Search Results

Overview

Uniprot IDP00367
Protein NameGlutamate dehydrogenase 1, mitochondrial
Gene NameGLUD1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
110 RGILRIIKPCNHVLS
147 SQHRTPCKGGIRYST
162 DVSVDEVKALASLMT
183 DVPFGGAKAGVKINP
187 GGAKAGVKINPKNYT
191 AGVKINPKNYTDNEL
200 YTDNELEKITRRFTM
211 RFTMELAKKGFIGPG
212 FTMELAKKGFIGPGI
258 AHACVTGKPISQGGI
352 PKELEDFKLQHGSIL
363 GSILGFPKAKPYEGS
365 ILGFPKAKPYEGSIL
386 LIPAASEKQLTKSNA
390 ASEKQLTKSNAPRVK
399 NAPRVKAKIIAEGAN
415 PTTPEADKIFLERNI
457 SYGRLTFKYERDSNY
477 VQESLERKFGKHGGT
480 SLERKFGKHGGTIPI
503 RISGASEKDIVHSGL
527 QIMRTAMKYNLGLDL
545 AYVNAIEKVFKVYNE
548 NAIEKVFKVYNEAGV
84 GASIVEDKLVEDLRT
98 TRESEEQKRNRVRGI

Function

Mitochondrial glutamate dehydrogenase that catalyzes the conversion of L-glutamate into alpha-ketoglutarate. Plays a key role in glutamine anaplerosis by producing alpha-ketoglutarate, an important intermediate in the tricarboxylic acid cycle (PubMed:11032875, PubMed:11254391, PubMed:16023112, PubMed:16959573). Plays a role in insulin homeostasis (PubMed:11297618, PubMed:9571255). May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate (By similarity)

Protein Sequence

10 MYRYLGEALL 20 LSRAGPAALG 30 SASADSAALL 40 GWARGQPAAA 50 PQPGLALAAR 60 RHYSEAVADR 70 EDDPNFFKMV 80 EGFFDRGASI 90 VEDKLVEDLR 100 TRESEEQKRN 110 RVRGILRIIK 120 PCNHVLSLSF 130 PIRRDDGSWE 140 VIEGYRAQHS 150 QHRTPCKGGI 160 RYSTDVSVDE 170 VKALASLMTY 180 KCAVVDVPFG 190 GAKAGVKINP 200 KNYTDNELEK 210 ITRRFTMELA 220 KKGFIGPGID 230 VPAPDMSTGE 240 REMSWIADTY 250 ASTIGHYDIN 260 AHACVTGKPI 270 SQGGIHGRIS 280 ATGRGVFHGI 290 ENFINEASYM 300 SILGMTPGFG 310 DKTFVVQGFG 320 NVGLHSMRYL 330 HRFGAKCIAV 340 GESDGSIWNP 350 DGIDPKELED 360 FKLQHGSILG 370 FPKAKPYEGS 380 ILEADCDILI 390 PAASEKQLTK 400 SNAPRVKAKI 410 IAEGANGPTT 420 PEADKIFLER 430 NIMVIPDLYL 440 NAGGVTVSYF 450 EWLKNLNHVS 460 YGRLTFKYER 470 DSNYHLLMSV 480 QESLERKFGK 490 HGGTIPIVPT 500 AEFQDRISGA 510 SEKDIVHSGL 520 AYTMERSARQ 530 IMRTAMKYNL 540 GLDLRTAAYV 550 NAIEKVFKVY NEAGVTFT

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005783 endoplasmic reticulum
Cellular Component GO:0005759 mitochondrial matrix
Cellular Component GO:0005739 mitochondrion
Molecular Function GO:0043531 ADP binding
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0004352 glutamate dehydrogenase (NAD+) activity
Molecular Function GO:0004354 glutamate dehydrogenase (NADP+) activity
Molecular Function GO:0004353 glutamate dehydrogenase [NAD(P)+] activity
Molecular Function GO:0005525 GTP binding
Molecular Function GO:0070728 L-leucine binding
Molecular Function GO:0070403 NAD+ binding
Molecular Function GO:0042803 protein homodimerization activity
Biological Process GO:0006537 glutamate biosynthetic process
Biological Process GO:0006541 glutamine metabolic process
Biological Process GO:0006538 L-glutamate catabolic process
Biological Process GO:0032024 positive regulation of insulin secretion
Biological Process GO:0021762 substantia nigra development
Biological Process GO:0072350 tricarboxylic acid metabolic process

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] 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.

[4] 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.

[5] 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.

[6] 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.

[7] 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.

[8] 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.