Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P52789

- HXK2_HUMAN

UniProt

P52789 - HXK2_HUMAN

Protein

Hexokinase-2

Gene

HK2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 2 (07 Dec 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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

    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

    ArrayExpressiP52789.
    BgeeiP52789.
    CleanExiHS_HK2.
    GenevestigatoriP52789.

    Organism-specific databases

    HPAiHPA028587.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    BioGridi109346. 23 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 – 257
    Helixi27 – 293
    Helixi33 – 5119
    Turni53 – 553
    Helixi56 – 583
    Beta strandi78 – 9720
    Beta strandi106 – 1127
    Helixi116 – 1194
    Helixi123 – 14119
    Beta strandi148 – 1547
    Helixi185 – 19410
    Beta strandi201 – 2077
    Helixi209 – 21810
    Beta strandi224 – 24118
    Helixi242 – 2443
    Beta strandi252 – 2587
    Helixi261 – 2633
    Turni264 – 2674
    Turni269 – 2735
    Helixi276 – 2838
    Beta strandi285 – 2873
    Helixi292 – 2954
    Turni299 – 3013
    Helixi302 – 31514
    Helixi320 – 3223
    Helixi326 – 3294
    Helixi336 – 3449
    Beta strandi345 – 3473
    Helixi348 – 35811
    Helixi365 – 40137
    Beta strandi404 – 41310
    Helixi415 – 4195
    Beta strandi420 – 4223
    Helixi423 – 43412
    Beta strandi438 – 4447
    Helixi449 – 47426
    Helixi475 – 4773
    Helixi481 – 49919
    Helixi501 – 5044
    Beta strandi527 – 53610
    Beta strandi539 – 5457
    Beta strandi553 – 5597
    Helixi564 – 5685
    Helixi571 – 58818
    Beta strandi597 – 6026
    Beta strandi606 – 6105
    Beta strandi613 – 6164
    Helixi633 – 64210
    Beta strandi650 – 6556
    Helixi657 – 66610
    Beta strandi672 – 68918
    Turni690 – 6923
    Beta strandi699 – 7068
    Helixi709 – 7113
    Turni712 – 7154
    Turni717 – 7215
    Helixi724 – 7318
    Beta strandi733 – 7353
    Helixi742 – 7443
    Turni747 – 7493
    Helixi750 – 76314
    Helixi768 – 7703
    Turni774 – 7763
    Helixi785 – 7884
    Turni789 – 7913
    Helixi797 – 80610
    Helixi813 – 84836
    Beta strandi852 – 86110
    Helixi863 – 8675
    Helixi871 – 88212
    Beta strandi886 – 8927
    Helixi897 – 91115

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MIASHLLAYF FTELNHDQVQ KVDQYLYHMR LSDETLLEIS KRFRKEMEKG    50
    LGATTHPTAA VKMLPTFVRS TPDGTEHGEF LALDLGGTNF RVLWVKVTDN 100
    GLQKVEMENQ IYAIPEDIMR GSGTQLFDHI AECLANFMDK LQIKDKKLPL 150
    GFTFSFPCHQ TKLDESFLVS WTKGFKSSGV EGRDVVALIR KAIQRRGDFD 200
    IDIVAVVNDT VGTMMTCGYD DHNCEIGLIV GTGSNACYME EMRHIDMVEG 250
    DEGRMCINME WGAFGDDGSL NDIRTEFDQE IDMGSLNPGK QLFEKMISGM 300
    YMGELVRLIL VKMAKEELLF GGKLSPELLN TGRFETKDIS DIEGEKDGIR 350
    KAREVLMRLG LDPTQEDCVA THRICQIVST RSASLCAATL AAVLQRIKEN 400
    KGEERLRSTI GVDGSVYKKH PHFAKRLHKT VRRLVPGCDV RFLRSEDGSG 450
    KGAAMVTAVA YRLADQHRAR QKTLEHLQLS HDQLLEVKRR MKVEMERGLS 500
    KETHASAPVK MLPTYVCATP DGTEKGDFLA LDLGGTNFRV LLVRVRNGKW 550
    GGVEMHNKIY AIPQEVMHGT GDELFDHIVQ CIADFLEYMG MKGVSLPLGF 600
    TFSFPCQQNS LDESILLKWT KGFKASGCEG EDVVTLLKEA IHRREEFDLD 650
    VVAVVNDTVG TMMTCGFEDP HCEVGLIVGT GSNACYMEEM RNVELVEGEE 700
    GRMCVNMEWG AFGDNGCLDD FRTEFDVAVD ELSLNPGKQR FEKMISGMYL 750
    GEIVRNILID FTKRGLLFRG RISERLKTRG IFETKFLSQI ESDCLALLQV 800
    RAILQHLGLE STCDDSIIVK EVCTVVARRA AQLCGAGMAA VVDRIRENRG 850
    LDALKVTVGV DGTLYKLHPH FAKVMHETVK DLAPKCDVSF LQSEDGSGKG 900
    AALITAVACR IREAGQR 917
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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. 23 interactions.
    DIPi DIP-50110N.
    IntActi P52789. 4 interactions.
    MINTi MINT-1461614.
    STRINGi 9606.ENSP00000290573.

    Chemistry

    BindingDBi P52789.
    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.
    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

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

    Gene expression databases

    ArrayExpressi P52789.
    Bgeei P52789.
    CleanExi HS_HK2.
    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

    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: October 1, 2014
    This is version 148 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