Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P06745

- G6PI_MOUSE

UniProt

P06745 - G6PI_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Glucose-6-phosphate isomerase

Gene

Gpi

Organism
Mus musculus (Mouse)
Status
Reviewed - 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

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

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-KW
  3. extracellular space Source: UniProtKB-KW
  4. 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. 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 [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.

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

« 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.

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 29, 2014
This is version 134 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