Search Results

Overview

Uniprot ID	Q9BTT0
Protein Name	Acidic leucine-rich nuclear phosphoprotein 32 family member E
Gene Name	ANP32E
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
101	NLSGNKIKDLSTVEA
6	**MEMKKKINLELRN

Function

Histone chaperone that specifically mediates the genome-wide removal of histone H2A.Z/H2AZ1 from the nucleosome: removes H2A.Z/H2AZ1 from its normal sites of deposition, especially from enhancer and insulator regions. Not involved in deposition of H2A.Z/H2AZ1 in the nucleosome. May stabilize the evicted H2A.Z/H2AZ1-H2B dimer, thus shifting the equilibrium towards dissociation and the off-chromatin state (PubMed:24463511). Inhibits activity of protein phosphatase 2A (PP2A). Does not inhibit protein phosphatase 1. May play a role in cerebellar development and synaptogenesis

Protein Sequence

10 MEMKKKINLE 20 LRNRSPEEVT 30 ELVLDNCLCV 40 NGEIEGLNDT 50 FKELEFLSMA 60 NVELSSLARL 70 PSLNKLRKLE 80 LSDNIISGGL 90 EVLAEKCPNL 100 TYLNLSGNKI 110 KDLSTVEALQ 120 NLKNLKSLDL 130 FNCEITNLED 140 YRESIFELLQ 150 QITYLDGFDQ 160 EDNEAPDSEE 170 EDDEDGDEDD 180 EEEEENEAGP 190 PEGYEEEEEE 200 EEEEDEDEDE 210 DEDEAGSELG 220 EGEEEVGLSY 230 LMKEEIQDEE 240 DDDDYVEEGE 250 EEEEEEEGGL 260 RGEKRKRDAE DDGEEEDD

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0031410	cytoplasmic vesicle
Cellular Component	GO:0098978	glutamatergic synapse
Cellular Component	GO:0005634	nucleus
Cellular Component	GO:0098839	postsynaptic density membrane
Cellular Component	GO:0098895	postsynaptic endosome membrane
Cellular Component	GO:0000812	Swr1 complex
Cellular Component	GO:0030672	synaptic vesicle membrane
Molecular Function	GO:0042393	histone binding
Molecular Function	GO:0140713	histone chaperone activity
Molecular Function	GO:0019212	phosphatase inhibitor activity
Molecular Function	GO:0044183	protein folding chaperone
Biological Process	GO:0006325	chromatin organization
Biological Process	GO:0042981	regulation of apoptotic process

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] 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.

[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] 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.