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Overview

Uniprot IDP06744
Protein NameGlucose-6-phosphate isomerase
Gene NameGPI
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
116 TPILVDGKDVMPEVN
12 TRDPQFQKLQQWYRE
234 EWFLQAAKDPSAVAK
241 KDPSAVAKHFVALST
252 ALSTNTTKVKEFGID
34 RRLFDANKDRFNHFS
362 GDMESNGKYITKSGT
366 SNGKYITKSGTRVDH
423 IRKGLHHKILLANFL
447 KSTEEARKELQAAGK
454 KELQAAGKSPEDLER
466 LERLLPHKVFEGNRP
73 RMLVDLAKSRGVEAA
89 ERMFNGEKINYTEGR

Function

Isomerase that catalyzes the conversion of alpha-D-glucose-6-phosphate to beta-D-fructose-6-phosphate, the second step in glycolysis, and the reverse reaction in gluconeogenesis, within the cytoplasm (PubMed:28803808). Also shows C2-epimerase activity, interconverting D-glucose-6-phosphate (G6P) and D-mannose-6-phosphate (M6P) (By similarity). Also displays anomerase activity, interconverting alpha and beta-anomeric forms of G6P, D-fructose-6-phosphate and M6P (By similarity). In addition to its metabolic role, this enzyme functions extracellularly as a cytokine: acts as autocrine motility factor (AMF), a secreted angiogenic factor that enhances endothelial cell motility (PubMed:11437381). Functions as neuroleukin, a neurotrophic factor supporting the survival of spinal and sensory neurons (PubMed:11004567, PubMed:3352745). Released by lectin-stimulated T-cells to induce immunoglobulin secretion (PubMed:11004567, PubMed:3352745)

Protein Sequence

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

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005576 extracellular region
Cellular Component GO:1904813 ficolin-1-rich granule lumen
Cellular Component GO:0016020 membrane
Cellular Component GO:0034774 secretory granule lumen
Molecular Function GO:0097367 carbohydrate derivative binding
Molecular Function GO:0005125 cytokine activity
Molecular Function GO:0047938 glucose-6-phosphate 1-epimerase activity
Molecular Function GO:0004347 glucose-6-phosphate isomerase activity
Molecular Function GO:0008083 growth factor activity
Molecular Function GO:0048029 monosaccharide binding
Molecular Function GO:0016857 racemase and epimerase activity, acting on carbohydrates and derivatives
Molecular Function GO:0031625 ubiquitin protein ligase binding
Biological Process GO:0005975 carbohydrate metabolic process
Biological Process GO:0006002 fructose 6-phosphate metabolic process
Biological Process GO:0006094 gluconeogenesis
Biological Process GO:0051156 glucose 6-phosphate metabolic process
Biological Process GO:0006096 glycolytic process
Biological Process GO:0007599 hemostasis
Biological Process GO:0006959 humoral immune response
Biological Process GO:0007611 learning or memory
Biological Process GO:0043066 negative regulation of apoptotic process
Biological Process GO:0010595 positive regulation of endothelial cell migration
Biological Process GO:0002639 positive regulation of immunoglobulin production
Biological Process GO:0046686 response to cadmium ion
Biological Process GO:0032355 response to estradiol
Biological Process GO:0035902 response to immobilization stress
Biological Process GO:0035994 response to muscle stretch
Biological Process GO:0032570 response to progesterone
Biological Process GO:0033574 response to testosterone

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[3] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.

[4] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[5] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[6] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[7] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.