Search Results

Overview

Uniprot IDP28838
Protein NameCytosol aminopeptidase
Gene NameLAP3
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
104 VLVGLGKKAAGIDEQ
118 QENWHEGKENIRAAV
170 DDLKQKKKMAVSAKL
176 KKMAVSAKLYGSGDQ
221 RFAEIIEKNLKSASS
224 EIIEKNLKSASSKTE
229 NLKSASSKTEVHIRP
345 MPSGKANKPGDVVRA
356 VVRAKNGKTIQVDNT
45 LGIYSKEKEDDVPQF
455 ADVNNIGKYRSAGAC
476 KEFVTHPKWAHLDIA
66 FDKLLAGKLRETLNI
79 NISGPPLKAGKTRTF

Function

Cytosolic metallopeptidase that catalyzes the removal of unsubstituted N-terminal hydrophobic amino acids from various peptides. The presence of Zn(2+) ions is essential for the peptidase activity, and the association with other cofactors can modulate the substrate spectificity of the enzyme. For instance, in the presence of Mn(2+), it displays a specific Cys-Gly hydrolyzing activity of Cys-Gly-S-conjugates. Involved in the metabolism of glutathione and in the degradation of glutathione S-conjugates, which may play a role in the control of the cell redox status

Protein Sequence

10 MFLLPLPAAG 20 RVVVRRLAVR 30 RFGSRSLSTA 40 DMTKGLVLGI 50 YSKEKEDDVP 60 QFTSAGENFD 70 KLLAGKLRET 80 LNISGPPLKA 90 GKTRTFYGLH 100 QDFPSVVLVG 110 LGKKAAGIDE 120 QENWHEGKEN 130 IRAAVAAGCR 140 QIQDLELSSV 150 EVDPCGDAQA 160 AAEGAVLGLY 170 EYDDLKQKKK 180 MAVSAKLYGS 190 GDQEAWQKGV 200 LFASGQNLAR 210 QLMETPANEM 220 TPTRFAEIIE 230 KNLKSASSKT 240 EVHIRPKSWI 250 EEQAMGSFLS 260 VAKGSDEPPV 270 FLEIHYKGSP 280 NANEPPLVFV 290 GKGITFDSGG 300 ISIKASANMD 310 LMRADMGGAA 320 TICSAIVSAA 330 KLNLPINIIG 340 LAPLCENMPS 350 GKANKPGDVV 360 RAKNGKTIQV 370 DNTDAEGRLI 380 LADALCYAHT 390 FNPKVILNAA 400 TLTGAMDVAL 410 GSGATGVFTN 420 SSWLWNKLFE 430 ASIETGDRVW 440 RMPLFEHYTR 450 QVVDCQLADV 460 NNIGKYRSAG 470 ACTAAAFLKE 480 FVTHPKWAHL 490 DIAGVMTNKD 500 EVPYLRKGMT 510 GRPTRTLIEF LLRFSQDNA

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005925 focal adhesion
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005802 trans-Golgi network
Molecular Function GO:0004177 aminopeptidase activity
Molecular Function GO:0004180 carboxypeptidase activity
Molecular Function GO:0030145 manganese ion binding
Molecular Function GO:0070006 metalloaminopeptidase activity
Molecular Function GO:0008235 metalloexopeptidase activity
Molecular Function GO:0008233 peptidase activity
Biological Process GO:0006508 proteolysis

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] 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.

[4] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[5] 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.

[6] 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.

[7] 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.