Search Results

Overview

Uniprot IDP40925
Protein NameMalate dehydrogenase, cytoplasmic
Gene NameMDH1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
103 MERKDLLKANVKIFK
107 DLLKANVKIFKSQGA
110 KANVKIFKSQGAALD
118 SQGAALDKYAKKSVK
125 KYAKKSVKVIVVGNP
142 TNCLTASKSAPSIPK
149 KSAPSIPKENFSCLT
164 RLDHNRAKAQIALKL
170 AKAQIALKLGVTAND
199 YPDVNHAKVKLQGKE
205 AKVKLQGKEVGVYEA
214 VGVYEALKDDSWLKG
236 QRGAAVIKARKLSSA
239 AAVIKARKLSSAMSA
248 SSAMSAAKAICDHVR
312 INDFSREKMDLTAKE
318 EKMDLTAKELTEEKE
73 KDVIATDKEDVAFKD

Function

Catalyzes the reduction of aromatic alpha-keto acids in the presence of NADH (PubMed:2449162, PubMed:3052244). Plays essential roles in the malate-aspartate shuttle and the tricarboxylic acid cycle, important in mitochondrial NADH supply for oxidative phosphorylation (PubMed:31538237). Catalyzes the reduction of 2-oxoglutarate to 2-hydroxyglutarate, leading to elevated reactive oxygen species (ROS) (PubMed:34012073)

Protein Sequence

10 MSEPIRVLVT 20 GAAGQIAYSL 30 LYSIGNGSVF 40 GKDQPIILVL 50 LDITPMMGVL 60 DGVLMELQDC 70 ALPLLKDVIA 80 TDKEDVAFKD 90 LDVAILVGSM 100 PRREGMERKD 110 LLKANVKIFK 120 SQGAALDKYA 130 KKSVKVIVVG 140 NPANTNCLTA 150 SKSAPSIPKE 160 NFSCLTRLDH 170 NRAKAQIALK 180 LGVTANDVKN 190 VIIWGNHSST 200 QYPDVNHAKV 210 KLQGKEVGVY 220 EALKDDSWLK 230 GEFVTTVQQR 240 GAAVIKARKL 250 SSAMSAAKAI 260 CDHVRDIWFG 270 TPEGEFVSMG 280 VISDGNSYGV 290 PDDLLYSFPV 300 VIKNKTWKFV 310 EGLPINDFSR 320 EKMDLTAKEL 330 TEEKESAFEF LSSA

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005615 extracellular space
Molecular Function GO:0047995 (2R)-hydroxyphenylpyruvate reductase [NAD(P)H] activity
Molecular Function GO:0030060 L-malate dehydrogenase (NAD+) activity
Molecular Function GO:0004470 malic enzyme activity
Biological Process GO:0006108 malate metabolic process
Biological Process GO:0043490 malate-aspartate shuttle
Biological Process GO:0019674 NAD+ metabolic process
Biological Process GO:0006739 NADP+ metabolic process
Biological Process GO:0006107 oxaloacetate metabolic process
Biological Process GO:0006099 tricarboxylic acid cycle

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] 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] 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.

[6] 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.