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P06745

- G6PI_MOUSE

UniProt

P06745 - G6PI_MOUSE

Protein

Glucose-6-phosphate isomerase

Gene

Gpi

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 4 (01 May 2007)
      Previous versions | rss
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    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

    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
    2. protein binding Source: IntAct

    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

    Keywords - Molecular functioni

    Cytokine, Growth factor, Isomerase

    Keywords - Biological processi

    Angiogenesis, Gluconeogenesis, Glycolysis

    Enzyme and pathway databases

    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
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:95797. Gpi1.

    Subcellular locationi

    GO - Cellular componenti

    1. ciliary membrane Source: MGI
    2. cytoplasm Source: UniProtKB-SubCell
    3. extracellular space Source: UniProtKB-KW
    4. plasma membrane Source: MGI

    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. 3 interactions.
    IntActiP06745. 6 interactions.
    MINTiMINT-1869738.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    OMAiNCHFVAN.
    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

    MAALTRNPQF QKLLEWHRAN SANLKLRELF EADPERFNNF SLNLNTNHGH    50
    ILVDYSKNLV NKEVMQMLVE LAKSRGVEAA RDNMFSGSKI NYTENRAVLH 100
    VALRNRSNTP IKVDGKDVMP EVNRVLDKMK SFCQRVRSGD WKGYTGKSIT 150
    DIINIGIGGS DLGPLMVTEA LKPYSKGGPR VWFVSNIDGT HIAKTLASLS 200
    PETSLFIIAS KTFTTQETIT NAETAKEWFL EAAKDPSAVA KHFVALSTNT 250
    AKVKEFGIDP QNMFEFWDWV GGRYSLWSAI GLSIALHVGF DHFEQLLSGA 300
    HWMDQHFLKT PLEKNAPVLL ALLGIWYINC YGCETHALLP YDQYMHRFAA 350
    YFQQGDMESN GKYITKSGAR VDHQTGPIVW GEPGTNGQHA FYQLIHQGTK 400
    MIPCDFLIPV QTQHPIRKGL HHKILLANFL AQTEALMKGK LPEEARKELQ 450
    AAGKSPEDLE KLLPHKVFEG NRPTNSIVFT KLTPFILGAL IAMYEHKIFV 500
    QGIMWDINSF DQWGVELGKQ LAKKIEPELE GSSAVTSHDS STNGLISFIK 550
    QQRDTKLE 558
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS21138.1.
    PIRi A24439. NUMS.
    RefSeqi NP_032181.2. NM_008155.4.
    UniGenei Mm.589.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1U0E X-ray 1.60 A/B 1-558 [» ]
    1U0F X-ray 1.60 A/B 1-558 [» ]
    1U0G X-ray 1.70 A/B 1-558 [» ]
    2CVP X-ray 1.80 A/B 1-557 [» ]
    2CXN X-ray 1.40 A/B 1-557 [» ]
    2CXO X-ray 1.80 A/B 1-557 [» ]
    2CXP X-ray 1.70 A/B 1-557 [» ]
    2CXQ X-ray 1.50 A/B 1-557 [» ]
    2CXR X-ray 1.70 A/B 1-557 [» ]
    2CXS X-ray 1.50 A/B 1-557 [» ]
    2CXT X-ray 1.50 A/B 1-557 [» ]
    2CXU X-ray 1.65 A/B 1-557 [» ]
    ProteinModelPortali P06745.
    SMRi P06745. Positions 1-557.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 200021. 3 interactions.
    IntActi P06745. 6 interactions.
    MINTi MINT-1869738.

    PTM databases

    PhosphoSitei P06745.

    Proteomic databases

    MaxQBi P06745.
    PaxDbi P06745.
    PRIDEi P06745.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000038027 ; ENSMUSP00000049355 ; ENSMUSG00000036427 .
    GeneIDi 14751.
    KEGGi mmu:14751.
    UCSCi uc009gix.2. mouse.

    Organism-specific databases

    CTDi 14751.
    MGIi MGI:95797. Gpi1.

    Phylogenomic databases

    eggNOGi COG0166.
    GeneTreei ENSGT00390000000707.
    HOVERGENi HBG002877.
    InParanoidi P06745.
    KOi K01810.
    OMAi NCHFVAN.
    OrthoDBi EOG7FXZXV.
    PhylomeDBi P06745.
    TreeFami TF300436.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00181 .
    SABIO-RK P06745.

    Miscellaneous databases

    EvolutionaryTracei P06745.
    NextBioi 286815.
    PROi P06745.
    SOURCEi Search...

    Gene expression databases

    Bgeei P06745.
    CleanExi MM_GPI1.
    Genevestigatori P06745.

    Family and domain databases

    Gene3Di 1.10.1390.10. 1 hit.
    HAMAPi MF_00473. G6P_isomerase.
    InterProi IPR001672. G6P_Isomerase.
    IPR023096. G6P_Isomerase_C.
    IPR018189. Phosphoglucose_isomerase_CS.
    [Graphical view ]
    PANTHERi PTHR11469. PTHR11469. 1 hit.
    Pfami PF00342. PGI. 1 hit.
    [Graphical view ]
    PRINTSi PR00662. G6PISOMERASE.
    PROSITEi PS00765. P_GLUCOSE_ISOMERASE_1. 1 hit.
    PS00174. P_GLUCOSE_ISOMERASE_2. 1 hit.
    PS51463. P_GLUCOSE_ISOMERASE_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    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: October 1, 2014
    This is version 133 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