Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P06745 (G6PI_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glucose-6-phosphate isomerase

Short name=GPI
EC=5.3.1.9
Alternative name(s):
Autocrine motility factor
Short name=AMF
Neuroleukin
Short name=NLK
Phosphoglucose isomerase
Short name=PGI
Phosphohexose isomerase
Short name=PHI
Gene names
Name:Gpi
Synonyms:Gpi1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length558 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. HAMAP-Rule MF_00473

Catalytic activity

D-glucose 6-phosphate = D-fructose 6-phosphate. HAMAP-Rule MF_00473

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4. HAMAP-Rule MF_00473

Subunit structure

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

Subcellular location

Cytoplasm. Secreted HAMAP-Rule MF_00473.

Post-translational modification

ISGylated. Ref.10

Sequence similarities

Belongs to the GPI family.

Sequence caution

The sequence BAC36335.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processAngiogenesis
Gluconeogenesis
Glycolysis
   Cellular componentCytoplasm
Secreted
   Molecular functionCytokine
Growth factor
Isomerase
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

erythrocyte homeostasis

Inferred from mutant phenotype PubMed 8417789. Source: MGI

gluconeogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

glucose homeostasis

Inferred from mutant phenotype PubMed 8417789. Source: MGI

glycolytic process

Inferred from direct assay PubMed 15665293. Source: MGI

in utero embryonic development

Inferred from mutant phenotype PubMed 1582174. Source: MGI

mesoderm formation

Inferred from mutant phenotype PubMed 8922529. Source: MGI

   Cellular_componentciliary membrane

Inferred from direct assay PubMed 22179047. Source: MGI

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular space

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from direct assay PubMed 22179047. Source: MGI

   Molecular_functionglucose-6-phosphate isomerase activity

Inferred from direct assay PubMed 1180875PubMed 1235912PubMed 15155459PubMed 1582174PubMed 204065PubMed 2344351PubMed 7277315PubMed 7323947PubMed 7444718PubMed 8417789. Source: MGI

protein binding

Inferred from physical interaction PubMed 17875708. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Parp14Q2EMV94EBI-1534927,EBI-1534943

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 558557Glucose-6-phosphate isomerase HAMAP-Rule MF_00473
PRO_0000180538

Sites

Active site3581Proton donor Ref.12
Active site3891 Ref.12
Active site5191 Ref.12

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue121N6-acetyllysine By similarity
Modified residue1091Phosphothreonine By similarity
Modified residue1421N6-acetyllysine Ref.11
Modified residue1851Phosphoserine; by CK2 By similarity
Modified residue4541N6-malonyllysine By similarity

Experimental info

Sequence conflict951N → D in AAA39825. Ref.1
Sequence conflict951N → D in BAE41301. Ref.1
Sequence conflict1191M → K in BAE21866. Ref.2
Sequence conflict1911H → R in BAE22329. Ref.2
Sequence conflict2381A → E in AAC36515. Ref.6
Sequence conflict264 – 2663FEF → LEL in AAC36515. Ref.6
Sequence conflict2851A → V in AAC36515. Ref.6
Sequence conflict3031M → T in AAC36515. Ref.6
Sequence conflict3131E → G in BAE35416. Ref.2
Sequence conflict3571M → V in AAC36515. Ref.6
Sequence conflict3721D → N in AAC36515. Ref.6
Sequence conflict3801W → L in AAC36515. Ref.6
Sequence conflict4991F → L in BAE23502. Ref.2

Secondary structure

................................................................................................. 558
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06745 [UniParc].

Last modified May 1, 2007. Version 4.
Checksum: 7299E98B12B4C375

FASTA55862,767
        10         20         30         40         50         60 
MAALTRNPQF QKLLEWHRAN SANLKLRELF EADPERFNNF SLNLNTNHGH ILVDYSKNLV 

        70         80         90        100        110        120 
NKEVMQMLVE LAKSRGVEAA RDNMFSGSKI NYTENRAVLH VALRNRSNTP IKVDGKDVMP 

       130        140        150        160        170        180 
EVNRVLDKMK SFCQRVRSGD WKGYTGKSIT DIINIGIGGS DLGPLMVTEA LKPYSKGGPR 

       190        200        210        220        230        240 
VWFVSNIDGT HIAKTLASLS PETSLFIIAS KTFTTQETIT NAETAKEWFL EAAKDPSAVA 

       250        260        270        280        290        300 
KHFVALSTNT AKVKEFGIDP QNMFEFWDWV GGRYSLWSAI GLSIALHVGF DHFEQLLSGA 

       310        320        330        340        350        360 
HWMDQHFLKT PLEKNAPVLL ALLGIWYINC YGCETHALLP YDQYMHRFAA YFQQGDMESN 

       370        380        390        400        410        420 
GKYITKSGAR VDHQTGPIVW GEPGTNGQHA FYQLIHQGTK MIPCDFLIPV QTQHPIRKGL 

       430        440        450        460        470        480 
HHKILLANFL AQTEALMKGK LPEEARKELQ AAGKSPEDLE KLLPHKVFEG NRPTNSIVFT 

       490        500        510        520        530        540 
KLTPFILGAL IAMYEHKIFV QGIMWDINSF DQWGVELGKQ LAKKIEPELE GSSAVTSHDS 

       550 
STNGLISFIK QQRDTKLE 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and expression of neuroleukin, a neurotrophic factor for spinal and sensory neurons."
Gurney M.E., Heinrich S.P., Lee M.R., Yin H.-S.
Science 234:566-574(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Salivary gland.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Bone marrow, Head, Heart, Olfactory bulb and Thymus.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
[5]Lubec G., Klug S., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 28-36; 63-73; 97-104; 107-124; 148-176; 181-234; 242-252; 255-273; 424-438; 455-461 AND 467-481, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain and Hippocampus.
[6]"Expressed genes in interleukin-4 treated B cells identified by cDNA representational difference analysis."
Chu C.C., Paul W.E.
Mol. Immunol. 35:487-502(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 235-393.
Strain: BALB/c.
Tissue: Spleen.
[7]"Identification of a novel tandemly repeated sequence present in an intron of the glucose phosphate isomerase (GPI) gene in mouse and man."
Faik P., Walker J.I., Morgan M.J.
Genomics 21:122-127(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 269-558.
[8]"Quantitative allelic discrimination of GPI-c and GPI-a using molecular beacons."
Bauchwitz R.P., Tyagi S., Marras S.A.E.
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 417-543.
Strain: 129.
[9]"Mouse glucose-6-phosphate isomerase and neuroleukin have identical 3' sequences."
Faik P., Walker J.I.H., Redmill A.A.M., Morgan M.J.
Nature 332:455-456(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTITY OF NEUROLEUKIN AS PGI.
[10]"Proteomic identification of proteins conjugated to ISG15 in mouse and human cells."
Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.
Biochem. Biophys. Res. Commun. 336:496-506(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ISGYLATION.
[11]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-142, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[12]"The crystal structure of mouse phosphoglucose isomerase at 1.6A resolution and its complex with glucose 6-phosphate reveals the catalytic mechanism of sugar ring opening."
Solomons J.T.G., Zimmerly E.M., Burns S., Krishnamurthy N., Swan M.K., Krings S., Muirhead H., Chirgwin J., Davies C.
J. Mol. Biol. 342:847-860(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH G6P, ACTIVE SITE.
[13]"Tumor cell autocrine motility factor is the neuroleukin/phosphohexose isomerase polypeptide."
Watanabe H., Takehana K., Date M., Shinozaki T., Raz A.
Cancer Res. 56:2960-2963(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTITY OF AMF AS PGI.
[14]"Crystal structures of mouse autocrine motility factor in complex with carbohydrate phosphate inhibitors provide insight into structure-activity relationship of the inhibitors."
Tanaka N., Haga A., Naba N., Shiraiwa K., Kusakabe Y., Hashimoto K., Funasaka T., Nagase H., Raz A., Nakamura K.T.
J. Mol. Biol. 356:312-324(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1-557 IN COMPLEX WITH INHIBITORS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS21138.1.
PIRNUMS. A24439.
RefSeqNP_032181.2. NM_008155.4.
UniGeneMm.589.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP06745.
SMRP06745. Positions 1-557.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200021. 3 interactions.
IntActP06745. 6 interactions.
MINTMINT-1869738.

PTM databases

PhosphoSiteP06745.

Proteomic databases

MaxQBP06745.
PaxDbP06745.
PRIDEP06745.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000038027; ENSMUSP00000049355; ENSMUSG00000036427.
GeneID14751.
KEGGmmu:14751.
UCSCuc009gix.2. mouse.

Organism-specific databases

CTD14751.
MGIMGI:95797. Gpi1.

Phylogenomic databases

eggNOGCOG0166.
GeneTreeENSGT00390000000707.
HOVERGENHBG002877.
InParanoidP06745.
KOK01810.
OMANCHFVAN.
OrthoDBEOG7FXZXV.
PhylomeDBP06745.
TreeFamTF300436.

Enzyme and pathway databases

SABIO-RKP06745.
UniPathwayUPA00109; UER00181.

Gene expression databases

BgeeP06745.
CleanExMM_GPI1.
GenevestigatorP06745.

Family and domain databases

Gene3D1.10.1390.10. 1 hit.
HAMAPMF_00473. G6P_isomerase.
InterProIPR001672. G6P_Isomerase.
IPR023096. G6P_Isomerase_C.
IPR018189. Phosphoglucose_isomerase_CS.
[Graphical view]
PANTHERPTHR11469. PTHR11469. 1 hit.
PfamPF00342. PGI. 1 hit.
[Graphical view]
PRINTSPR00662. G6PISOMERASE.
PROSITEPS00765. P_GLUCOSE_ISOMERASE_1. 1 hit.
PS00174. P_GLUCOSE_ISOMERASE_2. 1 hit.
PS51463. P_GLUCOSE_ISOMERASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP06745.
NextBio286815.
PROP06745.
SOURCESearch...

Entry information

Entry nameG6PI_MOUSE
AccessionPrimary (citable) accession number: P06745
Secondary accession number(s): O89062 expand/collapse secondary AC list , Q3TEE7, Q3TW50, Q3UUX1, Q3UY84, Q3UZJ1, Q5RJI3, Q8C675, Q9JM07
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: May 1, 2007
Last modified: July 9, 2014
This is version 131 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot