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Overview

Uniprot IDP05062
Protein NameFructose-bisphosphate aldolase B
Gene NameALDOB
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
101 FRNILKEKGIVVGIK
108 KGIVVGIKLDQGGAP
121 APLAGTNKETTIQGL
13 PALTQEQKKELSEIA
14 ALTQEQKKELSEIAQ
140 ERCAQYKKDGVDFGK
147 KDGVDFGKWRAVLRI
230 YLEGTLLKPNMVTAG
242 TAGHACTKKYTPEQV
243 AGHACTKKYTPEQVA
28 QSIVANGKGILAADE
297 CPLPKPWKLSFSYGR
317 ALAAWGGKAANKEAT
321 WGGKAANKEATQEAF
330 ATQEAFMKRAMANCQ
340 MANCQAAKGQYVHTG
48 GNRLQRIKVENTEEN
92 YQKDSQGKLFRNILK

Function

Catalyzes the aldol cleavage of fructose 1,6-biphosphate to form two triosephosphates dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate in glycolysis as well as the reverse stereospecific aldol addition reaction in gluconeogenesis. In fructolysis, metabolizes fructose 1-phosphate derived from the phosphorylation of dietary fructose by fructokinase into dihydroxyacetone phosphate and D-glyceraldehyde (PubMed:10970798, PubMed:12205126, PubMed:20848650). Acts as an adapter independently of its enzymatic activity, exerts a tumor suppressor role by stabilizing the ternary complex with G6PD and TP53 to inhibit G6PD activity and keep oxidative pentose phosphate metabolism in check (PubMed:35122041)

Protein Sequence

10 MAHRFPALTQ 20 EQKKELSEIA 30 QSIVANGKGI 40 LAADESVGTM 50 GNRLQRIKVE 60 NTEENRRQFR 70 EILFSVDSSI 80 NQSIGGVILF 90 HETLYQKDSQ 100 GKLFRNILKE 110 KGIVVGIKLD 120 QGGAPLAGTN 130 KETTIQGLDG 140 LSERCAQYKK 150 DGVDFGKWRA 160 VLRIADQCPS 170 SLAIQENANA 180 LARYASICQQ 190 NGLVPIVEPE 200 VIPDGDHDLE 210 HCQYVTEKVL 220 AAVYKALNDH 230 HVYLEGTLLK 240 PNMVTAGHAC 250 TKKYTPEQVA 260 MATVTALHRT 270 VPAAVPGICF 280 LSGGMSEEDA 290 TLNLNAINLC 300 PLPKPWKLSF 310 SYGRALQASA 320 LAAWGGKAAN 330 KEATQEAFMK 340 RAMANCQAAK 350 GQYVHTGSSG 360 AASTQSLFTA CYTY

Gene Ontology

Classification GO ID Description
Cellular Component GO:0034451 centriolar satellite
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005815 microtubule organizing center
Molecular Function GO:0051117 ATPase binding
Molecular Function GO:0008092 cytoskeletal protein binding
Molecular Function GO:0070061 fructose binding
Molecular Function GO:0061609 fructose-1-phosphate aldolase activity
Molecular Function GO:0004332 fructose-bisphosphate aldolase activity
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0060090 molecular adaptor activity
Biological Process GO:0030388 fructose 1,6-bisphosphate metabolic process
Biological Process GO:0061624 fructose catabolic process to hydroxyacetone phosphate and glyceraldehyde-3-phosphate
Biological Process GO:0006000 fructose metabolic process
Biological Process GO:0006094 gluconeogenesis
Biological Process GO:0006096 glycolytic process
Biological Process GO:1905856 negative regulation of pentose-phosphate shunt
Biological Process GO:0070072 vacuolar proton-transporting V-type ATPase complex assembly

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.