Search Results

Overview

Uniprot IDQ9Y263
Protein NamePhospholipase A-2-activating protein
Gene NamePLAA
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
315 EEIKAFEKELSHATI
325 SHATIDSKTGDLGDI
529 AYRSAASKTMNIYFP

Function

Plays a role in protein ubiquitination, sorting and degradation through its association with VCP (PubMed:27753622). Involved in ubiquitin-mediated membrane proteins trafficking to late endosomes in an ESCRT-dependent manner, and hence plays a role in synaptic vesicle recycling (By similarity). May play a role in macroautophagy, regulating for instance the clearance of damaged lysosomes (PubMed:27753622). Plays a role in cerebellar Purkinje cell development (By similarity). Positively regulates cytosolic and calcium-independent phospholipase A2 activities in a tumor necrosis factor alpha (TNF)- or lipopolysaccharide (LPS)-dependent manner, and hence prostaglandin E2 biosynthesis (PubMed:18291623, PubMed:28007986)

Protein Sequence

10 MTSGATRYRL 20 SCSLRGHELD 30 VRGLVCCAYP 40 PGAFVSVSRD 50 RTTRLWAPDS 60 PNRSFTEMHC 70 MSGHSNFVSC 80 VCIIPSSDIY 90 PHGLIATGGN 100 DHNICIFSLD 110 SPMPLYILKG 120 HKNTVCSLSS 130 GKFGTLLSGS 140 WDTTAKVWLN 150 DKCMMTLQGH 160 TAAVWAVKIL 170 PEQGLMLTGS 180 ADKTVKLWKA 190 GRCERTFSGH 200 EDCVRGLAIL 210 SETEFLSCAN 220 DASIRRWQIT 230 GECLEVYYGH 240 TNYIYSISVF 250 PNCRDFVTTA 260 EDRSLRIWKH 270 GECAQTIRLP 280 AQSIWCCCVL 290 DNGDIVVGAS 300 DGIIRVFTES 310 EDRTASAEEI 320 KAFEKELSHA 330 TIDSKTGDLG 340 DINAEQLPGR 350 EHLNEPGTRE 360 GQTRLIRDGE 370 KVEAYQWSVS 380 EGRWIKIGDV 390 VGSSGANQQT 400 SGKVLYEGKE 410 FDYVFSIDVN 420 EGGPSYKLPY 430 NTSDDPWLTA 440 YNFLQKNDLN 450 PMFLDQVAKF 460 IIDNTKGQML 470 GLGNPSFSDP 480 FTGGGRYVPG 490 SSGSSNTLPT 500 ADPFTGAGRY 510 VPGSASMGTT 520 MAGVDPFTGN 530 SAYRSAASKT 540 MNIYFPKKEA 550 VTFDQANPTQ 560 ILGKLKELNG 570 TAPEEKKLTE 580 DDLILLEKIL 590 SLICNSSSEK 600 PTVQQLQILW 610 KAINCPEDIV 620 FPALDILRLS 630 IKHPSVNENF 640 CNEKEGAQFS 650 SHLINLLNPK 660 GKPANQLLAL 670 RTFCNCFVGQ 680 AGQKLMMSQR 690 ESLMSHAIEL 700 KSGSNKNIHI 710 ALATLALNYS 720 VCFHKDHNIE 730 GKAQCLSLIS 740 TILEVVQDLE 750 ATFRLLVALG 760 TLISDDSNAV 770 QLAKSLGVDS 780 QIKKYSSVSE 790 PAKVSECCRF ILNLL

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0000153 cytoplasmic ubiquitin ligase complex
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:0045202 synapse
Molecular Function GO:0016005 phospholipase A2 activator activity
Molecular Function GO:0043130 ubiquitin binding
Biological Process GO:0071222 cellular response to lipopolysaccharide
Biological Process GO:0016236 macroautophagy
Biological Process GO:1900045 negative regulation of protein K63-linked ubiquitination
Biological Process GO:0007399 nervous system development
Biological Process GO:0006644 phospholipid metabolic process
Biological Process GO:1903861 positive regulation of dendrite extension
Biological Process GO:2001224 positive regulation of neuron migration
Biological Process GO:0031394 positive regulation of prostaglandin biosynthetic process
Biological Process GO:1903423 positive regulation of synaptic vesicle recycling
Biological Process GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process
Biological Process GO:0043335 protein unfolding
Biological Process GO:0007165 signal transduction
Biological Process GO:0010992 ubiquitin recycling
Biological Process GO:0043162 ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway

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] 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.

[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] 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.

[5] 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.