Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Hexokinase-2

Gene

HXK2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Main glucose phosphorylating enzyme. May play a regulatory role in both induction and repression of gene expression by glucose.

Catalytic activityi

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

Enzyme regulationi

Subject to allosteric control. Substrate inhibition by ATP.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei111 – 1111ATPSequence Analysis
Binding sitei158 – 1581Substrate; via carbonyl oxygenBy similarity
Binding sitei237 – 2371SubstrateBy similarity
Binding sitei269 – 2691SubstrateBy similarity
Binding sitei302 – 3021SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi86 – 916ATPBy similarity
Nucleotide bindingi307 – 3082ATPBy similarity
Nucleotide bindingi344 – 3485ATPBy similarity
Nucleotide bindingi419 – 4235ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. hexokinase activity Source: SGD

GO - Biological processi

  1. carbohydrate phosphorylation Source: GOC
  2. fructose import Source: SGD
  3. fructose metabolic process Source: SGD
  4. glucose import Source: SGD
  5. glucose metabolic process Source: SGD
  6. glycolytic process Source: SGD
  7. mannose metabolic process Source: SGD
  8. regulation of transcription by glucose Source: SGD
  9. replicative cell aging Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:YGL253W-MONOMER.
BRENDAi2.7.1.1. 984.
ReactomeiREACT_298577. Regulation of gene expression in beta cells.
REACT_302131. Glucose transport.
REACT_318658. Regulation of Glucokinase by Glucokinase Regulatory Protein.
SABIO-RKP04807.
UniPathwayiUPA00242.

Names & Taxonomyi

Protein namesi
Recommended name:
Hexokinase-2 (EC:2.7.1.1)
Alternative name(s):
Hexokinase PII
Hexokinase-B
Gene namesi
Name:HXK2
Synonyms:HEX1, HKB
Ordered Locus Names:YGL253W
ORF Names:NRB486
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL253W.
SGDiS000003222. HXK2.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: SGD
  2. mitochondrion Source: SGD
  3. nucleus Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 486485Hexokinase-2PRO_0000197602Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei15 – 151Phosphoserine3 Publications
Modified residuei38 – 381Phosphothreonine1 Publication
Modified residuei158 – 1581Phosphoserine2 Publications
Modified residuei245 – 2451Phosphoserine1 Publication
Modified residuei272 – 2721PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP04807.
PaxDbiP04807.
PeptideAtlasiP04807.

2D gel databases

SWISS-2DPAGEP04807.

Expressioni

Gene expression databases

GenevestigatoriP04807.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi33026. 150 interactions.
DIPiDIP-2380N.
IntActiP04807. 3 interactions.
MINTiMINT-2784874.
STRINGi4932.YGL253W.

Structurei

Secondary structure

1
486
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi21 – 3414Combined sources
Helixi38 – 5619Combined sources
Beta strandi79 – 879Combined sources
Beta strandi89 – 10315Combined sources
Beta strandi105 – 1139Combined sources
Helixi118 – 1203Combined sources
Helixi126 – 14217Combined sources
Beta strandi152 – 1565Combined sources
Beta strandi159 – 1624Combined sources
Helixi189 – 20012Combined sources
Beta strandi203 – 2097Combined sources
Helixi211 – 22212Combined sources
Beta strandi226 – 24217Combined sources
Helixi244 – 2463Combined sources
Helixi248 – 2503Combined sources
Beta strandi254 – 2563Combined sources
Beta strandi264 – 2674Combined sources
Turni271 – 2766Combined sources
Beta strandi278 – 2803Combined sources
Helixi284 – 2929Combined sources
Beta strandi293 – 2953Combined sources
Helixi300 – 3056Combined sources
Helixi307 – 3093Combined sources
Helixi310 – 32314Combined sources
Beta strandi326 – 3305Combined sources
Turni334 – 3363Combined sources
Helixi345 – 3528Combined sources
Beta strandi355 – 3573Combined sources
Helixi359 – 36911Combined sources
Helixi375 – 39622Combined sources
Helixi398 – 40710Combined sources
Beta strandi410 – 4189Combined sources
Helixi419 – 4235Combined sources
Helixi427 – 43913Combined sources
Helixi446 – 4483Combined sources
Beta strandi449 – 4557Combined sources
Turni459 – 4613Combined sources
Helixi462 – 47110Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IG8X-ray2.20A1-486[»]
2YHXX-ray2.10A152-471[»]
ProteinModelPortaliP04807.
SMRiP04807. Positions 18-486.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04807.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 469449HexokinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni75 – 209135Hexokinase small subdomainPROSITE-ProRule annotationAdd
BLAST
Regioni175 – 1762Substrate bindingBy similarity
Regioni210 – 458249Hexokinase large subdomainPROSITE-ProRule annotationAdd
BLAST
Regioni210 – 2112Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the hexokinase family.PROSITE-ProRule annotationCurated
Contains 1 hexokinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5026.
GeneTreeiENSGT00390000017159.
HOGENOMiHOG000162670.
InParanoidiP04807.
KOiK00844.
OMAiAIAIDGC.
OrthoDBiEOG79SF68.

Family and domain databases

InterProiIPR001312. Hexokinase.
IPR022673. Hexokinase_C.
IPR019807. Hexokinase_CS.
IPR022672. Hexokinase_N.
[Graphical view]
PANTHERiPTHR19443. PTHR19443. 1 hit.
PfamiPF00349. Hexokinase_1. 1 hit.
PF03727. Hexokinase_2. 1 hit.
[Graphical view]
PRINTSiPR00475. HEXOKINASE.
PROSITEiPS00378. HEXOKINASE_1. 1 hit.
PS51748. HEXOKINASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P04807-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVHLGPKKPQ ARKGSMADVP KELMQQIENF EKIFTVPTET LQAVTKHFIS
60 70 80 90 100
ELEKGLSKKG GNIPMIPGWV MDFPTGKESG DFLAIDLGGT NLRVVLVKLG
110 120 130 140 150
GDRTFDTTQS KYRLPDAMRT TQNPDELWEF IADSLKAFID EQFPQGISEP
160 170 180 190 200
IPLGFTFSFP ASQNKINEGI LQRWTKGFDI PNIENHDVVP MLQKQITKRN
210 220 230 240 250
IPIEVVALIN DTTGTLVASY YTDPETKMGV IFGTGVNGAY YDVCSDIEKL
260 270 280 290 300
QGKLSDDIPP SAPMAINCEY GSFDNEHVVL PRTKYDITID EESPRPGQQT
310 320 330 340 350
FEKMSSGYYL GEILRLALMD MYKQGFIFKN QDLSKFDKPF VMDTSYPARI
360 370 380 390 400
EEDPFENLED TDDLFQNEFG INTTVQERKL IRRLSELIGA RAARLSVCGI
410 420 430 440 450
AAICQKRGYK TGHIAADGSV YNRYPGFKEK AANALKDIYG WTQTSLDDYP
460 470 480
IKIVPAEDGS GAGAAVIAAL AQKRIAEGKS VGIIGA
Length:486
Mass (Da):53,942
Last modified:January 23, 2007 - v4
Checksum:iD55FF3F8992B2FEF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti29 – 291N → I in CAA27203 (PubMed:3003701).Curated
Sequence conflicti33 – 331I → N in AAA34697 (PubMed:3905511).Curated
Sequence conflicti33 – 331I → N in AAA34699 (PubMed:3905511).Curated
Sequence conflicti61 – 611G → V in CAA27203 (PubMed:3003701).Curated
Sequence conflicti197 – 1971T → S in CAA27203 (PubMed:3003701).Curated
Sequence conflicti202 – 2021P → H in AAA34699 (PubMed:3905511).Curated
Sequence conflicti421 – 4222YN → ST in AAA34697 (PubMed:3905511).Curated
Sequence conflicti421 – 4222YN → ST in AAA34699 (PubMed:3905511).Curated
Sequence conflicti444 – 4452TS → PH in AAA34697 (PubMed:3905511).Curated
Sequence conflicti444 – 4452TS → PH in AAA34699 (PubMed:3905511).Curated
Sequence conflicti453 – 4531I → V in AAA34697 (PubMed:3905511).Curated
Sequence conflicti453 – 4531I → V in AAA34699 (PubMed:3905511).Curated
Sequence conflicti462 – 4621A → P in AAA34697 (PubMed:3905511).Curated
Sequence conflicti462 – 4621A → P in AAA34699 (PubMed:3905511).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03483 Genomic DNA. Translation: CAA27203.1.
M11181 Genomic DNA. Translation: AAA34697.1.
M14411 mRNA. Translation: AAA34699.1.
X94357 Genomic DNA. Translation: CAA64134.1.
Z72775 Genomic DNA. Translation: CAA96973.1.
X67787 Genomic DNA. Translation: CAA48003.1.
BK006941 Genomic DNA. Translation: DAA07866.1.
PIRiS61608. KIBYHB.
RefSeqiNP_011261.1. NM_001181119.1.

Genome annotation databases

EnsemblFungiiYGL253W; YGL253W; YGL253W.
GeneIDi852639.
KEGGisce:YGL253W.

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03483 Genomic DNA. Translation: CAA27203.1.
M11181 Genomic DNA. Translation: AAA34697.1.
M14411 mRNA. Translation: AAA34699.1.
X94357 Genomic DNA. Translation: CAA64134.1.
Z72775 Genomic DNA. Translation: CAA96973.1.
X67787 Genomic DNA. Translation: CAA48003.1.
BK006941 Genomic DNA. Translation: DAA07866.1.
PIRiS61608. KIBYHB.
RefSeqiNP_011261.1. NM_001181119.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IG8X-ray2.20A1-486[»]
2YHXX-ray2.10A152-471[»]
ProteinModelPortaliP04807.
SMRiP04807. Positions 18-486.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33026. 150 interactions.
DIPiDIP-2380N.
IntActiP04807. 3 interactions.
MINTiMINT-2784874.
STRINGi4932.YGL253W.

2D gel databases

SWISS-2DPAGEP04807.

Proteomic databases

MaxQBiP04807.
PaxDbiP04807.
PeptideAtlasiP04807.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL253W; YGL253W; YGL253W.
GeneIDi852639.
KEGGisce:YGL253W.

Organism-specific databases

EuPathDBiFungiDB:YGL253W.
SGDiS000003222. HXK2.

Phylogenomic databases

eggNOGiCOG5026.
GeneTreeiENSGT00390000017159.
HOGENOMiHOG000162670.
InParanoidiP04807.
KOiK00844.
OMAiAIAIDGC.
OrthoDBiEOG79SF68.

Enzyme and pathway databases

UniPathwayiUPA00242.
BioCyciYEAST:YGL253W-MONOMER.
BRENDAi2.7.1.1. 984.
ReactomeiREACT_298577. Regulation of gene expression in beta cells.
REACT_302131. Glucose transport.
REACT_318658. Regulation of Glucokinase by Glucokinase Regulatory Protein.
SABIO-RKP04807.

Miscellaneous databases

EvolutionaryTraceiP04807.
NextBioi971888.
PROiP04807.

Gene expression databases

GenevestigatoriP04807.

Family and domain databases

InterProiIPR001312. Hexokinase.
IPR022673. Hexokinase_C.
IPR019807. Hexokinase_CS.
IPR022672. Hexokinase_N.
[Graphical view]
PANTHERiPTHR19443. PTHR19443. 1 hit.
PfamiPF00349. Hexokinase_1. 1 hit.
PF03727. Hexokinase_2. 1 hit.
[Graphical view]
PRINTSiPR00475. HEXOKINASE.
PROSITEiPS00378. HEXOKINASE_1. 1 hit.
PS51748. HEXOKINASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification, cloning and sequence determination of the genes specifying hexokinase A and B from yeast."
    Stachelek C., Stachelek J., Swan J., Botstein D., Konigsberg W.
    Nucleic Acids Res. 14:945-963(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The primary structure of the yeast hexokinase PII gene (HXK2) which is responsible for glucose repression."
    Froehlich K.-U., Entian K.-D., Mecke D.
    Gene 36:105-111(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Sequence of a 39,411 bp DNA fragment covering the left end of chromosome VII of Saccharomyces cerevisiae."
    Coissac E., Maillier E., Robineau S., Netter P.
    Yeast 12:1555-1562(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. "Identification of a gene encoding a novel zinc finger protein in Saccharomyces cerevisiae."
    Breitwieser W., Price C., Schuster T.
    Yeast 9:551-556(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 1-247.
    Strain: ATCC 200060 / W303.
  7. "Gene linkage of two-dimensional polyacrylamide gel electrophoresis resolved proteins from isogene families in Saccharomyces cerevisiae by microsequencing of in-gel trypsin generated peptides."
    Norbeck J., Blomberg A.
    Electrophoresis 16:149-156(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 119-127; 176-185 AND 304-314.
    Strain: ATCC 38531 / Y41.
  8. "In vivo phosphorylation site of hexokinase 2 in Saccharomyces cerevisiae."
    Kriegel T.M., Rush J., Vojtek A.B., Clifton D., Fraenkel D.G.
    Biochemistry 33:148-152(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-15.
  9. "Autophosphorylation-inactivation site of hexokinase 2 in Saccharomyces cerevisiae."
    Heidrich K., Otto A., Behlke J., Rush J., Wenzel K.W., Kriegel T.
    Biochemistry 36:1960-1964(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-158.
  10. "Hexokinase 2 from Saccharomyces cerevisiae: regulation of oligomeric structure by in vivo phosphorylation at serine-14."
    Behlke J., Heidrich K., Naumann M., Mueller E.-C., Otto A., Reuter R., Kriegel T.
    Biochemistry 37:11989-11995(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-19, PHOSPHORYLATION AT SER-15.
  11. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  12. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-38 AND SER-158, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-245, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Sequencing a protein by X-ray crystallography. II. Refinement of yeast hexokinase B co-ordinates and sequence at 2.1-A resolution."
    Anderson C.M., Stenkamp R.E., Steitz T.A.
    J. Mol. Biol. 123:15-33(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).

Entry informationi

Entry nameiHXKB_YEAST
AccessioniPrimary (citable) accession number: P04807
Secondary accession number(s): D6VV82, Q05838
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: April 29, 2015
This is version 161 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

In yeast there are three glucose-phosphorylating isoenzymes, designated hexokinase I, II and glucokinase.
Present with 114000 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.