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Protein

Glucose-6-phosphate isomerase

Gene

GPI

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.2 Publications

Catalytic activityi

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

Pathway:iglycolysis

This protein is involved in step 2 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Glucose-6-phosphate isomerase, Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase
  3. ATP-dependent 6-phosphofructokinase (PFKM), ATP-dependent 6-phosphofructokinase, liver type (PFKL), ATP-dependent 6-phosphofructokinase, muscle type (PFKM), ATP-dependent 6-phosphofructokinase, platelet type (PFKP)
  4. Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (ALDOB), Fructose-bisphosphate aldolase (ALDOB), Fructose-bisphosphate aldolase (ALDOC), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (ALDOC), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (ALDOA), Fructose-bisphosphate aldolase (ALDOA), Fructose-bisphosphate aldolase C (ALDOC), Fructose-bisphosphate aldolase (HEL-S-87p), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (ALDOC), Fructose-bisphosphate aldolase (ALDOC), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (ALDOB), Fructose-bisphosphate aldolase (ALDOB), Fructose-bisphosphate aldolase (ALDOA), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (ALDOA), Fructose-bisphosphate aldolase (ALDOA), Fructose-bisphosphate aldolase (ALDOC), Fructose-bisphosphate aldolase (ALDOC), Fructose-bisphosphate aldolase (ALDOA), Fructose-bisphosphate aldolase (ALDOA), Fructose-bisphosphate aldolase (ALDOA), Fructose-bisphosphate aldolase B (ALDOB), Fructose-bisphosphate aldolase (ALDOA), Fructose-bisphosphate aldolase (ALDOA), Fructose-bisphosphate aldolase A (ALDOA), Fructose-bisphosphate aldolase (ALDOC), Fructose-bisphosphate aldolase (ALDOC), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (ALDOC)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose, the pathway glycolysis and in Carbohydrate degradation.

Sites

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Cytokine, Growth factor, Isomerase

Keywords - Biological processi

Angiogenesis, Gluconeogenesis, Glycolysis

Enzyme and pathway databases

BioCyciMetaCyc:HS02693-MONOMER.
BRENDAi5.3.1.9. 2681.
ReactomeiREACT_1383. Glycolysis.
REACT_1520. Gluconeogenesis.
REACT_355377. TP53 Regulates Metabolic Genes.
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 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:4458. GPI.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB-KW
  • membrane Source: UniProtKB
  • neuron projection Source: Ensembl
  • nucleoplasm Source: HPA
  • 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)

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA form of anemia in which there is no abnormal hemoglobin or spherocytosis. It is caused by glucose phosphate isomerase deficiency.

See also OMIM:613470
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.

Polymorphism and mutation databases

BioMutaiGPI.
DMDMi17380385.

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 – 1091Phosphothreonine3 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.2 Publications
ISGylated.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP06744.
PaxDbiP06744.
PeptideAtlasiP06744.
PRIDEiP06744.

PTM databases

PhosphoSiteiP06744.

Expressioni

Gene expression databases

BgeeiP06744.
CleanExiHS_GPI.
ExpressionAtlasiP06744. baseline and differential.
GenevisibleiP06744. HS.

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. 20 interactions.
IntActiP06744. 4 interactions.
MINTiMINT-4999095.

Structurei

Secondary structure

1
558
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 64Combined sources
Helixi8 – 2013Combined sources
Helixi21 – 233Combined sources
Helixi26 – 327Combined sources
Helixi36 – 394Combined sources
Beta strandi41 – 455Combined sources
Beta strandi50 – 545Combined sources
Beta strandi57 – 593Combined sources
Helixi62 – 7413Combined sources
Helixi77 – 859Combined sources
Turni92 – 954Combined sources
Helixi100 – 1034Combined sources
Beta strandi116 – 1183Combined sources
Helixi119 – 13719Combined sources
Beta strandi151 – 1555Combined sources
Helixi158 – 1603Combined sources
Helixi162 – 1709Combined sources
Helixi172 – 1743Combined sources
Beta strandi180 – 1845Combined sources
Helixi189 – 1968Combined sources
Helixi201 – 2033Combined sources
Beta strandi204 – 2096Combined sources
Beta strandi211 – 2133Combined sources
Helixi216 – 23318Combined sources
Helixi236 – 2383Combined sources
Helixi239 – 2424Combined sources
Beta strandi243 – 2486Combined sources
Helixi250 – 2567Combined sources
Helixi260 – 2623Combined sources
Beta strandi263 – 2653Combined sources
Helixi272 – 2743Combined sources
Turni276 – 2783Combined sources
Helixi279 – 2813Combined sources
Helixi282 – 2887Combined sources
Helixi290 – 30920Combined sources
Helixi312 – 3143Combined sources
Helixi316 – 32914Combined sources
Beta strandi335 – 3417Combined sources
Helixi343 – 3453Combined sources
Helixi348 – 36013Combined sources
Beta strandi378 – 3803Combined sources
Helixi386 – 3894Combined sources
Helixi392 – 3976Combined sources
Beta strandi398 – 4003Combined sources
Beta strandi404 – 4118Combined sources
Helixi416 – 4194Combined sources
Helixi420 – 43819Combined sources
Helixi442 – 45110Combined sources
Helixi456 – 4627Combined sources
Helixi463 – 4664Combined sources
Beta strandi474 – 4818Combined sources
Helixi484 – 50522Combined sources
Helixi513 – 5153Combined sources
Helixi516 – 52813Combined sources
Beta strandi530 – 5323Combined sources
Helixi540 – 55213Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000000707.
HOGENOMiHOG000261370.
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. AlignAdd to basket

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

        10         20         30         40         50
MAALTRDPQF QKLQQWYREH RSELNLRRLF DANKDRFNHF SLTLNTNHGH
60 70 80 90 100
ILVDYSKNLV TEDVMRMLVD LAKSRGVEAA RERMFNGEKI NYTEGRAVLH
110 120 130 140 150
VALRNRSNTP ILVDGKDVMP EVNKVLDKMK SFCQRVRSGD WKGYTGKTIT
160 170 180 190 200
DVINIGIGGS DLGPLMVTEA LKPYSSGGPR VWYVSNIDGT HIAKTLAQLN
210 220 230 240 250
PESSLFIIAS KTFTTQETIT NAETAKEWFL QAAKDPSAVA KHFVALSTNT
260 270 280 290 300
TKVKEFGIDP QNMFEFWDWV GGRYSLWSAI GLSIALHVGF DNFEQLLSGA
310 320 330 340 350
HWMDQHFRTT PLEKNAPVLL ALLGIWYINC FGCETHAMLP YDQYLHRFAA
360 370 380 390 400
YFQQGDMESN GKYITKSGTR VDHQTGPIVW GEPGTNGQHA FYQLIHQGTK
410 420 430 440 450
MIPCDFLIPV QTQHPIRKGL HHKILLANFL AQTEALMRGK STEEARKELQ
460 470 480 490 500
AAGKSPEDLE RLLPHKVFEG NRPTNSIVFT KLTPFMLGAL VAMYEHKIFV
510 520 530 540 550
QGIIWDINSF DQWGVELGKQ LAKKIEPELD GSAQVTSHDA STNGLINFIK

QQREARVQ
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 (Ref. 1) Curated
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:
EMBLi
GenBanki
DDBJi
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.
ENST00000415930; ENSP00000405573; ENSG00000105220. [P06744-2]
GeneIDi2821.
KEGGihsa:2821.
UCSCiuc002nvf.3. human. [P06744-1]
uc010xrv.2. human. [P06744-2]

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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi109082. 20 interactions.
IntActiP06744. 4 interactions.
MINTiMINT-4999095.

PTM databases

PhosphoSiteiP06744.

Polymorphism and mutation databases

BioMutaiGPI.
DMDMi17380385.

Proteomic databases

MaxQBiP06744.
PaxDbiP06744.
PeptideAtlasiP06744.
PRIDEiP06744.

Protocols and materials databases

DNASUi2821.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2821.
GeneCardsiGC19P034855.
HGNCiHGNC:4458. GPI.
HPAiCAB018655.
CAB040563.
HPA024305.
MIMi172400. gene.
613470. phenotype.
neXtProtiNX_P06744.
Orphaneti712. Hemolytic anemia due to glucophosphate isomerase deficiency.
PharmGKBiPA28841.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0166.
GeneTreeiENSGT00390000000707.
HOGENOMiHOG000261370.
HOVERGENiHBG002877.
InParanoidiP06744.
KOiK01810.
OrthoDBiEOG7FXZXV.
PhylomeDBiP06744.
TreeFamiTF300436.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00181.
BioCyciMetaCyc:HS02693-MONOMER.
BRENDAi5.3.1.9. 2681.
ReactomeiREACT_1383. Glycolysis.
REACT_1520. Gluconeogenesis.
REACT_355377. TP53 Regulates Metabolic Genes.
SABIO-RKP06744.

Miscellaneous databases

ChiTaRSiGPI. human.
EvolutionaryTraceiP06744.
GeneWikiiGlucose-6-phosphate_isomerase.
GenomeRNAii2821.
NextBioi11117.
PROiP06744.
SOURCEiSearch...

Gene expression databases

BgeeiP06744.
CleanExiHS_GPI.
ExpressionAtlasiP06744. baseline and differential.
GenevisibleiP06744. HS.

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]
ProtoNetiSearch...

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], CLEAVAGE OF INITIATOR METHIONINE [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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-109, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  22. "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.
  23. "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.
  24. "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.
  25. "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.
  26. "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.
  27. "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.
  28. "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.
  29. "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.
  30. "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.
  31. "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: July 22, 2015
This is version 179 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.