Search Results

Overview

Uniprot IDP07954
Protein NameFumarate hydratase, mitochondrial
Gene NameFH
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
100 IKAFGILKRAAAEVN
115 QDYGLDPKIANAIMK
122 KIANAIMKAADEVAE
172 LGGELGSKIPVHPND
221 LHDALDAKSKEFAQI
223 DALDAKSKEFAQIIK
230 KEFAQIIKIGRTHTQ
263 KYAMTRIKAAMPRIY
292 TRIGFAEKVAAKVAA
473 DKAAKIAKTAHKNGS
477 KIAKTAHKNGSTLKE
61 YDTFGELKVPNDKYY
66 ELKVPNDKYYGAQTV
80 VRSTMNFKIGGVTER

Function

Catalyzes the reversible stereospecific interconversion of fumarate to L-malate (PubMed:30761759). Experiments in other species have demonstrated that specific isoforms of this protein act in defined pathways and favor one direction over the other (Probable)

Protein Sequence

10 MYRALRLLAR 20 SRPLVRAPAA 30 ALASAPGLGG 40 AAVPSFWPPN 50 AARMASQNSF 60 RIEYDTFGEL 70 KVPNDKYYGA 80 QTVRSTMNFK 90 IGGVTERMPT 100 PVIKAFGILK 110 RAAAEVNQDY 120 GLDPKIANAI 130 MKAADEVAEG 140 KLNDHFPLVV 150 WQTGSGTQTN 160 MNVNEVISNR 170 AIEMLGGELG 180 SKIPVHPNDH 190 VNKSQSSNDT 200 FPTAMHIAAA 210 IEVHEVLLPG 220 LQKLHDALDA 230 KSKEFAQIIK 240 IGRTHTQDAV 250 PLTLGQEFSG 260 YVQQVKYAMT 270 RIKAAMPRIY 280 ELAAGGTAVG 290 TGLNTRIGFA 300 EKVAAKVAAL 310 TGLPFVTAPN 320 KFEALAAHDA 330 LVELSGAMNT 340 TACSLMKIAN 350 DIRFLGSGPR 360 SGLGELILPE 370 NEPGSSIMPG 380 KVNPTQCEAM 390 TMVAAQVMGN 400 HVAVTVGGSN 410 GHFELNVFKP 420 MMIKNVLHSA 430 RLLGDASVSF 440 TENCVVGIQA 450 NTERINKLMN 460 ESLMLVTALN 470 PHIGYDKAAK 480 IAKTAHKNGS 490 TLKETAIELG 500 YLTAEQFDEW 510 VKPKDMLGPK

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005694 chromosome
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005759 mitochondrial matrix
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0005634 nucleus
Cellular Component GO:0035861 site of double-strand break
Molecular Function GO:0004333 fumarate hydratase activity
Molecular Function GO:0042393 histone binding
Biological Process GO:0006525 arginine metabolic process
Biological Process GO:0006974 DNA damage response
Biological Process GO:0006281 DNA repair
Biological Process GO:0006106 fumarate metabolic process
Biological Process GO:0006108 malate metabolic process
Biological Process GO:0120162 positive regulation of cold-induced thermogenesis
Biological Process GO:2001034 positive regulation of double-strand break repair via nonhomologous end joining
Biological Process GO:0006099 tricarboxylic acid cycle
Biological Process GO:0000050 urea 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] 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] 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.