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 122 (18 Sep 2019)
Sequence version 1 (05 Jul 2004)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Glucose-6-phosphate isomerase

Gene

Gpi

Organism
Rattus norvegicus (Rat)
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 (PubMed:2709006). 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 similarity1 Publication

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

  1. KM=0.593 mM for glucose-6-phosphate1 Publication
  2. KM=0.095 mM for fructose-6-phosphate1 Publication
  1. Vmax=2.291 nmol/min/mg enzyme with glucose-6-phosphate as substrate1 Publication
  2. Vmax=98 nmol/min/mg enzyme with fructose-6-phosphate as substrate1 Publication

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

This protein is involved in step 2 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.1 Publication
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Hexokinase-3 (Hk3), Mutant type II hexokinase, Hexokinase-4 (Gck), Hexokinase-2 (Hk2), Hexokinase-3 (Hk3), Phosphotransferase (Gck), Hexokinase-1 (Hk1), Hexokinase 3, isoform CRA_a (Hk3), Phosphotransferase (Gck), Hexokinase-1 (Hk1), Uncharacterized protein
  2. Glucose-6-phosphate isomerase (Gpi)
  3. ATP-dependent 6-phosphofructokinase (Pfkm), ATP-dependent 6-phosphofructokinase (Pfkp), ATP-dependent 6-phosphofructokinase (Pfkl), ATP-dependent 6-phosphofructokinase, muscle type (Pfkm), ATP-dependent 6-phosphofructokinase, liver type (Pfkl), ATP-dependent 6-phosphofructokinase, platelet type (Pfkp), ATP-dependent 6-phosphofructokinase (Pfkm), ATP-dependent 6-phosphofructokinase (Pfkp)
  4. Fructose-bisphosphate aldolase A (Aldoa), Fructose-bisphosphate aldolase B (Aldob), Fructose-bisphosphate aldolase (Aldoc), Fructose-bisphosphate aldolase C (Aldoc), Fructose-bisphosphate aldolase (Aldoart2), Fructose-bisphosphate aldolase (Aldob)
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-phosphateBy similarity1
<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 donorBy similarity1
Binding sitei358Glucose-6-phosphateBy similarity1
Active sitei389By similarity1
Binding sitei389Glucose-6-phosphateBy similarity1
Active sitei519By similarity1
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

  • cytokine activity Source: UniProtKB-KW
  • glucose-6-phosphate isomerase activity Source: RGD
  • growth factor activity Source: UniProtKB-KW
  • intramolecular transferase activity Source: RGD
  • monosaccharide binding Source: RGD

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 functionCytokine, Growth factor, Isomerase
Biological processGluconeogenesis, Glycolysis

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-6798695 Neutrophil degranulation
R-RNO-70171 Glycolysis

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q6P6V0

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:5.3.1.91 Publication)
Short name:
GPIBy similarity
Alternative name(s):
Autocrine motility factorBy similarity
Short name:
AMFBy similarity
NeuroleukinBy similarity
Short name:
NLKBy similarity
Phosphoglucose isomeraseBy similarity
Short name:
PGIBy similarity
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:GpiImported
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Rat genome database

More...
RGDi
2727 Gpi

<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 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_00003491232 – 558Glucose-6-phosphate isomeraseBy similarityAdd 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 residuei86PhosphoserineCombined sources1
Modified residuei107PhosphoserineBy similarity1
Modified residuei142N6-acetyllysineBy similarity1
Modified residuei185Phosphoserine; by CK2By similarity1
Modified residuei250PhosphothreonineCombined sources1
Modified residuei454N6-acetyllysine; alternateBy similarity1
Modified residuei454N6-malonyllysine; alternateBy similarity1
Modified residuei454N6-succinyllysine; alternateBy similarity1
Modified residuei455PhosphoserineCombined sources1

<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, Phosphoprotein, Ubl conjugation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q6P6V0

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

More...
PaxDbi
Q6P6V0

PRoteomics IDEntifications database

More...
PRIDEi
Q6P6V0

2D gel databases

The World-2DPAGE database

More...
World-2DPAGEi
0004:Q6P6V0

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q6P6V0

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

More...
PhosphoSitePlusi
Q6P6V0

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q6P6V0

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000023150 Expressed in 10 organ(s), highest expression level in skeletal muscle tissue

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q6P6V0 RN

<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.

By similarity

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
253982, 1 interactor

Protein interaction database and analysis system

More...
IntActi
Q6P6V0, 2 interactors

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000029515

<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
Q6P6V0

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

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 bindingBy similarity2
Regioni210 – 215Glucose-6-phosphate bindingBy similarity6

<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

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000000707

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000261370

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q6P6V0

KEGG Orthology (KO)

More...
KOi
K01810

Identification of Orthologs from Complete Genome Data

More...
OMAi
TNSQHAF

Database of Orthologous Groups

More...
OrthoDBi
446616at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q6P6V0

TreeFam database of animal gene trees

More...
TreeFami
TF300436

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.

Q6P6V0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAALTRNPEF QKLLEWHRAN SANLKLRELF EADPERFNHF SLNLNTNHGH
60 70 80 90 100
ILLDYSKNLV NKEVLHMLVD LAKSRGVEAA RDNMFSGLKI NSTEDRAVLH
110 120 130 140 150
VALRNRSNRS IMMDGKDVMP EVNKVLDKMK SFCQRVRSGD WKGYTGKAIT
160 170 180 190 200
DIINIGIGGS DLGPLMVTEA LKPYSKGGPR VWFVSNIDGT HIAKTLANLN
210 220 230 240 250
PESSLFIIAS KTFTTQETIT NAETAKEWFL QAAKDPSAVA KHFVALSTNT
260 270 280 290 300
DKVKEFGIDP KNMFEFWDWV GGRYSLWSAI GLSIALHVGF DHFEQLLSGA
310 320 330 340 350
HWMDQHFMKT PLDKNAPVLL ALLGIWYINF YGCETHAMLP YDQYMHRFAA
360 370 380 390 400
YFQQGDMESN GKYITKSGAR VDYQTGPIVW GEPGTNGQHA FYQLIHQGTK
410 420 430 440 450
MIPCDFLIPV QTQHPIRNGL HHKILLANFL AQTEALMKGK SPEEARKELQ
460 470 480 490 500
AAGKSPEELE KLLPHKVFEG NRPTNSIVFT KLTPFILGAL IAMYEHKIFV
510 520 530 540 550
QGIIWDINSF DQWGVELGKQ LAKKIEPELD GSSAVTSHDS STNGLIGFIK

LQRDTKID
Length:558
Mass (Da):62,827
Last modified:July 5, 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:i2550ACB874E0302C
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
BC062005 mRNA Translation: AAH62005.1

NCBI Reference Sequences

More...
RefSeqi
NP_997475.1, NM_207592.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000032613; ENSRNOP00000029515; ENSRNOG00000023150

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
292804

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:292804

UCSC genome browser

More...
UCSCi
RGD:2727 rat

<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
BC062005 mRNA Translation: AAH62005.1
RefSeqiNP_997475.1, NM_207592.1

3D structure databases

SMRiQ6P6V0
ModBaseiSearch...

Protein-protein interaction databases

BioGridi253982, 1 interactor
IntActiQ6P6V0, 2 interactors
STRINGi10116.ENSRNOP00000029515

PTM databases

iPTMnetiQ6P6V0
PhosphoSitePlusiQ6P6V0
SwissPalmiQ6P6V0

2D gel databases

World-2DPAGEi0004:Q6P6V0

Proteomic databases

jPOSTiQ6P6V0
PaxDbiQ6P6V0
PRIDEiQ6P6V0

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000032613; ENSRNOP00000029515; ENSRNOG00000023150
GeneIDi292804
KEGGirno:292804
UCSCiRGD:2727 rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
2821
RGDi2727 Gpi

Phylogenomic databases

eggNOGiKOG2446 Eukaryota
COG0166 LUCA
GeneTreeiENSGT00390000000707
HOGENOMiHOG000261370
InParanoidiQ6P6V0
KOiK01810
OMAiTNSQHAF
OrthoDBi446616at2759
PhylomeDBiQ6P6V0
TreeFamiTF300436

Enzyme and pathway databases

UniPathwayiUPA00109;UER00181
ReactomeiR-RNO-6798695 Neutrophil degranulation
R-RNO-70171 Glycolysis
SABIO-RKiQ6P6V0

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q6P6V0

Gene expression databases

BgeeiENSRNOG00000023150 Expressed in 10 organ(s), highest expression level in skeletal muscle tissue
GenevisibleiQ6P6V0 RN

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_RAT
<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: Q6P6V0
<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: September 2, 2008
Last sequence update: July 5, 2004
Last modified: September 18, 2019
This is version 122 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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