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P06744

- G6PI_HUMAN

UniProt

P06744 - G6PI_HUMAN

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Protein
Glucose-6-phosphate isomerase
Gene
GPI
Organism
Homo sapiens (Human)
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.3 Publications

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei358 – 3581Proton donor3 Publications
Active sitei389 – 38913 Publications
Active sitei519 – 51913 Publications

GO - Molecular functioni

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

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
Complete GO annotation...

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. 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. neuron projection Source: Ensembl
  6. nucleus Source: HPA
  7. plasma membrane Source: HPA
Complete GO annotation...

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.6 Publications
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 – 11Removed1 Publication
Chaini2 – 558557Glucose-6-phosphate isomeraseUniRule annotation
PRO_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.UniRule annotation
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.1 Publication

Protein-protein interaction databases

BioGridi109082. 18 interactions.
IntActiP06744. 4 interactions.
MINTiMINT-4999095.
STRINGi9606.ENSP00000348877.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP06744.

Family & Domainsi

Sequence similaritiesi

Belongs to the GPI family.

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

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.
VSP_043475
Alternative sequencei135 – 16228Missing in isoform 2.
VSP_043476Add
BLAST

Sequence conflict

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

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...

Protein-protein interaction databases

BioGridi 109082. 18 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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 168 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

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