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P27881 (HXK2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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.

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
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic mitochondrial changes

Inferred from electronic annotation. Source: Ensembl

carbohydrate phosphorylation

Inferred from direct assay PubMed 3900069PubMed 6603359PubMed 8619630. Source: RGD

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 catabolic process

Traceable author statement Ref.3. Source: RGD

glycolysis

Inferred from Biological aspect of Ancestor. Source: RefGenome

lactation

Inferred from expression pattern PubMed 10562464. Source: RGD

regulation of glucose import

Inferred from electronic annotation. Source: Ensembl

response to ischemia

Inferred from direct assay PubMed 21410437. Source: RGD

   Cellular_componentcytosol

Inferred from Biological aspect of Ancestor. Source: RefGenome

mitochondrial outer membrane

Traceable author statement Ref.3. Source: RGD

mitochondrion

Inferred from direct assay PubMed 21410437. Source: RGD

   Molecular_functionATP binding

Inferred from direct assay PubMed 3900069PubMed 6603359. Source: RGD

fructokinase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

glucokinase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

glucose binding

Inferred from direct assay PubMed 3900069PubMed 6603359PubMed 8619630. Source: RGD

hexokinase activity

Inferred from direct assay PubMed 15138155PubMed 3900069PubMed 6603359PubMed 8619630. Source: RGD

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_0000197589

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
P27881 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 764EC189C0F90987

FASTA917102,544
        10         20         30         40         50         60 
MIASHMIACL FTELNQNQVQ KVDQFLYHMR 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 DIEEDKDGIE KAYQILMRLG 

       370        380        390        400        410        420 
LNPLQEDCVA 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 KETHAVAPVK 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 IHRREEFDLD 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

[1]"Complete amino acid sequence of the type II isozyme of rat hexokinase, deduced from the cloned cDNA: comparison with a hexokinase from novikoff ascites tumor."
Thelen A.P., Wilson J.E.
Arch. Biochem. Biophys. 286:645-651(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 11-18.
Tissue: Skeletal muscle.
[2]"Nucleotide sequence of the 5'-flanking region of the rat type II hexokinase gene."
Shinohara Y., Ichihara J., Kogure K., Terada H.
Biochim. Biophys. Acta 1260:365-368(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
Strain: Wistar.
[3]"Glucose catabolism in cancer cells. Isolation, sequence, and activity of the promoter for type II hexokinase."
Mathupala S.P., Rempel A., Pedersen P.L.
J. Biol. Chem. 270:16918-16925(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
Strain: Sprague-Dawley.
Tissue: Hepatoma.
[4]"Normal type II hexokinase promoter, first exon, and first intron from hepatocytes."
Rempel A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
Strain: Sprague-Dawley.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M68971 mRNA. Translation: AAA41333.1.
M68972 mRNA. Translation: AAA41334.1.
D26393 Genomic DNA. Translation: BAA05409.1.
U19605 Genomic DNA. Translation: AAB09025.1.
AY082375 Genomic DNA. Translation: AAL92551.1.
PIRS15885.
RefSeqNP_036867.1. NM_012735.2.
UniGeneRn.91375.

3D structure databases

ProteinModelPortalP27881.
SMRP27881. Positions 17-913.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid247136. 3 interactions.
DIPDIP-37314N.
IntActP27881. 1 interaction.
MINTMINT-1775746.
STRING10116.ENSRNOP00000008813.

Chemistry

BindingDBP27881.
ChEMBLCHEMBL5063.

PTM databases

PhosphoSiteP27881.

Proteomic databases

PaxDbP27881.
PRIDEP27881.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000008813; ENSRNOP00000008813; ENSRNOG00000006116.
GeneID25059.
KEGGrno:25059.
UCSCRGD:2797. rat.

Organism-specific databases

CTD3099.
RGD2797. Hk2.

Phylogenomic databases

eggNOGCOG5026.
GeneTreeENSGT00390000017159.
HOGENOMHOG000162671.
HOVERGENHBG005020.
InParanoidP27881.
KOK00844.
OMAHHLGLES.
OrthoDBEOG7S21X5.
PhylomeDBP27881.
TreeFamTF314238.

Enzyme and pathway databases

BRENDA2.7.1.1. 5301.
SABIO-RKP27881.
UniPathwayUPA00242.

Gene expression databases

GenevestigatorP27881.

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

NextBio605276.
PROP27881.

Entry information

Entry nameHXK2_RAT
AccessionPrimary (citable) accession number: P27881
Secondary accession number(s): Q9QWR1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: April 16, 2014
This is version 113 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