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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 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 complex binding Source: RGD
  7. protein homodimerization activity Source: RGD
  8. 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-KW
  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-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). Interacts (via N-terminal spermatogenic cell-specific region) with PFKM (via C-terminus) (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 – 2524Combined sources
Helixi27 – 293Combined sources
Helixi33 – 5119Combined sources
Turni53 – 553Combined sources
Helixi56 – 583Combined sources
Beta strandi78 – 9720Combined sources
Beta strandi106 – 1083Combined sources
Helixi123 – 14018Combined sources
Beta strandi144 – 1463Combined sources
Beta strandi149 – 1546Combined sources
Helixi185 – 19612Combined sources
Beta strandi202 – 2076Combined sources
Helixi209 – 22012Combined sources
Beta strandi224 – 24118Combined sources
Helixi242 – 2443Combined sources
Beta strandi252 – 2587Combined sources
Helixi261 – 2633Combined sources
Turni264 – 27310Combined sources
Helixi276 – 2838Combined sources
Beta strandi285 – 2873Combined sources
Helixi294 – 2974Combined sources
Turni299 – 3013Combined sources
Helixi302 – 31514Combined sources
Helixi320 – 3223Combined sources
Helixi326 – 3294Combined sources
Helixi336 – 3427Combined sources
Turni345 – 3473Combined sources
Helixi348 – 35811Combined sources
Helixi365 – 40137Combined sources
Beta strandi404 – 4063Combined sources
Beta strandi409 – 4135Combined sources
Helixi415 – 4195Combined sources
Helixi423 – 43412Combined sources
Beta strandi441 – 4444Combined sources
Helixi450 – 47425Combined sources
Helixi475 – 4773Combined sources
Helixi481 – 49919Combined sources
Turni501 – 5033Combined sources
Helixi504 – 5063Combined sources
Beta strandi511 – 5133Combined sources
Beta strandi526 – 53712Combined sources
Beta strandi539 – 5457Combined sources
Beta strandi553 – 5597Combined sources
Helixi564 – 5674Combined sources
Helixi571 – 58919Combined sources
Beta strandi596 – 6027Combined sources
Helixi633 – 64412Combined sources
Beta strandi649 – 6557Combined sources
Helixi657 – 66610Combined sources
Beta strandi672 – 68918Combined sources
Helixi690 – 6923Combined sources
Beta strandi700 – 7078Combined sources
Helixi709 – 7113Combined sources
Beta strandi714 – 7163Combined sources
Turni717 – 7215Combined sources
Helixi724 – 7318Combined sources
Beta strandi733 – 7353Combined sources
Helixi740 – 7434Combined sources
Turni747 – 7493Combined sources
Helixi750 – 76314Combined sources
Helixi768 – 7703Combined sources
Helixi774 – 7774Combined sources
Helixi784 – 7907Combined sources
Beta strandi793 – 7953Combined sources
Helixi797 – 80610Combined sources
Helixi813 – 84836Combined sources
Beta strandi857 – 8615Combined sources
Helixi863 – 8675Combined sources
Helixi871 – 88212Combined sources
Beta strandi889 – 8924Combined sources
Helixi896 – 90914Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP05708.
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

        10         20         30         40         50
MIAAQLLAYY FTELKDDQVK KIDKYLYAMR LSDEILIDIL TRFKKEMKNG
60 70 80 90 100
LSRDYNPTAS VKMLPTFVRS IPDGSEKGDF IALDLGGSSF RILRVQVNHE
110 120 130 140 150
KNQNVSMESE IYDTPENIVH GSGTQLFDHV ADCLGDFMEK KKIKDKKLPV
160 170 180 190 200
GFTFSFPCRQ SKIDEAVLIT WTKRFKASGV EGADVVKLLN KAIKKRGDYD
210 220 230 240 250
ANIVAVVNDT VGTMMTCGYD DQQCEVGLII GTGTNACYME ELRHIDLVEG
260 270 280 290 300
DEGRMCINTE WGAFGDDGSL EDIRTEFDRE LDRGSLNPGK QLFEKMVSGM
310 320 330 340 350
YMGELVRLIL VKMAKEGLLF EGRITPELLT RGKFNTSDVS AIEKDKEGIQ
360 370 380 390 400
NAKEILTRLG VEPSDVDCVS VQHICTIVSF RSANLVAATL GAILNRLRDN
410 420 430 440 450
KGTPRLRTTV GVDGSLYKMH PQYSRRFHKT LRRLVPDSDV RFLLSESGTG
460 470 480 490 500
KGAAMVTAVA YRLAEQHRQI EETLAHFRLS KQTLMEVKKR LRTEMEMGLR
510 520 530 540 550
KETNSKATVK MLPSFVRSIP DGTEHGDFLA LDLGGTNFRV LLVKIRSGKK
560 570 580 590 600
RTVEMHNKIY SIPLEIMQGT GDELFDHIVS CISDFLDYMG IKGPRMPLGF
610 620 630 640 650
TFSFPCHQTN LDCGILISWT KGFKATDCEG HDVASLLRDA VKRREEFDLD
660 670 680 690 700
VVAVVNDTVG TMMTCAYEEP TCEIGLIVGT GTNACYMEEM KNVEMVEGNQ
710 720 730 740 750
GQMCINMEWG AFGDNGCLDD IRTDFDKVVD EYSLNSGKQR FEKMISGMYL
760 770 780 790 800
GEIVRNILID FTKKGFLFRG QISEPLKTRG IFETKFLSQI ESDRLALLQV
810 820 830 840 850
RAILQQLGLN STCDDSILVK TVCGVVSKRA AQLCGAGMAA VVEKIRENRG
860 870 880 890 900
LDHLNVTVGV DGTLYKLHPH FSRIMHQTVK ELSPKCTVSF LLSEDGSGKG
910
AALITAVGVR LRGDPSIA
Length:918
Mass (Da):102,408
Last modified:May 30, 2000 - v4
Checksum:iD2200820F0FC41EE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P05708.
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: November 26, 2014
This is version 133 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