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

<p>Describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the ‘Names and taxonomy’ section.</p><p><a href='../manual/catalytic_activity' target='_top'>More...</a></p>Catalytic activityⁱ

<p>Provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.</p><p><a href='../manual/cofactor' target='_top'>More...</a></p>Cofactorⁱ

<p>Describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.</p><p><a href='../manual/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationⁱ

<p>Describes the metabolic pathway(s) associated with a protein.</p><p><a href='../manual/pathway' target='_top'>More...</a></p>Pathwayⁱ

Sites

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.</p><p><a href='../manual/binding' target='_top'>More...</a></p>Binding sitei	20 – 20	1	ATP; via amide nitrogenBy similarity
<p>Indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.</p><p><a href='../manual/metal' target='_top'>More...</a></p>Metal bindingi	112 – 112	1	Magnesium; catalyticBy similarity
<p>Is used for enzymes and indicates the residues directly involved in catalysis.</p><p><a href='../manual/act_site' target='_top'>More...</a></p>Active sitei	159 – 159	1	Proton acceptorBy similarity
<p>Describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.</p><p><a href='../manual/binding' target='_top'>More...</a></p>Binding sitei	194 – 194	1	Substrate; shared with dimeric partnerBy similarity
<p>Describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.</p><p><a href='../manual/binding' target='_top'>More...</a></p>Binding sitei	257 – 257	1	SubstrateBy similarity
<p>Describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.</p><p><a href='../manual/binding' target='_top'>More...</a></p>Binding sitei	285 – 285	1	Substrate; shared with dimeric partnerBy similarity
<p>Describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.</p><p><a href='../manual/binding' target='_top'>More...</a></p>Binding sitei	474 – 474	1	Allosteric activator fructose 2,6-bisphosphateBy similarity
<p>Describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.</p><p><a href='../manual/binding' target='_top'>More...</a></p>Binding sitei	632 – 632	1	Allosteric activator fructose 2,6-bisphosphateBy similarity
<p>Describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.</p><p><a href='../manual/binding' target='_top'>More...</a></p>Binding sitei	658 – 658	1	Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerBy similarity

Regions

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>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><p><a href='../manual/np_bind' target='_top'>More...</a></p>Nucleotide bindingi	81 – 82	2	ATPBy similarity
<p>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><p><a href='../manual/np_bind' target='_top'>More...</a></p>Nucleotide bindingi	111 – 114	4	ATPBy similarity

<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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

1. 6-phosphofructokinase activity Source: UniProtKB-EC
2. ATP binding Source: UniProtKB-KW
3. metal ion binding Source: UniProtKB-KW

<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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Biological processⁱ

1. fructose 6-phosphate metabolic process Source: InterPro
2. glycolytic process Source: UniProtKB-UniPathway

<p>UniProtKB Keywords constitute a <a target="_top" href="/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>Keywords - Molecular functionⁱ

<p>UniProtKB Keywords constitute a <a target="_top" href="/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>Keywords - Biological processⁱ

<p>UniProtKB Keywords constitute a <a target="_top" href="/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>Keywords - Ligandⁱ

Enzyme and pathway databases

<p>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><p><a href='../manual/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

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

<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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Cellular componentⁱ

1. cytoplasm Source: UniProtKB-SubCell

<p>UniProtKB Keywords constitute a <a target="_top" href="/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>Keywords - Cellular componentⁱ

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

Molecule processing

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the extent of a polypeptide chain in the mature protein following processing.</p><p><a href='../manual/chain' target='_top'>More...</a></p>Chaini	1 – 756	756	ATP-dependent 6-phosphofructokinase 2		PRO_0000112029	Add BLAST

Proteomic databases

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

<p>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 ‘Function’ section).</p><p><a href='../manual/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

Protein-protein interaction databases

<p>Provides information on the tertiary structure of a protein.</p><p><a href='../manual/structure_section' target='_top'>More...</a></p>Structureⁱ

3D structure databases

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

Region

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes a region of interest that cannot be described in other subsections.</p><p><a href='../manual/region' target='_top'>More...</a></p>Regioni	1 – 393	393	N-terminal catalytic PFK domain 1			Add BLAST
<p>Describes a region of interest that cannot be described in other subsections.</p><p><a href='../manual/region' target='_top'>More...</a></p>Regioni	157 – 159	3	Substrate bindingBy similarity
<p>Describes a region of interest that cannot be described in other subsections.</p><p><a href='../manual/region' target='_top'>More...</a></p>Regioni	201 – 203	3	Substrate bindingBy similarity
<p>Describes a region of interest that cannot be described in other subsections.</p><p><a href='../manual/region' target='_top'>More...</a></p>Regioni	291 – 294	4	Substrate bindingBy similarity
<p>Describes a region of interest that cannot be described in other subsections.</p><p><a href='../manual/region' target='_top'>More...</a></p>Regioni	394 – 404	11	Interdomain linker			Add BLAST
<p>Describes a region of interest that cannot be described in other subsections.</p><p><a href='../manual/region' target='_top'>More...</a></p>Regioni	405 – 756	352	C-terminal regulatory PFK domain 2			Add BLAST
<p>Describes a region of interest that cannot be described in other subsections.</p><p><a href='../manual/region' target='_top'>More...</a></p>Regioni	530 – 534	5	Allosteric activator fructose 2,6-bisphosphate bindingBy similarity
<p>Describes a region of interest that cannot be described in other subsections.</p><p><a href='../manual/region' target='_top'>More...</a></p>Regioni	575 – 577	3	Allosteric activator fructose 2,6-bisphosphate bindingBy similarity
<p>Describes a region of interest that cannot be described in other subsections.</p><p><a href='../manual/region' target='_top'>More...</a></p>Regioni	664 – 667	4	Allosteric activator fructose 2,6-bisphosphate bindingBy similarity

<p>Provides information about the sequence similarity with other proteins.</p><p><a href='../manual/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Phylogenomic databases

Family and domain databases

<p>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 length and molecular weight.</p><p><a href='../manual/sequences_section' target='_top'>More...</a></p>Sequenceⁱ

<p>Indicates if the canonical sequence displayed by default in the entry is complete or not.</p><p><a href='../manual/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

        10         20         30         40         50
MEQKFKKGKD HGVGVLTSGG DSQGMNAAVR SVVRETIRQG HRCYLIREGY 
        60         70         80         90        100
NGLINGNIEL AKWAHVANVT HLGGSMIGTS RCDEFRTTDG RKKAAAIMFD 
       110        120        130        140        150
KRIFHLIVIG GDGSLMGAQK LKEEWGRFGE ELFAEGKITE EVANEGRELH 
       160        170        180        190        200
LAGIVGSIDN DCIESDKSIG SDTALHRICE AIDGLVMTAQ SHQRVFVVEV 
       210        220        230        240        250
MGRHCGYLAL TAAIAVEADY VFYPEIPPDE KWPEQLCHQL GSVRKMGKRQ 
       260        270        280        290        300
NVIILGEGVT NSKGQRIDVR QVKEEIETRL QLEVRIATLG HLQRGGAPSF 
       310        320        330        340        350
LDRLIGLRMG YEAVQEVLKG KEEKEGAVVT GQKTIAKVMC LRGHNIQRNE 
       360        370        380        390        400
LSRVIRQTET ANEEIMQRHS DLACRLRGFG FLDKQTYLNF VSIPLSTTMP 
       410        420        430        440        450
SRTKTFAVVH IGSPCAGMNA ATYSFTRMAN HSGIQVIGIK HGWDGLKNKD 
       460        470        480        490        500
VKLLTWANVQ GWAQFGGSML GTKRQLPSEM DLIAEGLNSN NVDGLVIIGG 
       510        520        530        540        550
FMAFESALIL QQNRSEYTCL SIPIVVIPAT ISNNCPGTCM SLGVDTALNE 
       560        570        580        590        600
ICRQVDNISQ NAIGSKNKVM IIETMGSRSG FLATMTALST GSQFALIRQV 
       610        620        630        640        650
ETNEKDLEKL AIETKERLDS GNLEKFLLIR SEGASDEIYS PDVKKIFDKV 
       660        670        680        690        700
MKNKYGVRIT NLGYSQLGGH PSCFDRQMGI RMGVRAFEGI VNPVKMGDRD 
       710        720        730        740        750
CCVIGLRGSS LRYVPVQGLG KKVCFEHGVP HNMWWLDLHP LVEAMTKKPQ 

EAVLSS                                             

Sequence databases

Genome annotation databases

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

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>Contains the literature citations that are the sources of data used to annotate the entry. Each reference is numbered and contains several subsections allowing a precise description of a given citation.</p><p><a href='../manual/publications_section' target='_top'>More...</a></p>Publicationsⁱ

1. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
   The C. elegans sequencing consortium
   Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
   Strain: Bristol N2.
   

<p>Provides general information on the entry.</p><p><a href='../manual/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

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

<p>UniProtKB Keywords constitute a <a target="_top" href="/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>Keywords - Technical termⁱ

Documents

1. Caenorhabditis elegans
   Caenorhabditis elegans: entries, gene names and cross-references to WormBase
2. PATHWAY comments
   Index of metabolic and biosynthesis pathways
3. SIMILARITY comments
   Index of protein domains and families

External Data

<p>Provides links to the UniProt Reference Clusters (<a href="/help/uniref">UniRef</a>). UniRef consists of clusters for UniProtKB sequences (including isoforms) and selected UniParc sequences, in order to obtain complete coverage of the sequence space at resolutions of 100%, 90% and 50% identity.</p><p><a href='../manual/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ