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UniProtKB - P52789 (HXK2_HUMAN)

Entry version 196 (16 Oct 2019)
Sequence version 2 (07 Dec 2004)
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Protein

Hexokinase-2

Gene

HK2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the phosphorylation of hexose, such as D-glucose and D-fructose, to hexose 6-phosphate (D-glucose 6-phosphate and D-fructose 6-phosphate, respectively) (PubMed:23185017, PubMed:26985301, PubMed:29298880). Mediates the initial step of glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6-phosphate (PubMed:29298880). Plays a key role in maintaining the integrity of the outer mitochondrial membrane by preventing the release of apoptogenic molecules from the intermembrane space and subsequent apoptosis (PubMed:18350175).4 Publications

Caution

Hexokinase is known to act as a monomer in normal conditions (By similarity). It however homodimerizes at elevated protein concentrations used for crystallizations (PubMed:26985301, PubMed:29298880).By similarity2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Hexokinase activity is specifically inhibited by 2,6-disubstituted glucosamines.1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.21 mM for D-glucose1 Publication
  2. KM=1.13 mM for ATP1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: hexose metabolism

    This protein is involved in the pathway hexose metabolism, which is part of Carbohydrate metabolism.1 Publication
    View all proteins of this organism that are known to be involved in the pathway hexose metabolism and in Carbohydrate metabolism.

    Pathwayi: glycolysis

    This protein is involved in step 1 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.1 Publication
    Proteins known to be involved in the 4 steps of the subpathway in this organism are:
    1. Hexokinase 3 (White cell), isoform CRA_b (HK3), Hexokinase 3 variant, Hexokinase-3 (HK3), cDNA FLJ77931, Hexokinase-4 (GCK), cDNA FLJ46359 fis, clone TESTI4049786, highly similar to Hexokinase-1, Phosphotransferase (GCK), Phosphotransferase (HK2), Hexokinase-2 (HK2), Phosphotransferase (GCK), Hexokinase 1 isoform HKI variant, Phosphotransferase (GCK), Phosphotransferase, cDNA FLJ37767 fis, clone BRHIP2024911, highly similar to Homo sapiens hexokinase domain containing 1 (HKDC1), mRNA, Phosphotransferase, Hexokinase HKDC1 (HKDC1), Hexokinase-1 (HK1), cDNA FLJ56506, highly similar to Hexokinase-1, Phosphotransferase (HK1), Hexokinase-2 (HK2), Phosphotransferase (HK2), cDNA FLJ57348, highly similar to Homo sapiens hexokinase domain containing 1 (HKDC1), mRNA, Hexokinase 1, isoform CRA_c (HK1), cDNA FLJ78173, highly similar to Homo sapiens hexokinase 1 (HK1) mRNA, Phosphotransferase (GCK), cDNA FLJ75392, highly similar to Homo sapiens hexokinase II (HKII) mRNA, Uncharacterized protein DKFZp686M1669 (DKFZp686M1669), Phosphotransferase (HK3)
    2. Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase, Glucose-6-phosphate isomerase, Glucose-6-phosphate isomerase, Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase (GPI)
    3. ATP-dependent 6-phosphofructokinase, muscle type (PFKM), ATP-dependent 6-phosphofructokinase, platelet type (PFKP), ATP-dependent 6-phosphofructokinase (PFKM), ATP-dependent 6-phosphofructokinase, liver type (PFKL), ATP-dependent 6-phosphofructokinase (PFKM)
    4. Fructose-bisphosphate aldolase (ALDOC), Fructose-bisphosphate aldolase (ALDOB), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (ALDOB), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (ALDOB), Fructose-bisphosphate aldolase (ALDOA), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (ALDOA), Fructose-bisphosphate aldolase (ALDOA), Fructose-bisphosphate aldolase B (ALDOB), Fructose-bisphosphate aldolase C (ALDOC), Fructose-bisphosphate aldolase A (ALDOA), Fructose-bisphosphate aldolase (ALDOC), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (HEL-S-87p), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (ALDOA)
    This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose, the pathway glycolysis and in Carbohydrate degradation.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei30ATP 1By similarity1
    Binding sitei209Glucose-6-phosphate 1Combined sources1 Publication1
    Binding sitei232Glucose-6-phosphate 1Combined sources1 Publication1
    Binding sitei235Substrate 1Combined sources1 Publication1
    Binding sitei260Substrate 1Combined sources1 Publication1
    Binding sitei449Glucose-6-phosphate 1Combined sources1 Publication1
    Binding sitei657Glucose-6-phosphate 2Combined sources2 Publications1
    Binding sitei680ATP 2By similarity1
    Binding sitei680Glucose-6-phosphate 2Combined sources2 Publications1
    Binding sitei708Substrate 2Combined sources1 Publication1
    Binding sitei897Glucose-6-phosphate 2Combined sources2 Publications1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi84 – 89ATP 1By similarity6
    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

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    Complete GO annotation on QuickGO ...

    GO - Biological processi

    Complete GO annotation on QuickGO ...

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionAllosteric enzyme, Kinase, Transferase
    Biological processGlycolysis
    LigandATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		MetaCyc:HS08399-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		2.7.1.1 2681

    Reactome - a knowledgebase of biological pathways and processes

    More...    Reactomei    		R-HSA-70171 Glycolysis

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...    SABIO-RKi    		P52789

    SIGNOR Signaling Network Open Resource

    More...    SIGNORi    		P52789

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...    UniPathwayi    		UPA00109;UER00180
    UPA00242

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Hexokinase-2Curated (EC:2.7.1.13 Publications)
    Alternative name(s):
    Hexokinase type II2 Publications
    Short name:
    HK II2 Publications
    Hexokinase-BBy similarity
    Muscle form hexokinase1 Publication
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:HK2Imported
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 2

    Organism-specific databases

    Human Gene Nomenclature Database

    More...    HGNCi    		HGNC:4923 HK2

    Online Mendelian Inheritance in Man (OMIM)

    More...    MIMi    		601125 gene

    neXtProt; the human protein knowledge platform

    More...    neXtProti    		NX_P52789

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Mitochondrion, Mitochondrion outer membrane

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi209D → A: Decreased hexokinase activity. 1 Publication1
    Mutagenesisi468R → A: Induces a rapid dissociation of D-glucose. 1 Publication1
    Mutagenesisi657D → A: Decreased hexokinase activity. 1 Publication1

    Organism-specific databases

    DisGeNET

    More...    DisGeNETi    		3099

    Open Targets

    More...    OpenTargetsi    		ENSG00000159399

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...    PharmGKBi    		PA29301

    Miscellaneous databases

    Pharos NIH Druggable Genome Knowledgebase

    More...    Pharosi    		P52789

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...    ChEMBLi    		CHEMBL2640

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...    BioMutai    		HK2

    Domain mapping of disease mutations (DMDM)

    More...    DMDMi    		56405344

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001975871 – 917Hexokinase-2Add BLAST917

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1N-acetylmethionineCombined sources1

    Keywords - PTMi

    Acetylation

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...    EPDi    		P52789

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		P52789

    MassIVE - Mass Spectrometry Interactive Virtual Environment

    More...    MassIVEi    		P52789

    MaxQB - The MaxQuant DataBase

    More...    MaxQBi    		P52789

    PaxDb, a database of protein abundance averages across all three domains of life

    More...    PaxDbi    		P52789

    PeptideAtlas

    More...    PeptideAtlasi    		P52789

    PRoteomics IDEntifications database

    More...    PRIDEi    		P52789

    ProteomicsDB: a multi-organism proteome resource

    More...    ProteomicsDBi    		56533

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...    iPTMneti    		P52789

    Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

    More...    PhosphoSitePlusi    		P52789

    SwissPalm database of S-palmitoylation events

    More...    SwissPalmi    		P52789

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

    Predominant hexokinase isozyme expressed in insulin-responsive tissues such as skeletal muscle.1 Publication

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...    Bgeei    		ENSG00000159399 Expressed in 218 organ(s), highest expression level in colon

    ExpressionAtlas, Differential and Baseline Expression

    More...    ExpressionAtlasi    		P52789 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...    Genevisiblei    		P52789 HS

    Organism-specific databases

    Human Protein Atlas

    More...    HPAi    		HPA028587

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Monomer (By similarity).

    Interacts with TIGAR; the interaction increases hexokinase activity in a hypoxia- and HIF1A-dependent manner (PubMed:23185017).

    By similarity1 Publication

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...    BioGridi    		109346, 57 interactors

    Database of interacting proteins

    More...    DIPi    		DIP-50110N

    Protein interaction database and analysis system

    More...    IntActi    		P52789, 32 interactors

    Molecular INTeraction database

    More...    MINTi    		P52789

    STRING: functional protein association networks

    More...    STRINGi    		9606.ENSP00000290573

    Chemistry databases

    BindingDB database of measured binding affinities

    More...    BindingDBi    		P52789

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1917
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...    SMRi    		P52789

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    Protein Data Bank in Europe - Knowledge Base

    More...    PDBe-KBi    		Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...    EvolutionaryTracei    		P52789

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini16 – 458Hexokinase 1PROSITE-ProRule annotationAdd BLAST443
    Domaini464 – 906Hexokinase 2PROSITE-ProRule annotationAdd BLAST443

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 16Mitochondrial-binding peptide (MBP)1 PublicationAdd BLAST16
    Regioni73 – 207Hexokinase small subdomain 1PROSITE-ProRule annotationAdd BLAST135
    Regioni84 – 88Glucose-6-phosphate 1 bindingCombined sources1 Publication5
    Regioni155 – 156Substrate 1 bindingCombined sources1 Publication2
    Regioni172 – 173Substrate 1 bindingCombined sources1 Publication2
    Regioni208 – 447Hexokinase large subdomain 1PROSITE-ProRule annotationAdd BLAST240
    Regioni208 – 209Substrate 1 bindingCombined sources1 Publication2
    Regioni291 – 294Substrate 1 bindingCombined sources1 Publication4
    Regioni413 – 415Glucose-6-phosphate 1 bindingCombined sources1 Publication3
    Regioni521 – 655Hexokinase small subdomain 2PROSITE-ProRule annotationAdd BLAST135
    Regioni532 – 536Glucose-6-phosphate 2 bindingCombined sources2 Publications5
    Regioni603 – 604Substrate 2 bindingCombined sources1 Publication2
    Regioni620 – 621Substrate 2 bindingCombined sources1 Publication2
    Regioni656 – 895Hexokinase large subdomain 2PROSITE-ProRule annotationAdd BLAST240
    Regioni656 – 657Substrate 2 bindingCombined sources1 Publication2
    Regioni682 – 683Substrate 2 bindingCombined sources1 Publication2
    Regioni739 – 742Substrate 2 bindingCombined sources1 Publication4
    Regioni861 – 863Glucose-6-phosphate 2 bindingCombined sources2 Publications3

    <p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    The N- and C-terminal halves of the protein contain a hexokinase domain (PubMed:29298880). In contrast to hexokinase-1 and -3 (HK1 and HK3, respectively), both hexokinase domains display catalytic activity (PubMed:29298880). The region connecting the two hexokinase domains is required for the catalytic activity of the N-terminal hexokinase domain (PubMed:29298880). The N-terminal half regulates stability of the whole enzyme (PubMed:29298880).1 Publication

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the hexokinase family.PROSITE-ProRule annotationCurated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		KOG1369 Eukaryota
    COG5026 LUCA

    Ensembl GeneTree

    More...    GeneTreei    		ENSGT00950000182787

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		HOG000162671

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P52789

    KEGG Orthology (KO)

    More...    KOi    		K00844

    Identification of Orthologs from Complete Genome Data

    More...    OMAi    		RHIDTVE

    Database of Orthologous Groups

    More...    OrthoDBi    		1153545at2759

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P52789

    TreeFam database of animal gene trees

    More...    TreeFami    		TF314238

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR001312 Hexokinase
    IPR019807 Hexokinase_BS
    IPR022673 Hexokinase_C
    IPR022672 Hexokinase_N

    The PANTHER Classification System

    More...    PANTHERi    		PTHR19443 PTHR19443, 2 hits

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF00349 Hexokinase_1, 2 hits
    PF03727 Hexokinase_2, 2 hits

    PROSITE; a protein domain and family database

    More...    PROSITEi    		View protein in PROSITE
    PS00378 HEXOKINASE_1, 2 hits
    PS51748 HEXOKINASE_2, 2 hits

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

    P52789-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MIASHLLAYF FTELNHDQVQ KVDQYLYHMR LSDETLLEIS KRFRKEMEKG 
            60         70         80         90        100
    LGATTHPTAA VKMLPTFVRS TPDGTEHGEF LALDLGGTNF RVLWVKVTDN 
           110        120        130        140        150
    GLQKVEMENQ IYAIPEDIMR GSGTQLFDHI AECLANFMDK LQIKDKKLPL 
           160        170        180        190        200
    GFTFSFPCHQ TKLDESFLVS WTKGFKSSGV EGRDVVALIR KAIQRRGDFD 
           210        220        230        240        250
    IDIVAVVNDT VGTMMTCGYD DHNCEIGLIV GTGSNACYME EMRHIDMVEG 
           260        270        280        290        300
    DEGRMCINME WGAFGDDGSL NDIRTEFDQE IDMGSLNPGK QLFEKMISGM 
           310        320        330        340        350
    YMGELVRLIL VKMAKEELLF GGKLSPELLN TGRFETKDIS DIEGEKDGIR 
           360        370        380        390        400
    KAREVLMRLG LDPTQEDCVA THRICQIVST RSASLCAATL AAVLQRIKEN 
           410        420        430        440        450
    KGEERLRSTI GVDGSVYKKH PHFAKRLHKT VRRLVPGCDV RFLRSEDGSG 
           460        470        480        490        500
    KGAAMVTAVA YRLADQHRAR QKTLEHLQLS HDQLLEVKRR MKVEMERGLS 
           510        520        530        540        550
    KETHASAPVK MLPTYVCATP DGTEKGDFLA LDLGGTNFRV LLVRVRNGKW 
           560        570        580        590        600
    GGVEMHNKIY AIPQEVMHGT GDELFDHIVQ CIADFLEYMG MKGVSLPLGF 
           610        620        630        640        650
    TFSFPCQQNS LDESILLKWT KGFKASGCEG EDVVTLLKEA IHRREEFDLD 
           660        670        680        690        700
    VVAVVNDTVG TMMTCGFEDP HCEVGLIVGT GSNACYMEEM RNVELVEGEE 
           710        720        730        740        750
    GRMCVNMEWG AFGDNGCLDD FRTEFDVAVD ELSLNPGKQR FEKMISGMYL 
           760        770        780        790        800
    GEIVRNILID FTKRGLLFRG RISERLKTRG IFETKFLSQI ESDCLALLQV 
           810        820        830        840        850
    RAILQHLGLE STCDDSIIVK EVCTVVARRA AQLCGAGMAA VVDRIRENRG 
           860        870        880        890        900
    LDALKVTVGV DGTLYKLHPH FAKVMHETVK DLAPKCDVSF LQSEDGSGKG 
           910 
    AALITAVACR IREAGQR
    Length:917
    Mass (Da):102,380
    Last modified:December 7, 2004 - v2
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iF17CE1938CF13880
    GO

    <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

    There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    		Gene namesLengthAnnotation
    E9PB90E9PB90_HUMAN
    Hexokinase-2
    HK2
    		889Annotation score:

    Annotation score:2 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti803I → T in CAA86511 (PubMed:8250948).Curated1
    Sequence conflicti870Missing in CAA86476 (PubMed:8786021).Curated1

    <p>This subsection of the ‘Sequence’ section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement_in_disease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi

    Although found in NIDDM patients, genetic variations of HK2 do not contribute to the disease (PubMed:7883122, PubMed:7883123).2 Publications

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_003691142Q → H Does not affect activity. 4 PublicationsCorresponds to variant dbSNP:rs2229621Ensembl.1
    Natural variantiVAR_010577148L → F1 Publication1
    Natural variantiVAR_020504274R → C1 PublicationCorresponds to variant dbSNP:rs28363006Ensembl.1
    Natural variantiVAR_020505314A → P1 PublicationCorresponds to variant dbSNP:rs28363015Ensembl.1
    Natural variantiVAR_010578314A → V1 Publication1
    Natural variantiVAR_020506331T → I1 PublicationCorresponds to variant dbSNP:rs28363016Ensembl.1
    Natural variantiVAR_010579353R → C1 PublicationCorresponds to variant dbSNP:rs61748096Ensembl.1
    Natural variantiVAR_020507387A → S1 PublicationCorresponds to variant dbSNP:rs28363029Ensembl.1
    Natural variantiVAR_010580497R → Q1 PublicationCorresponds to variant dbSNP:rs145124653Ensembl.1
    Natural variantiVAR_010581775R → Q1 PublicationCorresponds to variant dbSNP:rs185927605Ensembl.1
    Natural variantiVAR_020508801R → Q1 PublicationCorresponds to variant dbSNP:rs28363057Ensembl.1
    Natural variantiVAR_010582844R → K2 PublicationsCorresponds to variant dbSNP:rs2229629Ensembl.1
    Natural variantiVAR_020509881D → N1 PublicationCorresponds to variant dbSNP:rs28363065Ensembl.1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...    EMBLi

    GenBank nucleotide sequence database

    More...    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...    DDBJi
    Links Updated
    		Z46376 mRNA Translation: CAA86511.1
    Z46354
    , Z46355, Z46604, Z46356, Z46357, Z46358, Z46359, Z46360, Z46361, Z46362, Z46363, Z46364, Z46365, Z46366, Z46367, Z46368, Z46369 Genomic DNA Translation: CAA86476.2
    AF148513 mRNA Translation: AAD30174.1
    AY623118 Genomic DNA Translation: AAT38114.1
    CH471053 Genomic DNA Translation: EAW99601.1
    CH471053 Genomic DNA Translation: EAW99602.1
    BC021116 mRNA Translation: AAH21116.1
    BC064369 mRNA Translation: AAH64369.1
    D25412 Genomic DNA Translation: BAA04999.1

    The Consensus CDS (CCDS) project

    More...    CCDSi    		CCDS1956.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		S48809 JC2025

    NCBI Reference Sequences

    More...    RefSeqi    		NP_000180.2, NM_000189.4

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...    Ensembli    		ENST00000290573; ENSP00000290573; ENSG00000159399

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		3099

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		hsa:3099

    UCSC genome browser

    More...    UCSCi    		uc002snd.4 human

    Keywords - Coding sequence diversityi

    Polymorphism

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    <p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

    NIEHS-SNPs
    Wikipedia

    Hexokinase entry

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    		Z46376 mRNA Translation: CAA86511.1
    Z46354
    , Z46355, Z46604, Z46356, Z46357, Z46358, Z46359, Z46360, Z46361, Z46362, Z46363, Z46364, Z46365, Z46366, Z46367, Z46368, Z46369 Genomic DNA Translation: CAA86476.2
    AF148513 mRNA Translation: AAD30174.1
    AY623118 Genomic DNA Translation: AAT38114.1
    CH471053 Genomic DNA Translation: EAW99601.1
    CH471053 Genomic DNA Translation: EAW99602.1
    BC021116 mRNA Translation: AAH21116.1
    BC064369 mRNA Translation: AAH64369.1
    D25412 Genomic DNA Translation: BAA04999.1
    CCDSiCCDS1956.1
    PIRiS48809 JC2025
    RefSeqiNP_000180.2, NM_000189.4

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...    PDBei

    Protein Data Bank RCSB

    More...    RCSB PDBi

    Protein Data Bank Japan

    More...    PDBji
    Links Updated
    		PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2NZTX-ray2.45A/B17-916[»]
    5HEXX-ray2.73A/B17-917[»]
    5HFUX-ray2.92A/B17-917[»]
    5HG1X-ray2.76A17-916[»]
    SMRiP52789
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGridi109346, 57 interactors
    DIPiDIP-50110N
    IntActiP52789, 32 interactors
    MINTiP52789
    STRINGi9606.ENSP00000290573

    Chemistry databases

    BindingDBiP52789
    ChEMBLiCHEMBL2640

    PTM databases

    iPTMnetiP52789
    PhosphoSitePlusiP52789
    SwissPalmiP52789

    Polymorphism and mutation databases

    BioMutaiHK2
    DMDMi56405344

    Proteomic databases

    EPDiP52789
    jPOSTiP52789
    MassIVEiP52789
    MaxQBiP52789
    PaxDbiP52789
    PeptideAtlasiP52789
    PRIDEiP52789
    ProteomicsDBi56533

    Protocols and materials databases

    The DNASU plasmid repository

    More...    DNASUi    		3099

    Genome annotation databases

    EnsembliENST00000290573; ENSP00000290573; ENSG00000159399
    GeneIDi3099
    KEGGihsa:3099
    UCSCiuc002snd.4 human

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...    CTDi    		3099
    DisGeNETi3099

    GeneCards: human genes, protein and diseases

    More...    GeneCardsi    		HK2
    HGNCiHGNC:4923 HK2
    HPAiHPA028587
    MIMi601125 gene
    neXtProtiNX_P52789
    OpenTargetsiENSG00000159399
    PharmGKBiPA29301

    GenAtlas: human gene database

    More...    GenAtlasi    		Search...

    Phylogenomic databases

    eggNOGiKOG1369 Eukaryota
    COG5026 LUCA
    GeneTreeiENSGT00950000182787
    HOGENOMiHOG000162671
    InParanoidiP52789
    KOiK00844
    OMAiRHIDTVE
    OrthoDBi1153545at2759
    PhylomeDBiP52789
    TreeFamiTF314238

    Enzyme and pathway databases

    UniPathwayiUPA00109;UER00180
    UPA00242
    BioCyciMetaCyc:HS08399-MONOMER
    BRENDAi2.7.1.1 2681
    ReactomeiR-HSA-70171 Glycolysis
    SABIO-RKiP52789
    SIGNORiP52789

    Miscellaneous databases

    ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

    More...    ChiTaRSi    		HK2 human
    EvolutionaryTraceiP52789

    The Gene Wiki collection of pages on human genes and proteins

    More...    GeneWikii    		HK2

    Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

    More...    GenomeRNAii    		3099
    PharosiP52789

    Protein Ontology

    More...    PROi    		PR:P52789

    The Stanford Online Universal Resource for Clones and ESTs

    More...    SOURCEi    		Search...

    Gene expression databases

    BgeeiENSG00000159399 Expressed in 218 organ(s), highest expression level in colon
    ExpressionAtlasiP52789 baseline and differential
    GenevisibleiP52789 HS

    Family and domain databases

    InterProiView protein in InterPro
    IPR001312 Hexokinase
    IPR019807 Hexokinase_BS
    IPR022673 Hexokinase_C
    IPR022672 Hexokinase_N
    PANTHERiPTHR19443 PTHR19443, 2 hits
    PfamiView protein in Pfam
    PF00349 Hexokinase_1, 2 hits
    PF03727 Hexokinase_2, 2 hits
    PROSITEiView protein in PROSITE
    PS00378 HEXOKINASE_1, 2 hits
    PS51748 HEXOKINASE_2, 2 hits

    ProtoNet; Automatic hierarchical classification of proteins

    More...    ProtoNeti    		Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...    MobiDBi    		Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiHXK2_HUMAN
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P52789
    Secondary accession number(s): D6W5J2, Q8WU87, Q9UN82
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: December 7, 2004
    Last modified: October 16, 2019
    This is version 196 of the entry and version 2 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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