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P06744 (G6PI_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 164. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·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
Sperm antigen 36
Short name=SA-36
Gene names
Name:GPI
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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. Ref.10 Ref.11 Ref.12

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. Ref.21

Subcellular location

Cytoplasm. Secreted Ref.11.

Post-translational modification

Phosphorylation at Ser-185 by CK2 has been shown to decrease enzymatic activity and may contribute to secretion by a non-classical secretory pathway. HAMAP-Rule MF_00473

ISGylated. Ref.13

Involvement in disease

Hemolytic anemia, non-spherocytic, due to glucose phosphate isomerase deficiency (HA-GPID) [MIM:613470]: A form of anemia in which there is no abnormal hemoglobin or spherocytosis. It is caused by glucose phosphate isomerase deficiency.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30

Sequence similarities

Belongs to the GPI family.

Ontologies

Keywords
   Biological processAngiogenesis
Gluconeogenesis
Glycolysis
   Cellular componentCytoplasm
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Hereditary hemolytic anemia
   Molecular functionCytokine
Growth factor
Isomerase
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processaldehyde catabolic process

Inferred from electronic annotation. Source: Ensembl

angiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

carbohydrate metabolic process

Traceable author statement. Source: Reactome

gluconeogenesis

Traceable author statement. Source: Reactome

glucose 6-phosphate metabolic process

Inferred from electronic annotation. Source: Ensembl

glucose metabolic process

Traceable author statement. Source: Reactome

glycolysis

Traceable author statement. Source: Reactome

hemostasis

Traceable author statement PubMed 7435496. Source: ProtInc

humoral immune response

Traceable author statement PubMed 3020690. Source: ProtInc

learning or memory

Inferred from electronic annotation. Source: Ensembl

methylglyoxal biosynthetic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

extracellular space

Inferred from electronic annotation. Source: UniProtKB-KW

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 19199708PubMed 20458337. Source: UniProt

neuron projection

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay. Source: HPA

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_functionglucose-6-phosphate isomerase activity

Traceable author statement. Source: Reactome

intramolecular transferase activity

Inferred from electronic annotation. Source: Ensembl

monosaccharide binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P06744-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P06744-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MVALCSLQHLGSSDPRALPTLPTATSGQRPAKRRRKSPAM
     135-162: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 558557Glucose-6-phosphate isomerase HAMAP-Rule MF_00473
PRO_0000180537

Sites

Active site3581Proton donor Ref.21 Ref.23 Ref.24
Active site3891 Ref.21 Ref.23 Ref.24
Active site5191 Ref.21 Ref.23 Ref.24

Amino acid modifications

Modified residue21N-acetylalanine Ref.8 Ref.16
Modified residue121N6-acetyllysine Ref.18
Modified residue1091Phosphothreonine Ref.15 Ref.17
Modified residue1421N6-acetyllysine Ref.18
Modified residue1851Phosphoserine; by CK2 Ref.10 Ref.14
Modified residue4541N6-malonyllysine Ref.20

Natural variations

Alternative sequence11M → MVALCSLQHLGSSDPRALPT LPTATSGQRPAKRRRKSPAM in isoform 2.
VSP_043475
Alternative sequence135 – 16228Missing in isoform 2.
VSP_043476
Natural variant51T → I in HA-GPID; GPI Matsumoto. Ref.28
VAR_002516
Natural variant201H → P in HA-GPID; severe form with neurological deficits; GPI Homburg. Ref.30
VAR_002517
Natural variant751R → G in HA-GPID; GPI Elyria. Ref.29
VAR_002518
Natural variant831R → W in HA-GPID. Ref.26
VAR_002519
Natural variant1011V → M in HA-GPID; GPI Sarcina. Ref.27
VAR_002521
Natural variant1591G → S in HA-GPID. Ref.25
VAR_002520
Natural variant1951T → I in HA-GPID; GPI Bari and Mola. Ref.27
VAR_002522
Natural variant2081I → T. Ref.3
Corresponds to variant rs8191371 [ dbSNP | Ensembl ].
VAR_018816
Natural variant2241T → M in HA-GPID; GPI Iwate. Ref.26 Ref.28
Corresponds to variant rs61754634 [ dbSNP | Ensembl ].
VAR_002523
Natural variant2731R → H in HA-GPID. Ref.26
VAR_002524
Natural variant2781S → L in HA-GPID. Ref.26
Corresponds to variant rs34306618 [ dbSNP | Ensembl ].
VAR_002525
Natural variant3001A → P in HA-GPID. Ref.29
VAR_002526
Natural variant3081R → H.
Corresponds to variant rs2230294 [ dbSNP | Ensembl ].
VAR_033943
Natural variant3391L → P in HA-GPID; severe form with neurological deficits; GPI Homburg. Ref.30
VAR_002527
Natural variant3431Q → R in HA-GPID; GPI Narita and Morcone. Ref.27 Ref.28
VAR_002528
Natural variant3471R → C in HA-GPID; GPI Mount Scopus. Ref.26 Ref.29
VAR_002529
Natural variant3471R → H in HA-GPID. Ref.25
VAR_002530
Natural variant3751T → R in HA-GPID; GPI Kinki. Ref.28
VAR_002531
Natural variant3891H → R in HA-GPID; severe form; GPI Calden. Ref.30
VAR_002532
Natural variant4721R → H in HA-GPID. Ref.29
VAR_002533
Natural variant4871L → F in HA-GPID. Ref.26
VAR_002534
Natural variant4951E → K in HA-GPID. Ref.26
VAR_002535
Natural variant5171L → V in HA-GPID; severe form; GPI Calden. Ref.30
VAR_002536
Natural variant5251I → T in HA-GPID. Ref.25 Ref.27
VAR_002537
Natural variant5391D → N in HA-GPID; GPI Fukuoka and Kinki. Ref.28
VAR_002538

Experimental info

Mutagenesis1851S → A: Retained full enzymatic activity. Ref.14
Mutagenesis1851S → E: Decreased enzymatic activity. Ref.14
Sequence conflict1581G → V in AAA36368. Ref.1
Sequence conflict4261L → V in AAF22645. Ref.2
Sequence conflict4361L → V in AAF22645. Ref.2

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 7C8E95277BDC79A6

FASTA55863,147
        10         20         30         40         50         60 
MAALTRDPQF QKLQQWYREH RSELNLRRLF DANKDRFNHF SLTLNTNHGH ILVDYSKNLV 

        70         80         90        100        110        120 
TEDVMRMLVD LAKSRGVEAA RERMFNGEKI NYTEGRAVLH VALRNRSNTP ILVDGKDVMP 

       130        140        150        160        170        180 
EVNKVLDKMK SFCQRVRSGD WKGYTGKTIT DVINIGIGGS DLGPLMVTEA LKPYSSGGPR 

       190        200        210        220        230        240 
VWYVSNIDGT HIAKTLAQLN PESSLFIIAS KTFTTQETIT NAETAKEWFL QAAKDPSAVA 

       250        260        270        280        290        300 
KHFVALSTNT TKVKEFGIDP QNMFEFWDWV GGRYSLWSAI GLSIALHVGF DNFEQLLSGA 

       310        320        330        340        350        360 
HWMDQHFRTT PLEKNAPVLL ALLGIWYINC FGCETHAMLP YDQYLHRFAA YFQQGDMESN 

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

       430        440        450        460        470        480 
HHKILLANFL AQTEALMRGK STEEARKELQ AAGKSPEDLE RLLPHKVFEG NRPTNSIVFT 

       490        500        510        520        530        540 
KLTPFMLGAL VAMYEHKIFV QGIIWDINSF DQWGVELGKQ LAKKIEPELD GSAQVTSHDA 

       550 
STNGLINFIK QQREARVQ 

« Hide

Isoform 2 [UniParc].

Checksum: 65537AD376C4FDF1
Show »

FASTA56964,325

References

« Hide 'large scale' references
[1]Gurney M.E.
Submitted (MAR-1987) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Cloning of a glucose phosphate isomerase/neuroleukin-like sperm antigen involved in sperm agglutination."
Yakirevich E., Naot Y.
Biol. Reprod. 62:1016-1023(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Testis.
[3]NIEHS SNPs program
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-208.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Amygdala.
[5]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORM 1).
Tissue: Skin.
[7]"Characterization of the 5' end of the gene for human glucose phosphate isomerase (GPI)."
Walker J.I.H., Faik P., Morgan M.J.
Genomics 7:638-643(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-71.
[8]Bienvenut W.V.
Submitted (OCT-2004) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-12; 58-73; 97-104; 181-226; 424-438 AND 455-461, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[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]"Phosphohexose isomerase/autocrine motility factor/neuroleukin/maturation factor is a multifunctional phosphoprotein."
Haga A., Niinaka Y., Raz A.
Biochim. Biophys. Acta 1480:235-244(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT SER-185.
[11]"Tumor autocrine motility factor is an angiogenic factor that stimulates endothelial cell motility."
Funasaka T., Haga A., Raz A., Nagase H.
Biochem. Biophys. Res. Commun. 285:118-128(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, FUNCTION.
[12]"Species specificity of the cytokine function of phosphoglucose isomerase."
Amraei M., Nabi I.R.
FEBS Lett. 525:151-155(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SPECIES SPECIFICITY OF THE CYTOKINE FUNCTION.
[13]"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.
[14]"Differential regulation of phosphoglucose isomerase/autocrine motility factor activities by protein kinase CK2 phosphorylation."
Yanagawa T., Funasaka T., Tsutsumi S., Raz T., Tanaka N., Raz A.
J. Biol. Chem. 280:10419-10426(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-185, MUTAGENESIS OF SER-185.
[15]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-109, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-109, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[18]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-12 AND LYS-142, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"The first identification of lysine malonylation substrates and its regulatory enzyme."
Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y., He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C., Dai J., Verdin E., Ye Y., Zhao Y.
Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: MALONYLATION AT LYS-454.
[21]"The crystal structure of human phosphoglucose isomerase at 1.6 A resolution: implications for catalytic mechanism, cytokine activity and haemolytic anaemia."
Read J., Pearce J., Li X., Muirhead H., Chirgwin J., Davies C.
J. Mol. Biol. 309:447-463(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS), SUBUNIT, ACTIVE SITE.
[22]"Inhibition mechanism of cytokine activity of human autocrine motility factor examined by crystal structure analyses and site-directed mutagenesis studies."
Tanaka N., Haga A., Uemura H., Akiyama H., Funasaka T., Nagase H., Raz A., Nakamura K.T.
J. Mol. Biol. 318:985-997(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) ALONE AND IN COMPLEX WITH INHIBITOR.
[23]"The structure of human phosphoglucose isomerase complexed with a transition-state analogue."
Davies C., Muirhead H., Chirgwin J.
Acta Crystallogr. D 59:1111-1113(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) IN COMPLEX WITH INHIBITOR, ACTIVE SITE.
[24]"Crystal structure of human phosphoglucose isomerase and analysis of the initial catalytic steps."
Cordeiro A.T., Godoi P.H., Silva C.H., Garratt R.C., Oliva G., Thiemann O.H.
Biochim. Biophys. Acta 1645:117-122(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), ACTIVE SITE.
[25]"DNA sequence abnormalities in human glucose 6-phosphate isomerase deficiency."
Walker J.I.H., Layton D.M., Bellingham A.J., Morgan M.J., Faik P.
Hum. Mol. Genet. 2:327-329(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HA-GPID SER-159; HIS-347 AND THR-525.
[26]"The characterization of gene mutations for human glucose phosphate isomerase deficiency associated with chronic hemolytic anemia."
Xu W., Beutler E.
J. Clin. Invest. 94:2326-2329(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HA-GPID TRP-83; MET-224; HIS-273; LEU-278; CYS-347; PHE-487 AND LYS-495.
[27]"Study of the molecular defects in glucose phosphate isomerase-deficient patients affected by chronic hemolytic anemia."
Baronciani L., Zanella A., Bianchi P., Zappa M., Alfinito F., Iolascon A., Tannoia N., Beutler E., Sirchia G.
Blood 88:2306-2310(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HA-GPID MET-101; ILE-195; ARG-343 AND THR-525.
[28]"Molecular analysis of glucose phosphate isomerase deficiency associated with hereditary hemolytic anemia."
Kanno H., Fujii H., Hirono A., Ishida Y., Ohga S., Fukumoto Y., Matsuzawa K., Ogawa S., Miwa S.
Blood 88:2321-2325(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HA-GPID ILE-5; MET-224; ARG-343; ARG-375 AND ASN-539.
[29]"Glucosephosphate isomerase (GPI) deficiency mutations associated with hereditary nonspherocytic hemolytic anemia (HNSHA)."
Beutler E., West C., Britton H.A., Harris J., Forman L.
Blood Cells Mol. Dis. 23:402-409(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HA-GPID GLY-75; PRO-300; CYS-347 AND HIS-472.
[30]"Molecular basis of neurological dysfunction coupled with haemolytic anaemia in human glucose-6-phosphate isomerase (GPI) deficiency."
Kugler W., Breme K., Laspe P., Muirhead H., Davies C., Winkler H., Schroter W., Lakomek M.
Hum. Genet. 103:450-454(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HA-GPID PRO-20; PRO-339; ARG-389 AND VAL-517.
+Additional computationally mapped references.

Web resources

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Phosphoglucose isomerase entry

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K03515 mRNA. Translation: AAA36368.1.
AF187554 mRNA. Translation: AAF22645.1.
AY324386 Genomic DNA. Translation: AAP72966.1.
AK294396 mRNA. Translation: BAG57650.1.
AC010504 Genomic DNA. No translation available.
AC092073 Genomic DNA. No translation available.
BC004982 mRNA. Translation: AAH04982.1.
AH002710 Genomic DNA. Translation: AAA52593.1.
PIRA35333.
RefSeqNP_000166.2. NM_000175.3.
NP_001171651.1. NM_001184722.1.
XP_005258821.1. XM_005258764.1.
UniGeneHs.466471.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IATX-ray1.62A2-558[»]
1IRIX-ray2.40A/B/C/D1-558[»]
1JIQX-ray1.90A/B/C/D1-558[»]
1JLHX-ray2.10A/B/C/D1-558[»]
1NUHX-ray2.51A1-558[»]
ProteinModelPortalP06744.
SMRP06744. Positions 2-557.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109082. 16 interactions.
IntActP06744. 4 interactions.
MINTMINT-4999095.
STRING9606.ENSP00000348877.

PTM databases

PhosphoSiteP06744.

Polymorphism databases

DMDM17380385.

Proteomic databases

PaxDbP06744.
PeptideAtlasP06744.
PRIDEP06744.

Protocols and materials databases

DNASU2821.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000356487; ENSP00000348877; ENSG00000105220. [P06744-1]
ENST00000415930; ENSP00000405573; ENSG00000105220. [P06744-2]
GeneID2821.
KEGGhsa:2821.
UCSCuc002nvf.3. human. [P06744-1]
uc010xrv.2. human. [P06744-2]

Organism-specific databases

CTD2821.
GeneCardsGC19P034855.
HGNCHGNC:4458. GPI.
HPACAB018655.
CAB040563.
HPA024305.
MIM172400. gene.
613470. phenotype.
neXtProtNX_P06744.
Orphanet712. Hemolytic anemia due to glucophosphate isomerase deficiency.
PharmGKBPA28841.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0166.
HOGENOMHOG000261371.
HOVERGENHBG002877.
InParanoidP06744.
KOK01810.
OMARLKYFAA.
OrthoDBEOG7FXZXV.
PhylomeDBP06744.
TreeFamTF300436.

Enzyme and pathway databases

BioCycMetaCyc:HS02693-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP06744.
UniPathwayUPA00109; UER00181.

Gene expression databases

ArrayExpressP06744.
BgeeP06744.
CleanExHS_GPI.
GenevestigatorP06744.

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

ChiTaRSGPI. human.
EvolutionaryTraceP06744.
GeneWikiGlucose-6-phosphate_isomerase.
GenomeRNAi2821.
NextBio11117.
PROP06744.
SOURCESearch...

Entry information

Entry nameG6PI_HUMAN
AccessionPrimary (citable) accession number: P06744
Secondary accession number(s): B4DG39 expand/collapse secondary AC list , Q9BRD3, Q9BSK5, Q9UHE6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 164 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM