Search Results

Overview

Uniprot IDO75874
Protein NameIsocitrate dehydrogenase [NADP] cytoplasmic
Gene NameIDH1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
115 FREAIICKNIPRLVS
126 RLVSGWVKPIIIGRH
212 WPLYLSTKNTILKKY
224 KKYDGRFKDIFQEIY
233 IFQEIYDKQYKSQFE
236 EIYDKQYKSQFEAQK
243 KSQFEAQKIWYEHRL
27 RIIWELIKEKLIFPY
301 VLVCPDGKTVEAEAA
345 RGLAHRAKLDNNKEL
381 KDLAACIKGLPNVQR
4 ****MSKKISGGSVV
406 DKLGENLKIKLAQAK
408 LGENLKIKLAQAKL*
58 ATNDQVTKDAAEAIK
66 DAAEAIKKHNVGVKC
72 KKHNVGVKCATITPD
81 ATITPDEKRVEEFKL
87 EKRVEEFKLKQMWKS
93 FKLKQMWKSPNGTIR

Function

Catalyzes the NADP(+)-dependent oxidative decarboxylation of isocitrate (D-threo-isocitrate) to 2-ketoglutarate (2-oxoglutarate), which is required by other enzymes such as the phytanoyl-CoA dioxygenase (PubMed:10521434, PubMed:19935646). Plays a critical role in the generation of NADPH, an important cofactor in many biosynthesis pathways (PubMed:10521434). May act as a corneal epithelial crystallin and may be involved in maintaining corneal epithelial transparency (By similarity)

Protein Sequence

10 MSKKISGGSV 20 VEMQGDEMTR 30 IIWELIKEKL 40 IFPYVELDLH 50 SYDLGIENRD 60 ATNDQVTKDA 70 AEAIKKHNVG 80 VKCATITPDE 90 KRVEEFKLKQ 100 MWKSPNGTIR 110 NILGGTVFRE 120 AIICKNIPRL 130 VSGWVKPIII 140 GRHAYGDQYR 150 ATDFVVPGPG 160 KVEITYTPSD 170 GTQKVTYLVH 180 NFEEGGGVAM 190 GMYNQDKSIE 200 DFAHSSFQMA 210 LSKGWPLYLS 220 TKNTILKKYD 230 GRFKDIFQEI 240 YDKQYKSQFE 250 AQKIWYEHRL 260 IDDMVAQAMK 270 SEGGFIWACK 280 NYDGDVQSDS 290 VAQGYGSLGM 300 MTSVLVCPDG 310 KTVEAEAAHG 320 TVTRHYRMYQ 330 KGQETSTNPI 340 ASIFAWTRGL 350 AHRAKLDNNK 360 ELAFFANALE 370 EVSIETIEAG 380 FMTKDLAACI 390 KGLPNVQRSD 400 YLNTFEFMDK 410 LGENLKIKLA QAKL

Gene Ontology

Classification GO ID Description
Biological Process GO:0006739 NADP+ metabolic process
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005576 extracellular region
Cellular Component GO:1904813 ficolin-1-rich granule lumen
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0005782 peroxisomal matrix
Cellular Component GO:0005777 peroxisome
Cellular Component GO:0034774 secretory granule lumen
Cellular Component GO:1904724 tertiary granule lumen
Molecular Function GO:0045296 cadherin binding
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0004450 isocitrate dehydrogenase (NADP+) activity
Molecular Function GO:0000287 magnesium ion binding
Molecular Function GO:0051287 NAD binding
Molecular Function GO:0050661 NADP binding
Molecular Function GO:0042803 protein homodimerization activity
Biological Process GO:0006103 2-oxoglutarate metabolic process
Biological Process GO:0008585 female gonad development
Biological Process GO:0006097 glyoxylate cycle
Biological Process GO:0006102 isocitrate metabolic process
Biological Process GO:0006740 NADPH regeneration
Biological Process GO:0048545 response to steroid hormone
Biological Process GO:0006099 tricarboxylic acid cycle

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] 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.

[4] 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.