Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - Q9N1E2 (G6PI_RABIT)

Entry version 119 (11 Dec 2019)
Sequence version 3 (23 Jan 2007)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Glucose-6-phosphate isomerase

Gene

GPI

Organism
Oryctolagus cuniculus (Rabbit)
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

In the cytoplasm, catalyzes the conversion of glucose-6-phosphate to fructose-6-phosphate, the second step in glycolysis, and the reverse reaction during gluconeogenesis (By similarity). Besides it's role as a glycolytic enzyme, also acts as a secreted cytokine: acts as an angiogenic factor (AMF) that stimulates endothelial cell motility. Acts as a neurotrophic factor, neuroleukin, for spinal and sensory neurons. It is secreted by lectin-stimulated T-cells and induces immunoglobulin secretion (By similarity).By similarity

<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 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 2 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 1 (HK1), Phosphotransferase (GCK), Hexokinase domain containing 1 (HKDC1), Hexokinase 3 (HK3), Hexokinase 2 (HK2), Phosphotransferase
  2. 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 (PFKP), ATP-dependent 6-phosphofructokinase (PFKM), ATP-dependent 6-phosphofructokinase (PFKP)
  4. Fructose-bisphosphate aldolase (ALDOC), Fructose-bisphosphate aldolase B (ALDOB), Fructose-bisphosphate aldolase A (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 sitei354Glucose-6-phosphateCombined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei358Proton donor2 Publications1
Binding sitei358Glucose-6-phosphateCombined sources1 Publication1
Active sitei3892 Publications1
Binding sitei389Glucose-6-phosphateCombined sources1 Publication1
Active sitei5192 Publications1
Binding sitei519Glucose-6-phosphateBy similarity1

<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 functionCytokine, Isomerase
Biological processGluconeogenesis, Glycolysis

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		5.3.1.9 1749

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		Q9N1E2

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

More...UniPathwayi		UPA00109;UER00181

<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:
Glucose-6-phosphate isomeraseBy similarity (EC:5.3.1.9By similarity)
Short name:
GPIBy similarity
Alternative name(s):
Autocrine motility factor1 Publication
Short name:
AMF1 Publication
Neuroleukin1 Publication
Short name:
NLK1 Publication
Phosphoglucose isomerase1 Publication
Short name:
PGI1 Publication
Phosphohexose isomeraseBy similarity
Short name:
PHIBy similarity
<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:GPIBy similarity
<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>OrganismiOryctolagus cuniculus (Rabbit)
<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 identifieri9986 [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 › Glires › Lagomorpha › Leporidae › Oryctolagus
<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
  • UP000001811 <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: 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, Secreted

<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

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL1770045

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
<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_00001805412 – 558Glucose-6-phosphate isomeraseAdd BLAST557

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 residuei2N-acetylalanineBy similarity1
Modified residuei12N6-acetyllysineBy similarity1
Modified residuei34N6-(2-hydroxyisobutyryl)lysineBy similarity1
Modified residuei107PhosphoserineBy similarity1
Modified residuei109PhosphothreonineBy similarity1
Modified residuei142N6-acetyllysineBy similarity1
Modified residuei185Phosphoserine; by CK2By similarity1
Modified residuei250PhosphothreonineBy similarity1
Modified residuei454N6-acetyllysine; alternateBy similarity1
Modified residuei454N6-malonyllysine; alternateBy similarity1
Modified residuei454N6-succinyllysine; alternateBy similarity1
Modified residuei455PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylation at Ser-185 by CK2 has been shown to decrease enzymatic activity and may contribute to secretion by a non-classical secretory pathway.By similarity
ISGylated.By similarity

Keywords - PTMi

Acetylation, Hydroxylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PRoteomics IDEntifications database

More...PRIDEi		Q9N1E2

<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

Homodimer in the catalytically active form, monomer in the secreted form.

5 Publications

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		9986.ENSOCUP00000001250

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q9N1E2

<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

1558
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		Q9N1E2

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		Q9N1E2

<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 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>Regioni159 – 160Glucose-6-phosphate bindingCombined sources1 Publication2
Regioni210 – 215Glucose-6-phosphate bindingCombined sources1 Publication6

<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 GPI family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG2446 Eukaryota
COG0166 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000261370

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9N1E2

KEGG Orthology (KO)

More...KOi		K01810

Database of Orthologous Groups

More...OrthoDBi		446616at2759

Family and domain databases

Conserved Domains Database

More...CDDi		cd05015 SIS_PGI_1, 1 hit
cd05016 SIS_PGI_2, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.1390.10, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_00473 G6P_isomerase, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001672 G6P_Isomerase
IPR023096 G6P_Isomerase_C
IPR018189 Phosphoglucose_isomerase_CS
IPR035476 SIS_PGI_1
IPR035482 SIS_PGI_2

The PANTHER Classification System

More...PANTHERi		PTHR11469 PTHR11469, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00342 PGI, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00662 G6PISOMERASE

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00765 P_GLUCOSE_ISOMERASE_1, 1 hit
PS00174 P_GLUCOSE_ISOMERASE_2, 1 hit
PS51463 P_GLUCOSE_ISOMERASE_3, 1 hit

<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>Sequencei

<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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q9N1E2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAALTRNPQF QKLQQWHREH GSELNLRHLF DTDKERFNHF SLTLNTNHGH 
        60         70         80         90        100
ILLDYSKNLV TEEVMHMLLD LAKSRGVEAA RESMFNGEKI NSTEDRAVLH 
       110        120        130        140        150
VALRNRSNTP IVVDGKDVMP EVNKVLDKMK AFCQRVRSGD WKGYTGKTIT 
       160        170        180        190        200
DVINIGIGGS DLGPLMVTEA LKPYSSGGPR VWFVSNIDGT HIAKTLACLN 
       210        220        230        240        250
PESSLFIIAS KTFTTQETIT NAETAKDWFL LSAKDPSTVA KHFVALSTNT 
       260        270        280        290        300
AKVKEFGIDP QNMFEFWDWV GGRYSLWSAI GLSIALHVGF DNFEQLLSGA 
       310        320        330        340        350
HWMDQHFRTT PLEKNAPVLL AMLGIWYINC FGCETQAVLP YDQYLHRFAA 
       360        370        380        390        400
YFQQGDMESN GKYITKSGAR VDHQTGPIVW GEPGTNGQHA FYQLIHQGTK 
       410        420        430        440        450
MIPCDFLIPV QTQHPIRKGL HHKILLANFL AQTEALMKGK STEEARKELQ 
       460        470        480        490        500
AAGKSPEDLM KLLPHKVFEG NRPTNSIVFT KLTPFILGAL IAMYEHKIFV 
       510        520        530        540        550
QGVVWDINSF DQWGVELGKQ LAKKIEPELD GSSPVTSHDS STNGLINFIK 

QQREAKIQ
Length:558
Mass (Da):62,747
Last modified:January 23, 2007 - v3
<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:iBB4E3AB31BBD55E4
GO

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 conflicti223E → K in AAF35988 (PubMed:10653639).Curated1

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
AF199601 mRNA Translation: AAF13713.2
AF222069 mRNA Translation: AAF35988.1

NCBI Reference Sequences

More...RefSeqi		NP_001075538.1, NM_001082069.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		100008744

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ocu:100008744

<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
AF199601 mRNA Translation: AAF13713.2
AF222069 mRNA Translation: AAF35988.1
RefSeqiNP_001075538.1, NM_001082069.2

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
1DQRX-ray2.50A/B2-558[»]
1G98X-ray1.90A/B1-558[»]
1HM5X-ray1.80A/B1-558[»]
1HOXX-ray2.10A/B1-558[»]
1KOJX-ray1.90A/B2-558[»]
1N8TX-ray2.50A/B2-558[»]
1XTBX-ray2.00A/B1-558[»]
SMRiQ9N1E2
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000001250

Chemistry databases

BindingDBiQ9N1E2
ChEMBLiCHEMBL1770045

Proteomic databases

PRIDEiQ9N1E2

Genome annotation databases

GeneIDi100008744
KEGGiocu:100008744

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		2821

Phylogenomic databases

eggNOGiKOG2446 Eukaryota
COG0166 LUCA
HOGENOMiHOG000261370
InParanoidiQ9N1E2
KOiK01810
OrthoDBi446616at2759

Enzyme and pathway databases

UniPathwayiUPA00109;UER00181
BRENDAi5.3.1.9 1749
SABIO-RKiQ9N1E2

Miscellaneous databases

EvolutionaryTraceiQ9N1E2

Protein Ontology

More...PROi		PR:Q9N1E2

Family and domain databases

CDDicd05015 SIS_PGI_1, 1 hit
cd05016 SIS_PGI_2, 1 hit
Gene3Di1.10.1390.10, 1 hit
HAMAPiMF_00473 G6P_isomerase, 1 hit
InterProiView protein in InterPro
IPR001672 G6P_Isomerase
IPR023096 G6P_Isomerase_C
IPR018189 Phosphoglucose_isomerase_CS
IPR035476 SIS_PGI_1
IPR035482 SIS_PGI_2
PANTHERiPTHR11469 PTHR11469, 1 hit
PfamiView protein in Pfam
PF00342 PGI, 1 hit
PRINTSiPR00662 G6PISOMERASE
PROSITEiView protein in PROSITE
PS00765 P_GLUCOSE_ISOMERASE_1, 1 hit
PS00174 P_GLUCOSE_ISOMERASE_2, 1 hit
PS51463 P_GLUCOSE_ISOMERASE_3, 1 hit

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 nameiG6PI_RABIT
<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: Q9N1E2
Secondary accession number(s): Q9N184
<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: November 2, 2001
Last sequence update: January 23, 2007
Last modified: December 11, 2019
This is version 119 of the entry and version 3 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

3D-structure, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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