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Protein

Hexokinase-1

Gene

Hk1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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: hexose metabolism

This protein is involved in the pathway hexose metabolism, which is part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the pathway hexose metabolism and in Carbohydrate metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei30ATP 1By similarity1
Binding sitei155Substrate 11
Binding sitei209Glucose-6-phosphate 11 Publication1
Binding sitei232Glucose-6-phosphate 11 Publication1
Binding sitei235Substrate 11
Binding sitei260Substrate 11
Binding sitei449Glucose-6-phosphate 11 Publication1
Binding sitei603Glucose-6-phosphate 21 Publication1
Binding sitei657Glucose-6-phosphate 21 Publication1
Binding sitei680ATP 2By similarity1
Binding sitei680Glucose-6-phosphate 21 Publication1
Binding sitei683Substrate 21
Binding sitei708Substrate 21
Binding sitei742Substrate 21
Binding sitei897Glucose-6-phosphate 21 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi84 – 89ATP 1Sequence analysis6
Nucleotide bindingi425 – 426ATP 1By similarity2
Nucleotide bindingi532 – 537ATP 2By similarity6
Nucleotide bindingi747 – 748ATP 2By similarity2
Nucleotide bindingi784 – 788ATP 2By similarity5
Nucleotide bindingi863 – 867ATP 2By similarity5

GO - Molecular functioni

  • ATPase activity Source: RGD
  • ATP binding Source: RGD
  • fructokinase activity Source: GO_Central
  • glucokinase activity Source: RGD
  • glucose binding Source: RGD
  • hexokinase activity Source: CACAO
  • mannokinase activity Source: GO_Central
  • protein complex binding Source: RGD
  • protein homodimerization activity Source: RGD
  • protein kinase activity Source: RGD

GO - Biological processi

  • carbohydrate phosphorylation Source: RGD
  • cellular glucose homeostasis Source: GO_Central
  • glycolytic process Source: RGD
  • hexose metabolic process Source: UniProtKB-UniPathway
  • negative regulation of apoptotic process Source: RGD
  • peptidyl-serine phosphorylation Source: RGD
  • peptidyl-threonine phosphorylation Source: RGD
  • peptidyl-tyrosine phosphorylation Source: RGD
  • protein autophosphorylation Source: RGD
  • protein phosphorylation Source: RGD
  • regulation of anion channel activity Source: RGD
  • response to brassinosteroid Source: RGD
  • response to ischemia Source: RGD
  • response to ketamine 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
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2796. Hk1.

Subcellular locationi

GO - Cellular componenti

  • caveola Source: RGD
  • cytosol Source: RGD
  • mitochondrial outer membrane Source: UniProtKB-SubCell
  • mitochondrion Source: CACAO
  • protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL4783.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001975861 – 918Hexokinase-1Add BLAST918

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei337PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiP05708.

2D gel databases

World-2DPAGE0004:P05708.

PTM databases

iPTMnetiP05708.
PhosphoSitePlusiP05708.

Expressioni

Tissue specificityi

Expressed in flagella of epididymal sperm.1 Publication

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

GO - Molecular functioni

  • protein complex binding Source: RGD
  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

BioGridi247135. 1 interactor.
IntActiP05708. 1 interactor.
MINTiMINT-4567991.

Structurei

Secondary structure

1918
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 25Combined sources24
Helixi27 – 29Combined sources3
Helixi33 – 51Combined sources19
Turni53 – 55Combined sources3
Helixi56 – 58Combined sources3
Beta strandi78 – 97Combined sources20
Beta strandi106 – 108Combined sources3
Helixi123 – 140Combined sources18
Beta strandi144 – 146Combined sources3
Beta strandi149 – 154Combined sources6
Helixi185 – 196Combined sources12
Beta strandi202 – 207Combined sources6
Helixi209 – 220Combined sources12
Beta strandi224 – 241Combined sources18
Helixi242 – 244Combined sources3
Beta strandi252 – 258Combined sources7
Helixi261 – 263Combined sources3
Turni264 – 273Combined sources10
Helixi276 – 283Combined sources8
Beta strandi285 – 287Combined sources3
Helixi294 – 297Combined sources4
Turni299 – 301Combined sources3
Helixi302 – 315Combined sources14
Helixi320 – 322Combined sources3
Helixi326 – 329Combined sources4
Helixi336 – 342Combined sources7
Turni345 – 347Combined sources3
Helixi348 – 358Combined sources11
Helixi365 – 401Combined sources37
Beta strandi404 – 406Combined sources3
Beta strandi409 – 413Combined sources5
Helixi415 – 419Combined sources5
Helixi423 – 434Combined sources12
Beta strandi441 – 444Combined sources4
Helixi450 – 474Combined sources25
Helixi475 – 477Combined sources3
Helixi481 – 499Combined sources19
Turni501 – 503Combined sources3
Helixi504 – 506Combined sources3
Beta strandi511 – 513Combined sources3
Beta strandi526 – 537Combined sources12
Beta strandi539 – 545Combined sources7
Beta strandi548 – 550Combined sources3
Beta strandi553 – 559Combined sources7
Helixi564 – 567Combined sources4
Helixi571 – 589Combined sources19
Beta strandi596 – 602Combined sources7
Helixi633 – 644Combined sources12
Beta strandi649 – 655Combined sources7
Helixi657 – 666Combined sources10
Beta strandi672 – 689Combined sources18
Helixi690 – 692Combined sources3
Beta strandi700 – 707Combined sources8
Helixi709 – 711Combined sources3
Beta strandi714 – 716Combined sources3
Turni717 – 721Combined sources5
Helixi724 – 731Combined sources8
Beta strandi733 – 735Combined sources3
Helixi740 – 743Combined sources4
Turni747 – 749Combined sources3
Helixi750 – 763Combined sources14
Helixi768 – 770Combined sources3
Helixi774 – 777Combined sources4
Helixi784 – 790Combined sources7
Beta strandi793 – 795Combined sources3
Helixi797 – 806Combined sources10
Helixi813 – 848Combined sources36
Beta strandi857 – 861Combined sources5
Helixi863 – 867Combined sources5
Helixi871 – 882Combined sources12
Beta strandi889 – 892Combined sources4
Helixi896 – 909Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BG3X-ray2.80A/B1-918[»]
ProteinModelPortaliP05708.
SMRiP05708.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05708.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini16 – 458Hexokinase 1PROSITE-ProRule annotationAdd BLAST443
Domaini464 – 906Hexokinase 2PROSITE-ProRule annotationAdd BLAST443

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 12HydrophobicAdd BLAST12
Regioni13 – 475RegulatoryAdd BLAST463
Regioni73 – 207Hexokinase small subdomain 1PROSITE-ProRule annotationAdd BLAST135
Regioni84 – 88Glucose-6-phosphate 1 binding5
Regioni172 – 173Substrate 1 binding2
Regioni208 – 447Hexokinase large subdomain 1PROSITE-ProRule annotationAdd BLAST240
Regioni208 – 209Substrate 1 binding2
Regioni291 – 294Substrate 1 binding4
Regioni413 – 415Glucose-6-phosphate 1 binding3
Regioni476 – 918CatalyticAdd BLAST443
Regioni521 – 655Hexokinase small subdomain 2PROSITE-ProRule annotationAdd BLAST135
Regioni532 – 536Glucose-6-phosphate 2 binding5
Regioni620 – 621Substrate 2 binding2
Regioni656 – 895Hexokinase large subdomain 2PROSITE-ProRule annotationAdd BLAST240
Regioni656 – 657Substrate 2 binding2
Regioni861 – 863Glucose-6-phosphate 2 binding3

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.PROSITE-ProRule annotationCurated
Contains 2 hexokinase domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

HOVERGENiHBG005020.
InParanoidiP05708.
KOiK00844.
PhylomeDBiP05708.

Family and domain databases

InterProiIPR001312. Hexokinase.
IPR019807. Hexokinase_BS.
IPR022673. Hexokinase_C.
IPR022672. Hexokinase_N.
[Graphical view]
PANTHERiPTHR19443. PTHR19443. 1 hit.
PfamiPF00349. Hexokinase_1. 2 hits.
PF03727. Hexokinase_2. 2 hits.
[Graphical view]
PROSITEiPS00378. HEXOKINASE_1. 2 hits.
PS51748. HEXOKINASE_2. 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.
PIRiA32521.
B32521.
C32521.
C59226.
RefSeqiNP_036866.1. NM_012734.1.
UniGeneiRn.11017.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BG3X-ray2.80A/B1-918[»]
ProteinModelPortaliP05708.
SMRiP05708.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247135. 1 interactor.
IntActiP05708. 1 interactor.
MINTiMINT-4567991.

Chemistry databases

ChEMBLiCHEMBL4783.

PTM databases

iPTMnetiP05708.
PhosphoSitePlusiP05708.

2D gel databases

World-2DPAGE0004:P05708.

Proteomic databases

PRIDEiP05708.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25058.
KEGGirno:25058.

Organism-specific databases

CTDi3098.
RGDi2796. Hk1.

Phylogenomic databases

HOVERGENiHBG005020.
InParanoidiP05708.
KOiK00844.
PhylomeDBiP05708.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP05708.
PROiP05708.

Family and domain databases

InterProiIPR001312. Hexokinase.
IPR019807. Hexokinase_BS.
IPR022673. Hexokinase_C.
IPR022672. Hexokinase_N.
[Graphical view]
PANTHERiPTHR19443. PTHR19443. 1 hit.
PfamiPF00349. Hexokinase_1. 2 hits.
PF03727. Hexokinase_2. 2 hits.
[Graphical view]
PROSITEiPS00378. HEXOKINASE_1. 2 hits.
PS51748. HEXOKINASE_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

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 2, 2016
This is version 149 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

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 one 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.