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P05708

- HXK1_RAT

UniProt

P05708 - HXK1_RAT

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Protein
Hexokinase-1
Gene
Hk1
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Enzyme regulationi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei30 – 301ATP 1 By similarity
Binding sitei155 – 1551Substrate 1
Binding sitei209 – 2091Glucose-6-phosphate 1
Binding sitei232 – 2321Glucose-6-phosphate 1
Binding sitei235 – 2351Substrate 1
Binding sitei260 – 2601Substrate 1
Binding sitei449 – 4491Glucose-6-phosphate 1
Binding sitei603 – 6031Glucose-6-phosphate 2
Binding sitei657 – 6571Glucose-6-phosphate 2
Binding sitei680 – 6801ATP 2 By similarity
Binding sitei680 – 6801Glucose-6-phosphate 2
Binding sitei683 – 6831Substrate 2
Binding sitei708 – 7081Substrate 2
Binding sitei742 – 7421Substrate 2
Binding sitei897 – 8971Glucose-6-phosphate 2

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi84 – 896ATP 1 Reviewed prediction
Nucleotide bindingi425 – 4262ATP 1 By similarity
Nucleotide bindingi532 – 5376ATP 2 By similarity
Nucleotide bindingi747 – 7482ATP 2 By similarity
Nucleotide bindingi784 – 7885ATP 2 By similarity
Nucleotide bindingi863 – 8675ATP 2 By similarity

GO - Molecular functioni

  1. ATP binding Source: RGD
  2. ATPase activity Source: RGD
  3. glucokinase activity Source: RGD
  4. glucose binding Source: RGD
  5. hexokinase activity Source: RGD
  6. protein binding Source: RGD
  7. protein complex binding Source: RGD
  8. protein homodimerization activity Source: RGD
  9. protein kinase activity Source: RGD

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. carbohydrate phosphorylation Source: RGD
  3. glucose 6-phosphate metabolic process Source: GOC
  4. glycolytic process Source: RGD
  5. hexose metabolic process Source: UniProtKB-UniPathway
  6. negative regulation of apoptotic process Source: RGD
  7. peptidyl-serine phosphorylation Source: RGD
  8. peptidyl-threonine phosphorylation Source: RGD
  9. peptidyl-tyrosine phosphorylation Source: RGD
  10. protein autophosphorylation Source: RGD
  11. protein phosphorylation Source: RGD
  12. regulation of anion channel activity Source: RGD
  13. response to ischemia Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.1.1. 5301.
SABIO-RKP05708.
UniPathwayiUPA00242.

Names & Taxonomyi

Protein namesi
Recommended name:
Hexokinase-1 (EC:2.7.1.1)
Alternative name(s):
Brain form hexokinase
Hexokinase type I
Short name:
HK I
Gene namesi
Name:Hk1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi2796. Hk1.

Subcellular locationi

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

GO - Cellular componenti

  1. caveola Source: RGD
  2. cytosol Source: RGD
  3. mitochondrial outer membrane Source: UniProtKB-SubCell
  4. mitochondrion Source: RGD
  5. protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 918918Hexokinase-1
PRO_0000197586Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP05708.

2D gel databases

World-2DPAGE0004:P05708.

PTM databases

PhosphoSiteiP05708.

Expressioni

Tissue specificityi

Expressed in flagella of epididymal sperm.1 Publication

Gene expression databases

GenevestigatoriP05708.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi247135. 1 interaction.
MINTiMINT-4567991.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 2524
Helixi27 – 293
Helixi33 – 5119
Turni53 – 553
Helixi56 – 583
Beta strandi78 – 9720
Beta strandi106 – 1083
Helixi123 – 14018
Beta strandi144 – 1463
Beta strandi149 – 1546
Helixi185 – 19612
Beta strandi202 – 2076
Helixi209 – 22012
Beta strandi224 – 24118
Helixi242 – 2443
Beta strandi252 – 2587
Helixi261 – 2633
Turni264 – 27310
Helixi276 – 2838
Beta strandi285 – 2873
Helixi294 – 2974
Turni299 – 3013
Helixi302 – 31514
Helixi320 – 3223
Helixi326 – 3294
Helixi336 – 3427
Turni345 – 3473
Helixi348 – 35811
Helixi365 – 40137
Beta strandi404 – 4063
Beta strandi409 – 4135
Helixi415 – 4195
Helixi423 – 43412
Beta strandi441 – 4444
Helixi450 – 47425
Helixi475 – 4773
Helixi481 – 49919
Turni501 – 5033
Helixi504 – 5063
Beta strandi511 – 5133
Beta strandi526 – 53712
Beta strandi539 – 5457
Beta strandi553 – 5597
Helixi564 – 5674
Helixi571 – 58919
Beta strandi596 – 6027
Helixi633 – 64412
Beta strandi649 – 6557
Helixi657 – 66610
Beta strandi672 – 68918
Helixi690 – 6923
Beta strandi700 – 7078
Helixi709 – 7113
Beta strandi714 – 7163
Turni717 – 7215
Helixi724 – 7318
Beta strandi733 – 7353
Helixi740 – 7434
Turni747 – 7493
Helixi750 – 76314
Helixi768 – 7703
Helixi774 – 7774
Helixi784 – 7907
Beta strandi793 – 7953
Helixi797 – 80610
Helixi813 – 84836
Beta strandi857 – 8615
Helixi863 – 8675
Helixi871 – 88212
Beta strandi889 – 8924
Helixi896 – 90914

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BG3X-ray2.80A/B1-918[»]
ProteinModelPortaliP05708.
SMRiP05708. Positions 1-911.

Miscellaneous databases

EvolutionaryTraceiP05708.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 221205Hexokinase type-1 1
Add
BLAST
Domaini223 – 462240Hexokinase type-2 1
Add
BLAST
Domaini465 – 668204Hexokinase type-1 2
Add
BLAST
Domaini671 – 909239Hexokinase type-2 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 1212Hydrophobic
Add
BLAST
Regioni13 – 475463Regulatory
Add
BLAST
Regioni84 – 885Glucose-6-phosphate 1 binding
Regioni172 – 1732Substrate 1 binding
Regioni208 – 2092Substrate 1 binding
Regioni291 – 2944Substrate 1 binding
Regioni413 – 4153Glucose-6-phosphate 1 binding
Regioni476 – 918443Catalytic
Add
BLAST
Regioni532 – 5365Glucose-6-phosphate 2 binding
Regioni620 – 6212Substrate 2 binding
Regioni656 – 6572Substrate 2 binding
Regioni861 – 8633Glucose-6-phosphate 2 binding

Domaini

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.

Sequence similaritiesi

Belongs to the hexokinase family.

Keywords - Domaini

Repeat

Phylogenomic databases

HOVERGENiHBG005020.
KOiK00844.
PhylomeDBiP05708.

Family and domain databases

InterProiIPR001312. Hexokinase.
IPR022673. Hexokinase_C.
IPR019807. Hexokinase_CS.
IPR022672. Hexokinase_N.
[Graphical view]
PANTHERiPTHR19443. PTHR19443. 1 hit.
PfamiPF00349. Hexokinase_1. 2 hits.
PF03727. Hexokinase_2. 2 hits.
[Graphical view]
PRINTSiPR00475. HEXOKINASE.
PROSITEiPS00378. HEXOKINASES. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P05708-1 [UniParc]FASTAAdd to Basket

« Hide

MIAAQLLAYY FTELKDDQVK KIDKYLYAMR LSDEILIDIL TRFKKEMKNG    50
LSRDYNPTAS VKMLPTFVRS IPDGSEKGDF IALDLGGSSF RILRVQVNHE 100
KNQNVSMESE IYDTPENIVH GSGTQLFDHV ADCLGDFMEK KKIKDKKLPV 150
GFTFSFPCRQ SKIDEAVLIT WTKRFKASGV EGADVVKLLN KAIKKRGDYD 200
ANIVAVVNDT VGTMMTCGYD DQQCEVGLII GTGTNACYME ELRHIDLVEG 250
DEGRMCINTE WGAFGDDGSL EDIRTEFDRE LDRGSLNPGK QLFEKMVSGM 300
YMGELVRLIL VKMAKEGLLF EGRITPELLT RGKFNTSDVS AIEKDKEGIQ 350
NAKEILTRLG VEPSDVDCVS VQHICTIVSF RSANLVAATL GAILNRLRDN 400
KGTPRLRTTV GVDGSLYKMH PQYSRRFHKT LRRLVPDSDV RFLLSESGTG 450
KGAAMVTAVA YRLAEQHRQI EETLAHFRLS KQTLMEVKKR LRTEMEMGLR 500
KETNSKATVK MLPSFVRSIP DGTEHGDFLA LDLGGTNFRV LLVKIRSGKK 550
RTVEMHNKIY SIPLEIMQGT GDELFDHIVS CISDFLDYMG IKGPRMPLGF 600
TFSFPCHQTN LDCGILISWT KGFKATDCEG HDVASLLRDA VKRREEFDLD 650
VVAVVNDTVG TMMTCAYEEP TCEIGLIVGT GTNACYMEEM KNVEMVEGNQ 700
GQMCINMEWG AFGDNGCLDD IRTDFDKVVD EYSLNSGKQR FEKMISGMYL 750
GEIVRNILID FTKKGFLFRG QISEPLKTRG IFETKFLSQI ESDRLALLQV 800
RAILQQLGLN STCDDSILVK TVCGVVSKRA AQLCGAGMAA VVEKIRENRG 850
LDHLNVTVGV DGTLYKLHPH FSRIMHQTVK ELSPKCTVSF LLSEDGSGKG 900
AALITAVGVR LRGDPSIA 918
Length:918
Mass (Da):102,408
Last modified:May 30, 2000 - v4
Checksum:iD2200820F0FC41EE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J04526 mRNA. Translation: AAC20075.1.
U27319 Genomic DNA. Translation: AAC52945.1.
U89160 Genomic DNA. Translation: AAB71376.1.
U89158 Genomic DNA. Translation: AAB71374.1.
PIRiA32521.
B32521.
C32521.
C59226.
RefSeqiNP_036866.1. NM_012734.1.
UniGeneiRn.11017.

Genome annotation databases

GeneIDi25058.
KEGGirno:25058.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J04526 mRNA. Translation: AAC20075.1 .
U27319 Genomic DNA. Translation: AAC52945.1 .
U89160 Genomic DNA. Translation: AAB71376.1 .
U89158 Genomic DNA. Translation: AAB71374.1 .
PIRi A32521.
B32521.
C32521.
C59226.
RefSeqi NP_036866.1. NM_012734.1.
UniGenei Rn.11017.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BG3 X-ray 2.80 A/B 1-918 [» ]
ProteinModelPortali P05708.
SMRi P05708. Positions 1-911.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 247135. 1 interaction.
MINTi MINT-4567991.

Chemistry

ChEMBLi CHEMBL4783.

PTM databases

PhosphoSitei P05708.

2D gel databases

World-2DPAGE 0004:P05708.

Proteomic databases

PRIDEi P05708.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 25058.
KEGGi rno:25058.

Organism-specific databases

CTDi 3098.
RGDi 2796. Hk1.

Phylogenomic databases

HOVERGENi HBG005020.
KOi K00844.
PhylomeDBi P05708.

Enzyme and pathway databases

UniPathwayi UPA00242 .
BRENDAi 2.7.1.1. 5301.
SABIO-RK P05708.

Miscellaneous databases

EvolutionaryTracei P05708.
NextBioi 605272.

Gene expression databases

Genevestigatori P05708.

Family and domain databases

InterProi IPR001312. Hexokinase.
IPR022673. Hexokinase_C.
IPR019807. Hexokinase_CS.
IPR022672. Hexokinase_N.
[Graphical view ]
PANTHERi PTHR19443. PTHR19443. 1 hit.
Pfami PF00349. Hexokinase_1. 2 hits.
PF03727. Hexokinase_2. 2 hits.
[Graphical view ]
PRINTSi PR00475. HEXOKINASE.
PROSITEi PS00378. HEXOKINASES. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Complete amino acid sequence of rat brain hexokinase, deduced from the cloned cDNA, and proposed structure of a mammalian hexokinase."
    Schwab D.A., Wilson J.E.
    Proc. Natl. Acad. Sci. U.S.A. 86:2563-2567(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-466.
    Tissue: Brain.
  2. "The complete amino acid sequence of the catalytic domain of rat brain hexokinase, deduced from the cloned cDNA."
    Schwab D.A., Wilson J.E.
    J. Biol. Chem. 263:3220-3224(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 467-918.
    Tissue: Brain.
  3. Wilson J.E.
    Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  4. "Rat brain hexokinase: amino acid sequence at the substrate hexose binding site is homologous to that of yeast hexokinase."
    Schirch D.M., Wilson J.E.
    Arch. Biochem. Biophys. 257:1-12(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 597-617; 625-636 AND 802-816.
    Tissue: Brain.
  5. White J.A., Liu W., Wilson J.E.
    Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE OF 1-21.
    Strain: Sprague-Dawley.
    Tissue: Liver.
  6. White J.A., Wilson J.E.
    Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE OF 221-246 AND 631-668.
  7. "Rat brain hexokinase: location of the substrate hexose binding site in a structural domain at the C-terminus of the enzyme."
    Schirch D.M., Wilson J.E.
    Arch. Biochem. Biophys. 254:385-396(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBSTRATE-BINDING SITE.
  8. "Identification of novel immunodominant epididymal sperm proteins using combinatorial approach."
    Khan S.A., Suryawanshi A.R., Ranpura S.A., Jadhav S.V., Khole V.V.
    Reproduction 138:81-93(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY.
  9. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH GLUCOSE AND GLUCOSE-6-PHOSPHATE.

Entry informationi

Entry nameiHXK1_RAT
AccessioniPrimary (citable) accession number: P05708
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: May 30, 2000
Last modified: June 11, 2014
This is version 130 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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

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

External Data

Dasty 3

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