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P06745 - G6PI_MOUSE

UniProt

P06745 - G6PI_MOUSE

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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

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei358 – 3581Proton donor1 Publication
Active sitei389 – 38911 Publication
Active sitei519 – 51911 Publication

GO - Molecular functioni

  1. glucose-6-phosphate isomerase activity Source: MGI

GO - Biological processi

  1. angiogenesis Source: UniProtKB-KW
  2. erythrocyte homeostasis Source: MGI
  3. gluconeogenesis Source: UniProtKB-KW
  4. glucose homeostasis Source: MGI
  5. glycolytic process Source: MGI
  6. glycolytic process through glucose-6-phosphate Source: MGI
  7. in utero embryonic development Source: MGI
  8. mesoderm formation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Cytokine, Growth factor, Isomerase

Keywords - Biological processi

Angiogenesis, Gluconeogenesis, Glycolysis

Enzyme and pathway databases

ReactomeiREACT_232322. Glycolysis.
REACT_263230. 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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:95797. Gpi1.

Subcellular locationi

Cytoplasm. Secreted

GO - Cellular componenti

  1. ciliary membrane Source: MGI
  2. cytoplasm Source: MGI
  3. extracellular space Source: UniProtKB-KW
  4. extracellular vesicular exosome Source: MGI
  5. membrane Source: MGI
  6. myelin sheath Source: UniProtKB
  7. nucleus Source: MGI
  8. plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 558557Glucose-6-phosphate isomerasePRO_0000180538Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei12 – 121N6-acetyllysineBy similarity
Modified residuei109 – 1091PhosphothreonineBy similarity
Modified residuei142 – 1421N6-acetyllysine1 Publication
Modified residuei185 – 1851Phosphoserine; by CK2By similarity
Modified residuei454 – 4541N6-malonyllysineBy similarity

Post-translational modificationi

ISGylated.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP06745.
PaxDbiP06745.
PRIDEiP06745.

PTM databases

PhosphoSiteiP06745.

Expressioni

Gene expression databases

BgeeiP06745.
CleanExiMM_GPI1.
GenevestigatoriP06745.

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

Protein-protein interaction databases

BioGridi200021. 4 interactions.
IntActiP06745. 6 interactions.
MINTiMINT-1869738.

Structurei

Secondary structure

1
558
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 64Combined sources
Helixi8 – 2013Combined sources
Helixi21 – 233Combined sources
Helixi26 – 327Combined sources
Helixi36 – 394Combined sources
Beta strandi41 – 455Combined sources
Beta strandi50 – 545Combined sources
Helixi62 – 7413Combined sources
Helixi77 – 859Combined sources
Turni92 – 954Combined sources
Helixi100 – 1034Combined sources
Beta strandi116 – 1183Combined sources
Helixi119 – 13719Combined sources
Beta strandi151 – 1555Combined sources
Helixi158 – 1603Combined sources
Helixi162 – 1709Combined sources
Helixi172 – 1754Combined sources
Beta strandi180 – 1845Combined sources
Helixi189 – 1968Combined sources
Turni201 – 2033Combined sources
Beta strandi204 – 2096Combined sources
Beta strandi211 – 2133Combined sources
Helixi216 – 23318Combined sources
Helixi236 – 2416Combined sources
Beta strandi243 – 2486Combined sources
Helixi250 – 2567Combined sources
Helixi260 – 2623Combined sources
Beta strandi263 – 2653Combined sources
Helixi272 – 2743Combined sources
Turni276 – 2783Combined sources
Helixi279 – 2813Combined sources
Helixi282 – 2887Combined sources
Helixi290 – 30920Combined sources
Helixi312 – 3143Combined sources
Helixi316 – 32914Combined sources
Beta strandi335 – 3417Combined sources
Helixi343 – 3453Combined sources
Helixi348 – 36013Combined sources
Beta strandi378 – 3803Combined sources
Turni384 – 3874Combined sources
Helixi388 – 39710Combined sources
Beta strandi404 – 4118Combined sources
Helixi417 – 4193Combined sources
Helixi420 – 43819Combined sources
Helixi442 – 45110Combined sources
Helixi456 – 4627Combined sources
Helixi463 – 4664Combined sources
Beta strandi474 – 4818Combined sources
Helixi484 – 50522Combined sources
Helixi513 – 5153Combined sources
Helixi516 – 52510Combined sources
Helixi526 – 5294Combined sources
Beta strandi530 – 5334Combined sources
Helixi540 – 55213Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-557.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06745.

Family & Domainsi

Sequence similaritiesi

Belongs to the GPI family.Curated

Phylogenomic databases

eggNOGiCOG0166.
GeneTreeiENSGT00390000000707.
HOVERGENiHBG002877.
InParanoidiP06745.
KOiK01810.
OMAiCETQAML.
OrthoDBiEOG7FXZXV.
PhylomeDBiP06745.
TreeFamiTF300436.

Family and domain databases

Gene3Di1.10.1390.10. 1 hit.
HAMAPiMF_00473. G6P_isomerase.
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 BAC36335.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti95 – 951N → D in AAA39825. (PubMed:3764429)Curated
Sequence conflicti95 – 951N → D in BAE41301. (PubMed:3764429)Curated
Sequence conflicti119 – 1191M → K in BAE21866. (PubMed:16141072)Curated
Sequence conflicti191 – 1911H → R in BAE22329. (PubMed:16141072)Curated
Sequence conflicti238 – 2381A → E in AAC36515. (PubMed:9798653)Curated
Sequence conflicti264 – 2663FEF → LEL in AAC36515. (PubMed:9798653)Curated
Sequence conflicti285 – 2851A → V in AAC36515. (PubMed:9798653)Curated
Sequence conflicti303 – 3031M → T in AAC36515. (PubMed:9798653)Curated
Sequence conflicti313 – 3131E → G in BAE35416. (PubMed:16141072)Curated
Sequence conflicti357 – 3571M → V in AAC36515. (PubMed:9798653)Curated
Sequence conflicti372 – 3721D → N in AAC36515. (PubMed:9798653)Curated
Sequence conflicti380 – 3801W → L in AAC36515. (PubMed:9798653)Curated
Sequence conflicti499 – 4991F → L in BAE23502. (PubMed:16141072)Curated

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.2. 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
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. Positions 1-557.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200021. 4 interactions.
IntActiP06745. 6 interactions.
MINTiMINT-1869738.

PTM databases

PhosphoSiteiP06745.

Proteomic databases

MaxQBiP06745.
PaxDbiP06745.
PRIDEiP06745.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000038027; ENSMUSP00000049355; ENSMUSG00000036427.
GeneIDi14751.
KEGGimmu:14751.
UCSCiuc009gix.2. mouse.

Organism-specific databases

CTDi14751.
MGIiMGI:95797. Gpi1.

Phylogenomic databases

eggNOGiCOG0166.
GeneTreeiENSGT00390000000707.
HOVERGENiHBG002877.
InParanoidiP06745.
KOiK01810.
OMAiCETQAML.
OrthoDBiEOG7FXZXV.
PhylomeDBiP06745.
TreeFamiTF300436.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00181.
ReactomeiREACT_232322. Glycolysis.
REACT_263230. Gluconeogenesis.
SABIO-RKP06745.

Miscellaneous databases

EvolutionaryTraceiP06745.
NextBioi286815.
PROiP06745.
SOURCEiSearch...

Gene expression databases

BgeeiP06745.
CleanExiMM_GPI1.
GenevestigatoriP06745.

Family and domain databases

Gene3Di1.10.1390.10. 1 hit.
HAMAPiMF_00473. G6P_isomerase.
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...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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.

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: February 4, 2015
This is version 137 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

External Data

Dasty 3

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 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.