Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 75 (07 Oct 2020)
Sequence version 1 (21 Dec 2004)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Hexokinase-1

Gene

HK1

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
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 transcript 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 various hexoses, such as D-glucose, D-glucosamine, D-fructose, D-mannose and 2-deoxy-D-glucose, to hexose 6-phosphate (D-glucose 6-phosphate, D-glucosamine 6-phosphate, D-fructose 6-phosphate, D-mannose 6-phosphate and 2-deoxy-D-glucose 6-phosphate, respectively). Does not phosphorylate N-acetyl-D-glucosamine (By similarity). Mediates the initial step of glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6-phosphate (By similarity). Involved in innate immunity and inflammation by acting as a pattern recognition receptor for bacterial peptidoglycan. When released in the cytosol, N-acetyl-D-glucosamine component of bacterial peptidoglycan inhibits the hexokinase activity of HK1 and causes its dissociation from mitochondrial outer membrane, thereby activating the NLRP3 inflammasome (By similarity).By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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%5Fsection">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 is an allosteric enzyme inhibited by its product D-glucose 6-phosphate. Hexokinase activity is inhibited by N-acetyl-D-glucosamine.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'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.By similarity
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.By similarity
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Hexokinase (HK1), Hexokinase (HKDC1), Hexokinase (CR201_G0049621), Phosphotransferase (GCK), Hexokinase (CR201_G0049621), Hexokinase-1 (HK1), Hexokinase (CR201_G0043659), Hexokinase (CR201_G0049621), Hexokinase (CR201_G0049621), Hexokinase (HK3), Phosphotransferase (CR201_G0049621), Hexokinase (CR201_G0051597), Phosphotransferase (CR201_G0040656), Hexokinase (CR201_G0051597), Hexokinase (CR201_G0049619), Phosphotransferase (CR201_G0040656), Hexokinase (HK2), Phosphotransferase (CR201_G0040656), Phosphotransferase (CR201_G0040656), Hexokinase (CR201_G0043659)
  2. Glucose-6-phosphate isomerase (CR201_G0049051), Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase (CR201_G0049051), Glucose-6-phosphate isomerase (CR201_G0049051), Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase (CR201_G0049051)
  3. PFKM isoform 8 (CR201_G0011728), ATP-dependent 6-phosphofructokinase (CR201_G0011728), PFKM isoform 1 (CR201_G0011728), ATP-dependent 6-phosphofructokinase, liver type (PFKL), PFKM isoform 3 (CR201_G0011728), PFKM isoform 2 (CR201_G0011728), ATP-dependent 6-phosphofructokinase, platelet type (PFKP), PFKM isoform 26 (CR201_G0011728), PFKP isoform 12 (CR201_G0046679), PFKP isoform 8 (CR201_G0046679), PFKP isoform 11 (CR201_G0046679), PFKP isoform 6 (CR201_G0046679), Uncharacterized protein, Uncharacterized protein, ATP-dependent 6-phosphofructokinase, muscle type (PFKM), 6-phosphofructokinase (CR201_G0048952), ATP-dependent 6-phosphofructokinase (CR201_G0048952), ATP-dependent 6-phosphofructokinase (CR201_G0011728), PFKM isoform 32 (CR201_G0011728), Phosphofructokinase, platelet, ATP-dependent 6-phosphofructokinase (DKFZp468O105), PFKM isoform 11 (CR201_G0011728), PFKM isoform 14 (CR201_G0011728), PFKM isoform 4 (CR201_G0011728), PFKM isoform 5 (CR201_G0011728), ATP-dependent 6-phosphofructokinase, liver type (PFKL), PFKP isoform 7 (CR201_G0046679), PFKL isoform 4 (CR201_G0048952), ATP-dependent 6-phosphofructokinase (CR201_G0046679), PFKP isoform 10 (CR201_G0046679), PFKP isoform 1 (CR201_G0046679), PFKM isoform 10 (CR201_G0011728), ATP-dependent 6-phosphofructokinase (CR201_G0011728), PFKM isoform 19 (CR201_G0011728), PFKM isoform 25 (CR201_G0011728), PFKM isoform 20 (CR201_G0011728)
  4. Fructose-bisphosphate aldolase (CR201_G0034412), Fructose-bisphosphate aldolase (CR201_G0034412), Fructose-bisphosphate aldolase (CR201_G0034412), Fructose-bisphosphate aldolase (ALDOB), Fructose-bisphosphate aldolase B (ALDOB), Fructose-bisphosphate aldolase (CR201_G0034412), Fructose-bisphosphate aldolase (CR201_G0034412), Fructose-bisphosphate aldolase A (ALDOA), Fructose-bisphosphate aldolase (CR201_G0034412), Fructose-bisphosphate aldolase (CR201_G0034412), Fructose-bisphosphate aldolase (CR201_G0034412), Fructose-bisphosphate aldolase (CR201_G0033506), Fructose-bisphosphate aldolase (ALDOC), Fructose-bisphosphate aldolase (CR201_G0033506), Fructose-bisphosphate aldolase (CR201_G0033506), Fructose-bisphosphate aldolase (ALDOA), Fructose-bisphosphate aldolase (CR201_G0033506), Fructose-bisphosphate aldolase (CR201_G0033506), Fructose-bisphosphate aldolase (CR201_G0033506), Fructose-bisphosphate aldolase (CR201_G0008177), Fructose-bisphosphate aldolase (CR201_G0008177), Fructose-bisphosphate aldolase (CR201_G0033506), Fructose-bisphosphate aldolase (CR201_G0034412)
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%5Fsection">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 sitei155Substrate 1By similarity1
Binding sitei209Glucose-6-phosphate 1By similarity1
Binding sitei232Glucose-6-phosphate 1By similarity1
Binding sitei235Substrate 1By similarity1
Binding sitei260Substrate 1By similarity1
Binding sitei345ATP 1By similarity1
Binding sitei449Glucose-6-phosphate 1By similarity1
Binding sitei657Glucose-6-phosphate 2By similarity1
Binding sitei680ATP 2By similarity1
Binding sitei680Glucose-6-phosphate 2By similarity1
Binding sitei708Substrate 2By similarity1
Binding sitei742Substrate 2By similarity1
Binding sitei897Glucose-6-phosphate 2By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

GO - Biological processi

<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, Immunity, Inflammatory response, Innate immunity
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

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%5Fand%5Ftaxonomy%5Fsection">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-1Curated (EC:2.7.1.1By similarity)
Alternative name(s):
Hexokinase type IBy similarity
Short name:
HK IBy similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:HK1By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri9601 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000001595 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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: Unplaced

<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 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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002860471 – 917Hexokinase-1Add 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-acetylmethionineBy similarity1
Modified residuei337PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer (By similarity).

Interacts with RABL2/RABL2A; binds preferentially to GTP-bound RABL2 (By similarity).

Interacts with VDAC1. The HK1-VDAC1 complex interacts with ATF2 (By similarity).

Interacts (via N-terminal spermatogenic cell-specific region) with PFKM (via C-terminus) (By similarity).

By similarity

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
9601.ENSPPYP00000002765

<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

3D structure databases

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

More...
SMRi
Q5RC71

Database of comparative protein structure models

More...
ModBasei
Search...

<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%5Fand%5Fdomains%5Fsection">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 – 10Mitochondrial-binding peptide (MBP)By similarity10
Regioni73 – 207Hexokinase small subdomain 1PROSITE-ProRule annotationAdd BLAST135
Regioni84 – 91Glucose-6-phosphate 1 bindingBy similarity8
Regioni172 – 173Substrate 1 bindingBy similarity2
Regioni208 – 447Hexokinase large subdomain 1PROSITE-ProRule annotationAdd BLAST240
Regioni208 – 209Substrate 1 bindingBy similarity2
Regioni291 – 294Substrate 1 bindingBy similarity4
Regioni413 – 415Glucose-6-phosphate 1 bindingBy similarity3
Regioni521 – 655Hexokinase small subdomain 2PROSITE-ProRule annotationAdd BLAST135
Regioni532 – 536Glucose-6-phosphate 2 bindingBy similarity5
Regioni603 – 604Substrate 2 bindingBy similarity2
Regioni620 – 621Substrate 2 bindingBy similarity2
Regioni656 – 895Hexokinase large subdomain 2PROSITE-ProRule annotationAdd BLAST240
Regioni656 – 657Substrate 2 bindingBy similarity2
Regioni682 – 683Substrate 2 bindingBy similarity2
Regioni861 – 863Glucose-6-phosphate 2 bindingBy similarity3

<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 this hexokinase contain a hexokinase domain. The catalytic activity is associated with the C-terminus while regulatory function is associated with the N-terminus. Each domain can bind a single D-glucose and D-glucose 6-phosphate molecule.By similarity

<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

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q5RC71

KEGG Orthology (KO)

More...
KOi
K00844

Database of Orthologous Groups

More...
OrthoDBi
1153545at2759

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR043129, ATPase_NBD
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

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53067, SSF53067, 4 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%5Flength">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>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

Q5RC71-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MIAAQLLAYY FTELKDDQVK KIDKYLYAMR LSDETLIDIM TRFRKEMKNG
60 70 80 90 100
LSRDFNPTAT VKMLPTFVRS IPDGSEKGDF IALDLGGSSF RILRVQVNHE
110 120 130 140 150
KNQNVHMESE VYDTPENIVH GSGSQLFDHV AECLGDFMEK RKIKDKKSPV
160 170 180 190 200
GFTFSFPCQQ SKIDEAVLIT WTKRFKASGV EGADVVKLLN KAIKKRGDYD
210 220 230 240 250
ANIVAVVNDT VGTMMTCGYD DQHCEVGLII GTGTNACYME ELRHIDLVEG
260 270 280 290 300
DEGRMCINTE WGAFGDDGSL EDIRTEFDRE IDRGSLNPGK QLFEKMVSGM
310 320 330 340 350
YLGELVRLIL VKMAKEGLLF EGRITPELLT RGKFNTSDVS AIEKNKEGLH
360 370 380 390 400
NAKEILTRLG VEPSDDDCVS VQHVCTIVSF RSANLVAATL GAILNRLRDN
410 420 430 440 450
KGTPRLRTTV GVDGSLYKTH PQYSRRFHKT LRRLVPDSDV RFLLSESGSG
460 470 480 490 500
KGAAMVTAVA YRLAEQHRQI EETLAHFHLT KDMLLEVKKR MRAEMELGLR
510 520 530 540 550
KQTHNNAAVK MLPSFVRRTP DGTENGDFLA LDLGGTNFRV LLVKIRSGKK
560 570 580 590 600
RTVEMHNKIY AIPIEIMQGT GEELFDHIVS CISDFLDYMG IKGPRMPLGF
610 620 630 640 650
TFSFPCKQTS LDAGILITWT KGFKATDCVG NDVATLLRDA IKRREEFDLD
660 670 680 690 700
VVAVVNDTVG TMMTCAYEEP TCEVGLIVGT GSNACYMEEM KNVEMVEGDQ
710 720 730 740 750
GQMCINMEWG AFGDNGCLDD IRTHYDRLVD EYSLNAGKQR YEKMISGMYL
760 770 780 790 800
GEIVRNILID FTKKGFLFRG QISEPLKTRG IFETKFLSQI ESDRLALLQV
810 820 830 840 850
RAILQQLGLN STCDDSILVK TVCGVVSRRA AQLCGAGMAA VVDKIRENRG
860 870 880 890 900
LDRLNVTVGV DGTLYKLHPH FSRIMHQTVK ELSPKCNVSF LLSEDGSGKG
910
AALITAVGVR LRTEASS
Length:917
Mass (Da):102,363
Last modified:December 21, 2004 - v1
<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:iBCB4765425999C79
GO

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
CR858409 mRNA Translation: CAH90636.1

NCBI Reference Sequences

More...
RefSeqi
NP_001125344.1, NM_001131872.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
100172246

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
pon:100172246

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR858409 mRNA Translation: CAH90636.1
RefSeqiNP_001125344.1, NM_001131872.1

3D structure databases

SMRiQ5RC71
ModBaseiSearch...

Protein-protein interaction databases

STRINGi9601.ENSPPYP00000002765

Genome annotation databases

GeneIDi100172246
KEGGipon:100172246

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
3098

Phylogenomic databases

eggNOGiKOG1369, Eukaryota
InParanoidiQ5RC71
KOiK00844
OrthoDBi1153545at2759

Enzyme and pathway databases

UniPathwayiUPA00109;UER00180
UPA00242

Family and domain databases

InterProiView protein in InterPro
IPR043129, ATPase_NBD
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
SUPFAMiSSF53067, SSF53067, 4 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 nameiHXK1_PONAB
<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: Q5RC71
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: December 21, 2004
Last modified: October 7, 2020
This is version 75 of the entry and version 1 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

<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

Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again