Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

P06744

- G6PI_HUMAN

UniProt

P06744 - G6PI_HUMAN

Protein

Glucose-6-phosphate isomerase

Gene

GPI

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 169 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.2 Publications

    Catalytic activityi

    D-glucose 6-phosphate = D-fructose 6-phosphate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei358 – 3581Proton donor
    Active sitei389 – 3891
    Active sitei519 – 5191

    GO - Molecular functioni

    1. glucose-6-phosphate isomerase activity Source: Reactome
    2. intramolecular transferase activity Source: Ensembl
    3. monosaccharide binding Source: Ensembl

    GO - Biological processi

    1. aldehyde catabolic process Source: Ensembl
    2. angiogenesis Source: UniProtKB-KW
    3. carbohydrate metabolic process Source: Reactome
    4. gluconeogenesis Source: Reactome
    5. glucose 6-phosphate metabolic process Source: Ensembl
    6. glucose metabolic process Source: Reactome
    7. glycolytic process Source: Reactome
    8. hemostasis Source: ProtInc
    9. humoral immune response Source: ProtInc
    10. learning or memory Source: Ensembl
    11. methylglyoxal biosynthetic process Source: Ensembl
    12. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
    13. negative regulation of neuron apoptotic process Source: Ensembl
    14. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Cytokine, Growth factor, Isomerase

    Keywords - Biological processi

    Angiogenesis, Gluconeogenesis, Glycolysis

    Enzyme and pathway databases

    BioCyciMetaCyc:HS02693-MONOMER.
    ReactomeiREACT_1383. Glycolysis.
    REACT_1520. Gluconeogenesis.
    SABIO-RKP06744.
    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
    Sperm antigen 36
    Short name:
    SA-36
    Gene namesi
    Name:GPI
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:4458. GPI.

    Subcellular locationi

    Cytoplasm 1 Publication. Secreted 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. extracellular space Source: UniProtKB-KW
    4. extracellular vesicular exosome Source: UniProt
    5. membrane Source: UniProtKB
    6. neuron projection Source: Ensembl
    7. nucleus Source: HPA
    8. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    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.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti5 – 51T → I in HA-GPID; GPI Matsumoto. 1 Publication
    VAR_002516
    Natural varianti20 – 201H → P in HA-GPID; severe form with neurological deficits; GPI Homburg. 1 Publication
    VAR_002517
    Natural varianti75 – 751R → G in HA-GPID; GPI Elyria. 1 Publication
    VAR_002518
    Natural varianti83 – 831R → W in HA-GPID. 1 Publication
    VAR_002519
    Natural varianti101 – 1011V → M in HA-GPID; GPI Sarcina. 1 Publication
    VAR_002521
    Natural varianti159 – 1591G → S in HA-GPID. 1 Publication
    VAR_002520
    Natural varianti195 – 1951T → I in HA-GPID; GPI Bari and Mola. 1 Publication
    VAR_002522
    Natural varianti224 – 2241T → M in HA-GPID; GPI Iwate. 2 Publications
    Corresponds to variant rs61754634 [ dbSNP | Ensembl ].
    VAR_002523
    Natural varianti273 – 2731R → H in HA-GPID. 1 Publication
    VAR_002524
    Natural varianti278 – 2781S → L in HA-GPID. 1 Publication
    Corresponds to variant rs34306618 [ dbSNP | Ensembl ].
    VAR_002525
    Natural varianti300 – 3001A → P in HA-GPID. 1 Publication
    VAR_002526
    Natural varianti339 – 3391L → P in HA-GPID; severe form with neurological deficits; GPI Homburg. 1 Publication
    VAR_002527
    Natural varianti343 – 3431Q → R in HA-GPID; GPI Narita and Morcone. 2 Publications
    VAR_002528
    Natural varianti347 – 3471R → C in HA-GPID; GPI Mount Scopus. 2 Publications
    VAR_002529
    Natural varianti347 – 3471R → H in HA-GPID. 1 Publication
    VAR_002530
    Natural varianti375 – 3751T → R in HA-GPID; GPI Kinki. 1 Publication
    VAR_002531
    Natural varianti389 – 3891H → R in HA-GPID; severe form; GPI Calden. 1 Publication
    VAR_002532
    Natural varianti472 – 4721R → H in HA-GPID. 1 Publication
    VAR_002533
    Natural varianti487 – 4871L → F in HA-GPID. 1 Publication
    VAR_002534
    Natural varianti495 – 4951E → K in HA-GPID. 1 Publication
    VAR_002535
    Natural varianti517 – 5171L → V in HA-GPID; severe form; GPI Calden. 1 Publication
    VAR_002536
    Natural varianti525 – 5251I → T in HA-GPID. 2 Publications
    VAR_002537
    Natural varianti539 – 5391D → N in HA-GPID; GPI Fukuoka and Kinki. 1 Publication
    VAR_002538

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi185 – 1851S → A: Retained full enzymatic activity. 1 Publication
    Mutagenesisi185 – 1851S → E: Decreased enzymatic activity. 1 Publication

    Keywords - Diseasei

    Disease mutation, Hereditary hemolytic anemia

    Organism-specific databases

    MIMi613470. phenotype.
    Orphaneti712. Hemolytic anemia due to glucophosphate isomerase deficiency.
    PharmGKBiPA28841.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 558557Glucose-6-phosphate isomerasePRO_0000180537Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei12 – 121N6-acetyllysine1 Publication
    Modified residuei109 – 1091Phosphothreonine2 Publications
    Modified residuei142 – 1421N6-acetyllysine1 Publication
    Modified residuei185 – 1851Phosphoserine; by CK22 Publications
    Modified residuei454 – 4541N6-malonyllysine1 Publication

    Post-translational modificationi

    Phosphorylation at Ser-185 by CK2 has been shown to decrease enzymatic activity and may contribute to secretion by a non-classical secretory pathway.4 Publications
    ISGylated.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP06744.
    PaxDbiP06744.
    PeptideAtlasiP06744.
    PRIDEiP06744.

    PTM databases

    PhosphoSiteiP06744.

    Expressioni

    Gene expression databases

    ArrayExpressiP06744.
    BgeeiP06744.
    CleanExiHS_GPI.
    GenevestigatoriP06744.

    Organism-specific databases

    HPAiCAB018655.
    CAB040563.
    HPA024305.

    Interactioni

    Subunit structurei

    Homodimer in the catalytically active form, monomer in the secreted form.3 Publications

    Protein-protein interaction databases

    BioGridi109082. 19 interactions.
    IntActiP06744. 4 interactions.
    MINTiMINT-4999095.
    STRINGi9606.ENSP00000348877.

    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
    Beta strandi57 – 593
    Helixi62 – 7413
    Helixi77 – 859
    Turni92 – 954
    Helixi100 – 1034
    Beta strandi116 – 1183
    Helixi119 – 13719
    Beta strandi151 – 1555
    Helixi158 – 1603
    Helixi162 – 1709
    Helixi172 – 1743
    Beta strandi180 – 1845
    Helixi189 – 1968
    Helixi201 – 2033
    Beta strandi204 – 2096
    Beta strandi211 – 2133
    Helixi216 – 23318
    Helixi236 – 2383
    Helixi239 – 2424
    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
    Helixi386 – 3894
    Helixi392 – 3976
    Beta strandi398 – 4003
    Beta strandi404 – 4118
    Helixi416 – 4194
    Helixi420 – 43819
    Helixi442 – 45110
    Helixi456 – 4627
    Helixi463 – 4664
    Beta strandi474 – 4818
    Helixi484 – 50522
    Helixi513 – 5153
    Helixi516 – 52813
    Beta strandi530 – 5323
    Helixi540 – 55213

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP06744.
    SMRiP06744. Positions 2-557.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06744.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the GPI family.Curated

    Phylogenomic databases

    eggNOGiCOG0166.
    HOGENOMiHOG000261371.
    HOVERGENiHBG002877.
    InParanoidiP06744.
    KOiK01810.
    OrthoDBiEOG7FXZXV.
    PhylomeDBiP06744.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P06744-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MAALTRDPQF QKLQQWYREH RSELNLRRLF DANKDRFNHF SLTLNTNHGH    50
    ILVDYSKNLV TEDVMRMLVD LAKSRGVEAA RERMFNGEKI NYTEGRAVLH 100
    VALRNRSNTP ILVDGKDVMP EVNKVLDKMK SFCQRVRSGD WKGYTGKTIT 150
    DVINIGIGGS DLGPLMVTEA LKPYSSGGPR VWYVSNIDGT HIAKTLAQLN 200
    PESSLFIIAS KTFTTQETIT NAETAKEWFL QAAKDPSAVA KHFVALSTNT 250
    TKVKEFGIDP QNMFEFWDWV GGRYSLWSAI GLSIALHVGF DNFEQLLSGA 300
    HWMDQHFRTT PLEKNAPVLL ALLGIWYINC FGCETHAMLP YDQYLHRFAA 350
    YFQQGDMESN GKYITKSGTR VDHQTGPIVW GEPGTNGQHA FYQLIHQGTK 400
    MIPCDFLIPV QTQHPIRKGL HHKILLANFL AQTEALMRGK STEEARKELQ 450
    AAGKSPEDLE RLLPHKVFEG NRPTNSIVFT KLTPFMLGAL VAMYEHKIFV 500
    QGIIWDINSF DQWGVELGKQ LAKKIEPELD GSAQVTSHDA STNGLINFIK 550
    QQREARVQ 558
    Length:558
    Mass (Da):63,147
    Last modified:January 23, 2007 - v4
    Checksum:i7C8E95277BDC79A6
    GO
    Isoform 2 (identifier: P06744-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MVALCSLQHLGSSDPRALPTLPTATSGQRPAKRRRKSPAM
         135-162: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:569
    Mass (Da):64,325
    Checksum:i65537AD376C4FDF1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti158 – 1581G → V in AAA36368. 1 PublicationCurated
    Sequence conflicti426 – 4261L → V in AAF22645. (PubMed:10727272)Curated
    Sequence conflicti436 – 4361L → V in AAF22645. (PubMed:10727272)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti5 – 51T → I in HA-GPID; GPI Matsumoto. 1 Publication
    VAR_002516
    Natural varianti20 – 201H → P in HA-GPID; severe form with neurological deficits; GPI Homburg. 1 Publication
    VAR_002517
    Natural varianti75 – 751R → G in HA-GPID; GPI Elyria. 1 Publication
    VAR_002518
    Natural varianti83 – 831R → W in HA-GPID. 1 Publication
    VAR_002519
    Natural varianti101 – 1011V → M in HA-GPID; GPI Sarcina. 1 Publication
    VAR_002521
    Natural varianti159 – 1591G → S in HA-GPID. 1 Publication
    VAR_002520
    Natural varianti195 – 1951T → I in HA-GPID; GPI Bari and Mola. 1 Publication
    VAR_002522
    Natural varianti208 – 2081I → T.1 Publication
    Corresponds to variant rs8191371 [ dbSNP | Ensembl ].
    VAR_018816
    Natural varianti224 – 2241T → M in HA-GPID; GPI Iwate. 2 Publications
    Corresponds to variant rs61754634 [ dbSNP | Ensembl ].
    VAR_002523
    Natural varianti273 – 2731R → H in HA-GPID. 1 Publication
    VAR_002524
    Natural varianti278 – 2781S → L in HA-GPID. 1 Publication
    Corresponds to variant rs34306618 [ dbSNP | Ensembl ].
    VAR_002525
    Natural varianti300 – 3001A → P in HA-GPID. 1 Publication
    VAR_002526
    Natural varianti308 – 3081R → H.
    Corresponds to variant rs2230294 [ dbSNP | Ensembl ].
    VAR_033943
    Natural varianti339 – 3391L → P in HA-GPID; severe form with neurological deficits; GPI Homburg. 1 Publication
    VAR_002527
    Natural varianti343 – 3431Q → R in HA-GPID; GPI Narita and Morcone. 2 Publications
    VAR_002528
    Natural varianti347 – 3471R → C in HA-GPID; GPI Mount Scopus. 2 Publications
    VAR_002529
    Natural varianti347 – 3471R → H in HA-GPID. 1 Publication
    VAR_002530
    Natural varianti375 – 3751T → R in HA-GPID; GPI Kinki. 1 Publication
    VAR_002531
    Natural varianti389 – 3891H → R in HA-GPID; severe form; GPI Calden. 1 Publication
    VAR_002532
    Natural varianti472 – 4721R → H in HA-GPID. 1 Publication
    VAR_002533
    Natural varianti487 – 4871L → F in HA-GPID. 1 Publication
    VAR_002534
    Natural varianti495 – 4951E → K in HA-GPID. 1 Publication
    VAR_002535
    Natural varianti517 – 5171L → V in HA-GPID; severe form; GPI Calden. 1 Publication
    VAR_002536
    Natural varianti525 – 5251I → T in HA-GPID. 2 Publications
    VAR_002537
    Natural varianti539 – 5391D → N in HA-GPID; GPI Fukuoka and Kinki. 1 Publication
    VAR_002538

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MVALCSLQHLGSSDPRALPT LPTATSGQRPAKRRRKSPAM in isoform 2. 1 PublicationVSP_043475
    Alternative sequencei135 – 16228Missing in isoform 2. 1 PublicationVSP_043476Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS12437.1. [P06744-1]
    CCDS54246.1. [P06744-2]
    PIRiA35333.
    RefSeqiNP_000166.2. NM_000175.3. [P06744-1]
    NP_001171651.1. NM_001184722.1. [P06744-2]
    XP_005258821.1. XM_005258764.1. [P06744-1]
    XP_006723211.1. XM_006723148.1. [P06744-1]
    UniGeneiHs.466471.
    Hs.515344.

    Genome annotation databases

    EnsembliENST00000356487; ENSP00000348877; ENSG00000105220. [P06744-1]
    ENST00000415930; ENSP00000405573; ENSG00000105220. [P06744-2]
    GeneIDi2821.
    KEGGihsa:2821.
    UCSCiuc002nvf.3. human. [P06744-1]
    uc010xrv.2. human. [P06744-2]

    Polymorphism databases

    DMDMi17380385.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    SHMPD

    The Singapore human mutation and polymorphism database

    Wikipedia

    Phosphoglucose isomerase entry

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS12437.1. [P06744-1 ]
    CCDS54246.1. [P06744-2 ]
    PIRi A35333.
    RefSeqi NP_000166.2. NM_000175.3. [P06744-1 ]
    NP_001171651.1. NM_001184722.1. [P06744-2 ]
    XP_005258821.1. XM_005258764.1. [P06744-1 ]
    XP_006723211.1. XM_006723148.1. [P06744-1 ]
    UniGenei Hs.466471.
    Hs.515344.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1IAT X-ray 1.62 A 2-558 [» ]
    1IRI X-ray 2.40 A/B/C/D 1-558 [» ]
    1JIQ X-ray 1.90 A/B/C/D 1-558 [» ]
    1JLH X-ray 2.10 A/B/C/D 1-558 [» ]
    1NUH X-ray 2.51 A 1-558 [» ]
    ProteinModelPortali P06744.
    SMRi P06744. Positions 2-557.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109082. 19 interactions.
    IntActi P06744. 4 interactions.
    MINTi MINT-4999095.
    STRINGi 9606.ENSP00000348877.

    PTM databases

    PhosphoSitei P06744.

    Polymorphism databases

    DMDMi 17380385.

    Proteomic databases

    MaxQBi P06744.
    PaxDbi P06744.
    PeptideAtlasi P06744.
    PRIDEi P06744.

    Protocols and materials databases

    DNASUi 2821.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000356487 ; ENSP00000348877 ; ENSG00000105220 . [P06744-1 ]
    ENST00000415930 ; ENSP00000405573 ; ENSG00000105220 . [P06744-2 ]
    GeneIDi 2821.
    KEGGi hsa:2821.
    UCSCi uc002nvf.3. human. [P06744-1 ]
    uc010xrv.2. human. [P06744-2 ]

    Organism-specific databases

    CTDi 2821.
    GeneCardsi GC19P034855.
    HGNCi HGNC:4458. GPI.
    HPAi CAB018655.
    CAB040563.
    HPA024305.
    MIMi 172400. gene.
    613470. phenotype.
    neXtProti NX_P06744.
    Orphaneti 712. Hemolytic anemia due to glucophosphate isomerase deficiency.
    PharmGKBi PA28841.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0166.
    HOGENOMi HOG000261371.
    HOVERGENi HBG002877.
    InParanoidi P06744.
    KOi K01810.
    OrthoDBi EOG7FXZXV.
    PhylomeDBi P06744.
    TreeFami TF300436.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00181 .
    BioCyci MetaCyc:HS02693-MONOMER.
    Reactomei REACT_1383. Glycolysis.
    REACT_1520. Gluconeogenesis.
    SABIO-RK P06744.

    Miscellaneous databases

    ChiTaRSi GPI. human.
    EvolutionaryTracei P06744.
    GeneWikii Glucose-6-phosphate_isomerase.
    GenomeRNAii 2821.
    NextBioi 11117.
    PROi P06744.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P06744.
    Bgeei P06744.
    CleanExi HS_GPI.
    Genevestigatori P06744.

    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. 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.
      , 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.
      , 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. 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.

    Entry informationi

    Entry nameiG6PI_HUMAN
    AccessioniPrimary (citable) accession number: P06744
    Secondary accession number(s): B4DG39
    , Q9BRD3, Q9BSK5, Q9UHE6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 169 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3