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P19367

- HXK1_HUMAN

UniProt

P19367 - HXK1_HUMAN

Protein

Hexokinase-1

Gene

HK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 180 (01 Oct 2014)
      Sequence version 3 (17 Oct 2006)
      Previous versions | rss
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    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 1
    Binding sitei155 – 1551Substrate 1
    Binding sitei209 – 2091Glucose-6-phosphate 12 Publications
    Binding sitei232 – 2321Glucose-6-phosphate 12 Publications
    Binding sitei235 – 2351Substrate 1
    Binding sitei260 – 2601Substrate 1
    Binding sitei345 – 3451ATP 1
    Binding sitei449 – 4491Glucose-6-phosphate 12 Publications
    Binding sitei657 – 6571Glucose-6-phosphate 22 Publications
    Binding sitei680 – 6801ATP 2
    Binding sitei680 – 6801Glucose-6-phosphate 22 Publications
    Binding sitei708 – 7081Substrate 2
    Binding sitei742 – 7421Substrate 2
    Binding sitei897 – 8971Glucose-6-phosphate 22 Publications

    Regions

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

    GO - Molecular functioni

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

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. carbohydrate phosphorylation Source: GOC
    3. cell death Source: UniProtKB-KW
    4. cellular glucose homeostasis Source: RefGenome
    5. glucose 6-phosphate metabolic process Source: GOC
    6. glucose transport Source: Reactome
    7. glycolytic process Source: RefGenome
    8. hexose metabolic process Source: UniProtKB-UniPathway
    9. hexose transport Source: Reactome
    10. small molecule metabolic process Source: Reactome
    11. transmembrane transport Source: Reactome

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS08136-MONOMER.
    ReactomeiREACT_212. Glucose transport.
    SABIO-RKP19367.
    UniPathwayiUPA00242.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hexokinase-1 (EC:2.7.1.1)
    Alternative name(s):
    Brain form hexokinase
    Hexokinase type I
    Short name:
    HK I
    Gene namesi
    Name:HK1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:4922. HK1.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. membrane raft Source: Ensembl
    3. mitochondrial outer membrane Source: UniProtKB-SubCell
    4. mitochondrion Source: UniProt

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion outer membrane

    Pathology & Biotechi

    Involvement in diseasei

    Hexokinase deficiency (HK deficiency) [MIM:235700]: Rare autosomal recessive disease with nonspherocytic hemolytic anemia as the predominant clinical feature.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti529 – 5291L → S in HK deficiency. 1 Publication
    VAR_009878
    Natural varianti680 – 6801T → S in HK deficiency; HK Utrecht. 1 Publication
    VAR_023780
    Hereditary motor and sensory neuropathy, Russe type (HMSNR) [MIM:605285]: An autosomal recessive progressive complex peripheral neuropathy characterized by onset in the first decade of distal lower limb weakness and muscle atrophy resulting in walking difficulties. Distal impairment of the upper limbs usually occurs later, as does proximal lower limb weakness. There is distal sensory impairment, with pes cavus and areflexia. Laboratory studies suggest that it is a myelinopathy resulting in reduced nerve conduction velocities in the demyelinating range as well as a length-dependent axonopathy.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Charcot-Marie-Tooth disease, Disease mutation, Neurodegeneration, Neuropathy

    Organism-specific databases

    MIMi235700. phenotype.
    605285. phenotype.
    Orphaneti99953. Charcot-Marie-Tooth disease type 4G.
    90031. Non-spherocytic hemolytic anemia due to hexokinase deficiency.
    PharmGKBiPA29300.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 917917Hexokinase-1PRO_0000197585Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP19367.
    PaxDbiP19367.
    PRIDEiP19367.

    PTM databases

    PhosphoSiteiP19367.

    Expressioni

    Tissue specificityi

    Isoform 2 is erythrocyte specific. Isoform 3 and isoform 4 are testis-specific.

    Gene expression databases

    ArrayExpressiP19367.
    BgeeiP19367.
    CleanExiHS_HK1.
    GenevestigatoriP19367.

    Organism-specific databases

    HPAiCAB010052.
    HPA007043.
    HPA007044.
    HPA011956.

    Interactioni

    Subunit structurei

    Monomer. Interacts with RABL2/RABL2A; binds preferentially to GTP-bound RABL2 By similarity. Interacts with VDAC1. The HK1-VDAC1 complex interacts with ATF2.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    VDAC1P217962EBI-713162,EBI-354158

    Protein-protein interaction databases

    BioGridi109345. 39 interactions.
    IntActiP19367. 10 interactions.
    MINTiMINT-1422832.
    STRINGi9606.ENSP00000348697.

    Structurei

    Secondary structure

    1
    917
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi17 – 259
    Helixi27 – 293
    Helixi33 – 5119
    Turni53 – 553
    Helixi56 – 583
    Beta strandi78 – 10023
    Beta strandi103 – 11210
    Helixi116 – 1194
    Beta strandi120 – 1223
    Helixi123 – 14119
    Beta strandi144 – 1463
    Beta strandi150 – 1545
    Beta strandi161 – 1644
    Turni179 – 1824
    Helixi185 – 19612
    Beta strandi203 – 2075
    Helixi209 – 22012
    Beta strandi224 – 24118
    Helixi242 – 2443
    Beta strandi252 – 2587
    Helixi261 – 2633
    Turni264 – 27310
    Helixi276 – 2838
    Beta strandi285 – 2873
    Helixi294 – 2974
    Helixi299 – 31517
    Helixi320 – 3223
    Turni326 – 3294
    Helixi336 – 3427
    Turni345 – 3473
    Helixi348 – 35811
    Helixi365 – 40137
    Beta strandi404 – 41310
    Helixi415 – 4195
    Helixi423 – 43412
    Beta strandi438 – 4447
    Helixi449 – 47527
    Helixi481 – 49919
    Helixi501 – 5044
    Beta strandi526 – 54621
    Beta strandi548 – 5503
    Beta strandi552 – 5609
    Helixi564 – 5674
    Beta strandi568 – 5703
    Helixi571 – 58919
    Beta strandi597 – 6026
    Beta strandi606 – 6105
    Beta strandi613 – 6164
    Helixi633 – 64412
    Beta strandi650 – 6556
    Helixi657 – 66610
    Beta strandi672 – 68918
    Turni690 – 6923
    Beta strandi700 – 7067
    Helixi709 – 7113
    Turni712 – 7154
    Turni717 – 7215
    Helixi724 – 7318
    Turni734 – 7374
    Helixi742 – 7443
    Turni747 – 7493
    Helixi750 – 76314
    Helixi768 – 7703
    Turni774 – 7774
    Helixi784 – 7907
    Helixi797 – 80711
    Helixi813 – 84836
    Beta strandi852 – 86110
    Helixi863 – 8675
    Helixi871 – 88212
    Beta strandi886 – 8927
    Helixi898 – 91215

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CZAX-ray1.90N1-917[»]
    1DGKX-ray2.80N1-917[»]
    1HKBX-ray2.80A/B1-917[»]
    1HKCX-ray2.80A1-917[»]
    1QHAX-ray2.25A/B1-917[»]
    4F9OX-ray2.65A/B1-914[»]
    4FOEX-ray2.70A/B1-917[»]
    4FOIX-ray2.40A/B1-917[»]
    4FPAX-ray2.48A/B1-917[»]
    4FPBX-ray3.00A/B1-917[»]
    ProteinModelPortaliP19367.
    SMRiP19367. Positions 12-914.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19367.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini17 – 221205Hexokinase type-1 1Add
    BLAST
    Domaini223 – 462240Hexokinase type-2 1Add
    BLAST
    Domaini465 – 668204Hexokinase type-1 2Add
    BLAST
    Domaini671 – 909239Hexokinase type-2 2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 1212HydrophobicAdd
    BLAST
    Regioni13 – 475463RegulatoryAdd
    BLAST
    Regioni84 – 885Glucose-6-phosphate 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
    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.
    HOVERGENiHBG005020.
    KOiK00844.
    OrthoDBiEOG7S21X5.
    PhylomeDBiP19367.
    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]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P19367-1) [UniParc]FASTAAdd to Basket

    Also known as: Common

    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

    MIAAQLLAYY FTELKDDQVK KIDKYLYAMR LSDETLIDIM TRFRKEMKNG    50
    LSRDFNPTAT VKMLPTFVRS IPDGSEKGDF IALDLGGSSF RILRVQVNHE 100
    KNQNVHMESE VYDTPENIVH GSGSQLFDHV AECLGDFMEK RKIKDKKLPV 150
    GFTFSFPCQQ SKIDEAILIT WTKRFKASGV EGADVVKLLN KAIKKRGDYD 200
    ANIVAVVNDT VGTMMTCGYD DQHCEVGLII GTGTNACYME ELRHIDLVEG 250
    DEGRMCINTE WGAFGDDGSL EDIRTEFDRE IDRGSLNPGK QLFEKMVSGM 300
    YLGELVRLIL VKMAKEGLLF EGRITPELLT RGKFNTSDVS AIEKNKEGLH 350
    NAKEILTRLG VEPSDDDCVS VQHVCTIVSF RSANLVAATL GAILNRLRDN 400
    KGTPRLRTTV GVDGSLYKTH PQYSRRFHKT LRRLVPDSDV RFLLSESGSG 450
    KGAAMVTAVA YRLAEQHRQI EETLAHFHLT KDMLLEVKKR MRAEMELGLR 500
    KQTHNNAVVK MLPSFVRRTP DGTENGDFLA LDLGGTNFRV LLVKIRSGKK 550
    RTVEMHNKIY AIPIEIMQGT GEELFDHIVS CISDFLDYMG IKGPRMPLGF 600
    TFSFPCQQTS LDAGILITWT KGFKATDCVG HDVVTLLRDA IKRREEFDLD 650
    VVAVVNDTVG TMMTCAYEEP TCEVGLIVGT GSNACYMEEM KNVEMVEGDQ 700
    GQMCINMEWG AFGDNGCLDD IRTHYDRLVD EYSLNAGKQR YEKMISGMYL 750
    GEIVRNILID FTKKGFLFRG QISETLKTRG IFETKFLSQI ESDRLALLQV 800
    RAILQQLGLN STCDDSILVK TVCGVVSRRA AQLCGAGMAA VVDKIRENRG 850
    LDRLNVTVGV DGTLYKLHPH FSRIMHQTVK ELSPKCNVSF LLSEDGSGKG 900
    AALITAVGVR LRTEASS 917
    Length:917
    Mass (Da):102,486
    Last modified:October 17, 2006 - v3
    Checksum:iF29A6837531C0594
    GO
    Isoform 2 (identifier: P19367-2) [UniParc]FASTAAdd to Basket

    Also known as: Erythrocyte, R

    The sequence of this isoform differs from the canonical sequence as follows:
         1-21: MIAAQLLAYYFTELKDDQVKK → MDCEHSLSLPCRGAEAWEIG

    Show »
    Length:916
    Mass (Da):102,201
    Checksum:i6E528FC4BEC5100B
    GO
    Isoform 3 (identifier: P19367-3) [UniParc]FASTAAdd to Basket

    Also known as: TA, TB

    The sequence of this isoform differs from the canonical sequence as follows:
         1-21: MIAAQLLAYYFTELKDDQVKK → MGQICQRESATAAEKPKLHLLAESE

    Show »
    Length:921
    Mass (Da):102,738
    Checksum:i329F41F87DF6E1D1
    GO
    Isoform 4 (identifier: P19367-4) [UniParc]FASTAAdd to Basket

    Also known as: TD

    The sequence of this isoform differs from the canonical sequence as follows:
         1-21: MIAAQLLAYYFTELKDDQVKK → MAKRALHDF

    Show »
    Length:905
    Mass (Da):101,085
    Checksum:iAE1BC4A3D2604AB0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti730 – 7301D → N in AAA52646. (PubMed:3207429)Curated
    Sequence conflicti730 – 7301D → N in CAA47379. (PubMed:1637300)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti529 – 5291L → S in HK deficiency. 1 Publication
    VAR_009878
    Natural varianti680 – 6801T → S in HK deficiency; HK Utrecht. 1 Publication
    VAR_023780
    Natural varianti776 – 7761L → M.2 Publications
    Corresponds to variant rs1054203 [ dbSNP | Ensembl ].
    VAR_023781

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2121MIAAQ…DQVKK → MDCEHSLSLPCRGAEAWEIG in isoform 2. CuratedVSP_002071Add
    BLAST
    Alternative sequencei1 – 2121MIAAQ…DQVKK → MGQICQRESATAAEKPKLHL LAESE in isoform 3. CuratedVSP_002072Add
    BLAST
    Alternative sequencei1 – 2121MIAAQ…DQVKK → MAKRALHDF in isoform 4. 1 PublicationVSP_002073Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M75126 mRNA. Translation: AAA52646.1.
    AF016365
    , AF016349, AF016351, AF016352, AF016353, AF016354, AF016355, AF016356, AF016357, AF016358, AF016359, AF016360, AF016361, AF016362, AF016363, AF016364 Genomic DNA. Translation: AAC15862.1.
    AF016365
    , AF016349, AF016351, AF016352, AF016353, AF016354, AF016355, AF016356, AF016357, AF016358, AF016359, AF016360, AF016361, AF016362, AF016363, AF016364 Genomic DNA. Translation: AAC15863.1.
    AF016365
    , AF163910, AF163911, AF016351, AF016352, AF016353, AF016354, AF016355, AF016356, AF016357, AF016358, AF016359, AF016360, AF016361, AF016362, AF016363, AF016364 Genomic DNA. Translation: AAF82319.1.
    AF016365
    , AF163912, AF016351, AF016352, AF016353, AF016354, AF016355, AF016356, AF016357, AF016358, AF016359, AF016360, AF016361, AF016362, AF016363, AF016364 Genomic DNA. Translation: AAF82320.1.
    AL596223, AC016821 Genomic DNA. Translation: CAH71506.1.
    AL672126 Genomic DNA. No translation available.
    BC008730 mRNA. Translation: AAH08730.1.
    AF073786 mRNA. Translation: AAC25424.1.
    AF029306 Genomic DNA. Translation: AAC00172.1.
    X66957 mRNA. Translation: CAA47379.1.
    CCDSiCCDS7289.1. [P19367-3]
    CCDS7290.1. [P19367-4]
    CCDS7291.1. [P19367-2]
    CCDS7292.1. [P19367-1]
    PIRiA31869.
    RefSeqiNP_000179.2. NM_000188.2. [P19367-1]
    NP_277031.1. NM_033496.2. [P19367-2]
    NP_277032.1. NM_033497.2. [P19367-3]
    NP_277033.1. NM_033498.2. [P19367-3]
    NP_277035.2. NM_033500.2. [P19367-4]
    XP_005269793.1. XM_005269736.1. [P19367-3]
    UniGeneiHs.370365.

    Genome annotation databases

    EnsembliENST00000298649; ENSP00000298649; ENSG00000156515. [P19367-2]
    ENST00000359426; ENSP00000352398; ENSG00000156515. [P19367-1]
    ENST00000360289; ENSP00000353433; ENSG00000156515. [P19367-4]
    GeneIDi3098.
    KEGGihsa:3098.
    UCSCiuc001jpg.4. human. [P19367-4]
    uc001jph.4. human. [P19367-3]
    uc001jpk.4. human. [P19367-2]
    uc001jpl.4. human. [P19367-1]

    Polymorphism databases

    DMDMi116242516.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Hexokinase entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M75126 mRNA. Translation: AAA52646.1 .
    AF016365
    , AF016349 , AF016351 , AF016352 , AF016353 , AF016354 , AF016355 , AF016356 , AF016357 , AF016358 , AF016359 , AF016360 , AF016361 , AF016362 , AF016363 , AF016364 Genomic DNA. Translation: AAC15862.1 .
    AF016365
    , AF016349 , AF016351 , AF016352 , AF016353 , AF016354 , AF016355 , AF016356 , AF016357 , AF016358 , AF016359 , AF016360 , AF016361 , AF016362 , AF016363 , AF016364 Genomic DNA. Translation: AAC15863.1 .
    AF016365
    , AF163910 , AF163911 , AF016351 , AF016352 , AF016353 , AF016354 , AF016355 , AF016356 , AF016357 , AF016358 , AF016359 , AF016360 , AF016361 , AF016362 , AF016363 , AF016364 Genomic DNA. Translation: AAF82319.1 .
    AF016365
    , AF163912 , AF016351 , AF016352 , AF016353 , AF016354 , AF016355 , AF016356 , AF016357 , AF016358 , AF016359 , AF016360 , AF016361 , AF016362 , AF016363 , AF016364 Genomic DNA. Translation: AAF82320.1 .
    AL596223 , AC016821 Genomic DNA. Translation: CAH71506.1 .
    AL672126 Genomic DNA. No translation available.
    BC008730 mRNA. Translation: AAH08730.1 .
    AF073786 mRNA. Translation: AAC25424.1 .
    AF029306 Genomic DNA. Translation: AAC00172.1 .
    X66957 mRNA. Translation: CAA47379.1 .
    CCDSi CCDS7289.1. [P19367-3 ]
    CCDS7290.1. [P19367-4 ]
    CCDS7291.1. [P19367-2 ]
    CCDS7292.1. [P19367-1 ]
    PIRi A31869.
    RefSeqi NP_000179.2. NM_000188.2. [P19367-1 ]
    NP_277031.1. NM_033496.2. [P19367-2 ]
    NP_277032.1. NM_033497.2. [P19367-3 ]
    NP_277033.1. NM_033498.2. [P19367-3 ]
    NP_277035.2. NM_033500.2. [P19367-4 ]
    XP_005269793.1. XM_005269736.1. [P19367-3 ]
    UniGenei Hs.370365.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CZA X-ray 1.90 N 1-917 [» ]
    1DGK X-ray 2.80 N 1-917 [» ]
    1HKB X-ray 2.80 A/B 1-917 [» ]
    1HKC X-ray 2.80 A 1-917 [» ]
    1QHA X-ray 2.25 A/B 1-917 [» ]
    4F9O X-ray 2.65 A/B 1-914 [» ]
    4FOE X-ray 2.70 A/B 1-917 [» ]
    4FOI X-ray 2.40 A/B 1-917 [» ]
    4FPA X-ray 2.48 A/B 1-917 [» ]
    4FPB X-ray 3.00 A/B 1-917 [» ]
    ProteinModelPortali P19367.
    SMRi P19367. Positions 12-914.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109345. 39 interactions.
    IntActi P19367. 10 interactions.
    MINTi MINT-1422832.
    STRINGi 9606.ENSP00000348697.

    Chemistry

    BindingDBi P19367.
    ChEMBLi CHEMBL2688.

    PTM databases

    PhosphoSitei P19367.

    Polymorphism databases

    DMDMi 116242516.

    Proteomic databases

    MaxQBi P19367.
    PaxDbi P19367.
    PRIDEi P19367.

    Protocols and materials databases

    DNASUi 3098.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000298649 ; ENSP00000298649 ; ENSG00000156515 . [P19367-2 ]
    ENST00000359426 ; ENSP00000352398 ; ENSG00000156515 . [P19367-1 ]
    ENST00000360289 ; ENSP00000353433 ; ENSG00000156515 . [P19367-4 ]
    GeneIDi 3098.
    KEGGi hsa:3098.
    UCSCi uc001jpg.4. human. [P19367-4 ]
    uc001jph.4. human. [P19367-3 ]
    uc001jpk.4. human. [P19367-2 ]
    uc001jpl.4. human. [P19367-1 ]

    Organism-specific databases

    CTDi 3098.
    GeneCardsi GC10P071031.
    HGNCi HGNC:4922. HK1.
    HPAi CAB010052.
    HPA007043.
    HPA007044.
    HPA011956.
    MIMi 142600. gene.
    235700. phenotype.
    605285. phenotype.
    neXtProti NX_P19367.
    Orphaneti 99953. Charcot-Marie-Tooth disease type 4G.
    90031. Non-spherocytic hemolytic anemia due to hexokinase deficiency.
    PharmGKBi PA29300.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5026.
    HOVERGENi HBG005020.
    KOi K00844.
    OrthoDBi EOG7S21X5.
    PhylomeDBi P19367.
    TreeFami TF314238.

    Enzyme and pathway databases

    UniPathwayi UPA00242 .
    BioCyci MetaCyc:HS08136-MONOMER.
    Reactomei REACT_212. Glucose transport.
    SABIO-RK P19367.

    Miscellaneous databases

    ChiTaRSi HK1. human.
    EvolutionaryTracei P19367.
    GenomeRNAii 3098.
    NextBioi 12293.
    PROi P19367.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P19367.
    Bgeei P19367.
    CleanExi HS_HK1.
    Genevestigatori P19367.

    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: sequences of amino- and carboxyl-terminal halves are homologous."
      Nishi S., Seino S., Bell G.I.
      Biochem. Biophys. Res. Commun. 157:937-943(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MET-776.
    2. "Structure of the human hexokinase type I gene and nucleotide sequence of the 5' flanking region."
      Ruzzo A., Andreoni F., Magnani M.
      Biochem. J. 331:607-613(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
    3. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] (ISOFORM 1).
      Tissue: Brain.
    5. "Structure of the 5' region of the human hexokinase type I (HKI) gene and identification of an additional testis-specific HKI mRNA."
      Andreoni F., Ruzzo A., Magnani M.
      Biochim. Biophys. Acta 1493:19-26(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-126 (ISOFORM 4), ALTERNATIVE SPLICING.
    6. "The erythrocyte-specific hexokinase isozyme (HKR) and the common hexokinase isozyme (HKI) are produced from a single gene by alternate promoters."
      Murakami K., Piomelli S.
      Blood 90:272-272(1998)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20 (ISOFORM 2).
    7. Bienvenut W.V., Waridel P., Quadroni M.
      Submitted (MAR-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-20; 31-42; 382-396 AND 900-910, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryonic kidney.
    8. "Human hexokinase type I microheterogeneity is due to different amino-terminal sequences."
      Magnani M., Serafini G., Bianchi M., Casabianca A., Stocchi V.
      J. Biol. Chem. 266:502-505(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 11-31 AND 103-120.
      Tissue: Placenta.
    9. "A recombinant human 'mini'-hexokinase is catalytically active and regulated by hexose 6-phosphates."
      Magnani M., Bianchi M., Casabianca A., Stocchi V., Daniele A., Altruda F., Ferrone M., Silengo L.
      Biochem. J. 285:193-199(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 287-917, VARIANT MET-776.
      Tissue: Placenta.
    10. "Identification of the cDNA for human red blood cell-specific hexokinase isozyme."
      Murakami K., Piomelli S.
      Blood 89:762-766(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING.
    11. "Crystallization and preliminary X-ray analysis of human brain hexokinase."
      Aleshin A.E., Zeng C., Fromm H.J., Honatko R.B.
      FEBS Lett. 391:9-10(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: CRYSTALLIZATION.
    12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "A mutation in an alternative untranslated exon of hexokinase 1 associated with hereditary motor and sensory neuropathy -- Russe (HMSNR)."
      Hantke J., Chandler D., King R., Wanders R.J., Angelicheva D., Tournev I., McNamara E., Kwa M., Guergueltcheva V., Kaneva R., Baas F., Kalaydjieva L.
      Eur. J. Hum. Genet. 17:1606-1614(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN HMSNR.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "PKCepsilon promotes oncogenic functions of ATF2 in the nucleus while blocking its apoptotic function at mitochondria."
      Lau E., Kluger H., Varsano T., Lee K., Scheffler I., Rimm D.L., Ideker T., Ronai Z.A.
      Cell 148:543-555(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATF2 AND VDAC1.
    16. "The mechanism of regulation of hexokinase: new insights from the crystal structure of recombinant human brain hexokinase complexed with glucose and glucose-6-phosphate."
      Aleshin A.E., Zeng C., Bourenkov G.P., Bartunik H.D., Fromm H.J., Honzatko R.B.
      Structure 6:39-50(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 16-914 IN COMPLEX WITH GLUCOSE AND GLUCOSE-6-PHOSPHATE, SUBUNIT.
    17. "Regulation of hexokinase I: crystal structure of recombinant human brain hexokinase complexed with glucose and phosphate."
      Aleshin A.E., Zeng C., Bartunik H.D., Fromm H.J., Honzatko R.B.
      J. Mol. Biol. 282:345-357(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 16-914.
    18. "Binding of non-catalytic ATP to human hexokinase I highlights the structural components for enzyme-membrane association control."
      Rosano C., Sabini E., Rizzi M., Deriu D., Murshudov G., Bianchi M., Serafini G., Magnani M., Bolognesi M.
      Structure 7:1427-1437(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH AMP-PNP AND MAGNESIUM, SUBUNIT.
    19. "Crystal structures of mutant monomeric hexokinase I reveal multiple ADP binding sites and conformational changes relevant to allosteric regulation."
      Aleshin A.E., Kirby C., Liu X., Bourenkov G.P., Bartunik H.D., Fromm H.J., Honzatko R.B.
      J. Mol. Biol. 296:1001-1015(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH GLUCOSE; GLUCOSE-6-PHOSPHATE AND ADP.
    20. "Hexokinase mutations that produce nonspherocytic hemolytic anemia."
      Bianchi M., Magnani M.
      Blood Cells Mol. Dis. 21:2-8(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HK DEFICIENCY SER-529.
    21. "HK Utrecht: missense mutation in the active site of human hexokinase associated with hexokinase deficiency and severe nonspherocytic hemolytic anemia."
      van Wijk R., Rijksen G., Huizinga E.G., Nieuwenhuis H.K., van Solinge W.W.
      Blood 101:345-347(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HK DEFICIENCY SER-680.

    Entry informationi

    Entry nameiHXK1_HUMAN
    AccessioniPrimary (citable) accession number: P19367
    Secondary accession number(s): E9PCK0
    , O43443, O43444, O75574, Q5VTC3, Q96HC8, Q9NNZ4, Q9NNZ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 180 of the entry and version 3 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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