GenomeNet

Database: UniProt/SWISS-PROT
Entry: HXK1_HUMAN
LinkDB: HXK1_HUMAN
Original site: HXK1_HUMAN 
ID   HXK1_HUMAN              Reviewed;         917 AA.
AC   P19367; E9PCK0; O43443; O43444; O75574; Q5VTC3; Q96HC8; Q9NNZ4;
AC   Q9NNZ5;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 3.
DT   05-DEC-2018, entry version 220.
DE   RecName: Full=Hexokinase-1;
DE            EC=2.7.1.1;
DE   AltName: Full=Brain form hexokinase;
DE   AltName: Full=Hexokinase type I;
DE            Short=HK I;
GN   Name=HK1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT MET-776.
RX   PubMed=3207429; DOI=10.1016/S0006-291X(88)80964-1;
RA   Nishi S., Seino S., Bell G.I.;
RT   "Human hexokinase: sequences of amino- and carboxyl-terminal halves
RT   are homologous.";
RL   Biochem. Biophys. Res. Commun. 157:937-943(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX   PubMed=9531504; DOI=10.1042/bj3310607;
RA   Ruzzo A., Andreoni F., Magnani M.;
RT   "Structure of the human hexokinase type I gene and nucleotide sequence
RT   of the 5' flanking region.";
RL   Biochem. J. 331:607-613(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA   Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA   Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA   Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA   Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA   Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA   Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA   Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA   Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA   Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA   Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA   Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA   Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA   Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA   Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA   Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA   Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA   Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-126 (ISOFORM 4), AND ALTERNATIVE
RP   SPLICING.
RX   PubMed=10978502; DOI=10.1016/S0167-4781(00)00147-0;
RA   Andreoni F., Ruzzo A., Magnani M.;
RT   "Structure of the 5' region of the human hexokinase type I (HKI) gene
RT   and identification of an additional testis-specific HKI mRNA.";
RL   Biochim. Biophys. Acta 1493:19-26(2000).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20 (ISOFORM 2).
RA   Murakami K., Piomelli S.;
RT   "The erythrocyte-specific hexokinase isozyme (HKR) and the common
RT   hexokinase isozyme (HKI) are produced from a single gene by alternate
RT   promoters.";
RL   Blood 90:272-272(1998).
RN   [7]
RP   PROTEIN SEQUENCE OF 1-20; 31-42; 382-396 AND 900-910, ACETYLATION AT
RP   MET-1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RA   Bienvenut W.V., Waridel P., Quadroni M.;
RL   Submitted (MAR-2009) to UniProtKB.
RN   [8]
RP   PROTEIN SEQUENCE OF 11-31 AND 103-120.
RC   TISSUE=Placenta;
RX   PubMed=1985912;
RA   Magnani M., Serafini G., Bianchi M., Casabianca A., Stocchi V.;
RT   "Human hexokinase type I microheterogeneity is due to different amino-
RT   terminal sequences.";
RL   J. Biol. Chem. 266:502-505(1991).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 287-917, AND VARIANT MET-776.
RC   TISSUE=Placenta;
RX   PubMed=1637300; DOI=10.1042/bj2850193;
RA   Magnani M., Bianchi M., Casabianca A., Stocchi V., Daniele A.,
RA   Altruda F., Ferrone M., Silengo L.;
RT   "A recombinant human 'mini'-hexokinase is catalytically active and
RT   regulated by hexose 6-phosphates.";
RL   Biochem. J. 285:193-199(1992).
RN   [10]
RP   ALTERNATIVE SPLICING.
RX   PubMed=9028305;
RA   Murakami K., Piomelli S.;
RT   "Identification of the cDNA for human red blood cell-specific
RT   hexokinase isozyme.";
RL   Blood 89:762-766(1997).
RN   [11]
RP   CRYSTALLIZATION.
RX   PubMed=8706938; DOI=10.1016/0014-5793(96)00688-6;
RA   Aleshin A.E., Zeng C., Fromm H.J., Honatko R.B.;
RT   "Crystallization and preliminary X-ray analysis of human brain
RT   hexokinase.";
RL   FEBS Lett. 391:9-10(1996).
RN   [12]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [13]
RP   INVOLVEMENT IN HMSNR.
RX   PubMed=19536174; DOI=10.1038/ejhg.2009.99;
RA   Hantke J., Chandler D., King R., Wanders R.J., Angelicheva D.,
RA   Tournev I., McNamara E., Kwa M., Guergueltcheva V., Kaneva R.,
RA   Baas F., Kalaydjieva L.;
RT   "A mutation in an alternative untranslated exon of hexokinase 1
RT   associated with hereditary motor and sensory neuropathy -- Russe
RT   (HMSNR).";
RL   Eur. J. Hum. Genet. 17:1606-1614(2009).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [15]
RP   INTERACTION WITH ATF2 AND VDAC1.
RX   PubMed=22304920; DOI=10.1016/j.cell.2012.01.016;
RA   Lau E., Kluger H., Varsano T., Lee K., Scheffler I., Rimm D.L.,
RA   Ideker T., Ronai Z.A.;
RT   "PKCepsilon promotes oncogenic functions of ATF2 in the nucleus while
RT   blocking its apoptotic function at mitochondria.";
RL   Cell 148:543-555(2012).
RN   [16]
RP   INVOLVEMENT IN RP79, AND VARIANT RP79 LYS-847.
RX   PubMed=25190649; DOI=10.1167/iovs.14-15419;
RA   Sullivan L.S., Koboldt D.C., Bowne S.J., Lang S., Blanton S.H.,
RA   Cadena E., Avery C.E., Lewis R.A., Webb-Jones K., Wheaton D.H.,
RA   Birch D.G., Coussa R., Ren H., Lopez I., Chakarova C., Koenekoop R.K.,
RA   Garcia C.A., Fulton R.S., Wilson R.K., Weinstock G.M., Daiger S.P.;
RT   "A dominant mutation in hexokinase 1 (HK1) causes retinitis
RT   pigmentosa.";
RL   Invest. Ophthalmol. Vis. Sci. 55:7147-7158(2014).
RN   [17]
RP   INVOLVEMENT IN RP79, VARIANT RP79 LYS-847, AND CHARACTERIZATION OF
RP   VARIANT RP79 LYS-847.
RX   PubMed=25316723; DOI=10.1167/iovs.14-15520;
RA   Wang F., Wang Y., Zhang B., Zhao L., Lyubasyuk V., Wang K., Xu M.,
RA   Li Y., Wu F., Wen C., Bernstein P.S., Lin D., Zhu S., Wang H.,
RA   Zhang K., Chen R.;
RT   "A missense mutation in HK1 leads to autosomal dominant retinitis
RT   pigmentosa.";
RL   Invest. Ophthalmol. Vis. Sci. 55:7159-7164(2014).
RN   [18]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
RA   Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [19]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 16-914 IN COMPLEX WITH
RP   GLUCOSE AND GLUCOSE-6-PHOSPHATE, AND SUBUNIT.
RX   PubMed=9493266; DOI=10.1016/S0969-2126(98)00006-9;
RA   Aleshin A.E., Zeng C., Bourenkov G.P., Bartunik H.D., Fromm H.J.,
RA   Honzatko R.B.;
RT   "The mechanism of regulation of hexokinase: new insights from the
RT   crystal structure of recombinant human brain hexokinase complexed with
RT   glucose and glucose-6-phosphate.";
RL   Structure 6:39-50(1998).
RN   [20]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 16-914.
RX   PubMed=9735292; DOI=10.1006/jmbi.1998.2017;
RA   Aleshin A.E., Zeng C., Bartunik H.D., Fromm H.J., Honzatko R.B.;
RT   "Regulation of hexokinase I: crystal structure of recombinant human
RT   brain hexokinase complexed with glucose and phosphate.";
RL   J. Mol. Biol. 282:345-357(1998).
RN   [21]
RP   X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH AMP-PNP AND
RP   MAGNESIUM, AND SUBUNIT.
RX   PubMed=10574795; DOI=10.1016/S0969-2126(00)80032-5;
RA   Rosano C., Sabini E., Rizzi M., Deriu D., Murshudov G., Bianchi M.,
RA   Serafini G., Magnani M., Bolognesi M.;
RT   "Binding of non-catalytic ATP to human hexokinase I highlights the
RT   structural components for enzyme-membrane association control.";
RL   Structure 7:1427-1437(1999).
RN   [22]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH GLUCOSE;
RP   GLUCOSE-6-PHOSPHATE AND ADP.
RX   PubMed=10686099; DOI=10.1006/jmbi.1999.3494;
RA   Aleshin A.E., Kirby C., Liu X., Bourenkov G.P., Bartunik H.D.,
RA   Fromm H.J., Honzatko R.B.;
RT   "Crystal structures of mutant monomeric hexokinase I reveal multiple
RT   ADP binding sites and conformational changes relevant to allosteric
RT   regulation.";
RL   J. Mol. Biol. 296:1001-1015(2000).
RN   [23]
RP   VARIANT HK DEFICIENCY SER-529.
RX   PubMed=7655856; DOI=10.1006/bcmd.1995.0002;
RA   Bianchi M., Magnani M.;
RT   "Hexokinase mutations that produce nonspherocytic hemolytic anemia.";
RL   Blood Cells Mol. Dis. 21:2-8(1995).
RN   [24]
RP   VARIANT HK DEFICIENCY SER-680.
RX   PubMed=12393545; DOI=10.1182/blood-2002-06-1851;
RA   van Wijk R., Rijksen G., Huizinga E.G., Nieuwenhuis H.K.,
RA   van Solinge W.W.;
RT   "HK Utrecht: missense mutation in the active site of human hexokinase
RT   associated with hexokinase deficiency and severe nonspherocytic
RT   hemolytic anemia.";
RL   Blood 101:345-347(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-hexose = ADP + D-hexose 6-phosphate + H(+);
CC         Xref=Rhea:RHEA:22740, ChEBI:CHEBI:4194, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61567, ChEBI:CHEBI:456216;
CC         EC=2.7.1.1;
CC   -!- ACTIVITY REGULATION: Hexokinase is an allosteric enzyme inhibited
CC       by its product Glc-6-P.
CC   -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC   -!- SUBUNIT: Monomer. Interacts with RABL2/RABL2A; binds
CC       preferentially to GTP-bound RABL2 (By similarity). Interacts with
CC       VDAC1. The HK1-VDAC1 complex interacts with ATF2. Interacts (via
CC       N-terminal spermatogenic cell-specific region) with PFKM (via C-
CC       terminus) (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:P17710, ECO:0000269|PubMed:10574795,
CC       ECO:0000269|PubMed:10686099, ECO:0000269|PubMed:22304920,
CC       ECO:0000269|PubMed:9493266}.
CC   -!- INTERACTION:
CC       Self; NbExp=2; IntAct=EBI-713162, EBI-713162;
CC       P12931:SRC; NbExp=2; IntAct=EBI-713162, EBI-621482;
CC       P05480:Src (xeno); NbExp=8; IntAct=EBI-713162, EBI-298680;
CC       P21796:VDAC1; NbExp=2; IntAct=EBI-713162, EBI-354158;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane. Note=Its
CC       hydrophobic N-terminal sequence may be involved in membrane
CC       binding.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=Common;
CC         IsoId=P19367-1; Sequence=Displayed;
CC       Name=2; Synonyms=Erythrocyte, R;
CC         IsoId=P19367-2; Sequence=VSP_002071;
CC       Name=3; Synonyms=TA, TB;
CC         IsoId=P19367-3; Sequence=VSP_002072;
CC       Name=4; Synonyms=TD;
CC         IsoId=P19367-4; Sequence=VSP_002073;
CC   -!- TISSUE SPECIFICITY: Isoform 2 is erythrocyte specific. Isoform 3
CC       and isoform 4 are testis-specific.
CC   -!- DOMAIN: The N- and C-terminal halves of this hexokinase show
CC       extensive sequence similarity to each other. The catalytic
CC       activity is associated with the C-terminus while regulatory
CC       function is associated with the N-terminus. Each domain can bind a
CC       single glucose and Gluc-6-P molecule.
CC   -!- DISEASE: Hexokinase deficiency (HK deficiency) [MIM:235700]: Rare
CC       autosomal recessive disease with nonspherocytic hemolytic anemia
CC       as the predominant clinical feature. {ECO:0000269|PubMed:12393545,
CC       ECO:0000269|PubMed:7655856}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Neuropathy, hereditary motor and sensory, Russe type
CC       (HMSNR) [MIM:605285]: An autosomal recessive progressive complex
CC       peripheral neuropathy characterized by onset in the first decade
CC       of distal lower limb weakness and muscle atrophy resulting in
CC       walking difficulties. Distal impairment of the upper limbs usually
CC       occurs later, as does proximal lower limb weakness. There is
CC       distal sensory impairment, with pes cavus and areflexia.
CC       Laboratory studies suggest that it is a myelinopathy resulting in
CC       reduced nerve conduction velocities in the demyelinating range as
CC       well as a length-dependent axonopathy.
CC       {ECO:0000269|PubMed:19536174}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Retinitis pigmentosa 79 (RP79) [MIM:617460]: A form of
CC       retinitis pigmentosa, a retinal dystrophy belonging to the group
CC       of pigmentary retinopathies. Retinitis pigmentosa is characterized
CC       by retinal pigment deposits visible on fundus examination and
CC       primary loss of rod photoreceptor cells followed by secondary loss
CC       of cone photoreceptors. Patients typically have night vision
CC       blindness and loss of midperipheral visual field. As their
CC       condition progresses, they lose their far peripheral visual field
CC       and eventually central vision as well. RP79 inheritance is
CC       autosomal dominant. {ECO:0000269|PubMed:25190649,
CC       ECO:0000269|PubMed:25316723}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- MISCELLANEOUS: In vertebrates there are four major glucose-
CC       phosphorylating isoenzymes, designated hexokinase I, II, III and
CC       IV (glucokinase).
CC   -!- SIMILARITY: Belongs to the hexokinase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01084, ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Hexokinase entry;
CC       URL="https://en.wikipedia.org/wiki/Hexokinase";
DR   EMBL; M75126; AAA52646.1; -; mRNA.
DR   EMBL; AF016365; AAC15862.1; -; Genomic_DNA.
DR   EMBL; AF016349; AAC15862.1; JOINED; Genomic_DNA.
DR   EMBL; AF016351; AAC15862.1; JOINED; Genomic_DNA.
DR   EMBL; AF016352; AAC15862.1; JOINED; Genomic_DNA.
DR   EMBL; AF016353; AAC15862.1; JOINED; Genomic_DNA.
DR   EMBL; AF016354; AAC15862.1; JOINED; Genomic_DNA.
DR   EMBL; AF016355; AAC15862.1; JOINED; Genomic_DNA.
DR   EMBL; AF016356; AAC15862.1; JOINED; Genomic_DNA.
DR   EMBL; AF016357; AAC15862.1; JOINED; Genomic_DNA.
DR   EMBL; AF016358; AAC15862.1; JOINED; Genomic_DNA.
DR   EMBL; AF016359; AAC15862.1; JOINED; Genomic_DNA.
DR   EMBL; AF016360; AAC15862.1; JOINED; Genomic_DNA.
DR   EMBL; AF016361; AAC15862.1; JOINED; Genomic_DNA.
DR   EMBL; AF016362; AAC15862.1; JOINED; Genomic_DNA.
DR   EMBL; AF016363; AAC15862.1; JOINED; Genomic_DNA.
DR   EMBL; AF016364; AAC15862.1; JOINED; Genomic_DNA.
DR   EMBL; AF016365; AAC15863.1; -; Genomic_DNA.
DR   EMBL; AF016349; AAC15863.1; JOINED; Genomic_DNA.
DR   EMBL; AF016351; AAC15863.1; JOINED; Genomic_DNA.
DR   EMBL; AF016352; AAC15863.1; JOINED; Genomic_DNA.
DR   EMBL; AF016353; AAC15863.1; JOINED; Genomic_DNA.
DR   EMBL; AF016354; AAC15863.1; JOINED; Genomic_DNA.
DR   EMBL; AF016355; AAC15863.1; JOINED; Genomic_DNA.
DR   EMBL; AF016356; AAC15863.1; JOINED; Genomic_DNA.
DR   EMBL; AF016357; AAC15863.1; JOINED; Genomic_DNA.
DR   EMBL; AF016358; AAC15863.1; JOINED; Genomic_DNA.
DR   EMBL; AF016359; AAC15863.1; JOINED; Genomic_DNA.
DR   EMBL; AF016360; AAC15863.1; JOINED; Genomic_DNA.
DR   EMBL; AF016361; AAC15863.1; JOINED; Genomic_DNA.
DR   EMBL; AF016362; AAC15863.1; JOINED; Genomic_DNA.
DR   EMBL; AF016363; AAC15863.1; JOINED; Genomic_DNA.
DR   EMBL; AF016364; AAC15863.1; JOINED; Genomic_DNA.
DR   EMBL; AF016365; AAF82319.1; -; Genomic_DNA.
DR   EMBL; AF163910; AAF82319.1; JOINED; Genomic_DNA.
DR   EMBL; AF163911; AAF82319.1; JOINED; Genomic_DNA.
DR   EMBL; AF016351; AAF82319.1; JOINED; Genomic_DNA.
DR   EMBL; AF016352; AAF82319.1; JOINED; Genomic_DNA.
DR   EMBL; AF016353; AAF82319.1; JOINED; Genomic_DNA.
DR   EMBL; AF016354; AAF82319.1; JOINED; Genomic_DNA.
DR   EMBL; AF016355; AAF82319.1; JOINED; Genomic_DNA.
DR   EMBL; AF016356; AAF82319.1; JOINED; Genomic_DNA.
DR   EMBL; AF016357; AAF82319.1; JOINED; Genomic_DNA.
DR   EMBL; AF016358; AAF82319.1; JOINED; Genomic_DNA.
DR   EMBL; AF016359; AAF82319.1; JOINED; Genomic_DNA.
DR   EMBL; AF016360; AAF82319.1; JOINED; Genomic_DNA.
DR   EMBL; AF016361; AAF82319.1; JOINED; Genomic_DNA.
DR   EMBL; AF016362; AAF82319.1; JOINED; Genomic_DNA.
DR   EMBL; AF016363; AAF82319.1; JOINED; Genomic_DNA.
DR   EMBL; AF016364; AAF82319.1; JOINED; Genomic_DNA.
DR   EMBL; AF016365; AAF82320.1; -; Genomic_DNA.
DR   EMBL; AF163912; AAF82320.1; JOINED; Genomic_DNA.
DR   EMBL; AF016351; AAF82320.1; JOINED; Genomic_DNA.
DR   EMBL; AF016352; AAF82320.1; JOINED; Genomic_DNA.
DR   EMBL; AF016353; AAF82320.1; JOINED; Genomic_DNA.
DR   EMBL; AF016354; AAF82320.1; JOINED; Genomic_DNA.
DR   EMBL; AF016355; AAF82320.1; JOINED; Genomic_DNA.
DR   EMBL; AF016356; AAF82320.1; JOINED; Genomic_DNA.
DR   EMBL; AF016357; AAF82320.1; JOINED; Genomic_DNA.
DR   EMBL; AF016358; AAF82320.1; JOINED; Genomic_DNA.
DR   EMBL; AF016359; AAF82320.1; JOINED; Genomic_DNA.
DR   EMBL; AF016360; AAF82320.1; JOINED; Genomic_DNA.
DR   EMBL; AF016361; AAF82320.1; JOINED; Genomic_DNA.
DR   EMBL; AF016362; AAF82320.1; JOINED; Genomic_DNA.
DR   EMBL; AF016363; AAF82320.1; JOINED; Genomic_DNA.
DR   EMBL; AF016364; AAF82320.1; JOINED; Genomic_DNA.
DR   EMBL; AC016821; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL596223; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL672126; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC008730; AAH08730.1; -; mRNA.
DR   EMBL; AF073786; AAC25424.1; -; mRNA.
DR   EMBL; AF029306; AAC00172.1; -; Genomic_DNA.
DR   EMBL; X66957; CAA47379.1; -; mRNA.
DR   CCDS; CCDS7289.1; -. [P19367-3]
DR   CCDS; CCDS7291.1; -. [P19367-2]
DR   CCDS; CCDS7292.1; -. [P19367-1]
DR   PIR; A31869; A31869.
DR   RefSeq; NP_000179.2; NM_000188.2. [P19367-1]
DR   RefSeq; NP_001309293.1; NM_001322364.1. [P19367-3]
DR   RefSeq; NP_277031.1; NM_033496.2. [P19367-2]
DR   RefSeq; NP_277032.1; NM_033497.2. [P19367-3]
DR   RefSeq; NP_277033.1; NM_033498.2. [P19367-3]
DR   RefSeq; NP_277035.2; NM_033500.2. [P19367-4]
DR   RefSeq; XP_011538034.1; XM_011539732.1. [P19367-4]
DR   UniGene; Hs.370365; -.
DR   PDB; 1CZA; X-ray; 1.90 A; N=1-917.
DR   PDB; 1DGK; X-ray; 2.80 A; N=1-917.
DR   PDB; 1HKB; X-ray; 2.80 A; A/B=1-917.
DR   PDB; 1HKC; X-ray; 2.80 A; A=1-917.
DR   PDB; 1QHA; X-ray; 2.25 A; A/B=1-917.
DR   PDB; 4F9O; X-ray; 2.65 A; A/B=1-914.
DR   PDB; 4FOE; X-ray; 2.70 A; A/B=1-917.
DR   PDB; 4FOI; X-ray; 2.40 A; A/B=1-917.
DR   PDB; 4FPA; X-ray; 2.48 A; A/B=1-917.
DR   PDB; 4FPB; X-ray; 3.00 A; A/B=1-917.
DR   PDBsum; 1CZA; -.
DR   PDBsum; 1DGK; -.
DR   PDBsum; 1HKB; -.
DR   PDBsum; 1HKC; -.
DR   PDBsum; 1QHA; -.
DR   PDBsum; 4F9O; -.
DR   PDBsum; 4FOE; -.
DR   PDBsum; 4FOI; -.
DR   PDBsum; 4FPA; -.
DR   PDBsum; 4FPB; -.
DR   ProteinModelPortal; P19367; -.
DR   SMR; P19367; -.
DR   BioGrid; 109345; 54.
DR   CORUM; P19367; -.
DR   DIP; DIP-56245N; -.
DR   IntAct; P19367; 44.
DR   MINT; P19367; -.
DR   STRING; 9606.ENSP00000384774; -.
DR   BindingDB; P19367; -.
DR   ChEMBL; CHEMBL2688; -.
DR   DrugBank; DB02007; alpha-D-glucose 6-phosphate.
DR   DrugBank; DB02379; Beta-D-Glucose.
DR   DrugBank; DB09502; Fludeoxyglucose F-18.
DR   DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
DR   CarbonylDB; P19367; -.
DR   iPTMnet; P19367; -.
DR   PhosphoSitePlus; P19367; -.
DR   SwissPalm; P19367; -.
DR   BioMuta; HK1; -.
DR   DMDM; 116242516; -.
DR   EPD; P19367; -.
DR   MaxQB; P19367; -.
DR   PaxDb; P19367; -.
DR   PeptideAtlas; P19367; -.
DR   PRIDE; P19367; -.
DR   ProteomicsDB; 53648; -.
DR   ProteomicsDB; 53649; -. [P19367-2]
DR   ProteomicsDB; 53650; -. [P19367-3]
DR   ProteomicsDB; 53651; -. [P19367-4]
DR   DNASU; 3098; -.
DR   Ensembl; ENST00000298649; ENSP00000298649; ENSG00000156515. [P19367-2]
DR   Ensembl; ENST00000359426; ENSP00000352398; ENSG00000156515. [P19367-1]
DR   Ensembl; ENST00000360289; ENSP00000353433; ENSG00000156515. [P19367-4]
DR   Ensembl; ENST00000436817; ENSP00000415949; ENSG00000156515. [P19367-3]
DR   Ensembl; ENST00000448642; ENSP00000402103; ENSG00000156515. [P19367-3]
DR   Ensembl; ENST00000643399; ENSP00000494664; ENSG00000156515. [P19367-3]
DR   GeneID; 3098; -.
DR   KEGG; hsa:3098; -.
DR   UCSC; uc001jpg.5; human. [P19367-1]
DR   CTD; 3098; -.
DR   DisGeNET; 3098; -.
DR   EuPathDB; HostDB:ENSG00000156515.21; -.
DR   GeneCards; HK1; -.
DR   HGNC; HGNC:4922; HK1.
DR   HPA; CAB010052; -.
DR   HPA; HPA007043; -.
DR   HPA; HPA007044; -.
DR   MalaCards; HK1; -.
DR   MIM; 142600; gene.
DR   MIM; 235700; phenotype.
DR   MIM; 605285; phenotype.
DR   MIM; 617460; phenotype.
DR   neXtProt; NX_P19367; -.
DR   OpenTargets; ENSG00000156515; -.
DR   Orphanet; 99953; Charcot-Marie-Tooth disease type 4G.
DR   Orphanet; 90031; Non-spherocytic hemolytic anemia due to hexokinase deficiency.
DR   PharmGKB; PA29300; -.
DR   eggNOG; KOG1369; Eukaryota.
DR   eggNOG; COG5026; LUCA.
DR   GeneTree; ENSGT00940000153811; -.
DR   HOVERGEN; HBG005020; -.
DR   InParanoid; P19367; -.
DR   KO; K00844; -.
DR   OMA; HMESEIY; -.
DR   PhylomeDB; P19367; -.
DR   TreeFam; TF314238; -.
DR   BioCyc; MetaCyc:HS08136-MONOMER; -.
DR   BRENDA; 2.7.1.1; 2681.
DR   Reactome; R-HSA-5619056; Defective HK1 causes hexokinase deficiency (HK deficiency).
DR   Reactome; R-HSA-70171; Glycolysis.
DR   SABIO-RK; P19367; -.
DR   SIGNOR; P19367; -.
DR   UniPathway; UPA00242; -.
DR   ChiTaRS; HK1; human.
DR   EvolutionaryTrace; P19367; -.
DR   GenomeRNAi; 3098; -.
DR   PRO; PR:P19367; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   Bgee; ENSG00000156515; Expressed in 230 organ(s), highest expression level in cerebellum.
DR   CleanEx; HS_HK1; -.
DR   ExpressionAtlas; P19367; baseline and differential.
DR   Genevisible; P19367; HS.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008865; F:fructokinase activity; IBA:GO_Central.
DR   GO; GO:0004340; F:glucokinase activity; IBA:GO_Central.
DR   GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR   GO; GO:0004396; F:hexokinase activity; IMP:CAFA.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0019158; F:mannokinase activity; IBA:GO_Central.
DR   GO; GO:0042834; F:peptidoglycan binding; IDA:CAFA.
DR   GO; GO:0061621; P:canonical glycolysis; TAS:Reactome.
DR   GO; GO:0046835; P:carbohydrate phosphorylation; IMP:CAFA.
DR   GO; GO:0001678; P:cellular glucose homeostasis; IBA:GO_Central.
DR   GO; GO:0072655; P:establishment of protein localization to mitochondrion; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR   GO; GO:0072656; P:maintenance of protein location in mitochondrion; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0002741; P:positive regulation of cytokine secretion involved in immune response; IEA:Ensembl.
DR   GO; GO:0050718; P:positive regulation of interleukin-1 beta secretion; IEA:Ensembl.
DR   InterPro; IPR001312; Hexokinase.
DR   InterPro; IPR019807; Hexokinase_BS.
DR   InterPro; IPR022673; Hexokinase_C.
DR   InterPro; IPR022672; Hexokinase_N.
DR   PANTHER; PTHR19443; PTHR19443; 4.
DR   Pfam; PF00349; Hexokinase_1; 2.
DR   Pfam; PF03727; Hexokinase_2; 2.
DR   PROSITE; PS00378; HEXOKINASE_1; 2.
DR   PROSITE; PS51748; HEXOKINASE_2; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Allosteric enzyme; Alternative splicing;
KW   ATP-binding; Charcot-Marie-Tooth disease; Complete proteome;
KW   Direct protein sequencing; Disease mutation; Glycolysis; Kinase;
KW   Membrane; Mitochondrion; Mitochondrion outer membrane;
KW   Neurodegeneration; Neuropathy; Nucleotide-binding; Phosphoprotein;
KW   Polymorphism; Reference proteome; Repeat; Retinitis pigmentosa;
KW   Transferase.
FT   CHAIN         1    917       Hexokinase-1.
FT                                /FTId=PRO_0000197585.
FT   DOMAIN       16    458       Hexokinase 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01084}.
FT   DOMAIN      464    906       Hexokinase 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01084}.
FT   NP_BIND      84     89       ATP 1. {ECO:0000244|PDB:1DGK,
FT                                ECO:0000244|PDB:1HKC,
FT                                ECO:0000269|PubMed:10686099,
FT                                ECO:0000269|PubMed:9735292}.
FT   NP_BIND     425    426       ATP 1. {ECO:0000244|PDB:1CZA,
FT                                ECO:0000244|PDB:1DGK,
FT                                ECO:0000244|PDB:1QHA,
FT                                ECO:0000269|PubMed:10574795,
FT                                ECO:0000269|PubMed:10686099}.
FT   NP_BIND     532    537       ATP 2. {ECO:0000244|PDB:1DGK,
FT                                ECO:0000269|PubMed:10686099}.
FT   NP_BIND     747    748       ATP 2. {ECO:0000244|PDB:1DGK,
FT                                ECO:0000269|PubMed:10686099}.
FT   NP_BIND     784    788       ATP 2. {ECO:0000244|PDB:1DGK,
FT                                ECO:0000269|PubMed:10686099}.
FT   NP_BIND     863    867       ATP 2. {ECO:0000244|PDB:1DGK,
FT                                ECO:0000244|PDB:1HKC,
FT                                ECO:0000269|PubMed:10686099,
FT                                ECO:0000269|PubMed:9735292}.
FT   REGION        1     12       Hydrophobic.
FT   REGION       13    475       Regulatory.
FT   REGION       73    207       Hexokinase small subdomain 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01084}.
FT   REGION       84     91       Glucose-6-phosphate 1 binding.
FT                                {ECO:0000244|PDB:1CZA,
FT                                ECO:0000244|PDB:1HKB,
FT                                ECO:0000244|PDB:1QHA,
FT                                ECO:0000244|PDB:4FOE,
FT                                ECO:0000244|PDB:4FOI,
FT                                ECO:0000244|PDB:4FPA,
FT                                ECO:0000269|PubMed:10574795,
FT                                ECO:0000269|PubMed:10686099,
FT                                ECO:0000269|PubMed:9493266}.
FT   REGION      172    173       Substrate 1 binding.
FT                                {ECO:0000244|PDB:1CZA,
FT                                ECO:0000244|PDB:1DGK,
FT                                ECO:0000244|PDB:1HKB,
FT                                ECO:0000244|PDB:1HKC,
FT                                ECO:0000244|PDB:1QHA,
FT                                ECO:0000244|PDB:4F9O,
FT                                ECO:0000244|PDB:4FOE,
FT                                ECO:0000244|PDB:4FOI,
FT                                ECO:0000244|PDB:4FPA,
FT                                ECO:0000244|PDB:4FPB,
FT                                ECO:0000269|PubMed:10574795,
FT                                ECO:0000269|PubMed:10686099,
FT                                ECO:0000269|PubMed:9493266,
FT                                ECO:0000269|PubMed:9735292}.
FT   REGION      208    447       Hexokinase large subdomain 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01084}.
FT   REGION      208    209       Substrate 1 binding.
FT                                {ECO:0000244|PDB:1CZA,
FT                                ECO:0000244|PDB:1DGK,
FT                                ECO:0000244|PDB:1HKB,
FT                                ECO:0000244|PDB:1HKC,
FT                                ECO:0000244|PDB:1QHA,
FT                                ECO:0000244|PDB:4F9O,
FT                                ECO:0000244|PDB:4FOE,
FT                                ECO:0000244|PDB:4FOI,
FT                                ECO:0000244|PDB:4FPA,
FT                                ECO:0000244|PDB:4FPB,
FT                                ECO:0000269|PubMed:10574795,
FT                                ECO:0000269|PubMed:10686099,
FT                                ECO:0000269|PubMed:9493266,
FT                                ECO:0000269|PubMed:9735292}.
FT   REGION      291    294       Substrate 1 binding.
FT                                {ECO:0000244|PDB:1CZA,
FT                                ECO:0000244|PDB:1DGK,
FT                                ECO:0000244|PDB:1HKB,
FT                                ECO:0000244|PDB:1HKC,
FT                                ECO:0000244|PDB:1QHA,
FT                                ECO:0000244|PDB:4F9O,
FT                                ECO:0000244|PDB:4FOE,
FT                                ECO:0000244|PDB:4FOI,
FT                                ECO:0000244|PDB:4FPA,
FT                                ECO:0000244|PDB:4FPB,
FT                                ECO:0000269|PubMed:10574795,
FT                                ECO:0000269|PubMed:10686099,
FT                                ECO:0000269|PubMed:9493266,
FT                                ECO:0000269|PubMed:9735292}.
FT   REGION      413    415       Glucose-6-phosphate 1 binding.
FT                                {ECO:0000244|PDB:1CZA,
FT                                ECO:0000244|PDB:1HKB,
FT                                ECO:0000244|PDB:1QHA,
FT                                ECO:0000244|PDB:4F9O,
FT                                ECO:0000244|PDB:4FOE,
FT                                ECO:0000244|PDB:4FOI,
FT                                ECO:0000244|PDB:4FPA,
FT                                ECO:0000244|PDB:4FPB,
FT                                ECO:0000269|PubMed:10574795,
FT                                ECO:0000269|PubMed:10686099,
FT                                ECO:0000269|PubMed:9493266}.
FT   REGION      476    917       Catalytic.
FT   REGION      521    655       Hexokinase small subdomain 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01084}.
FT   REGION      532    536       Glucose-6-phosphate 2 binding.
FT                                {ECO:0000244|PDB:1CZA,
FT                                ECO:0000244|PDB:1QHA,
FT                                ECO:0000244|PDB:4FOE,
FT                                ECO:0000244|PDB:4FOI,
FT                                ECO:0000244|PDB:4FPA,
FT                                ECO:0000269|PubMed:10574795,
FT                                ECO:0000269|PubMed:10686099}.
FT   REGION      603    604       Substrate 2 binding.
FT                                {ECO:0000244|PDB:1DGK,
FT                                ECO:0000244|PDB:1HKB,
FT                                ECO:0000244|PDB:4F9O,
FT                                ECO:0000244|PDB:4FOE,
FT                                ECO:0000244|PDB:4FOI,
FT                                ECO:0000244|PDB:4FPA,
FT                                ECO:0000244|PDB:4FPB,
FT                                ECO:0000269|PubMed:10686099,
FT                                ECO:0000269|PubMed:9493266}.
FT   REGION      620    621       Substrate 2 binding.
FT                                {ECO:0000244|PDB:1CZA,
FT                                ECO:0000244|PDB:1DGK,
FT                                ECO:0000244|PDB:1HKB,
FT                                ECO:0000244|PDB:1QHA,
FT                                ECO:0000244|PDB:4F9O,
FT                                ECO:0000244|PDB:4FOE,
FT                                ECO:0000244|PDB:4FOI,
FT                                ECO:0000244|PDB:4FPA,
FT                                ECO:0000244|PDB:4FPB,
FT                                ECO:0000269|PubMed:10574795,
FT                                ECO:0000269|PubMed:10686099,
FT                                ECO:0000269|PubMed:9493266}.
FT   REGION      656    895       Hexokinase large subdomain 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01084}.
FT   REGION      656    657       Substrate 2 binding.
FT                                {ECO:0000244|PDB:1CZA,
FT                                ECO:0000244|PDB:1DGK,
FT                                ECO:0000244|PDB:1HKB,
FT                                ECO:0000244|PDB:1QHA,
FT                                ECO:0000244|PDB:4F9O,
FT                                ECO:0000244|PDB:4FOE,
FT                                ECO:0000244|PDB:4FOI,
FT                                ECO:0000244|PDB:4FPA,
FT                                ECO:0000244|PDB:4FPB,
FT                                ECO:0000269|PubMed:10574795,
FT                                ECO:0000269|PubMed:10686099,
FT                                ECO:0000269|PubMed:9493266}.
FT   REGION      682    683       Substrate 2 binding.
FT                                {ECO:0000244|PDB:1CZA,
FT                                ECO:0000244|PDB:1DGK,
FT                                ECO:0000244|PDB:1HKB,
FT                                ECO:0000244|PDB:1QHA,
FT                                ECO:0000244|PDB:4F9O,
FT                                ECO:0000244|PDB:4FOE,
FT                                ECO:0000244|PDB:4FOI,
FT                                ECO:0000244|PDB:4FPA,
FT                                ECO:0000244|PDB:4FPB,
FT                                ECO:0000269|PubMed:10574795,
FT                                ECO:0000269|PubMed:10686099,
FT                                ECO:0000269|PubMed:9493266}.
FT   REGION      861    863       Glucose-6-phosphate 2 binding.
FT                                {ECO:0000244|PDB:1CZA,
FT                                ECO:0000244|PDB:1HKB,
FT                                ECO:0000244|PDB:1QHA,
FT                                ECO:0000244|PDB:4F9O,
FT                                ECO:0000244|PDB:4FOE,
FT                                ECO:0000244|PDB:4FOI,
FT                                ECO:0000244|PDB:4FPA,
FT                                ECO:0000244|PDB:4FPB,
FT                                ECO:0000269|PubMed:10574795,
FT                                ECO:0000269|PubMed:10686099,
FT                                ECO:0000269|PubMed:9493266}.
FT   BINDING      30     30       ATP 1. {ECO:0000244|PDB:1CZA,
FT                                ECO:0000244|PDB:1DGK,
FT                                ECO:0000244|PDB:1QHA,
FT                                ECO:0000269|PubMed:10574795,
FT                                ECO:0000269|PubMed:10686099}.
FT   BINDING     155    155       Substrate 1. {ECO:0000244|PDB:1DGK,
FT                                ECO:0000244|PDB:1HKB,
FT                                ECO:0000244|PDB:1HKC,
FT                                ECO:0000244|PDB:4F9O,
FT                                ECO:0000244|PDB:4FOE,
FT                                ECO:0000244|PDB:4FOI,
FT                                ECO:0000244|PDB:4FPA,
FT                                ECO:0000269|PubMed:10686099,
FT                                ECO:0000269|PubMed:9493266,
FT                                ECO:0000269|PubMed:9735292}.
FT   BINDING     209    209       Glucose-6-phosphate 1.
FT                                {ECO:0000244|PDB:1CZA,
FT                                ECO:0000244|PDB:1HKB,
FT                                ECO:0000244|PDB:1QHA,
FT                                ECO:0000244|PDB:4FOE,
FT                                ECO:0000244|PDB:4FOI,
FT                                ECO:0000244|PDB:4FPA,
FT                                ECO:0000269|PubMed:10574795,
FT                                ECO:0000269|PubMed:10686099,
FT                                ECO:0000269|PubMed:9493266}.
FT   BINDING     232    232       Glucose-6-phosphate 1.
FT                                {ECO:0000244|PDB:1CZA,
FT                                ECO:0000244|PDB:1HKB,
FT                                ECO:0000244|PDB:1QHA,
FT                                ECO:0000244|PDB:4F9O,
FT                                ECO:0000244|PDB:4FOE,
FT                                ECO:0000244|PDB:4FOI,
FT                                ECO:0000244|PDB:4FPA,
FT                                ECO:0000244|PDB:4FPB,
FT                                ECO:0000269|PubMed:10574795,
FT                                ECO:0000269|PubMed:10686099,
FT                                ECO:0000269|PubMed:9493266}.
FT   BINDING     235    235       Substrate 1. {ECO:0000244|PDB:1CZA,
FT                                ECO:0000244|PDB:1DGK,
FT                                ECO:0000244|PDB:1HKB,
FT                                ECO:0000244|PDB:1HKC,
FT                                ECO:0000244|PDB:1QHA,
FT                                ECO:0000244|PDB:4F9O,
FT                                ECO:0000244|PDB:4FOE,
FT                                ECO:0000244|PDB:4FOI,
FT                                ECO:0000244|PDB:4FPA,
FT                                ECO:0000244|PDB:4FPB,
FT                                ECO:0000269|PubMed:10574795,
FT                                ECO:0000269|PubMed:10686099,
FT                                ECO:0000269|PubMed:9493266,
FT                                ECO:0000269|PubMed:9735292}.
FT   BINDING     260    260       Substrate 1. {ECO:0000244|PDB:1CZA,
FT                                ECO:0000244|PDB:1DGK,
FT                                ECO:0000244|PDB:1HKB,
FT                                ECO:0000244|PDB:1HKC,
FT                                ECO:0000244|PDB:1QHA,
FT                                ECO:0000244|PDB:4F9O,
FT                                ECO:0000244|PDB:4FOE,
FT                                ECO:0000244|PDB:4FOI,
FT                                ECO:0000244|PDB:4FPA,
FT                                ECO:0000244|PDB:4FPB,
FT                                ECO:0000269|PubMed:10574795,
FT                                ECO:0000269|PubMed:10686099,
FT                                ECO:0000269|PubMed:9493266,
FT                                ECO:0000269|PubMed:9735292}.
FT   BINDING     345    345       ATP 1. {ECO:0000244|PDB:1QHA,
FT                                ECO:0000269|PubMed:10574795}.
FT   BINDING     449    449       Glucose-6-phosphate 1.
FT                                {ECO:0000244|PDB:1CZA,
FT                                ECO:0000244|PDB:1HKB,
FT                                ECO:0000244|PDB:1QHA,
FT                                ECO:0000244|PDB:4F9O,
FT                                ECO:0000244|PDB:4FOE,
FT                                ECO:0000244|PDB:4FOI,
FT                                ECO:0000244|PDB:4FPA,
FT                                ECO:0000244|PDB:4FPB,
FT                                ECO:0000269|PubMed:10574795,
FT                                ECO:0000269|PubMed:10686099,
FT                                ECO:0000269|PubMed:9493266}.
FT   BINDING     657    657       Glucose-6-phosphate 2.
FT                                {ECO:0000244|PDB:1CZA,
FT                                ECO:0000244|PDB:1HKB,
FT                                ECO:0000244|PDB:1QHA,
FT                                ECO:0000244|PDB:4FOI,
FT                                ECO:0000244|PDB:4FPA,
FT                                ECO:0000269|PubMed:10574795,
FT                                ECO:0000269|PubMed:10686099,
FT                                ECO:0000269|PubMed:9493266}.
FT   BINDING     680    680       ATP 2. {ECO:0000244|PDB:1DGK,
FT                                ECO:0000244|PDB:1HKC,
FT                                ECO:0000269|PubMed:10686099,
FT                                ECO:0000269|PubMed:9735292}.
FT   BINDING     680    680       Glucose-6-phosphate 2.
FT                                {ECO:0000244|PDB:1CZA,
FT                                ECO:0000244|PDB:1HKB,
FT                                ECO:0000244|PDB:1QHA,
FT                                ECO:0000244|PDB:4F9O,
FT                                ECO:0000244|PDB:4FOE,
FT                                ECO:0000244|PDB:4FOI,
FT                                ECO:0000244|PDB:4FPA,
FT                                ECO:0000244|PDB:4FPB,
FT                                ECO:0000269|PubMed:10574795,
FT                                ECO:0000269|PubMed:10686099,
FT                                ECO:0000269|PubMed:9493266}.
FT   BINDING     708    708       Substrate 2. {ECO:0000244|PDB:1CZA,
FT                                ECO:0000244|PDB:1DGK,
FT                                ECO:0000244|PDB:1HKB,
FT                                ECO:0000244|PDB:1QHA,
FT                                ECO:0000244|PDB:4F9O,
FT                                ECO:0000244|PDB:4FOE,
FT                                ECO:0000244|PDB:4FOI,
FT                                ECO:0000244|PDB:4FPA,
FT                                ECO:0000244|PDB:4FPB,
FT                                ECO:0000269|PubMed:10574795,
FT                                ECO:0000269|PubMed:10686099,
FT                                ECO:0000269|PubMed:9493266}.
FT   BINDING     742    742       Substrate 2. {ECO:0000244|PDB:1CZA,
FT                                ECO:0000244|PDB:1DGK,
FT                                ECO:0000244|PDB:1HKB,
FT                                ECO:0000244|PDB:1QHA,
FT                                ECO:0000244|PDB:4F9O,
FT                                ECO:0000244|PDB:4FOE,
FT                                ECO:0000244|PDB:4FOI,
FT                                ECO:0000244|PDB:4FPA,
FT                                ECO:0000244|PDB:4FPB,
FT                                ECO:0000269|PubMed:10574795,
FT                                ECO:0000269|PubMed:10686099,
FT                                ECO:0000269|PubMed:9493266}.
FT   BINDING     897    897       Glucose-6-phosphate 2.
FT                                {ECO:0000244|PDB:1CZA,
FT                                ECO:0000244|PDB:1HKB,
FT                                ECO:0000244|PDB:1QHA,
FT                                ECO:0000244|PDB:4F9O,
FT                                ECO:0000244|PDB:4FOI,
FT                                ECO:0000244|PDB:4FPA,
FT                                ECO:0000244|PDB:4FPB,
FT                                ECO:0000269|PubMed:10574795,
FT                                ECO:0000269|PubMed:10686099,
FT                                ECO:0000269|PubMed:9493266}.
FT   MOD_RES       1      1       N-acetylmethionine.
FT                                {ECO:0000244|PubMed:19413330,
FT                                ECO:0000244|PubMed:25944712,
FT                                ECO:0000269|Ref.7}.
FT   MOD_RES     337    337       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P05708}.
FT   VAR_SEQ       1     21       MIAAQLLAYYFTELKDDQVKK -> MDCEHSLSLPCRGAEA
FT                                WEIG (in isoform 2). {ECO:0000305}.
FT                                /FTId=VSP_002071.
FT   VAR_SEQ       1     21       MIAAQLLAYYFTELKDDQVKK -> MGQICQRESATAAEKP
FT                                KLHLLAESE (in isoform 3). {ECO:0000305}.
FT                                /FTId=VSP_002072.
FT   VAR_SEQ       1     21       MIAAQLLAYYFTELKDDQVKK -> MAKRALHDF (in
FT                                isoform 4).
FT                                {ECO:0000303|PubMed:10978502}.
FT                                /FTId=VSP_002073.
FT   VARIANT     529    529       L -> S (in HK deficiency;
FT                                dbSNP:rs137853249).
FT                                {ECO:0000269|PubMed:7655856}.
FT                                /FTId=VAR_009878.
FT   VARIANT     680    680       T -> S (in HK deficiency; HK Utrecht;
FT                                dbSNP:rs398122379).
FT                                {ECO:0000269|PubMed:12393545}.
FT                                /FTId=VAR_023780.
FT   VARIANT     776    776       L -> M (in dbSNP:rs1054203).
FT                                {ECO:0000269|PubMed:1637300,
FT                                ECO:0000269|PubMed:3207429}.
FT                                /FTId=VAR_023781.
FT   VARIANT     847    847       E -> K (in RP79; unknown pathological
FT                                significance; no effect on hexokinase
FT                                activity; no effect on protein abundance;
FT                                dbSNP:rs777849213).
FT                                {ECO:0000269|PubMed:25190649,
FT                                ECO:0000269|PubMed:25316723}.
FT                                /FTId=VAR_078923.
FT   CONFLICT    730    730       D -> N (in Ref. 1; AAA52646 and 9;
FT                                CAA47379). {ECO:0000305}.
FT   HELIX        17     25       {ECO:0000244|PDB:1CZA}.
FT   HELIX        27     29       {ECO:0000244|PDB:1CZA}.
FT   HELIX        33     51       {ECO:0000244|PDB:1CZA}.
FT   TURN         53     55       {ECO:0000244|PDB:1CZA}.
FT   HELIX        56     58       {ECO:0000244|PDB:1CZA}.
FT   STRAND       78    100       {ECO:0000244|PDB:1CZA}.
FT   STRAND      103    112       {ECO:0000244|PDB:1CZA}.
FT   HELIX       116    119       {ECO:0000244|PDB:1CZA}.
FT   STRAND      120    122       {ECO:0000244|PDB:1CZA}.
FT   HELIX       123    141       {ECO:0000244|PDB:1CZA}.
FT   STRAND      144    146       {ECO:0000244|PDB:4FOI}.
FT   STRAND      150    154       {ECO:0000244|PDB:1CZA}.
FT   STRAND      161    164       {ECO:0000244|PDB:4FPB}.
FT   TURN        179    182       {ECO:0000244|PDB:4FPB}.
FT   HELIX       185    196       {ECO:0000244|PDB:1CZA}.
FT   STRAND      203    207       {ECO:0000244|PDB:1CZA}.
FT   HELIX       209    220       {ECO:0000244|PDB:1CZA}.
FT   STRAND      224    241       {ECO:0000244|PDB:1CZA}.
FT   HELIX       242    244       {ECO:0000244|PDB:1CZA}.
FT   STRAND      252    258       {ECO:0000244|PDB:1CZA}.
FT   HELIX       261    263       {ECO:0000244|PDB:1CZA}.
FT   TURN        264    273       {ECO:0000244|PDB:1CZA}.
FT   HELIX       276    283       {ECO:0000244|PDB:1CZA}.
FT   STRAND      285    287       {ECO:0000244|PDB:1CZA}.
FT   HELIX       294    297       {ECO:0000244|PDB:1CZA}.
FT   HELIX       299    315       {ECO:0000244|PDB:1CZA}.
FT   HELIX       320    322       {ECO:0000244|PDB:1CZA}.
FT   TURN        326    329       {ECO:0000244|PDB:1CZA}.
FT   HELIX       336    342       {ECO:0000244|PDB:1CZA}.
FT   TURN        345    347       {ECO:0000244|PDB:1CZA}.
FT   HELIX       348    358       {ECO:0000244|PDB:1CZA}.
FT   HELIX       365    401       {ECO:0000244|PDB:1CZA}.
FT   STRAND      404    413       {ECO:0000244|PDB:1CZA}.
FT   HELIX       415    419       {ECO:0000244|PDB:1CZA}.
FT   HELIX       423    434       {ECO:0000244|PDB:1CZA}.
FT   STRAND      438    444       {ECO:0000244|PDB:1CZA}.
FT   HELIX       449    475       {ECO:0000244|PDB:1CZA}.
FT   HELIX       481    499       {ECO:0000244|PDB:1CZA}.
FT   HELIX       501    504       {ECO:0000244|PDB:1CZA}.
FT   STRAND      526    546       {ECO:0000244|PDB:1CZA}.
FT   STRAND      548    550       {ECO:0000244|PDB:1QHA}.
FT   STRAND      552    560       {ECO:0000244|PDB:1CZA}.
FT   HELIX       564    567       {ECO:0000244|PDB:1CZA}.
FT   STRAND      568    570       {ECO:0000244|PDB:4F9O}.
FT   HELIX       571    589       {ECO:0000244|PDB:1CZA}.
FT   STRAND      597    602       {ECO:0000244|PDB:1CZA}.
FT   STRAND      606    610       {ECO:0000244|PDB:1CZA}.
FT   STRAND      613    616       {ECO:0000244|PDB:1CZA}.
FT   HELIX       633    644       {ECO:0000244|PDB:1CZA}.
FT   STRAND      650    655       {ECO:0000244|PDB:1CZA}.
FT   HELIX       657    666       {ECO:0000244|PDB:1CZA}.
FT   STRAND      672    689       {ECO:0000244|PDB:1CZA}.
FT   TURN        690    692       {ECO:0000244|PDB:1CZA}.
FT   STRAND      700    706       {ECO:0000244|PDB:1CZA}.
FT   HELIX       709    711       {ECO:0000244|PDB:1CZA}.
FT   TURN        712    715       {ECO:0000244|PDB:1CZA}.
FT   TURN        717    721       {ECO:0000244|PDB:1CZA}.
FT   HELIX       724    731       {ECO:0000244|PDB:1CZA}.
FT   TURN        734    737       {ECO:0000244|PDB:1CZA}.
FT   HELIX       742    744       {ECO:0000244|PDB:1CZA}.
FT   TURN        747    749       {ECO:0000244|PDB:1CZA}.
FT   HELIX       750    763       {ECO:0000244|PDB:1CZA}.
FT   HELIX       768    770       {ECO:0000244|PDB:1CZA}.
FT   TURN        774    777       {ECO:0000244|PDB:1CZA}.
FT   HELIX       784    790       {ECO:0000244|PDB:1CZA}.
FT   HELIX       797    807       {ECO:0000244|PDB:1CZA}.
FT   HELIX       813    848       {ECO:0000244|PDB:1CZA}.
FT   STRAND      852    861       {ECO:0000244|PDB:1CZA}.
FT   HELIX       863    867       {ECO:0000244|PDB:1CZA}.
FT   HELIX       871    882       {ECO:0000244|PDB:1CZA}.
FT   STRAND      886    892       {ECO:0000244|PDB:1CZA}.
FT   HELIX       898    912       {ECO:0000244|PDB:1CZA}.
SQ   SEQUENCE   917 AA;  102486 MW;  F29A6837531C0594 CRC64;
     MIAAQLLAYY FTELKDDQVK KIDKYLYAMR LSDETLIDIM TRFRKEMKNG LSRDFNPTAT
     VKMLPTFVRS IPDGSEKGDF IALDLGGSSF RILRVQVNHE KNQNVHMESE VYDTPENIVH
     GSGSQLFDHV AECLGDFMEK RKIKDKKLPV GFTFSFPCQQ SKIDEAILIT WTKRFKASGV
     EGADVVKLLN KAIKKRGDYD ANIVAVVNDT VGTMMTCGYD DQHCEVGLII GTGTNACYME
     ELRHIDLVEG DEGRMCINTE WGAFGDDGSL EDIRTEFDRE IDRGSLNPGK QLFEKMVSGM
     YLGELVRLIL VKMAKEGLLF EGRITPELLT RGKFNTSDVS AIEKNKEGLH NAKEILTRLG
     VEPSDDDCVS VQHVCTIVSF RSANLVAATL GAILNRLRDN KGTPRLRTTV GVDGSLYKTH
     PQYSRRFHKT LRRLVPDSDV RFLLSESGSG KGAAMVTAVA YRLAEQHRQI EETLAHFHLT
     KDMLLEVKKR MRAEMELGLR KQTHNNAVVK MLPSFVRRTP DGTENGDFLA LDLGGTNFRV
     LLVKIRSGKK RTVEMHNKIY AIPIEIMQGT GEELFDHIVS CISDFLDYMG IKGPRMPLGF
     TFSFPCQQTS LDAGILITWT KGFKATDCVG HDVVTLLRDA IKRREEFDLD VVAVVNDTVG
     TMMTCAYEEP TCEVGLIVGT GSNACYMEEM KNVEMVEGDQ GQMCINMEWG AFGDNGCLDD
     IRTHYDRLVD EYSLNAGKQR YEKMISGMYL GEIVRNILID FTKKGFLFRG QISETLKTRG
     IFETKFLSQI ESDRLALLQV RAILQQLGLN STCDDSILVK TVCGVVSRRA AQLCGAGMAA
     VVDKIRENRG LDRLNVTVGV DGTLYKLHPH FSRIMHQTVK ELSPKCNVSF LLSEDGSGKG
     AALITAVGVR LRTEASS
//
DBGET integrated database retrieval system