<p>An evidence describes the source of an annotation, e.g. an experiment that has been published in the scientific literature, an orthologous protein, a record from another database, etc.</p>
<p><a href="/manual/evidences">More…</a></p>
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome.<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>
Select a section on the left to see content.
<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
Essential for rapid growth and for sporulation. Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 2-509 IN COMPLEX WITH MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVE SITE.
<p>This subsection of the ‘Function’ section 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><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 2-509 IN COMPLEX WITH MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVE SITE.
<p>This subsection of the ‘Function’ section 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><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 2-509 IN COMPLEX WITH MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVE SITE.
Note: Binds 2 manganese ions per subunit.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 2-509 IN COMPLEX WITH MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVE SITE.
<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: glycolysis
This protein is involved in step 3 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.UniRule annotation
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p>
<p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 2-509 IN COMPLEX WITH MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVE SITE.
1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 2-509 IN COMPLEX WITH MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVE SITE.
1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 2-509 IN COMPLEX WITH MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVE SITE.
1
<p>This subsection of the ‘Function’ 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 sitei
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p>
<p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi
<p>This subsection of the ‘Function’ 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 sitei
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p>
<p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi
<p>This subsection of the ‘Function’ 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 sitei
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p>
<p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi
<p>This subsection of the ‘Function’ 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 sitei
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p>
<p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 2-509 IN COMPLEX WITH MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVE SITE.
1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 2-509 IN COMPLEX WITH MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVE SITE.
1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 2-509 IN COMPLEX WITH MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVE SITE.
1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 2-509 IN COMPLEX WITH MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVE SITE.
1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 2-509 IN COMPLEX WITH MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVE SITE.
1
<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
2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity Source: UniProtKB
<p>Inferred from Direct Assay</p>
<p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
manganese ion binding Source: UniProtKB
<p>Inferred from Direct Assay</p>
<p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
glycolytic process Source: TIGR
<p>Inferred from Sequence or Structural Similarity<br />Used for any analysis based on sequence alignment, structure comparison, or evaluation of sequence features such as composition.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iss">GO evidence code guide</a></p> Inferred from sequence or structural similarityi
regulation of sporulation Source: UniProtKB
<p>Inferred from Direct Assay</p>
<p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<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
<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 ‘Names and Taxonomy’ 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
<p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p>
<p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 2-509 IN COMPLEX WITH MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVE SITE.
)
Short name:
BPG-independent PGAM1 Publication
<p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p>
<p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini
Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 2-509 IN COMPLEX WITH MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVE SITE.
Short name:
Phosphoglyceromutase1 Publication
<p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p>
<p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini
Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 2-509 IN COMPLEX WITH MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVE SITE.
Short name:
iPGM1 Publication
<p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p>
<p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini
Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 2-509 IN COMPLEX WITH MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVE SITE.
<p>This subsection of the ‘Names and taxonomy’ 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:gpmIUniRule annotation
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p>
<p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi
<p>This subsection of the ‘Names and taxonomy’ 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>Organismi
<p>This subsection of the ‘Names and taxonomy’ section shows the unique identifier assigned by the <span class="caps">NCBI</span> 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 identifieri
<p>This subsection of the ‘Names and taxonomy’ 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 lineagei
<p>This subsection of the “Names and Taxonomy” 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
UP000000594
<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. <br></br>These range from a single component such as Viral genomes to several components as in the case of eukaryotic chromosomes. They may also represent different stages in a genome project and include components such as contigs, scaffolds or Whole Genome Shotgun (WGS) master records.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
<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
<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 - Cellular componenti
<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_0000212119
<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 residuei
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p>
<p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi
<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>Keywords - PTMi
<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.UniRule annotation
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p>
<p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi
<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
Legend: HelixTurnBeta strandPDB Structure known for this area
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the <span class="caps">DSSP</span> secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the <span class="caps">DSSP</span> secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the <span class="caps">DSSP</span> secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the <span class="caps">DSSP</span> secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the <span class="caps">DSSP</span> secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<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
Region
Feature key
Position(s)
DescriptionActions
Graphical view
Length
<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>Regioni
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p>
<p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi
<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>Regioni
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p>
<p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi
<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
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p>
<p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi
<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 length and molecular weight.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the ‘Sequence’ 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.
<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:i37C82D810978B430
<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 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 namei
GPMI_BACAN
<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>Accessioni
<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 historyi
Integrated into UniProtKB/Swiss-Prot:
November 14, 2003
Last sequence update:
June 1, 2003
Last modified:
August 30, 2017
This is version 114 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 statusi
<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
<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>Keywords - Technical termi
