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Protein

Glucose-6-phosphate isomerase

Gene

Gpi

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Besides it's role as a glycolytic enzyme, mammalian GPI can function as a tumor-secreted cytokine and an angiogenic factor (AMF) that stimulates endothelial cell motility. GPI is also a neurotrophic factor (Neuroleukin) for spinal and sensory neurons.

Catalytic activityi

D-glucose 6-phosphate = D-fructose 6-phosphate.

Pathwayi: glycolysis

This protein is involved in step 2 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Glucose-6-phosphate isomerase (Gpi), Glucose-6-phosphate isomerase (Gpi1), Glucose-6-phosphate isomerase (Gpi1), Glucose-6-phosphate isomerase (Gpi1)
  3. ATP-dependent 6-phosphofructokinase, liver type (Pfkl), ATP-dependent 6-phosphofructokinase (Pfkp), ATP-dependent 6-phosphofructokinase (Pfkm), ATP-dependent 6-phosphofructokinase, platelet type (Pfkp), ATP-dependent 6-phosphofructokinase, muscle type (Pfkm)
  4. Fructose-bisphosphate aldolase (Aldoart1), Fructose-bisphosphate aldolase (Aldoa), Fructose-bisphosphate aldolase (Aldoa), Fructose-bisphosphate aldolase (Aldoart2), Fructose-bisphosphate aldolase (Aldoart1), Fructose-bisphosphate aldolase (Aldoa), Fructose-bisphosphate aldolase (Aldoa), Fructose-bisphosphate aldolase (Aldob), Fructose-bisphosphate aldolase C (Aldoc), Fructose-bisphosphate aldolase A (Aldoa), Fructose-bisphosphate aldolase B (Aldob), 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
Active sitei358Proton donor1 Publication1
Active sitei3891 Publication1
Active sitei5191 Publication1

GO - Molecular functioni

GO - Biological processi

  • aldehyde catabolic process Source: Ensembl
  • angiogenesis Source: UniProtKB-KW
  • erythrocyte homeostasis Source: MGI
  • gluconeogenesis Source: UniProtKB-KW
  • glucose 6-phosphate metabolic process Source: Ensembl
  • glucose homeostasis Source: MGI
  • glycolytic process Source: MGI
  • glycolytic process through glucose-6-phosphate Source: MGI
  • in utero embryonic development Source: MGI
  • learning or memory Source: Ensembl
  • mesoderm formation Source: MGI
  • methylglyoxal biosynthetic process Source: Ensembl
  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
  • negative regulation of neuron apoptotic process Source: Ensembl
  • response to cadmium ion Source: Ensembl
  • response to estradiol Source: Ensembl
  • response to immobilization stress Source: Ensembl
  • response to morphine Source: Ensembl
  • response to muscle stretch Source: Ensembl
  • response to progesterone Source: Ensembl
  • response to testosterone Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Cytokine, Growth factor, Isomerase

Keywords - Biological processi

Angiogenesis, Gluconeogenesis, Glycolysis

Enzyme and pathway databases

BRENDAi5.3.1.9. 3474.
ReactomeiR-MMU-5628897. TP53 Regulates Metabolic Genes.
R-MMU-6798695. Neutrophil degranulation.
R-MMU-70171. Glycolysis.
R-MMU-70263. Gluconeogenesis.
SABIO-RKP06745.
UniPathwayiUPA00109; UER00181.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucose-6-phosphate isomerase (EC:5.3.1.9)
Short name:
GPI
Alternative name(s):
Autocrine motility factor
Short name:
AMF
Neuroleukin
Short name:
NLK
Phosphoglucose isomerase
Short name:
PGI
Phosphohexose isomerase
Short name:
PHI
Gene namesi
Name:Gpi
Synonyms:Gpi1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:95797. Gpi1.

Subcellular locationi

GO - Cellular componenti

  • ciliary membrane Source: MGI
  • cytoplasm Source: MGI
  • cytosol Source: Ensembl
  • extracellular exosome Source: MGI
  • extracellular space Source: UniProtKB-KW
  • membrane Source: MGI
  • myelin sheath Source: UniProtKB
  • neuron projection Source: Ensembl
  • nucleoplasm Source: MGI
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001805382 – 558Glucose-6-phosphate isomeraseAdd BLAST557

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei12N6-acetyllysineBy similarity1
Modified residuei86PhosphoserineBy similarity1
Modified residuei107PhosphoserineBy similarity1
Modified residuei109PhosphothreonineBy similarity1
Modified residuei142N6-acetyllysineCombined sources1
Modified residuei185Phosphoserine; by CK2By similarity1
Modified residuei250PhosphothreonineBy similarity1
Modified residuei454N6-acetyllysine; alternateCombined sources1
Modified residuei454N6-malonyllysine; alternateBy similarity1
Modified residuei454N6-succinyllysine; alternateCombined sources1
Modified residuei455PhosphoserineCombined sources1

Post-translational modificationi

ISGylated.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP06745.
MaxQBiP06745.
PaxDbiP06745.
PeptideAtlasiP06745.
PRIDEiP06745.

PTM databases

iPTMnetiP06745.
PhosphoSitePlusiP06745.
SwissPalmiP06745.

Expressioni

Gene expression databases

BgeeiENSMUSG00000036427.
CleanExiMM_GPI1.
ExpressionAtlasiP06745. baseline and differential.
GenevisibleiP06745. MM.

Interactioni

Subunit structurei

Homodimer in the catalytically active form, monomer in the secreted form.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Parp14Q2EMV94EBI-1534927,EBI-1534943

GO - Molecular functioni

Protein-protein interaction databases

BioGridi200021. 5 interactors.
IntActiP06745. 6 interactors.
MINTiMINT-1869738.
STRINGi10090.ENSMUSP00000049355.

Structurei

Secondary structure

1558
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 6Combined sources4
Helixi8 – 20Combined sources13
Helixi21 – 23Combined sources3
Helixi26 – 32Combined sources7
Helixi36 – 39Combined sources4
Beta strandi41 – 45Combined sources5
Beta strandi50 – 54Combined sources5
Helixi62 – 74Combined sources13
Helixi77 – 85Combined sources9
Turni92 – 95Combined sources4
Helixi100 – 103Combined sources4
Beta strandi116 – 118Combined sources3
Helixi119 – 137Combined sources19
Beta strandi151 – 155Combined sources5
Helixi158 – 160Combined sources3
Helixi162 – 170Combined sources9
Helixi172 – 175Combined sources4
Beta strandi180 – 184Combined sources5
Helixi189 – 196Combined sources8
Turni201 – 203Combined sources3
Beta strandi204 – 209Combined sources6
Beta strandi211 – 213Combined sources3
Helixi216 – 233Combined sources18
Helixi236 – 241Combined sources6
Beta strandi243 – 248Combined sources6
Helixi250 – 256Combined sources7
Helixi260 – 262Combined sources3
Beta strandi263 – 265Combined sources3
Helixi272 – 274Combined sources3
Turni276 – 278Combined sources3
Helixi279 – 281Combined sources3
Helixi282 – 288Combined sources7
Helixi290 – 309Combined sources20
Helixi312 – 314Combined sources3
Helixi316 – 329Combined sources14
Beta strandi335 – 341Combined sources7
Helixi343 – 345Combined sources3
Helixi348 – 360Combined sources13
Beta strandi378 – 380Combined sources3
Turni384 – 387Combined sources4
Helixi388 – 397Combined sources10
Beta strandi404 – 411Combined sources8
Helixi417 – 419Combined sources3
Helixi420 – 438Combined sources19
Helixi442 – 451Combined sources10
Helixi456 – 462Combined sources7
Helixi463 – 466Combined sources4
Beta strandi474 – 481Combined sources8
Helixi484 – 505Combined sources22
Helixi513 – 515Combined sources3
Helixi516 – 525Combined sources10
Helixi526 – 529Combined sources4
Beta strandi530 – 533Combined sources4
Helixi540 – 552Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1U0EX-ray1.60A/B1-558[»]
1U0FX-ray1.60A/B1-558[»]
1U0GX-ray1.70A/B1-558[»]
2CVPX-ray1.80A/B1-557[»]
2CXNX-ray1.40A/B1-557[»]
2CXOX-ray1.80A/B1-557[»]
2CXPX-ray1.70A/B1-557[»]
2CXQX-ray1.50A/B1-557[»]
2CXRX-ray1.70A/B1-557[»]
2CXSX-ray1.50A/B1-557[»]
2CXTX-ray1.50A/B1-557[»]
2CXUX-ray1.65A/B1-557[»]
ProteinModelPortaliP06745.
SMRiP06745.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06745.

Family & Domainsi

Sequence similaritiesi

Belongs to the GPI family.Curated

Phylogenomic databases

eggNOGiKOG2446. Eukaryota.
COG0166. LUCA.
GeneTreeiENSGT00390000000707.
HOVERGENiHBG002877.
InParanoidiP06745.
KOiK01810.
OMAiWLLEHSK.
OrthoDBiEOG091G03ZI.
PhylomeDBiP06745.
TreeFamiTF300436.

Family and domain databases

Gene3Di1.10.1390.10. 1 hit.
HAMAPiMF_00473. G6P_isomerase. 1 hit.
InterProiIPR001672. G6P_Isomerase.
IPR023096. G6P_Isomerase_C.
IPR018189. Phosphoglucose_isomerase_CS.
[Graphical view]
PANTHERiPTHR11469. PTHR11469. 1 hit.
PfamiPF00342. PGI. 1 hit.
[Graphical view]
PRINTSiPR00662. G6PISOMERASE.
PROSITEiPS00765. P_GLUCOSE_ISOMERASE_1. 1 hit.
PS00174. P_GLUCOSE_ISOMERASE_2. 1 hit.
PS51463. P_GLUCOSE_ISOMERASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P06745-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAALTRNPQF QKLLEWHRAN SANLKLRELF EADPERFNNF SLNLNTNHGH
60 70 80 90 100
ILVDYSKNLV NKEVMQMLVE LAKSRGVEAA RDNMFSGSKI NYTENRAVLH
110 120 130 140 150
VALRNRSNTP IKVDGKDVMP EVNRVLDKMK SFCQRVRSGD WKGYTGKSIT
160 170 180 190 200
DIINIGIGGS DLGPLMVTEA LKPYSKGGPR VWFVSNIDGT HIAKTLASLS
210 220 230 240 250
PETSLFIIAS KTFTTQETIT NAETAKEWFL EAAKDPSAVA KHFVALSTNT
260 270 280 290 300
AKVKEFGIDP QNMFEFWDWV GGRYSLWSAI GLSIALHVGF DHFEQLLSGA
310 320 330 340 350
HWMDQHFLKT PLEKNAPVLL ALLGIWYINC YGCETHALLP YDQYMHRFAA
360 370 380 390 400
YFQQGDMESN GKYITKSGAR VDHQTGPIVW GEPGTNGQHA FYQLIHQGTK
410 420 430 440 450
MIPCDFLIPV QTQHPIRKGL HHKILLANFL AQTEALMKGK LPEEARKELQ
460 470 480 490 500
AAGKSPEDLE KLLPHKVFEG NRPTNSIVFT KLTPFILGAL IAMYEHKIFV
510 520 530 540 550
QGIMWDINSF DQWGVELGKQ LAKKIEPELE GSSAVTSHDS STNGLISFIK

QQRDTKLE
Length:558
Mass (Da):62,767
Last modified:May 1, 2007 - v4
Checksum:i7299E98B12B4C375
GO

Sequence cautioni

The sequence BAC36335 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti95N → D in AAA39825 (PubMed:3764429).Curated1
Sequence conflicti95N → D in BAE41301 (PubMed:3764429).Curated1
Sequence conflicti119M → K in BAE21866 (PubMed:16141072).Curated1
Sequence conflicti191H → R in BAE22329 (PubMed:16141072).Curated1
Sequence conflicti238A → E in AAC36515 (PubMed:9798653).Curated1
Sequence conflicti264 – 266FEF → LEL in AAC36515 (PubMed:9798653).Curated3
Sequence conflicti285A → V in AAC36515 (PubMed:9798653).Curated1
Sequence conflicti303M → T in AAC36515 (PubMed:9798653).Curated1
Sequence conflicti313E → G in BAE35416 (PubMed:16141072).Curated1
Sequence conflicti357M → V in AAC36515 (PubMed:9798653).Curated1
Sequence conflicti372D → N in AAC36515 (PubMed:9798653).Curated1
Sequence conflicti380W → L in AAC36515 (PubMed:9798653).Curated1
Sequence conflicti499F → L in BAE23502 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14220 mRNA. Translation: AAA39825.1.
AK076424 mRNA. Translation: BAC36335.1. Different initiation.
AK133827 mRNA. Translation: BAE21866.1.
AK134890 mRNA. Translation: BAE22329.1.
AK137805 mRNA. Translation: BAE23502.1.
AK147124 mRNA. Translation: BAE27695.1.
AK150341 mRNA. Translation: BAE29481.1.
AK159838 mRNA. Translation: BAE35416.1.
AK169681 mRNA. Translation: BAE41301.1.
BX537302 Genomic DNA. Translation: CAM21756.1.
BC086640 mRNA. Translation: AAH86640.1.
BC088995 mRNA. Translation: AAH88995.1.
U89408 mRNA. Translation: AAC36515.1.
L09104 mRNA. Translation: AAA65641.1.
AF108354 mRNA. Translation: AAF28799.1.
CCDSiCCDS21138.1.
PIRiA24439. NUMS.
RefSeqiNP_032181.2. NM_008155.4.
UniGeneiMm.589.

Genome annotation databases

EnsembliENSMUST00000038027; ENSMUSP00000049355; ENSMUSG00000036427.
GeneIDi14751.
KEGGimmu:14751.
UCSCiuc009gix.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14220 mRNA. Translation: AAA39825.1.
AK076424 mRNA. Translation: BAC36335.1. Different initiation.
AK133827 mRNA. Translation: BAE21866.1.
AK134890 mRNA. Translation: BAE22329.1.
AK137805 mRNA. Translation: BAE23502.1.
AK147124 mRNA. Translation: BAE27695.1.
AK150341 mRNA. Translation: BAE29481.1.
AK159838 mRNA. Translation: BAE35416.1.
AK169681 mRNA. Translation: BAE41301.1.
BX537302 Genomic DNA. Translation: CAM21756.1.
BC086640 mRNA. Translation: AAH86640.1.
BC088995 mRNA. Translation: AAH88995.1.
U89408 mRNA. Translation: AAC36515.1.
L09104 mRNA. Translation: AAA65641.1.
AF108354 mRNA. Translation: AAF28799.1.
CCDSiCCDS21138.1.
PIRiA24439. NUMS.
RefSeqiNP_032181.2. NM_008155.4.
UniGeneiMm.589.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1U0EX-ray1.60A/B1-558[»]
1U0FX-ray1.60A/B1-558[»]
1U0GX-ray1.70A/B1-558[»]
2CVPX-ray1.80A/B1-557[»]
2CXNX-ray1.40A/B1-557[»]
2CXOX-ray1.80A/B1-557[»]
2CXPX-ray1.70A/B1-557[»]
2CXQX-ray1.50A/B1-557[»]
2CXRX-ray1.70A/B1-557[»]
2CXSX-ray1.50A/B1-557[»]
2CXTX-ray1.50A/B1-557[»]
2CXUX-ray1.65A/B1-557[»]
ProteinModelPortaliP06745.
SMRiP06745.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200021. 5 interactors.
IntActiP06745. 6 interactors.
MINTiMINT-1869738.
STRINGi10090.ENSMUSP00000049355.

PTM databases

iPTMnetiP06745.
PhosphoSitePlusiP06745.
SwissPalmiP06745.

Proteomic databases

EPDiP06745.
MaxQBiP06745.
PaxDbiP06745.
PeptideAtlasiP06745.
PRIDEiP06745.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000038027; ENSMUSP00000049355; ENSMUSG00000036427.
GeneIDi14751.
KEGGimmu:14751.
UCSCiuc009gix.3. mouse.

Organism-specific databases

CTDi14751.
MGIiMGI:95797. Gpi1.

Phylogenomic databases

eggNOGiKOG2446. Eukaryota.
COG0166. LUCA.
GeneTreeiENSGT00390000000707.
HOVERGENiHBG002877.
InParanoidiP06745.
KOiK01810.
OMAiWLLEHSK.
OrthoDBiEOG091G03ZI.
PhylomeDBiP06745.
TreeFamiTF300436.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00181.
BRENDAi5.3.1.9. 3474.
ReactomeiR-MMU-5628897. TP53 Regulates Metabolic Genes.
R-MMU-6798695. Neutrophil degranulation.
R-MMU-70171. Glycolysis.
R-MMU-70263. Gluconeogenesis.
SABIO-RKP06745.

Miscellaneous databases

EvolutionaryTraceiP06745.
PROiP06745.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000036427.
CleanExiMM_GPI1.
ExpressionAtlasiP06745. baseline and differential.
GenevisibleiP06745. MM.

Family and domain databases

Gene3Di1.10.1390.10. 1 hit.
HAMAPiMF_00473. G6P_isomerase. 1 hit.
InterProiIPR001672. G6P_Isomerase.
IPR023096. G6P_Isomerase_C.
IPR018189. Phosphoglucose_isomerase_CS.
[Graphical view]
PANTHERiPTHR11469. PTHR11469. 1 hit.
PfamiPF00342. PGI. 1 hit.
[Graphical view]
PRINTSiPR00662. G6PISOMERASE.
PROSITEiPS00765. P_GLUCOSE_ISOMERASE_1. 1 hit.
PS00174. P_GLUCOSE_ISOMERASE_2. 1 hit.
PS51463. P_GLUCOSE_ISOMERASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiG6PI_MOUSE
AccessioniPrimary (citable) accession number: P06745
Secondary accession number(s): O89062
, Q3TEE7, Q3TW50, Q3UUX1, Q3UY84, Q3UZJ1, Q5RJI3, Q8C675, Q9JM07
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: May 1, 2007
Last modified: November 30, 2016
This is version 154 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.