muscle and Placenta.
  3. Malkki M., Heikkinen S., Deeb S.S., Laakso M.
    Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Skeletal muscle.
  4. NIEHS SNPs program
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-142; CYS-274; PRO-314; ILE-331; SER-387; GLN-801; LYS-844 AND ASN-881.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Placenta and Testis.
  7. "Steady state transcript levels of the type II hexokinase and type 1 glucose transporter in human tumor cell lines."
    Shinohara Y., Yamamoto K., Kogure K., Ichihara J., Terada H.
    Cancer Lett. 82:27-32(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 614-739.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Crystal structure of human hexokinase II."
    Structural genomics consortium (SGC)
    Submitted (DEC-2006) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 17-916 IN COMPLEX WITH GLUCOSE AND GLUCOSE-6-PHOSPHATE.
  10. "Amino acid substitutions in hexokinase II among patients with NIDDM."
    Laakso M., Malkki M., Deeb S.S.
    Diabetes 44:330-334(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS VAL-314; CYS-353 AND GLN-775.
  11. "Analysis of the hexokinase II gene in subjects with insulin resistance and NIDDM and detection of a Gln142-->His substitution."
    Vidal-Puig A., Printz R.L., Stratton I.M., Granner D.K., Moller D.E.
    Diabetes 44:340-346(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HIS-142.
  12. "Identification of four amino acid substitutions in hexokinase II and studies of relationships to NIDDM, glucose effectiveness, and insulin sensitivity."
    Echwald S.M., Bjoerbaek C., Hansen T., Clausen J.O., Vestergaard H., Zierath J.R., Printz R.L., Granner D.K., Pedersen O.
    Diabetes 44:347-353(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS HIS-142; PHE-148; GLN-497 AND LYS-844.

Entry informationi

Entry nameiHXK2_HUMAN
AccessioniPrimary (citable) accession number: P52789
Secondary accession number(s): D6W5J2, Q8WU87, Q9UN82
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: December 7, 2004
Last modified: November 26, 2014
This is version 150 of the entry and version 2 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 2
    Human chromosome 2: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3