SubmitCancel

Skip Header

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

P19367

- HXK1_HUMAN

UniProt

P19367 - HXK1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Hexokinase-1

Gene
HK1
Organism
Homo sapiens (Human)
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
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 sitei345 – 3451ATP 1
Binding sitei449 – 4491Glucose-6-phosphate 1
Binding sitei657 – 6571Glucose-6-phosphate 2
Binding sitei680 – 6801ATP 2
Binding sitei680 – 6801Glucose-6-phosphate 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
Nucleotide bindingi532 – 5376ATP 2
Nucleotide bindingi747 – 7482ATP 2
Nucleotide bindingi784 – 7885ATP 2
Nucleotide bindingi863 – 8675ATP 2

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. fructokinase activity Source: RefGenome
  3. glucokinase activity Source: RefGenome
  4. hexokinase activity Source: ProtInc
  5. mannokinase activity Source: RefGenome
  6. protein binding Source: IntAct

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. carbohydrate phosphorylation Source: GOC
  3. cell death Source: UniProtKB-KW
  4. cellular glucose homeostasis Source: RefGenome
  5. glucose 6-phosphate metabolic process Source: GOC
  6. glucose transport Source: Reactome
  7. glycolytic process Source: RefGenome
  8. hexose metabolic process Source: UniProtKB-UniPathway
  9. hexose transport Source: Reactome
  10. small molecule metabolic process Source: Reactome
  11. transmembrane transport Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS08136-MONOMER.
ReactomeiREACT_212. Glucose transport.
SABIO-RKP19367.
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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:4922. HK1.

Subcellular locationi

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

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. membrane raft Source: Ensembl
  3. mitochondrial outer membrane Source: UniProtKB-SubCell
  4. mitochondrion Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Involvement in diseasei

Hexokinase deficiency (HK deficiency) [MIM:235700]: Rare autosomal recessive disease with nonspherocytic hemolytic anemia as the predominant clinical feature.
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti529 – 5291L → S in HK deficiency. 1 Publication
VAR_009878
Natural varianti680 – 6801T → S in HK deficiency; HK Utrecht. 1 Publication
VAR_023780
Hereditary motor and sensory neuropathy, Russe type (HMSNR) [MIM:605285]: An autosomal recessive progressive complex peripheral neuropathy characterized by onset in the first decade of distal lower limb weakness and muscle atrophy resulting in walking difficulties. Distal impairment of the upper limbs usually occurs later, as does proximal lower limb weakness. There is distal sensory impairment, with pes cavus and areflexia. Laboratory studies suggest that it is a myelinopathy resulting in reduced nerve conduction velocities in the demyelinating range as well as a length-dependent axonopathy.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication

Keywords - Diseasei

Charcot-Marie-Tooth disease, Disease mutation, Neurodegeneration, Neuropathy

Organism-specific databases

MIMi235700. phenotype.
605285. phenotype.
Orphaneti99953. Charcot-Marie-Tooth disease type 4G.
90031. Non-spherocytic hemolytic anemia due to hexokinase deficiency.
PharmGKBiPA29300.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 917917Hexokinase-1PRO_0000197585Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP19367.
PaxDbiP19367.
PRIDEiP19367.

PTM databases

PhosphoSiteiP19367.

Expressioni

Tissue specificityi

Isoform 2 is erythrocyte specific. Isoform 3 and isoform 4 are testis-specific.

Gene expression databases

ArrayExpressiP19367.
BgeeiP19367.
CleanExiHS_HK1.
GenevestigatoriP19367.

Organism-specific databases

HPAiCAB010052.
HPA007043.
HPA007044.
HPA011956.

Interactioni

Subunit structurei

Monomer. Interacts with RABL2/RABL2A; binds preferentially to GTP-bound RABL2 By similarity. Interacts with VDAC1. The HK1-VDAC1 complex interacts with ATF2.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
VDAC1P217962EBI-713162,EBI-354158

Protein-protein interaction databases

BioGridi109345. 38 interactions.
IntActiP19367. 10 interactions.
MINTiMINT-1422832.
STRINGi9606.ENSP00000348697.

Structurei

Secondary structure

1
917
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi17 – 259
Helixi27 – 293
Helixi33 – 5119
Turni53 – 553
Helixi56 – 583
Beta strandi78 – 10023
Beta strandi103 – 11210
Helixi116 – 1194
Beta strandi120 – 1223
Helixi123 – 14119
Beta strandi144 – 1463
Beta strandi150 – 1545
Beta strandi161 – 1644
Turni179 – 1824
Helixi185 – 19612
Beta strandi203 – 2075
Helixi209 – 22012
Beta strandi224 – 24118
Helixi242 – 2443
Beta strandi252 – 2587
Helixi261 – 2633
Turni264 – 27310
Helixi276 – 2838
Beta strandi285 – 2873
Helixi294 – 2974
Helixi299 – 31517
Helixi320 – 3223
Turni326 – 3294
Helixi336 – 3427
Turni345 – 3473
Helixi348 – 35811
Helixi365 – 40137
Beta strandi404 – 41310
Helixi415 – 4195
Helixi423 – 43412
Beta strandi438 – 4447
Helixi449 – 47527
Helixi481 – 49919
Helixi501 – 5044
Beta strandi526 – 54621
Beta strandi548 – 5503
Beta strandi552 – 5609
Helixi564 – 5674
Beta strandi568 – 5703
Helixi571 – 58919
Beta strandi597 – 6026
Beta strandi606 – 6105
Beta strandi613 – 6164
Helixi633 – 64412
Beta strandi650 – 6556
Helixi657 – 66610
Beta strandi672 – 68918
Turni690 – 6923
Beta strandi700 – 7067
Helixi709 – 7113
Turni712 – 7154
Turni717 – 7215
Helixi724 – 7318
Turni734 – 7374
Helixi742 – 7443
Turni747 – 7493
Helixi750 – 76314
Helixi768 – 7703
Turni774 – 7774
Helixi784 – 7907
Helixi797 – 80711
Helixi813 – 84836
Beta strandi852 – 86110
Helixi863 – 8675
Helixi871 – 88212
Beta strandi886 – 8927
Helixi898 – 91215

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CZAX-ray1.90N1-917[»]
1DGKX-ray2.80N1-917[»]
1HKBX-ray2.80A/B1-917[»]
1HKCX-ray2.80A1-917[»]
1QHAX-ray2.25A/B1-917[»]
4F9OX-ray2.65A/B1-914[»]
4FOEX-ray2.70A/B1-917[»]
4FOIX-ray2.40A/B1-917[»]
4FPAX-ray2.48A/B1-917[»]
4FPBX-ray3.00A/B1-917[»]
ProteinModelPortaliP19367.
SMRiP19367. Positions 12-914.

Miscellaneous databases

EvolutionaryTraceiP19367.

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 – 917442CatalyticAdd
BLAST
Regioni532 – 5365Glucose-6-phosphate 2 binding
Regioni603 – 6042Substrate 2 binding
Regioni620 – 6212Substrate 2 binding
Regioni656 – 6572Substrate 2 binding
Regioni682 – 6832Substrate 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

eggNOGiCOG5026.
HOVERGENiHBG005020.
KOiK00844.
OrthoDBiEOG7S21X5.
PhylomeDBiP19367.
TreeFamiTF314238.

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]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P19367-1) [UniParc]FASTAAdd to Basket

Also known as: Common

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MIAAQLLAYY FTELKDDQVK KIDKYLYAMR LSDETLIDIM TRFRKEMKNG    50
LSRDFNPTAT VKMLPTFVRS IPDGSEKGDF IALDLGGSSF RILRVQVNHE 100
KNQNVHMESE VYDTPENIVH GSGSQLFDHV AECLGDFMEK RKIKDKKLPV 150
GFTFSFPCQQ SKIDEAILIT WTKRFKASGV EGADVVKLLN KAIKKRGDYD 200
ANIVAVVNDT VGTMMTCGYD DQHCEVGLII GTGTNACYME ELRHIDLVEG 250
DEGRMCINTE WGAFGDDGSL EDIRTEFDRE IDRGSLNPGK QLFEKMVSGM 300
YLGELVRLIL VKMAKEGLLF EGRITPELLT RGKFNTSDVS AIEKNKEGLH 350
NAKEILTRLG VEPSDDDCVS VQHVCTIVSF RSANLVAATL GAILNRLRDN 400
KGTPRLRTTV GVDGSLYKTH PQYSRRFHKT LRRLVPDSDV RFLLSESGSG 450
KGAAMVTAVA YRLAEQHRQI EETLAHFHLT KDMLLEVKKR MRAEMELGLR 500
KQTHNNAVVK MLPSFVRRTP DGTENGDFLA LDLGGTNFRV LLVKIRSGKK 550
RTVEMHNKIY AIPIEIMQGT GEELFDHIVS CISDFLDYMG IKGPRMPLGF 600
TFSFPCQQTS LDAGILITWT KGFKATDCVG HDVVTLLRDA IKRREEFDLD 650
VVAVVNDTVG TMMTCAYEEP TCEVGLIVGT GSNACYMEEM KNVEMVEGDQ 700
GQMCINMEWG AFGDNGCLDD IRTHYDRLVD EYSLNAGKQR YEKMISGMYL 750
GEIVRNILID FTKKGFLFRG QISETLKTRG IFETKFLSQI ESDRLALLQV 800
RAILQQLGLN STCDDSILVK TVCGVVSRRA AQLCGAGMAA VVDKIRENRG 850
LDRLNVTVGV DGTLYKLHPH FSRIMHQTVK ELSPKCNVSF LLSEDGSGKG 900
AALITAVGVR LRTEASS 917
Length:917
Mass (Da):102,486
Last modified:October 17, 2006 - v3
Checksum:iF29A6837531C0594
GO
Isoform 2 (identifier: P19367-2) [UniParc]FASTAAdd to Basket

Also known as: Erythrocyte, R

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: MIAAQLLAYYFTELKDDQVKK → MDCEHSLSLPCRGAEAWEIG

Show »
Length:916
Mass (Da):102,201
Checksum:i6E528FC4BEC5100B
GO
Isoform 3 (identifier: P19367-3) [UniParc]FASTAAdd to Basket

Also known as: TA, TB

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: MIAAQLLAYYFTELKDDQVKK → MGQICQRESATAAEKPKLHLLAESE

Show »
Length:921
Mass (Da):102,738
Checksum:i329F41F87DF6E1D1
GO
Isoform 4 (identifier: P19367-4) [UniParc]FASTAAdd to Basket

Also known as: TD

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: MIAAQLLAYYFTELKDDQVKK → MAKRALHDF

Show »
Length:905
Mass (Da):101,085
Checksum:iAE1BC4A3D2604AB0
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti529 – 5291L → S in HK deficiency. 1 Publication
VAR_009878
Natural varianti680 – 6801T → S in HK deficiency; HK Utrecht. 1 Publication
VAR_023780
Natural varianti776 – 7761L → M.2 Publications
Corresponds to variant rs1054203 [ dbSNP | Ensembl ].
VAR_023781

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2121MIAAQ…DQVKK → MDCEHSLSLPCRGAEAWEIG in isoform 2. VSP_002071Add
BLAST
Alternative sequencei1 – 2121MIAAQ…DQVKK → MGQICQRESATAAEKPKLHL LAESE in isoform 3. VSP_002072Add
BLAST
Alternative sequencei1 – 2121MIAAQ…DQVKK → MAKRALHDF in isoform 4. VSP_002073Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti730 – 7301D → N in AAA52646. 1 Publication
Sequence conflicti730 – 7301D → N in CAA47379. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M75126 mRNA. Translation: AAA52646.1.
AF016365
, AF016349, AF016351, AF016352, AF016353, AF016354, AF016355, AF016356, AF016357, AF016358, AF016359, AF016360, AF016361, AF016362, AF016363, AF016364 Genomic DNA. Translation: AAC15862.1.
AF016365
, AF016349, AF016351, AF016352, AF016353, AF016354, AF016355, AF016356, AF016357, AF016358, AF016359, AF016360, AF016361, AF016362, AF016363, AF016364 Genomic DNA. Translation: AAC15863.1.
AF016365
, AF163910, AF163911, AF016351, AF016352, AF016353, AF016354, AF016355, AF016356, AF016357, AF016358, AF016359, AF016360, AF016361, AF016362, AF016363, AF016364 Genomic DNA. Translation: AAF82319.1.
AF016365
, AF163912, AF016351, AF016352, AF016353, AF016354, AF016355, AF016356, AF016357, AF016358, AF016359, AF016360, AF016361, AF016362, AF016363, AF016364 Genomic DNA. Translation: AAF82320.1.
AL596223, AC016821 Genomic DNA. Translation: CAH71506.1.
AL672126 Genomic DNA. No translation available.
BC008730 mRNA. Translation: AAH08730.1.
AF073786 mRNA. Translation: AAC25424.1.
AF029306 Genomic DNA. Translation: AAC00172.1.
X66957 mRNA. Translation: CAA47379.1.
CCDSiCCDS7289.1. [P19367-3]
CCDS7290.1. [P19367-4]
CCDS7291.1. [P19367-2]
CCDS7292.1. [P19367-1]
PIRiA31869.
RefSeqiNP_000179.2. NM_000188.2. [P19367-1]
NP_277031.1. NM_033496.2. [P19367-2]
NP_277032.1. NM_033497.2. [P19367-3]
NP_277033.1. NM_033498.2. [P19367-3]
NP_277035.2. NM_033500.2. [P19367-4]
XP_005269793.1. XM_005269736.1. [P19367-3]
UniGeneiHs.370365.

Genome annotation databases

EnsembliENST00000298649; ENSP00000298649; ENSG00000156515. [P19367-2]
ENST00000359426; ENSP00000352398; ENSG00000156515. [P19367-1]
ENST00000360289; ENSP00000353433; ENSG00000156515. [P19367-4]
ENST00000404387; ENSP00000384774; ENSG00000156515. [P19367-3]
GeneIDi3098.
KEGGihsa:3098.
UCSCiuc001jpg.4. human. [P19367-4]
uc001jph.4. human. [P19367-3]
uc001jpk.4. human. [P19367-2]
uc001jpl.4. human. [P19367-1]

Polymorphism databases

DMDMi116242516.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Hexokinase entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M75126 mRNA. Translation: AAA52646.1 .
AF016365
, AF016349 , AF016351 , AF016352 , AF016353 , AF016354 , AF016355 , AF016356 , AF016357 , AF016358 , AF016359 , AF016360 , AF016361 , AF016362 , AF016363 , AF016364 Genomic DNA. Translation: AAC15862.1 .
AF016365
, AF016349 , AF016351 , AF016352 , AF016353 , AF016354 , AF016355 , AF016356 , AF016357 , AF016358 , AF016359 , AF016360 , AF016361 , AF016362 , AF016363 , AF016364 Genomic DNA. Translation: AAC15863.1 .
AF016365
, AF163910 , AF163911 , AF016351 , AF016352 , AF016353 , AF016354 , AF016355 , AF016356 , AF016357 , AF016358 , AF016359 , AF016360 , AF016361 , AF016362 , AF016363 , AF016364 Genomic DNA. Translation: AAF82319.1 .
AF016365
, AF163912 , AF016351 , AF016352 , AF016353 , AF016354 , AF016355 , AF016356 , AF016357 , AF016358 , AF016359 , AF016360 , AF016361 , AF016362 , AF016363 , AF016364 Genomic DNA. Translation: AAF82320.1 .
AL596223 , AC016821 Genomic DNA. Translation: CAH71506.1 .
AL672126 Genomic DNA. No translation available.
BC008730 mRNA. Translation: AAH08730.1 .
AF073786 mRNA. Translation: AAC25424.1 .
AF029306 Genomic DNA. Translation: AAC00172.1 .
X66957 mRNA. Translation: CAA47379.1 .
CCDSi CCDS7289.1. [P19367-3 ]
CCDS7290.1. [P19367-4 ]
CCDS7291.1. [P19367-2 ]
CCDS7292.1. [P19367-1 ]
PIRi A31869.
RefSeqi NP_000179.2. NM_000188.2. [P19367-1 ]
NP_277031.1. NM_033496.2. [P19367-2 ]
NP_277032.1. NM_033497.2. [P19367-3 ]
NP_277033.1. NM_033498.2. [P19367-3 ]
NP_277035.2. NM_033500.2. [P19367-4 ]
XP_005269793.1. XM_005269736.1. [P19367-3 ]
UniGenei Hs.370365.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CZA X-ray 1.90 N 1-917 [» ]
1DGK X-ray 2.80 N 1-917 [» ]
1HKB X-ray 2.80 A/B 1-917 [» ]
1HKC X-ray 2.80 A 1-917 [» ]
1QHA X-ray 2.25 A/B 1-917 [» ]
4F9O X-ray 2.65 A/B 1-914 [» ]
4FOE X-ray 2.70 A/B 1-917 [» ]
4FOI X-ray 2.40 A/B 1-917 [» ]
4FPA X-ray 2.48 A/B 1-917 [» ]
4FPB X-ray 3.00 A/B 1-917 [» ]
ProteinModelPortali P19367.
SMRi P19367. Positions 12-914.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109345. 38 interactions.
IntActi P19367. 10 interactions.
MINTi MINT-1422832.
STRINGi 9606.ENSP00000348697.

Chemistry

BindingDBi P19367.
ChEMBLi CHEMBL2688.

PTM databases

PhosphoSitei P19367.

Polymorphism databases

DMDMi 116242516.

Proteomic databases

MaxQBi P19367.
PaxDbi P19367.
PRIDEi P19367.

Protocols and materials databases

DNASUi 3098.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000298649 ; ENSP00000298649 ; ENSG00000156515 . [P19367-2 ]
ENST00000359426 ; ENSP00000352398 ; ENSG00000156515 . [P19367-1 ]
ENST00000360289 ; ENSP00000353433 ; ENSG00000156515 . [P19367-4 ]
ENST00000404387 ; ENSP00000384774 ; ENSG00000156515 . [P19367-3 ]
GeneIDi 3098.
KEGGi hsa:3098.
UCSCi uc001jpg.4. human. [P19367-4 ]
uc001jph.4. human. [P19367-3 ]
uc001jpk.4. human. [P19367-2 ]
uc001jpl.4. human. [P19367-1 ]

Organism-specific databases

CTDi 3098.
GeneCardsi GC10P071031.
HGNCi HGNC:4922. HK1.
HPAi CAB010052.
HPA007043.
HPA007044.
HPA011956.
MIMi 142600. gene.
235700. phenotype.
605285. phenotype.
neXtProti NX_P19367.
Orphaneti 99953. Charcot-Marie-Tooth disease type 4G.
90031. Non-spherocytic hemolytic anemia due to hexokinase deficiency.
PharmGKBi PA29300.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5026.
HOVERGENi HBG005020.
KOi K00844.
OrthoDBi EOG7S21X5.
PhylomeDBi P19367.
TreeFami TF314238.

Enzyme and pathway databases

UniPathwayi UPA00242 .
BioCyci MetaCyc:HS08136-MONOMER.
Reactomei REACT_212. Glucose transport.
SABIO-RK P19367.

Miscellaneous databases

ChiTaRSi HK1. human.
EvolutionaryTracei P19367.
GenomeRNAii 3098.
NextBioi 12293.
PROi P19367.
SOURCEi Search...

Gene expression databases

ArrayExpressi P19367.
Bgeei P19367.
CleanExi HS_HK1.
Genevestigatori P19367.

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

« Hide 'large scale' publications
  1. "Human hexokinase: sequences of amino- and carboxyl-terminal halves are homologous."
    Nishi S., Seino S., Bell G.I.
    Biochem. Biophys. Res. Commun. 157:937-943(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MET-776.
  2. "Structure of the human hexokinase type I gene and nucleotide sequence of the 5' flanking region."
    Ruzzo A., Andreoni F., Magnani M.
    Biochem. J. 331:607-613(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
  3. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  5. "Structure of the 5' region of the human hexokinase type I (HKI) gene and identification of an additional testis-specific HKI mRNA."
    Andreoni F., Ruzzo A., Magnani M.
    Biochim. Biophys. Acta 1493:19-26(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-126 (ISOFORM 4), ALTERNATIVE SPLICING.
  6. "The erythrocyte-specific hexokinase isozyme (HKR) and the common hexokinase isozyme (HKI) are produced from a single gene by alternate promoters."
    Murakami K., Piomelli S.
    Blood 90:272-272(1998)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20 (ISOFORM 2).
  7. Bienvenut W.V., Waridel P., Quadroni M.
    Submitted (MAR-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-20; 31-42; 382-396 AND 900-910, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryonic kidney.
  8. "Human hexokinase type I microheterogeneity is due to different amino-terminal sequences."
    Magnani M., Serafini G., Bianchi M., Casabianca A., Stocchi V.
    J. Biol. Chem. 266:502-505(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 11-31 AND 103-120.
    Tissue: Placenta.
  9. "A recombinant human 'mini'-hexokinase is catalytically active and regulated by hexose 6-phosphates."
    Magnani M., Bianchi M., Casabianca A., Stocchi V., Daniele A., Altruda F., Ferrone M., Silengo L.
    Biochem. J. 285:193-199(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 287-917, VARIANT MET-776.
    Tissue: Placenta.
  10. "Identification of the cDNA for human red blood cell-specific hexokinase isozyme."
    Murakami K., Piomelli S.
    Blood 89:762-766(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING.
  11. "Crystallization and preliminary X-ray analysis of human brain hexokinase."
    Aleshin A.E., Zeng C., Fromm H.J., Honatko R.B.
    FEBS Lett. 391:9-10(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION.
  12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "A mutation in an alternative untranslated exon of hexokinase 1 associated with hereditary motor and sensory neuropathy -- Russe (HMSNR)."
    Hantke J., Chandler D., King R., Wanders R.J., Angelicheva D., Tournev I., McNamara E., Kwa M., Guergueltcheva V., Kaneva R., Baas F., Kalaydjieva L.
    Eur. J. Hum. Genet. 17:1606-1614(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN HMSNR.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "PKCepsilon promotes oncogenic functions of ATF2 in the nucleus while blocking its apoptotic function at mitochondria."
    Lau E., Kluger H., Varsano T., Lee K., Scheffler I., Rimm D.L., Ideker T., Ronai Z.A.
    Cell 148:543-555(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ATF2 AND VDAC1.
  16. "The mechanism of regulation of hexokinase: new insights from the crystal structure of recombinant human brain hexokinase complexed with glucose and glucose-6-phosphate."
    Aleshin A.E., Zeng C., Bourenkov G.P., Bartunik H.D., Fromm H.J., Honzatko R.B.
    Structure 6:39-50(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 16-914 IN COMPLEX WITH GLUCOSE AND GLUCOSE-6-PHOSPHATE, SUBUNIT.
  17. "Regulation of hexokinase I: crystal structure of recombinant human brain hexokinase complexed with glucose and phosphate."
    Aleshin A.E., Zeng C., Bartunik H.D., Fromm H.J., Honzatko R.B.
    J. Mol. Biol. 282:345-357(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 16-914.
  18. "Binding of non-catalytic ATP to human hexokinase I highlights the structural components for enzyme-membrane association control."
    Rosano C., Sabini E., Rizzi M., Deriu D., Murshudov G., Bianchi M., Serafini G., Magnani M., Bolognesi M.
    Structure 7:1427-1437(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH AMP-PNP AND MAGNESIUM, SUBUNIT.
  19. "Crystal structures of mutant monomeric hexokinase I reveal multiple ADP binding sites and conformational changes relevant to allosteric regulation."
    Aleshin A.E., Kirby C., Liu X., Bourenkov G.P., Bartunik H.D., Fromm H.J., Honzatko R.B.
    J. Mol. Biol. 296:1001-1015(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH GLUCOSE; GLUCOSE-6-PHOSPHATE AND ADP.
  20. "Hexokinase mutations that produce nonspherocytic hemolytic anemia."
    Bianchi M., Magnani M.
    Blood Cells Mol. Dis. 21:2-8(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HK DEFICIENCY SER-529.
  21. "HK Utrecht: missense mutation in the active site of human hexokinase associated with hexokinase deficiency and severe nonspherocytic hemolytic anemia."
    van Wijk R., Rijksen G., Huizinga E.G., Nieuwenhuis H.K., van Solinge W.W.
    Blood 101:345-347(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HK DEFICIENCY SER-680.

Entry informationi

Entry nameiHXK1_HUMAN
AccessioniPrimary (citable) accession number: P19367
Secondary accession number(s): E9PCK0
, O43443, O43444, O75574, Q5VTC3, Q96HC8, Q9NNZ4, Q9NNZ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: October 17, 2006
Last modified: September 3, 2014
This is version 179 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi