Search Results

Overview

Uniprot IDP00558
Protein NamePhosphoglycerate kinase 1
Gene NamePGK1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
11 SNKLTLDKLDVKGKR
131 FHVEEEGKGKDASGN
139 GKDASGNKVKAEPAK
141 DASGNKVKAEPAKIE
146 KVKAEPAKIEAFRAS
156 AFRASLSKLGDVYVN
184 VGVNLPQKAGGFLMK
191 KAGGFLMKKELNYFA
192 AGGFLMKKELNYFAK
216 LAILGGAKVADKIQL
220 GGAKVADKIQLINNM
267 EEGAKIVKDLMSKAE
275 DLMSKAEKNGVKITL
291 VDFVTADKFDENAKT
30 VDFNVPMKNNQITNN
323 CGPESSKKYAEAVTR
353 EAFARGTKALMDEVV
361 ALMDEVVKATSRGCI
41 ITNNQRIKAAVPSIK
48 KAAVPSIKFCLDNGA
6 **MSLSNKLTLDKLD
86 EPVAVELKSLLGKDV
91 ELKSLLGKDVLFLKD
97 GKDVLFLKDCVGPEV

Function

Catalyzes one of the two ATP producing reactions in the glycolytic pathway via the reversible conversion of 1,3-diphosphoglycerate to 3-phosphoglycerate (PubMed:30323285, PubMed:7391028). Both L- and D- forms of purine and pyrimidine nucleotides can be used as substrates, but the activity is much lower on pyrimidines (PubMed:18463139). In addition to its role as a glycolytic enzyme, it seems that PGK1 acts as a polymerase alpha cofactor protein (primer recognition protein) (PubMed:2324090). Acts as a protein kinase when localized to the mitochondrion where it phosphorylates pyruvate dehydrogenase kinase PDK1 to inhibit pyruvate dehydrogenase complex activity and suppress the formation of acetyl-coenzyme A from pyruvate, and consequently inhibit oxidative phosphorylation and promote glycolysis (PubMed:26942675, PubMed:36849569). May play a role in sperm motility (PubMed:26677959)

Protein Sequence

10 MSLSNKLTLD 20 KLDVKGKRVV 30 MRVDFNVPMK 40 NNQITNNQRI 50 KAAVPSIKFC 60 LDNGAKSVVL 70 MSHLGRPDGV 80 PMPDKYSLEP 90 VAVELKSLLG 100 KDVLFLKDCV 110 GPEVEKACAN 120 PAAGSVILLE 130 NLRFHVEEEG 140 KGKDASGNKV 150 KAEPAKIEAF 160 RASLSKLGDV 170 YVNDAFGTAH 180 RAHSSMVGVN 190 LPQKAGGFLM 200 KKELNYFAKA 210 LESPERPFLA 220 ILGGAKVADK 230 IQLINNMLDK 240 VNEMIIGGGM 250 AFTFLKVLNN 260 MEIGTSLFDE 270 EGAKIVKDLM 280 SKAEKNGVKI 290 TLPVDFVTAD 300 KFDENAKTGQ 310 ATVASGIPAG 320 WMGLDCGPES 330 SKKYAEAVTR 340 AKQIVWNGPV 350 GVFEWEAFAR 360 GTKALMDEVV 370 KATSRGCITI 380 IGGGDTATCC 390 AKWNTEDKVS 400 HVSTGGGASL 410 ELLEGKVLPG VDALSNI

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005615 extracellular space
Cellular Component GO:0016020 membrane
Cellular Component GO:0045121 membrane raft
Cellular Component GO:0005759 mitochondrial matrix
Molecular Function GO:0043531 ADP binding
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0046872 metal ion binding
Molecular Function GO:0004618 phosphoglycerate kinase activity
Molecular Function GO:0106310 protein serine kinase activity
Molecular Function GO:0004674 protein serine/threonine kinase activity
Molecular Function GO:0047134 protein-disulfide reductase [NAD(P)H] activity
Molecular Function GO:0044325 transmembrane transporter binding
Biological Process GO:0061621 canonical glycolysis
Biological Process GO:0071456 cellular response to hypoxia
Biological Process GO:0030855 epithelial cell differentiation
Biological Process GO:0006094 gluconeogenesis
Biological Process GO:0006096 glycolytic process
Biological Process GO:0016525 negative regulation of angiogenesis
Biological Process GO:0160218 negative regulation of pyruvate decarboxylation to acetyl-CoA
Biological Process GO:0031639 plasminogen activation

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] 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.

[3] 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.

[4] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.

[5] 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.

[6] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[7] 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.

[8] 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.

[9] 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.

[10] 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.