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P19367 (HXK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 175. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hexokinase-1

EC=2.7.1.1
Alternative name(s):
Brain form hexokinase
Hexokinase type I
Short name=HK I
Gene names
Name:HK1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length917 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Enzyme regulation

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

Pathway

Carbohydrate metabolism; hexose metabolism.

Subunit structure

Monomer. Interacts with RABL2/RABL2A; binds preferentially to GTP-bound RABL2 By similarity. Interacts with VDAC1. The HK1-VDAC1 complex interacts with ATF2. Ref.15 Ref.16 Ref.18

Subcellular location

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

Tissue specificity

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

Domain

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.

Involvement in disease

Hexokinase deficiency (HK deficiency) [MIM:235700]: Rare autosomal recessive disease with nonspherocytic hemolytic anemia as the predominant clinical feature.
Note: The disease is caused by mutations affecting the gene represented in this entry.

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13

Miscellaneous

In vertebrates there are four major glucose-phosphorylating isoenzymes, designated hexokinase I, II, III and IV (glucokinase).

Sequence similarities

Belongs to the hexokinase family.

Contains 2 hexokinase type-1 domains.

Contains 2 hexokinase type-2 domains.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentMembrane
Mitochondrion
Mitochondrion outer membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCharcot-Marie-Tooth disease
Disease mutation
Neurodegeneration
Neuropathy
   DomainRepeat
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMAcetylation
   Technical term3D-structure
Allosteric enzyme
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Traceable author statement. Source: Reactome

carbohydrate phosphorylation

Inferred from Biological aspect of Ancestor. Source: GOC

cell death

Inferred from electronic annotation. Source: UniProtKB-KW

cellular glucose homeostasis

Inferred from Biological aspect of Ancestor. Source: RefGenome

glucose 6-phosphate metabolic process

Inferred from Biological aspect of Ancestor. Source: GOC

glucose transport

Traceable author statement. Source: Reactome

glycolysis

Inferred from Biological aspect of Ancestor. Source: RefGenome

hexose transport

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

transmembrane transport

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

membrane raft

Inferred from electronic annotation. Source: Ensembl

mitochondrial outer membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay PubMed 20833797. Source: UniProt

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

fructokinase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

glucokinase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

hexokinase activity

Traceable author statement Ref.1. Source: ProtInc

mannokinase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

VDAC1P217962EBI-713162,EBI-354158

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P19367-1)

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.
Isoform 2 (identifier: P19367-2)

Also known as: Erythrocyte; R;

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: MIAAQLLAYYFTELKDDQVKK → MDCEHSLSLPCRGAEAWEIG
Isoform 3 (identifier: P19367-3)

Also known as: TA; TB;

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: MIAAQLLAYYFTELKDDQVKK → MGQICQRESATAAEKPKLHLLAESE
Isoform 4 (identifier: P19367-4)

Also known as: TD;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 917917Hexokinase-1
PRO_0000197585

Regions

Domain17 – 221205Hexokinase type-1 1
Domain223 – 462240Hexokinase type-2 1
Domain465 – 668204Hexokinase type-1 2
Domain671 – 909239Hexokinase type-2 2
Nucleotide binding84 – 896ATP 1 Potential
Nucleotide binding425 – 4262ATP 1
Nucleotide binding532 – 5376ATP 2
Nucleotide binding747 – 7482ATP 2
Nucleotide binding784 – 7885ATP 2
Nucleotide binding863 – 8675ATP 2
Region1 – 1212Hydrophobic
Region13 – 475463Regulatory
Region84 – 885Glucose-6-phosphate 1 binding
Region172 – 1732Substrate 1 binding
Region208 – 2092Substrate 1 binding
Region291 – 2944Substrate 1 binding
Region413 – 4153Glucose-6-phosphate 1 binding
Region476 – 917442Catalytic
Region532 – 5365Glucose-6-phosphate 2 binding
Region603 – 6042Substrate 2 binding
Region620 – 6212Substrate 2 binding
Region656 – 6572Substrate 2 binding
Region682 – 6832Substrate 2 binding
Region861 – 8633Glucose-6-phosphate 2 binding

Sites

Binding site301ATP 1
Binding site1551Substrate 1
Binding site2091Glucose-6-phosphate 1
Binding site2321Glucose-6-phosphate 1
Binding site2351Substrate 1
Binding site2601Substrate 1
Binding site3451ATP 1
Binding site4491Glucose-6-phosphate 1
Binding site6571Glucose-6-phosphate 2
Binding site6801ATP 2
Binding site6801Glucose-6-phosphate 2
Binding site7081Substrate 2
Binding site7421Substrate 2
Binding site8971Glucose-6-phosphate 2

Amino acid modifications

Modified residue11N-acetylmethionine Ref.7 Ref.12

Natural variations

Alternative sequence1 – 2121MIAAQ…DQVKK → MDCEHSLSLPCRGAEAWEIG in isoform 2.
VSP_002071
Alternative sequence1 – 2121MIAAQ…DQVKK → MGQICQRESATAAEKPKLHL LAESE in isoform 3.
VSP_002072
Alternative sequence1 – 2121MIAAQ…DQVKK → MAKRALHDF in isoform 4.
VSP_002073
Natural variant5291L → S in HK deficiency. Ref.20
VAR_009878
Natural variant6801T → S in HK deficiency; HK Utrecht. Ref.21
VAR_023780
Natural variant7761L → M. Ref.1 Ref.9
Corresponds to variant rs1054203 [ dbSNP | Ensembl ].
VAR_023781

Experimental info

Sequence conflict7301D → N in AAA52646. Ref.1
Sequence conflict7301D → N in CAA47379. Ref.9

Secondary structure

...................................................................................................................................... 917
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Common) [UniParc].

Last modified October 17, 2006. Version 3.
Checksum: F29A6837531C0594

FASTA917102,486
        10         20         30         40         50         60 
MIAAQLLAYY FTELKDDQVK KIDKYLYAMR LSDETLIDIM TRFRKEMKNG LSRDFNPTAT 

        70         80         90        100        110        120 
VKMLPTFVRS IPDGSEKGDF IALDLGGSSF RILRVQVNHE KNQNVHMESE VYDTPENIVH 

       130        140        150        160        170        180 
GSGSQLFDHV AECLGDFMEK RKIKDKKLPV GFTFSFPCQQ SKIDEAILIT WTKRFKASGV 

       190        200        210        220        230        240 
EGADVVKLLN KAIKKRGDYD ANIVAVVNDT VGTMMTCGYD DQHCEVGLII GTGTNACYME 

       250        260        270        280        290        300 
ELRHIDLVEG DEGRMCINTE WGAFGDDGSL EDIRTEFDRE IDRGSLNPGK QLFEKMVSGM 

       310        320        330        340        350        360 
YLGELVRLIL VKMAKEGLLF EGRITPELLT RGKFNTSDVS AIEKNKEGLH NAKEILTRLG 

       370        380        390        400        410        420 
VEPSDDDCVS VQHVCTIVSF RSANLVAATL GAILNRLRDN KGTPRLRTTV GVDGSLYKTH 

       430        440        450        460        470        480 
PQYSRRFHKT LRRLVPDSDV RFLLSESGSG KGAAMVTAVA YRLAEQHRQI EETLAHFHLT 

       490        500        510        520        530        540 
KDMLLEVKKR MRAEMELGLR KQTHNNAVVK MLPSFVRRTP DGTENGDFLA LDLGGTNFRV 

       550        560        570        580        590        600 
LLVKIRSGKK RTVEMHNKIY AIPIEIMQGT GEELFDHIVS CISDFLDYMG IKGPRMPLGF 

       610        620        630        640        650        660 
TFSFPCQQTS LDAGILITWT KGFKATDCVG HDVVTLLRDA IKRREEFDLD VVAVVNDTVG 

       670        680        690        700        710        720 
TMMTCAYEEP TCEVGLIVGT GSNACYMEEM KNVEMVEGDQ GQMCINMEWG AFGDNGCLDD 

       730        740        750        760        770        780 
IRTHYDRLVD EYSLNAGKQR YEKMISGMYL GEIVRNILID FTKKGFLFRG QISETLKTRG 

       790        800        810        820        830        840 
IFETKFLSQI ESDRLALLQV RAILQQLGLN STCDDSILVK TVCGVVSRRA AQLCGAGMAA 

       850        860        870        880        890        900 
VVDKIRENRG LDRLNVTVGV DGTLYKLHPH FSRIMHQTVK ELSPKCNVSF LLSEDGSGKG 

       910 
AALITAVGVR LRTEASS 

« Hide

Isoform 2 (Erythrocyte) (R) [UniParc].

Checksum: 6E528FC4BEC5100B
Show »

FASTA916102,201
Isoform 3 (TA) (TB) [UniParc].

Checksum: 329F41F87DF6E1D1
Show »

FASTA921102,738
Isoform 4 (TD) [UniParc].

Checksum: AE1BC4A3D2604AB0
Show »

FASTA905101,085

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Wikipedia

Hexokinase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M75126 mRNA. Translation: AAA52646.1.
AF016365 expand/collapse EMBL AC list , AF016349, AF016351, AF016352, AF016353, AF016354, AF016355, AF016356, AF016357, AF016358, AF016359, AF016360, AF016361, AF016362, AF016363, AF016364 Genomic DNA. Translation: AAC15862.1.
AF016365 expand/collapse EMBL AC list , AF016349, AF016351, AF016352, AF016353, AF016354, AF016355, AF016356, AF016357, AF016358, AF016359, AF016360, AF016361, AF016362, AF016363, AF016364 Genomic DNA. Translation: AAC15863.1.
AF016365 expand/collapse EMBL AC list , AF163910, AF163911, AF016351, AF016352, AF016353, AF016354, AF016355, AF016356, AF016357, AF016358, AF016359, AF016360, AF016361, AF016362, AF016363, AF016364 Genomic DNA. Translation: AAF82319.1.
AF016365 expand/collapse EMBL AC list , 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.
PIRA31869.
RefSeqNP_000179.2. NM_000188.2.
NP_277031.1. NM_033496.2.
NP_277032.1. NM_033497.2.
NP_277033.1. NM_033498.2.
NP_277035.2. NM_033500.2.
XP_005269793.1. XM_005269736.1.
UniGeneHs.370365.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP19367.
SMRP19367. Positions 12-914.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109345. 35 interactions.
IntActP19367. 9 interactions.
MINTMINT-1422832.
STRING9606.ENSP00000348697.

Chemistry

BindingDBP19367.
ChEMBLCHEMBL2688.

PTM databases

PhosphoSiteP19367.

Polymorphism databases

DMDM116242516.

Proteomic databases

PaxDbP19367.
PRIDEP19367.

Protocols and materials databases

DNASU3098.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000298649; ENSP00000298649; ENSG00000156515. [P19367-2]
ENST00000359426; ENSP00000352398; ENSG00000156515. [P19367-1]
ENST00000360289; ENSP00000353433; ENSG00000156515. [P19367-4]
ENST00000404387; ENSP00000384774; ENSG00000156515. [P19367-3]
GeneID3098.
KEGGhsa:3098.
UCSCuc001jpg.4. human. [P19367-4]
uc001jph.4. human. [P19367-3]
uc001jpk.4. human. [P19367-2]
uc001jpl.4. human. [P19367-1]

Organism-specific databases

CTD3098.
GeneCardsGC10P071031.
HGNCHGNC:4922. HK1.
HPACAB010052.
HPA007043.
HPA007044.
HPA011956.
MIM142600. gene.
235700. phenotype.
605285. phenotype.
neXtProtNX_P19367.
Orphanet99953. Charcot-Marie-Tooth disease type 4G.
90031. Non-spherocytic hemolytic anemia due to hexokinase deficiency.
PharmGKBPA29300.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5026.
HOVERGENHBG005020.
KOK00844.
OrthoDBEOG7S21X5.
PhylomeDBP19367.
TreeFamTF314238.

Enzyme and pathway databases

BioCycMetaCyc:HS08136-MONOMER.
ReactomeREACT_111217. Metabolism.
REACT_15518. Transmembrane transport of small molecules.
SABIO-RKP19367.
UniPathwayUPA00242.

Gene expression databases

ArrayExpressP19367.
BgeeP19367.
CleanExHS_HK1.
GenevestigatorP19367.

Family and domain databases

InterProIPR001312. Hexokinase.
IPR022673. Hexokinase_C.
IPR019807. Hexokinase_CS.
IPR022672. Hexokinase_N.
[Graphical view]
PANTHERPTHR19443. PTHR19443. 1 hit.
PfamPF00349. Hexokinase_1. 2 hits.
PF03727. Hexokinase_2. 2 hits.
[Graphical view]
PRINTSPR00475. HEXOKINASE.
PROSITEPS00378. HEXOKINASES. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHK1. human.
EvolutionaryTraceP19367.
GenomeRNAi3098.
NextBio12293.
PROP19367.
SOURCESearch...

Entry information

Entry nameHXK1_HUMAN
AccessionPrimary (citable) accession number: P19367
Secondary accession number(s): E9PCK0 expand/collapse secondary AC list , O43443, O43444, O75574, Q5VTC3, Q96HC8, Q9NNZ4, Q9NNZ5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: October 17, 2006
Last modified: April 16, 2014
This is version 175 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM