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O08528 (HXK2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hexokinase-2

EC=2.7.1.1
Alternative name(s):
Hexokinase type II
Short name=HK II
Gene names
Name:Hk2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length917 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 By similarity.

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
   DomainRepeat
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termAllosteric enzyme
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic mitochondrial changes

Inferred from genetic interaction PubMed 18350175. Source: MGI

carbohydrate phosphorylation

Inferred from mutant phenotype PubMed 10428828. Source: MGI

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 metabolic process

Inferred from mutant phenotype PubMed 10428828. Source: MGI

glycolytic process

Inferred from Biological aspect of Ancestor. Source: RefGenome

lactation

Inferred from electronic annotation. Source: Ensembl

regulation of glucose import

Inferred from mutant phenotype PubMed 17639019. Source: MGI

   Cellular_componentcytosol

Inferred from Biological aspect of Ancestor. Source: RefGenome

mitochondrial outer membrane

Inferred from electronic annotation. Source: Ensembl

mitochondrion

Inferred from direct assay PubMed 18614015. Source: MGI

   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

glucose binding

Inferred from electronic annotation. Source: Ensembl

hexokinase activity

Inferred from direct assay PubMed 18165236. Source: MGI

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 – 917917Hexokinase-2
PRO_0000197588

Regions

Domain17 – 221205Hexokinase type-1 1
Domain223 – 462240Hexokinase type-2 1
Domain465 – 669205Hexokinase type-1 2
Domain671 – 910240Hexokinase type-2 2
Nucleotide binding84 – 896ATP 1 Potential
Nucleotide binding425 – 4262ATP 1 By similarity
Nucleotide binding532 – 5376ATP 2 By similarity
Nucleotide binding747 – 7482ATP 2 By similarity
Nucleotide binding784 – 7885ATP 2 By similarity
Nucleotide binding863 – 8675ATP 2 By similarity
Region1 – 1212Hydrophobic
Region13 – 475463Regulatory
Region84 – 885Glucose-6-phosphate 1 binding By similarity
Region155 – 1562Substrate 1 binding By similarity
Region172 – 1732Substrate 1 binding By similarity
Region208 – 2092Substrate 1 binding By similarity
Region291 – 2944Substrate 1 binding By similarity
Region413 – 4153Glucose-6-phosphate 1 binding By similarity
Region476 – 917442Catalytic
Region532 – 5365Glucose-6-phosphate 2 binding By similarity
Region603 – 6042Substrate 2 binding By similarity
Region620 – 6212Substrate 2 binding By similarity
Region656 – 6572Substrate 2 binding By similarity
Region739 – 7424Substrate 2 binding By similarity
Region861 – 8633Glucose-6-phosphate 2 binding By similarity

Sites

Binding site301ATP 1 By similarity
Binding site2091Glucose-6-phosphate 1 By similarity
Binding site2321Glucose-6-phosphate 1 By similarity
Binding site2351Substrate 1 By similarity
Binding site2601Substrate 1 By similarity
Binding site4491Glucose-6-phosphate 1 By similarity
Binding site5581ATP 2 Potential
Binding site6571Glucose-6-phosphate 2 By similarity
Binding site6801ATP 2 By similarity
Binding site6801Glucose-6-phosphate 2 By similarity
Binding site6831Substrate 2 By similarity
Binding site7081Substrate 2 By similarity
Binding site8971Glucose-6-phosphate 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
O08528 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 44293E7A92D724B3

FASTA917102,535
        10         20         30         40         50         60 
MIASHMIACL FTELNQNQVQ KVDQYLYHMR LSDETLLEIS RRFRKEMEKG LGATTHPTAA 

        70         80         90        100        110        120 
VKMLPTFVRS TPDGTEHGEF LALDLGGTNF RVLRVRVTDN GLQRVEMENQ IYAIPEDIMR 

       130        140        150        160        170        180 
GSGTQLFDHI AECLANFMDK LQIKEKKLPL GFTFSFPCHQ TKLDESFLVS WTKGFKSSGV 

       190        200        210        220        230        240 
EGRDVVDLIR KAIQRRGDFD IDIVAVVNDT VGTMMTCGYD DQNCEIGLIV GTGSNACYME 

       250        260        270        280        290        300 
EMRHIDMVEG DEGRMCINME WGAFGDDGTL NDIRTEFDRE IDMGSLNPGK QLFEKMISGM 

       310        320        330        340        350        360 
YMGELVRLIL VKMAKAELLF QGKLSPELLT TGSFETKDVS DIEDDKDGIQ KAYQILVRLG 

       370        380        390        400        410        420 
LSPLQEDCVA THRICQIVST RSASLCAATL AAVLWRIKEN KGEERLRSTI GVDGSVYKKH 

       430        440        450        460        470        480 
PHFAKRLHKA VRRLVPDCDV RFLRSEDGSG KGAAMVTAVA YRLADQHRAR QKTLESLKLS 

       490        500        510        520        530        540 
HEQLLEVKRR MKVEMEQGLS KETHEAAPVK MLPTYVCATP DGTEKGDFLA LDLGGTNFRV 

       550        560        570        580        590        600 
LLVRVRNGKR RGVEMHNKIY SIPQEVMHGT GEELFDHIVQ CIADFLEYMG MKGVSLPLGF 

       610        620        630        640        650        660 
TFSFPCQQNS LDQSILLKWT KGFKASGCEG EDVVTLLKEA IRRREEFDLD VVAVVNDTVG 

       670        680        690        700        710        720 
TMMTCGYEDP HCEVGLIVGT GSNACYMEEM RNVELVDGEE GRMCVNMEWG AFGDNGCLDD 

       730        740        750        760        770        780 
LRTVFDVAVD ELSLNPGKQR FEKMISGMYL GEIVRNILID FTKRGLLFRG RISERLKTRG 

       790        800        810        820        830        840 
IFETKFLSQI ESDCLALLQV RAILRHLGLE STCDDSIIVK EVCTVVARRA AQLCGAGMAA 

       850        860        870        880        890        900 
VVDKIRENRG LDNLKVTVGV DGTLYKLHPH FAKVMHETVR DLAPKCDVSF LESEDGSGKG 

       910 
AALITAVACR IREAGQR 

« Hide

References

« Hide 'large scale' references
[1]"Mouse hexokinase II gene: structure, cDNA, promoter analysis, and expression pattern."
Heikkinen S., Suppola S., Malkki M., Deeb S.S., Janne J., Laakso M.
Mamm. Genome 11:91-96(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: 129/SvJ.
Tissue: Liver.
[2]"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: Eye.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y11666, Y11667, Y11668 Genomic DNA. Translation: CAA72366.1.
AJ238540 mRNA. Translation: CAB72257.1.
BC054472 mRNA. Translation: AAH54472.1.
CCDSCCDS20263.1.
RefSeqNP_038848.1. NM_013820.3.
UniGeneMm.255848.
Mm.469167.

3D structure databases

ProteinModelPortalO08528.
SMRO08528. Positions 17-913.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200316. 3 interactions.
DIPDIP-41484N.
IntActO08528. 1 interaction.
MINTMINT-262872.
STRING10090.ENSMUSP00000000642.

PTM databases

PhosphoSiteO08528.

Proteomic databases

MaxQBO08528.
PaxDbO08528.
PRIDEO08528.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000000642; ENSMUSP00000000642; ENSMUSG00000000628.
GeneID15277.
KEGGmmu:15277.
UCSCuc009cll.2. mouse.

Organism-specific databases

CTD3099.
MGIMGI:1315197. Hk2.

Phylogenomic databases

eggNOGCOG5026.
GeneTreeENSGT00390000017159.
HOGENOMHOG000162671.
HOVERGENHBG005020.
InParanoidO08528.
KOK00844.
OMAHHLGLES.
OrthoDBEOG7S21X5.
PhylomeDBO08528.
TreeFamTF314238.

Enzyme and pathway databases

SABIO-RKO08528.
UniPathwayUPA00242.

Gene expression databases

ArrayExpressO08528.
BgeeO08528.
CleanExMM_HK2.
GenevestigatorO08528.

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

ChiTaRSHK2. mouse.
NextBio287909.
PROO08528.
SOURCESearch...

Entry information

Entry nameHXK2_MOUSE
AccessionPrimary (citable) accession number: O08528
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 1, 1997
Last modified: July 9, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot