Search Results

Overview

Uniprot IDP00505
Protein NameAspartate aminotransferase, mitochondrial
Gene NameGOT2
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
122 GENSEVLKSGRFVTV
159 SRDVFLPKPTWGNHT
185 GYRYYDPKTCGFDFT
227 DPRPEQWKEIATVVK
234 KEIATVVKKRNLFAF
235 EIATVVKKRNLFAFF
279 CLCQSYAKNMGLYGE
296 GAFTMVCKDADEAKR
302 CKDADEAKRVESQLK
309 KRVESQLKILIRPMY
338 LNTPDLRKQWLQEVK
363 TQLVSNLKKEGSTHN
364 QLVSNLKKEGSTHNW
396 EQVERLIKEFSIYMT
404 EFSIYMTKDGRISVA
59 KRDTNSKKMNLGVGA
73 AYRDDNGKPYVLPSV
82 YVLPSVRKAEAQIAA
90 AEAQIAAKNLDKEYL

Function

Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). As a member of the malate-aspartate shuttle, it has a key role in the intracellular NAD(H) redox balance. Is important for metabolite exchange between mitochondria and cytosol, and for amino acid metabolism. Facilitates cellular uptake of long-chain free fatty acids

Protein Sequence

10 MALLHSGRVL 20 PGIAAAFHPG 30 LAAAASARAS 40 SWWTHVEMGP 50 PDPILGVTEA 60 FKRDTNSKKM 70 NLGVGAYRDD 80 NGKPYVLPSV 90 RKAEAQIAAK 100 NLDKEYLPIG 110 GLAEFCKASA 120 ELALGENSEV 130 LKSGRFVTVQ 140 TISGTGALRI 150 GASFLQRFFK 160 FSRDVFLPKP 170 TWGNHTPIFR 180 DAGMQLQGYR 190 YYDPKTCGFD 200 FTGAVEDISK 210 IPEQSVLLLH 220 ACAHNPTGVD 230 PRPEQWKEIA 240 TVVKKRNLFA 250 FFDMAYQGFA 260 SGDGDKDAWA 270 VRHFIEQGIN 280 VCLCQSYAKN 290 MGLYGERVGA 300 FTMVCKDADE 310 AKRVESQLKI 320 LIRPMYSNPP 330 LNGARIAAAI 340 LNTPDLRKQW 350 LQEVKVMADR 360 IIGMRTQLVS 370 NLKKEGSTHN 380 WQHITDQIGM 390 FCFTGLKPEQ 400 VERLIKEFSI 410 YMTKDGRISV 420 AGVTSSNVGY 430 LAHAIHQVTK

Gene Ontology

Classification GO ID Description
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005759 mitochondrial matrix
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0005886 plasma membrane
Molecular Function GO:0016212 kynurenine-oxoglutarate transaminase activity
Molecular Function GO:0004069 L-aspartate:2-oxoglutarate aminotransferase activity
Molecular Function GO:0030170 pyridoxal phosphate binding
Molecular Function GO:0003723 RNA binding
Biological Process GO:0006103 2-oxoglutarate metabolic process
Biological Process GO:0006531 aspartate metabolic process
Biological Process GO:0015908 fatty acid transport
Biological Process GO:0006536 glutamate metabolic process
Biological Process GO:0006533 L-aspartate catabolic process
Biological Process GO:0043490 malate-aspartate shuttle
Biological Process GO:0045471 response to ethanol
Biological Process GO:0019470 trans-4-hydroxy-L-proline catabolic 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] 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.

[4] 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.

[5] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.

[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.