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P52790 (HXK3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hexokinase-3

EC=2.7.1.1
Alternative name(s):
Hexokinase type III
Short name=HK III
Gene names
Name:HK3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length923 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 By similarity.

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.

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
   Coding sequence diversityPolymorphism
   DomainRepeat
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical term3D-structure
Allosteric enzyme
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Traceable author statement. Source: Reactome

carbohydrate phosphorylation

Inferred from direct assay Ref.4. Source: GOC

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

glycolytic process

Inferred from electronic annotation. Source: UniProtKB-KW

hexose metabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

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

mitochondrion

Inferred from electronic annotation. Source: Ensembl

protein complex

Inferred from electronic annotation. Source: Ensembl

   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

Inferred from direct assay Ref.4. Source: MGI

hormone binding

Inferred from electronic annotation. Source: Ensembl

mannokinase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 923923Hexokinase-3
PRO_0000197590

Regions

Domain28 – 231204Hexokinase type-1 1
Domain237 – 475239Hexokinase type-2 1
Domain480 – 675196Hexokinase type-1 2
Domain677 – 916240Hexokinase type-2 2
Nucleotide binding95 – 1006ATP Potential
Nucleotide binding542 – 5476ATP Potential
Region1 – 488488Regulatory
Region162 – 18827Glucose-binding Potential
Region489 – 923435Catalytic
Region603 – 62927Glucose-binding Potential

Natural variations

Natural variant2811G → R.
Corresponds to variant rs35610191 [ dbSNP | Ensembl ].
VAR_034004
Natural variant4801R → W in a colorectal cancer sample; somatic mutation. Ref.5
VAR_036186
Natural variant4991A → V in a breast cancer sample; somatic mutation. Ref.5
VAR_036187

Experimental info

Sequence conflict2771F → L in AAC50732. Ref.1
Sequence conflict4201Q → L in AAC50422. Ref.4
Sequence conflict4311E → Q in AAC50422. Ref.4
Sequence conflict4391V → I in AAC50422. Ref.4
Sequence conflict5101K → R in AAC50422. Ref.4
Sequence conflict512 – 5132LR → SE in AAC50422. Ref.4
Sequence conflict5161A → S in AAC50422. Ref.4
Sequence conflict5191L → S in AAC50422. Ref.4
Sequence conflict530 – 5312PD → LT in AAC50422. Ref.4
Sequence conflict577 – 5782GQ → AE in AAC50422. Ref.4
Sequence conflict6041L → T in AAC50422. Ref.4
Sequence conflict7081R → H in AAC50422. Ref.4
Sequence conflict7181F → L in AAC50422. Ref.4
Sequence conflict7281S → R in AAC50422. Ref.4
Sequence conflict7501M → I in AAC50422. Ref.4
Sequence conflict8311A → V in AAC50422. Ref.4
Sequence conflict8361A → P in AAC50422. Ref.4
Sequence conflict8531E → G in AAC50732. Ref.1
Sequence conflict9181A → T in AAC50422. Ref.4

Secondary structure

......................................................... 923
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P52790 [UniParc].

Last modified September 23, 2008. Version 2.
Checksum: DA75F2A9DBB895FF

FASTA92399,025
        10         20         30         40         50         60 
MDSIGSSGLR QGEETLSCSE EGLPGPSDSS ELVQECLQQF KVTRAQLQQI QASLLGSMEQ 

        70         80         90        100        110        120 
ALRGQASPAP AVRMLPTYVG STPHGTEQGD FVVLELGATG ASLRVLWVTL TGIEGHRVEP 

       130        140        150        160        170        180 
RSQEFVIPQE VMLGAGQQLF DFAAHCLSEF LDAQPVNKQG LQLGFSFSFP CHQTGLDRST 

       190        200        210        220        230        240 
LISWTKGFRC SGVEGQDVVQ LLRDAIRRQG AYNIDVVAVV NDTVGTMMGC EPGVRPCEVG 

       250        260        270        280        290        300 
LVVDTGTNAC YMEEARHVAV LDEDRGRVCV SVEWGSFSDD GALGPVLTTF DHTLDHESLN 

       310        320        330        340        350        360 
PGAQRFEKMI GGLYLGELVR LVLAHLARCG VLFGGCTSPA LLSQGSILLE HVAEMEDPST 

       370        380        390        400        410        420 
GAARVHAILQ DLGLSPGASD VELVQHVCAA VCTRAAQLCA AALAAVLSCL QHSREQQTLQ 

       430        440        450        460        470        480 
VAVATGGRVC ERHPRFCSVL QGTVMLLAPE CDVSLIPSVD GGGRGVAMVT AVAARLAAHR 

       490        500        510        520        530        540 
RLLEETLAPF RLNHDQLAAV QAQMRKAMAK GLRGEASSLR MLPTFVRATP DGSERGDFLA 

       550        560        570        580        590        600 
LDLGGTNFRV LLVRVTTGVQ ITSEIYSIPE TVAQGSGQQL FDHIVDCIVD FQQKQGLSGQ 

       610        620        630        640        650        660 
SLPLGFTFSF PCRQLGLDQG ILLNWTKGFK ASDCEGQDVV SLLREAITRR QAVELNVVAI 

       670        680        690        700        710        720 
VNDTVGTMMS CGYEDPRCEI GLIVGTGTNA CYMEELRNVA GVPGDSGRMC INMEWGAFGD 

       730        740        750        760        770        780 
DGSLAMLSTR FDASVDQASI NPGKQRFEKM ISGMYLGEIV RHILLHLTSL GVLFRGQQIQ 

       790        800        810        820        830        840 
RLQTRDIFKT KFLSEIESDS LALRQVRAIL EDLGLPLTSD DALMVLEVCQ AVSQRAAQLC 

       850        860        870        880        890        900 
GAGVAAVVEK IRENRGLEEL AVSVGVDGTL YKLHPRFSSL VAATVRELAP RCVVTFLQSE 

       910        920 
DGSGKGAALV TAVACRLAQL TRV 

« Hide

References

« Hide 'large scale' references
[1]"Sequence of human hexokinase III cDNA and assignment of the human hexokinase III gene (HK3) to chromosome band 5q35.2 by fluorescence in situ hybridization."
Furuta H., Nishi S., Le Beau M.M., Fernald A.A., Yano H., Bell G.I.
Genomics 36:206-209(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Blood.
[4]"Purification and characterization of the carboxyl-domain of human hexokinase type III expressed as fusion protein."
Palma F., Agostini D., Mason P., Dacha M., Piccoli G., Biagiarelli B., Fiorani M., Stocchi V.
Mol. Cell. Biochem. 155:23-29(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 358-923.
Tissue: Liver.
[5]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] TRP-480 AND VAL-499.
+Additional computationally mapped references.

Web resources

Wikipedia

Hexokinase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U51333 mRNA. Translation: AAC50732.1.
CH471195 Genomic DNA. Translation: EAW85048.1.
BC028129 mRNA. Translation: AAH28129.1.
U42303 mRNA. Translation: AAC50422.1.
CCDSCCDS4407.1.
RefSeqNP_002106.2. NM_002115.2.
UniGeneHs.411695.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3HM8X-ray2.80A/B/C/D480-922[»]
ProteinModelPortalP52790.
SMRP52790. Positions 28-919.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109348. 3 interactions.
IntActP52790. 3 interactions.
STRING9606.ENSP00000292432.

Chemistry

BindingDBP52790.
ChEMBLCHEMBL2709.

PTM databases

PhosphoSiteP52790.

Polymorphism databases

DMDM206729871.

Proteomic databases

MaxQBP52790.
PaxDbP52790.
PRIDEP52790.

Protocols and materials databases

DNASU3101.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000292432; ENSP00000292432; ENSG00000160883.
GeneID3101.
KEGGhsa:3101.
UCSCuc003mez.3. human.

Organism-specific databases

CTD3101.
GeneCardsGC05M176240.
HGNCHGNC:4925. HK3.
MIM142570. gene.
neXtProtNX_P52790.
PharmGKBPA29303.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5026.
HOGENOMHOG000162671.
HOVERGENHBG005020.
InParanoidP52790.
KOK00844.
OMAHGTEQGD.
OrthoDBEOG7S21X5.
PhylomeDBP52790.
TreeFamTF314238.

Enzyme and pathway databases

BioCycMetaCyc:HS08548-MONOMER.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
REACT_15518. Transmembrane transport of small molecules.
SABIO-RKP52790.
UniPathwayUPA00242.

Gene expression databases

ArrayExpressP52790.
BgeeP52790.
CleanExHS_HK3.
GenevestigatorP52790.

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. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP52790.
GeneWikiHK3.
GenomeRNAi3101.
NextBio12311.
PROP52790.
SOURCESearch...

Entry information

Entry nameHXK3_HUMAN
AccessionPrimary (citable) accession number: P52790
Secondary accession number(s): Q8N1E7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: September 23, 2008
Last modified: July 9, 2014
This is version 130 of the entry and version 2 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 5

Human chromosome 5: entries, gene names and cross-references to MIM