P19367 (HXK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Hexokinase-1
EC=2.7.1.1

Alternative name(s):
Brain form hexokinase
Hexokinase type I
Short name=HK I

Gene names

Name:

HK1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	917 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	ATP + D-hexose = ADP + D-hexose 6-phosphate.
Enzyme regulation	Hexokinase is an allosteric enzyme inhibited by its product Glc-6-P.
Pathway	Carbohydrate metabolism; hexose metabolism.
Subunit structure	Monomer. Ref.13 Ref.15
Subcellular location	Mitochondrion outer membrane. Note: Its hydrophobic N-terminal sequence may be involved in membrane binding.
Tissue specificity	Isoform 2 is erythrocyte specific. Isoform 3 and isoform 4 are testis-specific.
Domain	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.
Involvement in disease	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.
Miscellaneous	In vertebrates there are four major glucose-phosphorylating isoenzymes, designated hexokinase I, II, III and IV (glucokinase).
Sequence similarities	Belongs to the hexokinase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Membrane Mitochondrion Mitochondrion outer membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	Repeat
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Allosteric enzyme Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular glucose homeostasis Inferred from Biological aspect of Ancestor. Source: RefGenome glucose transport Traceable author statement. Source: Reactome glycolysis Inferred from Biological aspect of Ancestor. Source: RefGenome small molecule metabolic process Traceable author statement. Source: Reactome transmembrane transport Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome membrane raft Inferred from electronic annotation. Source: Compara mitochondrial outer membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay. Source: HPA nucleus Inferred from direct assay. Source: HPA
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW fructokinase activity Inferred from Biological aspect of Ancestor. Source: RefGenome glucokinase activity Inferred from Biological aspect of Ancestor. Source: RefGenome mannokinase activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
VDAC1	P21796	2	EBI-713162,EBI-354158

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P19367-1)

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.

Isoform 2 (identifier: P19367-2)

Also known as: Erythrocyte; R;

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

Isoform 3 (identifier: P19367-3)

Also known as: TA; TB;

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

Isoform 4 (identifier: P19367-4)

Also known as: TD;

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 917

917

Hexokinase-1

PRO_0000197585

Regions

Nucleotide binding

84 – 89

6

ATP 1 Potential

Nucleotide binding

425 – 426

2

ATP 1

Nucleotide binding

532 – 537

6

ATP 2

Nucleotide binding

747 – 748

2

ATP 2

Nucleotide binding

784 – 788

5

ATP 2

Nucleotide binding

863 – 867

5

ATP 2

Region

1 – 12

12

Hydrophobic

Region

13 – 475

463

Regulatory

Region

84 – 88

5

Glucose-6-phosphate 1 binding

Region

172 – 173

2

Substrate 1 binding

Region

208 – 209

2

Substrate 1 binding

Region

291 – 294

4

Substrate 1 binding

Region

413 – 415

3

Glucose-6-phosphate 1 binding

Region

476 – 917

442

Catalytic

Region

532 – 536

5

Glucose-6-phosphate 2 binding

Region

603 – 604

2

Substrate 2 binding

Region

620 – 621

2

Substrate 2 binding

Region

656 – 657

2

Substrate 2 binding

Region

682 – 683

2

Substrate 2 binding

Region

861 – 863

3

Glucose-6-phosphate 2 binding

Sites

Binding site

30

1

ATP 1

Binding site

155

1

Substrate 1

Binding site

209

1

Glucose-6-phosphate 1

Binding site

232

1

Glucose-6-phosphate 1

Binding site

235

1

Substrate 1

Binding site

260

1

Substrate 1

Binding site

345

1

ATP 1

Binding site

449

1

Glucose-6-phosphate 1

Binding site

657

1

Glucose-6-phosphate 2

Binding site

680

1

ATP 2

Binding site

680

1

Glucose-6-phosphate 2

Binding site

708

1

Substrate 2

Binding site

742

1

Substrate 2

Binding site

897

1

Glucose-6-phosphate 2

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.7

Modified residue

27

1

Phosphotyrosine By similarity

Natural variations

Alternative sequence

1 – 21

21

MIAAQ…DQVKK → MDCEHSLSLPCRGAEAWEIG in isoform 2.

VSP_002071

Alternative sequence

1 – 21

21

MIAAQ…DQVKK → MGQICQRESATAAEKPKLHL LAESE in isoform 3.

VSP_002072

Alternative sequence

1 – 21

21

MIAAQ…DQVKK → MAKRALHDF in isoform 4.

VSP_002073

Natural variant

529

1

L → S in HK deficiency. Ref.17

VAR_009878

Natural variant

680

1

T → S in HK deficiency; HK Utrecht. Ref.18

VAR_023780

Natural variant

776

1

L → M. Ref.1 Ref.9
Corresponds to variant rs1054203 [ dbSNP | Ensembl ].

VAR_023781

Experimental info

Sequence conflict

730

1

D → N in AAA52646. Ref.1

Sequence conflict

730

1

D → N in CAA47379. Ref.9

Secondary structure

1

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917

Helix Strand Turn

Details...

Helix

17 – 25

9

Helix

27 – 29

3

Helix

33 – 51

19

Turn

53 – 55

3

Helix

56 – 58

3

Beta strand

78 – 100

23

Beta strand

103 – 112

10

Helix

116 – 119

4

Beta strand

120 – 122

3

Helix

123 – 141

19

Beta strand

144 – 146

3

Beta strand

150 – 154

5

Helix

185 – 196

12

Beta strand

203 – 207

5

Helix

209 – 220

12

Beta strand

224 – 241

18

Helix

242 – 244

3

Beta strand

252 – 258

7

Helix

261 – 263

3

Turn

264 – 273

10

Helix

276 – 283

8

Beta strand

285 – 287

3

Helix

294 – 297

4

Helix

299 – 315

17

Helix

320 – 322

3

Turn

326 – 329

4

Helix

336 – 342

7

Turn

345 – 347

3

Helix

348 – 358

11

Helix

365 – 401

37

Beta strand

404 – 413

10

Helix

415 – 419

5

Helix

423 – 434

12

Beta strand

438 – 444

7

Helix

449 – 475

27

Helix

481 – 499

19

Helix

501 – 504

4

Beta strand

526 – 546

21

Beta strand

548 – 550

3

Beta strand

552 – 560

9

Helix

564 – 567

4

Helix

571 – 589

19

Beta strand

597 – 602

6

Beta strand

606 – 610

5

Beta strand

613 – 616

4

Helix

633 – 644

12

Beta strand

650 – 655

6

Helix

657 – 666

10

Beta strand

672 – 689

18

Turn

690 – 692

3

Beta strand

700 – 706

7

Helix

709 – 711

3

Turn

712 – 715

4

Turn

717 – 721

5

Helix

724 – 731

8

Turn

734 – 737

4

Helix

742 – 744

3

Turn

747 – 749

3

Helix

750 – 763

14

Helix

768 – 770

3

Turn

774 – 777

4

Helix

784 – 790

7

Helix

797 – 807

11

Helix

813 – 848

36

Beta strand

852 – 861

10

Helix

863 – 867

5

Helix

871 – 882

12

Beta strand

886 – 892

7

Helix

898 – 912

15

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Common) [UniParc]. Last modified October 17, 2006. Version 3. Checksum: F29A6837531C0594	FASTA	917	102,486
	10 20 30 40 50 60 MIAAQLLAYY FTELKDDQVK KIDKYLYAMR LSDETLIDIM TRFRKEMKNG LSRDFNPTAT 70 80 90 100 110 120 VKMLPTFVRS IPDGSEKGDF IALDLGGSSF RILRVQVNHE KNQNVHMESE VYDTPENIVH 130 140 150 160 170 180 GSGSQLFDHV AECLGDFMEK RKIKDKKLPV GFTFSFPCQQ SKIDEAILIT WTKRFKASGV 190 200 210 220 230 240 EGADVVKLLN KAIKKRGDYD ANIVAVVNDT VGTMMTCGYD DQHCEVGLII GTGTNACYME 250 260 270 280 290 300 ELRHIDLVEG DEGRMCINTE WGAFGDDGSL EDIRTEFDRE IDRGSLNPGK QLFEKMVSGM 310 320 330 340 350 360 YLGELVRLIL VKMAKEGLLF EGRITPELLT RGKFNTSDVS AIEKNKEGLH NAKEILTRLG 370 380 390 400 410 420 VEPSDDDCVS VQHVCTIVSF RSANLVAATL GAILNRLRDN KGTPRLRTTV GVDGSLYKTH 430 440 450 460 470 480 PQYSRRFHKT LRRLVPDSDV RFLLSESGSG KGAAMVTAVA YRLAEQHRQI EETLAHFHLT 490 500 510 520 530 540 KDMLLEVKKR MRAEMELGLR KQTHNNAVVK MLPSFVRRTP DGTENGDFLA LDLGGTNFRV 550 560 570 580 590 600 LLVKIRSGKK RTVEMHNKIY AIPIEIMQGT GEELFDHIVS CISDFLDYMG IKGPRMPLGF 610 620 630 640 650 660 TFSFPCQQTS LDAGILITWT KGFKATDCVG HDVVTLLRDA IKRREEFDLD VVAVVNDTVG 670 680 690 700 710 720 TMMTCAYEEP TCEVGLIVGT GSNACYMEEM KNVEMVEGDQ GQMCINMEWG AFGDNGCLDD 730 740 750 760 770 780 IRTHYDRLVD EYSLNAGKQR YEKMISGMYL GEIVRNILID FTKKGFLFRG QISETLKTRG 790 800 810 820 830 840 IFETKFLSQI ESDRLALLQV RAILQQLGLN STCDDSILVK TVCGVVSRRA AQLCGAGMAA 850 860 870 880 890 900 VVDKIRENRG LDRLNVTVGV DGTLYKLHPH FSRIMHQTVK ELSPKCNVSF LLSEDGSGKG 910 AALITAVGVR LRTEASS
	Isoform 2 (Erythrocyte) (R) [UniParc]. Checksum: 6E528FC4BEC5100B	FASTA	916	102,201
	10 20 30 40 50 60 MDCEHSLSLP CRGAEAWEIG IDKYLYAMRL SDETLIDIMT RFRKEMKNGL SRDFNPTATV 70 80 90 100 110 120 KMLPTFVRSI PDGSEKGDFI ALDLGGSSFR ILRVQVNHEK NQNVHMESEV YDTPENIVHG 130 140 150 160 170 180 SGSQLFDHVA ECLGDFMEKR KIKDKKLPVG FTFSFPCQQS KIDEAILITW TKRFKASGVE 190 200 210 220 230 240 GADVVKLLNK AIKKRGDYDA NIVAVVNDTV GTMMTCGYDD QHCEVGLIIG TGTNACYMEE 250 260 270 280 290 300 LRHIDLVEGD EGRMCINTEW GAFGDDGSLE DIRTEFDREI DRGSLNPGKQ LFEKMVSGMY 310 320 330 340 350 360 LGELVRLILV KMAKEGLLFE GRITPELLTR GKFNTSDVSA IEKNKEGLHN AKEILTRLGV 370 380 390 400 410 420 EPSDDDCVSV QHVCTIVSFR SANLVAATLG AILNRLRDNK GTPRLRTTVG VDGSLYKTHP 430 440 450 460 470 480 QYSRRFHKTL RRLVPDSDVR FLLSESGSGK GAAMVTAVAY RLAEQHRQIE ETLAHFHLTK 490 500 510 520 530 540 DMLLEVKKRM RAEMELGLRK QTHNNAVVKM LPSFVRRTPD GTENGDFLAL DLGGTNFRVL 550 560 570 580 590 600 LVKIRSGKKR TVEMHNKIYA IPIEIMQGTG EELFDHIVSC ISDFLDYMGI KGPRMPLGFT 610 620 630 640 650 660 FSFPCQQTSL DAGILITWTK GFKATDCVGH DVVTLLRDAI KRREEFDLDV VAVVNDTVGT 670 680 690 700 710 720 MMTCAYEEPT CEVGLIVGTG SNACYMEEMK NVEMVEGDQG QMCINMEWGA FGDNGCLDDI 730 740 750 760 770 780 RTHYDRLVDE YSLNAGKQRY EKMISGMYLG EIVRNILIDF TKKGFLFRGQ ISETLKTRGI 790 800 810 820 830 840 FETKFLSQIE SDRLALLQVR AILQQLGLNS TCDDSILVKT VCGVVSRRAA QLCGAGMAAV 850 860 870 880 890 900 VDKIRENRGL DRLNVTVGVD GTLYKLHPHF SRIMHQTVKE LSPKCNVSFL LSEDGSGKGA 910 ALITAVGVRL RTEASS
	Isoform 3 (TA) (TB) [UniParc]. Checksum: 329F41F87DF6E1D1	FASTA	921	102,738
	10 20 30 40 50 60 MGQICQRESA TAAEKPKLHL LAESEIDKYL YAMRLSDETL IDIMTRFRKE MKNGLSRDFN 70 80 90 100 110 120 PTATVKMLPT FVRSIPDGSE KGDFIALDLG GSSFRILRVQ VNHEKNQNVH MESEVYDTPE 130 140 150 160 170 180 NIVHGSGSQL FDHVAECLGD FMEKRKIKDK KLPVGFTFSF PCQQSKIDEA ILITWTKRFK 190 200 210 220 230 240 ASGVEGADVV KLLNKAIKKR GDYDANIVAV VNDTVGTMMT CGYDDQHCEV GLIIGTGTNA 250 260 270 280 290 300 CYMEELRHID LVEGDEGRMC INTEWGAFGD DGSLEDIRTE FDREIDRGSL NPGKQLFEKM 310 320 330 340 350 360 VSGMYLGELV RLILVKMAKE GLLFEGRITP ELLTRGKFNT SDVSAIEKNK EGLHNAKEIL 370 380 390 400 410 420 TRLGVEPSDD DCVSVQHVCT IVSFRSANLV AATLGAILNR LRDNKGTPRL RTTVGVDGSL 430 440 450 460 470 480 YKTHPQYSRR FHKTLRRLVP DSDVRFLLSE SGSGKGAAMV TAVAYRLAEQ HRQIEETLAH 490 500 510 520 530 540 FHLTKDMLLE VKKRMRAEME LGLRKQTHNN AVVKMLPSFV RRTPDGTENG DFLALDLGGT 550 560 570 580 590 600 NFRVLLVKIR SGKKRTVEMH NKIYAIPIEI MQGTGEELFD HIVSCISDFL DYMGIKGPRM 610 620 630 640 650 660 PLGFTFSFPC QQTSLDAGIL ITWTKGFKAT DCVGHDVVTL LRDAIKRREE FDLDVVAVVN 670 680 690 700 710 720 DTVGTMMTCA YEEPTCEVGL IVGTGSNACY MEEMKNVEMV EGDQGQMCIN MEWGAFGDNG 730 740 750 760 770 780 CLDDIRTHYD RLVDEYSLNA GKQRYEKMIS GMYLGEIVRN ILIDFTKKGF LFRGQISETL 790 800 810 820 830 840 KTRGIFETKF LSQIESDRLA LLQVRAILQQ LGLNSTCDDS ILVKTVCGVV SRRAAQLCGA 850 860 870 880 890 900 GMAAVVDKIR ENRGLDRLNV TVGVDGTLYK LHPHFSRIMH QTVKELSPKC NVSFLLSEDG 910 920 SGKGAALITA VGVRLRTEAS S
	Isoform 4 (TD) [UniParc]. Checksum: AE1BC4A3D2604AB0	FASTA	905	101,085
	10 20 30 40 50 60 MAKRALHDFI DKYLYAMRLS DETLIDIMTR FRKEMKNGLS RDFNPTATVK MLPTFVRSIP 70 80 90 100 110 120 DGSEKGDFIA LDLGGSSFRI LRVQVNHEKN QNVHMESEVY DTPENIVHGS GSQLFDHVAE 130 140 150 160 170 180 CLGDFMEKRK IKDKKLPVGF TFSFPCQQSK IDEAILITWT KRFKASGVEG ADVVKLLNKA 190 200 210 220 230 240 IKKRGDYDAN IVAVVNDTVG TMMTCGYDDQ HCEVGLIIGT GTNACYMEEL RHIDLVEGDE 250 260 270 280 290 300 GRMCINTEWG AFGDDGSLED IRTEFDREID RGSLNPGKQL FEKMVSGMYL GELVRLILVK 310 320 330 340 350 360 MAKEGLLFEG RITPELLTRG KFNTSDVSAI EKNKEGLHNA KEILTRLGVE PSDDDCVSVQ 370 380 390 400 410 420 HVCTIVSFRS ANLVAATLGA ILNRLRDNKG TPRLRTTVGV DGSLYKTHPQ YSRRFHKTLR 430 440 450 460 470 480 RLVPDSDVRF LLSESGSGKG AAMVTAVAYR LAEQHRQIEE TLAHFHLTKD MLLEVKKRMR 490 500 510 520 530 540 AEMELGLRKQ THNNAVVKML PSFVRRTPDG TENGDFLALD LGGTNFRVLL VKIRSGKKRT 550 560 570 580 590 600 VEMHNKIYAI PIEIMQGTGE ELFDHIVSCI SDFLDYMGIK GPRMPLGFTF SFPCQQTSLD 610 620 630 640 650 660 AGILITWTKG FKATDCVGHD VVTLLRDAIK RREEFDLDVV AVVNDTVGTM MTCAYEEPTC 670 680 690 700 710 720 EVGLIVGTGS NACYMEEMKN VEMVEGDQGQ MCINMEWGAF GDNGCLDDIR THYDRLVDEY 730 740 750 760 770 780 SLNAGKQRYE KMISGMYLGE IVRNILIDFT KKGFLFRGQI SETLKTRGIF ETKFLSQIES 790 800 810 820 830 840 DRLALLQVRA ILQQLGLNST CDDSILVKTV CGVVSRRAAQ LCGAGMAAVV DKIRENRGLD 850 860 870 880 890 900 RLNVTVGVDG TLYKLHPHFS RIMHQTVKEL SPKCNVSFLL SEDGSGKGAA LITAVGVRLR TEASS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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, 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]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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.
[18]	"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.
+	Additional computationally mapped references.

Web resources

Wikipedia

Hexokinase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00018246.
IPI00220663.
IPI00220665.
IPI00220667.

PIR

A31869.

RefSeq

NP_000179.2. NM_000188.2.
NP_277031.1. NM_033496.2.
NP_277032.1. NM_033497.2.
NP_277033.1. NM_033498.2.
NP_277035.2. NM_033500.2.

UniGene

Hs.370365.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P19367.

ModBase

Search...

Protein-protein interaction databases

IntAct

P19367. 8 interactions.

MINT

MINT-1422832.

STRING

9606.ENSP00000348697.

PTM databases

PhosphoSite

P19367.

Polymorphism databases

DMDM

116242516.

Proteomic databases

PaxDb

P19367.

PRIDE

P19367.

Protocols and materials databases

DNASU

3098.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000298649; ENSP00000298649; ENSG00000156515.
ENST00000359426; ENSP00000352398; ENSG00000156515.
ENST00000360289; ENSP00000353433; ENSG00000156515.
ENST00000404387; ENSP00000384774; ENSG00000156515.

GeneID

3098.

KEGG

hsa:3098.

UCSC

uc001jph.4. human.
uc001jpk.4. human.
uc001jpl.4. human.

Organism-specific databases

CTD

3098.

GeneCards

GC10P071031.

HGNC

HGNC:4922. HK1.

HPA

CAB010052.
HPA007043.
HPA007044.
HPA011956.

MIM

142600. gene.
235700. phenotype.

neXtProt

NX_P19367.

Orphanet

99953. Charcot-Marie-Tooth disease type 4G.
90031. Nonspherocytic hemolytic anemia due to hexokinase deficiency.

PharmGKB

PA29300.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5026.

HOVERGEN

HBG005020.

KO

K00844.

OrthoDB

EOG47WNMX.

Enzyme and pathway databases

Pathway_Interaction_DB

hif1_tfpathway. HIF-1-alpha transcription factor network.

Reactome

REACT_111217. Metabolism.
REACT_15518. Transmembrane transport of small molecules.

SABIO-RK

P19367.

UniPathway

UPA00242.

Gene expression databases

ArrayExpress

P19367.

Bgee

P19367.

CleanEx

HS_HK1.

Genevestigator

P19367.

GermOnline

ENSG00000156515. Homo sapiens.

Family and domain databases

InterPro

IPR001312. Hexokinase.
IPR022673. Hexokinase_C.
IPR019807. Hexokinase_CS.
IPR022672. Hexokinase_N.
[Graphical view]

PANTHER

PTHR19443. PTHR19443. 1 hit.

Pfam

PF00349. Hexokinase_1. 2 hits.
PF03727. Hexokinase_2. 2 hits.
[Graphical view]

PRINTS

PR00475. HEXOKINASE.

PROSITE

PS00378. HEXOKINASES. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P19367.

ChEMBL

CHEMBL2688.

ChiTaRS

HK1. human.

EvolutionaryTrace

P19367.

GenomeRNAi

3098.

NextBio

12293.

SOURCE

Search...

Entry information

Entry name

HXK1_HUMAN

Accession

Primary (citable) accession number: P19367
Secondary accession number(s): E9PCK0 , O43443, O43444, O75574, Q5VTC3, Q96HC8, Q9NNZ4, Q9NNZ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	October 17, 2006
Last modified:	May 1, 2013
This is version 165 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.