Search Results

Overview

Uniprot ID	P04075
Protein Name	Fructose-bisphosphate aldolase A
Gene Name	ALDOA
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
101	FPQVIKSKGGVVGIK
108	KGGVVGIKVDKGVVP
13	PALTPEQKKELSDIA
14	ALTPEQKKELSDIAH
140	ERCAQYKKDGADFAK
147	KDGADFAKWRCVLKI
200	PDGDHDLKRCQYVTE
208	RCQYVTEKVLAAVYK
230	YLEGTLLKPNMVTPG
28	HRIVAPGKGILAADE
312	ALQASALKAWGGKKE
322	GGKKENLKAAQEEYV
330	AAQEEYVKRALANSL
342	NSLACQGKYTPSGQA
42	ESTGSIAKRLQSIGT
87	FHETLYQKADDGRPF
99	RPFPQVIKSKGGVVG

Function

Catalyzes the reversible conversion of beta-D-fructose 1,6-bisphosphate (FBP) into two triose phosphate and plays a key role in glycolysis and gluconeogenesis (PubMed:14766013). In addition, also functions as a scaffolding protein (By similarity). In response to glucose deprivation, FBP dissociates from aldolase and acts as an adapter that promotes AMP-activated protein kinase (AMPK) activity: mechanistically, associates with transient receptor potential channels TrpV (TRPV1-TRPV4), promoting inhibition of the V-ATPase complex on lysosomes and AMPK activation via the AXIN1-STK11/LKB1 axis (By similarity)

Protein Sequence

10 MPYQYPALTP 20 EQKKELSDIA 30 HRIVAPGKGI 40 LAADESTGSI 50 AKRLQSIGTE 60 NTEENRRFYR 70 QLLLTADDRV 80 NPCIGGVILF 90 HETLYQKADD 100 GRPFPQVIKS 110 KGGVVGIKVD 120 KGVVPLAGTN 130 GETTTQGLDG 140 LSERCAQYKK 150 DGADFAKWRC 160 VLKIGEHTPS 170 ALAIMENANV 180 LARYASICQQ 190 NGIVPIVEPE 200 ILPDGDHDLK 210 RCQYVTEKVL 220 AAVYKALSDH 230 HIYLEGTLLK 240 PNMVTPGHAC 250 TQKFSHEEIA 260 MATVTALRRT 270 VPPAVTGITF 280 LSGGQSEEEA 290 SINLNAINKC 300 PLLKPWALTF 310 SYGRALQASA 320 LKAWGGKKEN 330 LKAAQEEYVK 340 RALANSLACQ 350 GKYTPSGQAG 360 AAASESLFVS NHAY

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0016020	membrane
Cellular Component	GO:0005634	nucleus
Cellular Component	GO:0031093	platelet alpha granule lumen
Cellular Component	GO:0034774	secretory granule lumen
Cellular Component	GO:0061827	sperm head
Cellular Component	GO:1904724	tertiary granule lumen
Molecular Function	GO:0003779	actin binding
Molecular Function	GO:0045296	cadherin binding
Molecular Function	GO:0008092	cytoskeletal protein binding
Molecular Function	GO:0070061	fructose binding
Molecular Function	GO:0004332	fructose-bisphosphate aldolase activity
Molecular Function	GO:0042802	identical protein binding
Molecular Function	GO:0003723	RNA binding
Molecular Function	GO:0015631	tubulin binding
Biological Process	GO:0007015	actin filament organization
Biological Process	GO:0006754	ATP biosynthetic process
Biological Process	GO:0007339	binding of sperm to zona pellucida
Biological Process	GO:0061621	canonical glycolysis
Biological Process	GO:0030388	fructose 1,6-bisphosphate metabolic process
Biological Process	GO:0006000	fructose metabolic process
Biological Process	GO:0006096	glycolytic process
Biological Process	GO:0046716	muscle cell cellular homeostasis
Biological Process	GO:0035774	positive regulation of insulin secretion involved in cellular response to glucose stimulus
Biological Process	GO:0051289	protein homotetramerization
Biological Process	GO:0008360	regulation of cell shape
Biological Process	GO:0006941	striated muscle contraction
Cellular Component	GO:0015629	actin cytoskeleton
Cellular Component	GO:0005829	cytosol
Cellular Component	GO:0070062	extracellular exosome
Cellular Component	GO:0005576	extracellular region
Cellular Component	GO:0005615	extracellular space
Cellular Component	GO:1904813	ficolin-1-rich granule lumen
Cellular Component	GO:0031674	I band
Cellular Component	GO:0031430	M band

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] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.

[7] 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.

[8] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[9] 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.

[10] 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.

[11] 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.

[12] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.

[13] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.

[14] 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.