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P05708

- HXK1_RAT

UniProt

P05708 - HXK1_RAT

Protein

Hexokinase-1

Gene

Hk1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 4 (30 May 2000)
      Previous versions | rss
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    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 1By similarity
    Binding sitei155 – 1551Substrate 1
    Binding sitei209 – 2091Glucose-6-phosphate 11 Publication
    Binding sitei232 – 2321Glucose-6-phosphate 11 Publication
    Binding sitei235 – 2351Substrate 1
    Binding sitei260 – 2601Substrate 1
    Binding sitei449 – 4491Glucose-6-phosphate 11 Publication
    Binding sitei603 – 6031Glucose-6-phosphate 21 Publication
    Binding sitei657 – 6571Glucose-6-phosphate 21 Publication
    Binding sitei680 – 6801ATP 2By similarity
    Binding sitei680 – 6801Glucose-6-phosphate 21 Publication
    Binding sitei683 – 6831Substrate 2
    Binding sitei708 – 7081Substrate 2
    Binding sitei742 – 7421Substrate 2
    Binding sitei897 – 8971Glucose-6-phosphate 21 Publication

    Regions

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

    GO - Molecular functioni

    1. ATPase activity Source: RGD
    2. ATP binding 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

    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

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion outer membrane

    PTM / Processingi

    Molecule processing

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

    Amino acid modifications

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

    Protein-protein interaction databases

    BioGridi247135. 1 interaction.
    MINTiMINT-4567991.

    Structurei

    Secondary structure

    1
    918
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05708.

    Family & Domainsi

    Domains and Repeats

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

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 1212HydrophobicAdd
    BLAST
    Regioni13 – 475463RegulatoryAdd
    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 – 918443CatalyticAdd
    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.Curated
    Contains 2 hexokinase type-1 domains.Curated
    Contains 2 hexokinase type-2 domains.Curated

    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: October 1, 2014
    This is version 131 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