P06744 (G6PI_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glucose-6-phosphate isomerase
Short name=GPI
EC=5.3.1.9

Alternative name(s):
Autocrine motility factor
Short name=AMF
Neuroleukin
Short name=NLK
Phosphoglucose isomerase
Short name=PGI
Phosphohexose isomerase
Short name=PHI
Sperm antigen 36
Short name=SA-36

Gene names

Name:

GPI

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	558 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Besides it's role as a glycolytic enzyme, mammalian GPI can function as a tumor-secreted cytokine and an angiogenic factor (AMF) that stimulates endothelial cell motility. GPI is also a neurotrophic factor (Neuroleukin) for spinal and sensory neurons. Ref.10 Ref.11 Ref.12
Catalytic activity	D-glucose 6-phosphate = D-fructose 6-phosphate.
Pathway	Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4.
Subunit structure	Homodimer in the catalytically active form, monomer in the secreted form. Ref.20
Subcellular location	Cytoplasm. Secreted Ref.11.
Post-translational modification	Phosphorylation at Ser-185 by CK2 has been shown to decrease enzymatic activity and may contribute to secretion by a non-classical secretory pathway. ISGylated. Ref.13
Involvement in disease	Hemolytic anemia, non-spherocytic, due to glucose phosphate isomerase deficiency (HA-GPID) [MIM:613470]: A form of anemia in which there is no abnormal hemoglobin or spherocytosis. It is caused by glucose phosphate isomerase deficiency. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29
Sequence similarities	Belongs to the GPI family.

Ontologies

Keywords
Biological process	Angiogenesis Gluconeogenesis Glycolysis
Cellular component	Cytoplasm Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Hereditary hemolytic anemia
Molecular function	Cytokine Growth factor Isomerase
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	aldehyde catabolic process Inferred from electronic annotation. Source: Compara angiogenesis Inferred from electronic annotation. Source: UniProtKB-KW gluconeogenesis Traceable author statement. Source: Reactome glucose 6-phosphate metabolic process Inferred from electronic annotation. Source: Compara glycolysis Traceable author statement. Source: Reactome hemostasis Traceable author statement PubMed 7435496. Source: ProtInc humoral immune response Traceable author statement PubMed 3020690. Source: ProtInc learning or memory Inferred from electronic annotation. Source: Compara methylglyoxal biosynthetic process Inferred from electronic annotation. Source: Compara negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of neuron apoptotic process Inferred from electronic annotation. Source: Compara small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome extracellular space Inferred from electronic annotation. Source: UniProtKB-KW neuron projection Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay. Source: HPA plasma membrane Inferred from direct assay. Source: HPA
Molecular_function	glucose-6-phosphate isomerase activity Traceable author statement. Source: Reactome intramolecular transferase activity Inferred from electronic annotation. Source: Compara monosaccharide binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P06744-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P06744-2)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.8

Chain

2 – 558

557

Glucose-6-phosphate isomerase

PRO_0000180537

Sites

Active site

358

1

Proton donor Ref.20 Ref.22 Ref.23

Active site

389

1

Ref.20 Ref.22 Ref.23

Active site

519

1

Ref.20 Ref.22 Ref.23

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.8

Modified residue

12

1

N6-acetyllysine Ref.17

Modified residue

109

1

Phosphothreonine Ref.15 Ref.16

Modified residue

142

1

N6-acetyllysine Ref.17

Modified residue

185

1

Phosphoserine; by CK2 Ref.10 Ref.14

Modified residue

454

1

N6-malonyllysine Ref.19

Natural variations

Alternative sequence

1

1

M → MVALCSLQHLGSSDPRALPT LPTATSGQRPAKRRRKSPAM in isoform 2.

VSP_043475

Alternative sequence

135 – 162

28

Missing in isoform 2.

VSP_043476

Natural variant

5

1

T → I in HA-GPID; GPI Matsumoto. Ref.27

VAR_002516

Natural variant

20

1

H → P in HA-GPID; severe form with neurological deficits; GPI Homburg. Ref.29

VAR_002517

Natural variant

75

1

R → G in HA-GPID; GPI Elyria. Ref.28

VAR_002518

Natural variant

83

1

R → W in HA-GPID. Ref.25

VAR_002519

Natural variant

101

1

V → M in HA-GPID; GPI Sarcina. Ref.26

VAR_002521

Natural variant

159

1

G → S in HA-GPID. Ref.24

VAR_002520

Natural variant

195

1

T → I in HA-GPID; GPI Bari and Mola. Ref.26

VAR_002522

Natural variant

208

1

I → T. Ref.3
Corresponds to variant rs8191371 [ dbSNP | Ensembl ].

VAR_018816

Natural variant

224

1

T → M in HA-GPID; GPI Iwate. Ref.25 Ref.27

VAR_002523

Natural variant

273

1

R → H in HA-GPID. Ref.25

VAR_002524

Natural variant

278

1

S → L in HA-GPID. Ref.25
Corresponds to variant rs34306618 [ dbSNP | Ensembl ].

VAR_002525

Natural variant

300

1

A → P in HA-GPID. Ref.28

VAR_002526

Natural variant

308

1

R → H.
Corresponds to variant rs2230294 [ dbSNP | Ensembl ].

VAR_033943

Natural variant

339

1

L → P in HA-GPID; severe form with neurological deficits; GPI Homburg. Ref.29

VAR_002527

Natural variant

343

1

Q → R in HA-GPID; GPI Narita and Morcone. Ref.26 Ref.27

VAR_002528

Natural variant

347

1

R → C in HA-GPID; GPI Mount Scopus. Ref.25 Ref.28

VAR_002529

Natural variant

347

1

R → H in HA-GPID. Ref.24

VAR_002530

Natural variant

375

1

T → R in HA-GPID; GPI Kinki. Ref.27

VAR_002531

Natural variant

389

1

H → R in HA-GPID; severe form; GPI Calden. Ref.29

VAR_002532

Natural variant

472

1

R → H in HA-GPID. Ref.28

VAR_002533

Natural variant

487

1

L → F in HA-GPID. Ref.25

VAR_002534

Natural variant

495

1

E → K in HA-GPID. Ref.25

VAR_002535

Natural variant

517

1

L → V in HA-GPID; severe form; GPI Calden. Ref.29

VAR_002536

Natural variant

525

1

I → T in HA-GPID. Ref.24 Ref.26

VAR_002537

Natural variant

539

1

D → N in HA-GPID; GPI Fukuoka and Kinki. Ref.27

VAR_002538

Experimental info

Mutagenesis

185

1

S → A: Retained full enzymatic activity. Ref.14

Mutagenesis

185

1

S → E: Decreased enzymatic activity. Ref.14

Sequence conflict

158

1

G → V in AAA36368. Ref.1

Sequence conflict

426

1

L → V in AAF22645. Ref.2

Sequence conflict

436

1

L → V in AAF22645. Ref.2

Secondary structure

1

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558

Helix Strand Turn

Details...

Helix

3 – 6

4

Helix

8 – 20

13

Helix

21 – 23

3

Helix

26 – 32

7

Helix

36 – 39

4

Beta strand

41 – 45

5

Beta strand

50 – 54

5

Beta strand

57 – 59

3

Helix

62 – 74

13

Helix

77 – 85

9

Turn

92 – 95

4

Helix

100 – 103

4

Beta strand

116 – 118

3

Helix

119 – 137

19

Beta strand

151 – 155

5

Helix

158 – 160

3

Helix

162 – 170

9

Helix

172 – 174

3

Beta strand

180 – 184

5

Helix

189 – 196

8

Helix

201 – 203

3

Beta strand

204 – 209

6

Beta strand

211 – 213

3

Helix

216 – 233

18

Helix

236 – 238

3

Helix

239 – 242

4

Beta strand

243 – 248

6

Helix

250 – 256

7

Helix

260 – 262

3

Beta strand

263 – 265

3

Helix

272 – 274

3

Turn

276 – 278

3

Helix

279 – 281

3

Helix

282 – 288

7

Helix

290 – 309

20

Helix

312 – 314

3

Helix

316 – 329

14

Beta strand

335 – 341

7

Helix

343 – 345

3

Helix

348 – 360

13

Beta strand

378 – 380

3

Helix

386 – 389

4

Helix

392 – 397

6

Beta strand

398 – 400

3

Beta strand

404 – 411

8

Helix

416 – 419

4

Helix

420 – 438

19

Helix

442 – 451

10

Helix

456 – 462

7

Helix

463 – 466

4

Beta strand

474 – 481

8

Helix

484 – 505

22

Helix

513 – 515

3

Helix

516 – 528

13

Beta strand

530 – 532

3

Helix

540 – 552

13

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 7C8E95277BDC79A6	FASTA	558	63,147
	10 20 30 40 50 60 MAALTRDPQF QKLQQWYREH RSELNLRRLF DANKDRFNHF SLTLNTNHGH ILVDYSKNLV 70 80 90 100 110 120 TEDVMRMLVD LAKSRGVEAA RERMFNGEKI NYTEGRAVLH VALRNRSNTP ILVDGKDVMP 130 140 150 160 170 180 EVNKVLDKMK SFCQRVRSGD WKGYTGKTIT DVINIGIGGS DLGPLMVTEA LKPYSSGGPR 190 200 210 220 230 240 VWYVSNIDGT HIAKTLAQLN PESSLFIIAS KTFTTQETIT NAETAKEWFL QAAKDPSAVA 250 260 270 280 290 300 KHFVALSTNT TKVKEFGIDP QNMFEFWDWV GGRYSLWSAI GLSIALHVGF DNFEQLLSGA 310 320 330 340 350 360 HWMDQHFRTT PLEKNAPVLL ALLGIWYINC FGCETHAMLP YDQYLHRFAA YFQQGDMESN 370 380 390 400 410 420 GKYITKSGTR VDHQTGPIVW GEPGTNGQHA FYQLIHQGTK MIPCDFLIPV QTQHPIRKGL 430 440 450 460 470 480 HHKILLANFL AQTEALMRGK STEEARKELQ AAGKSPEDLE RLLPHKVFEG NRPTNSIVFT 490 500 510 520 530 540 KLTPFMLGAL VAMYEHKIFV QGIIWDINSF DQWGVELGKQ LAKKIEPELD GSAQVTSHDA 550 STNGLINFIK QQREARVQ
	Isoform 2 [UniParc]. Checksum: 65537AD376C4FDF1	FASTA	569	64,325
	10 20 30 40 50 60 MVALCSLQHL GSSDPRALPT LPTATSGQRP AKRRRKSPAM AALTRDPQFQ KLQQWYREHR 70 80 90 100 110 120 SELNLRRLFD ANKDRFNHFS LTLNTNHGHI LVDYSKNLVT EDVMRMLVDL AKSRGVEAAR 130 140 150 160 170 180 ERMFNGEKIN YTEGRAVLHV ALRNRSNTPI LVDGKDVMPE VNKVLDKMKS FCQGPLMVTE 190 200 210 220 230 240 ALKPYSSGGP RVWYVSNIDG THIAKTLAQL NPESSLFIIA SKTFTTQETI TNAETAKEWF 250 260 270 280 290 300 LQAAKDPSAV AKHFVALSTN TTKVKEFGID PQNMFEFWDW VGGRYSLWSA IGLSIALHVG 310 320 330 340 350 360 FDNFEQLLSG AHWMDQHFRT TPLEKNAPVL LALLGIWYIN CFGCETHAML PYDQYLHRFA 370 380 390 400 410 420 AYFQQGDMES NGKYITKSGT RVDHQTGPIV WGEPGTNGQH AFYQLIHQGT KMIPCDFLIP 430 440 450 460 470 480 VQTQHPIRKG LHHKILLANF LAQTEALMRG KSTEEARKEL QAAGKSPEDL ERLLPHKVFE 490 500 510 520 530 540 GNRPTNSIVF TKLTPFMLGA LVAMYEHKIF VQGIIWDINS FDQWGVELGK QLAKKIEPEL 550 560 DGSAQVTSHD ASTNGLINFI KQQREARVQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Gurney M.E. Submitted (MAR-1987) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Cloning of a glucose phosphate isomerase/neuroleukin-like sperm antigen involved in sperm agglutination." Yakirevich E., Naot Y. Biol. Reprod. 62:1016-1023(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Testis.
[3]	NIEHS SNPs program Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-208.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , 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, 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, CYTOKINE AND ANGIOGENIC FUNCTIONS.
[12]	"Species specificity of the cytokine function of phosphoglucose isomerase." Amraei M., Nabi I.R. FEBS Lett. 525:151-155(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SPECIES SPECIFICITY OF THE CYTOKINE FUNCTION.
[13]	"Proteomic identification of proteins conjugated to ISG15 in mouse and human cells." Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E. Biochem. Biophys. Res. Commun. 336:496-506(2005) [PubMed] [Europe PMC] [Abstract] Cited for: ISGYLATION.
[14]	"Differential regulation of phosphoglucose isomerase/autocrine motility factor activities by protein kinase CK2 phosphorylation." Yanagawa T., Funasaka T., Tsutsumi S., Raz T., Tanaka N., Raz A. J. Biol. Chem. 280:10419-10426(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-185, MUTAGENESIS OF SER-185.
[15]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-109, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[17]	"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, MASS SPECTROMETRY.
[18]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]	"The first identification of lysine malonylation substrates and its regulatory enzyme." Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y., He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C., Dai J., Verdin E., Ye Y., Zhao Y. Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011) [PubMed] [Europe PMC] [Abstract] Cited for: MALONYLATION AT LYS-454.
[20]	"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.
[21]	"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.
[22]	"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.
[23]	"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.
[24]	"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.
[25]	"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.
[26]	"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.
[27]	"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.
[28]	"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.
[29]	"Molecular basis of neurological dysfunction coupled with haemolytic anaemia in human glucose-6-phosphate isomerase (GPI) deficiency." Kugler W., Breme K., Laspe P., Muirhead H., Davies C., Winkler H., Schroter W., Lakomek M. Hum. Genet. 103:450-454(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HA-GPID PRO-20; PRO-339; ARG-389 AND VAL-517.
+	Additional computationally mapped references.

Web resources

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Phosphoglucose isomerase entry

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

K03515 mRNA. Translation: AAA36368.1.
AF187554 mRNA. Translation: AAF22645.1.
AY324386 Genomic DNA. Translation: AAP72966.1.
AK294396 mRNA. Translation: BAG57650.1.
AC010504 Genomic DNA. No translation available.
AC092073 Genomic DNA. No translation available.
BC004982 mRNA. Translation: AAH04982.1.
AH002710 Genomic DNA. Translation: AAA52593.1.

IPI

IPI00027497.
IPI00910781.

PIR

A35333.

RefSeq

NP_000166.2. NM_000175.3.
NP_001171651.1. NM_001184722.1.

UniGene

Hs.466471.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P06744.

ModBase

Search...

Protein-protein interaction databases

IntAct

P06744. 4 interactions.

STRING

9606.ENSP00000348877.

PTM databases

PhosphoSite

P06744.

Polymorphism databases

DMDM

17380385.

Proteomic databases

PaxDb

P06744.

PeptideAtlas

P06744.

PRIDE

P06744.

Protocols and materials databases

DNASU

2821.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000356487; ENSP00000348877; ENSG00000105220.
ENST00000415930; ENSP00000405573; ENSG00000105220.
ENST00000588991; ENSP00000465858; ENSG00000105220.

GeneID

2821.

KEGG

hsa:2821.

UCSC

uc002nvf.3. human.

Organism-specific databases

CTD

2821.

GeneCards

GC19P034855.

HGNC

HGNC:4458. GPI.

HPA

CAB018655.
CAB040563.
HPA024305.

MIM

172400. gene.
613470. phenotype.

neXtProt

NX_P06744.

Orphanet

712. Hemolytic anemia due to glucophosphate isomerase deficiency.

PharmGKB

PA28841.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0166.

HOGENOM

HOG000261371.

HOVERGEN

HBG002877.

InParanoid

P06744.

KO

K01810.

OMA

LKMHFVS.

PhylomeDB

P06744.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

SABIO-RK

P06744.

UniPathway

UPA00109; UER00181.

Gene expression databases

ArrayExpress

P06744.

Bgee

P06744.

CleanEx

HS_GPI.

Genevestigator

P06744.

GermOnline

ENSG00000105220. Homo sapiens.

Family and domain databases

Gene3D

1.10.1390.10. 1 hit.

InterPro

IPR001672. G6P_Isomerase.
IPR023096. G6P_Isomerase_C.
IPR018189. Phosphoglucose_isomerase_CS.
[Graphical view]

PANTHER

PTHR11469. PTHR11469. 1 hit.

Pfam

PF00342. PGI. 1 hit.
[Graphical view]

PRINTS

PR00662. G6PISOMERASE.

PROSITE

PS00765. P_GLUCOSE_ISOMERASE_1. 1 hit.
PS00174. P_GLUCOSE_ISOMERASE_2. 1 hit.
PS51463. P_GLUCOSE_ISOMERASE_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

GPI. human.

EvolutionaryTrace

P06744.

GenomeRNAi

2821.

NextBio

11117.

SOURCE

Search...

Entry information

Entry name

G6PI_HUMAN

Accession

Primary (citable) accession number: P06744
Secondary accession number(s): B4DG39 , Q9BRD3, Q9BSK5, Q9UHE6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 154 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.