Search Results

Overview

Uniprot ID	P39687
Protein Name	Acidic leucine-rich nuclear phosphoprotein 32 family member A
Gene Name	ANP32A
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
20	NRTPSDVKELVLDNS
238	EERGQKRKREPEDEG
68	PKLNKLKKLELSDNR

Function

Multifunctional protein that is involved in the regulation of many processes including tumor suppression, apoptosis, cell cycle progression or transcription (PubMed:10400610, PubMed:11360199, PubMed:16341127, PubMed:18439902). Promotes apoptosis by favouring the activation of caspase-9/CASP9 and allowing apoptosome formation (PubMed:18439902). In addition, plays a role in the modulation of histone acetylation and transcription as part of the INHAT (inhibitor of histone acetyltransferases) complex. Inhibits the histone-acetyltransferase activity of EP300/CREBBP (CREB-binding protein) and EP300/CREBBP-associated factor by histone masking (PubMed:11830591). Preferentially binds to unmodified histone H3 and sterically inhibiting its acetylation and phosphorylation leading to cell growth inhibition (PubMed:16341127). Participates in other biochemical processes such as regulation of mRNA nuclear-to-cytoplasmic translocation and stability by its association with ELAVL1 (Hu-antigen R) (PubMed:18180367). Plays a role in E4F1-mediated transcriptional repression as well as inhibition of protein phosphatase 2A (PubMed:15642345, PubMed:17557114)

Protein Sequence

10 MEMGRRIHLE 20 LRNRTPSDVK 30 ELVLDNSRSN 40 EGKLEGLTDE 50 FEELEFLSTI 60 NVGLTSIANL 70 PKLNKLKKLE 80 LSDNRVSGGL 90 EVLAEKCPNL 100 THLNLSGNKI 110 KDLSTIEPLK 120 KLENLKSLDL 130 FNCEVTNLND 140 YRENVFKLLP 150 QLTYLDGYDR 160 DDKEAPDSDA 170 EGYVEGLDDE 180 EEDEDEEEYD 190 EDAQVVEDEE 200 DEDEEEEGEE 210 EDVSGEEEED 220 EEGYNDGEVD 230 DEEDEEELGE 240 EERGQKRKRE PEDEGEDDD

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0005737	cytoplasm
Cellular Component	GO:0005829	cytosol
Cellular Component	GO:0005783	endoplasmic reticulum
Cellular Component	GO:0005654	nucleoplasm
Cellular Component	GO:0005634	nucleus
Cellular Component	GO:0048471	perinuclear region of cytoplasm
Molecular Function	GO:0042393	histone binding
Molecular Function	GO:0003723	RNA binding
Biological Process	GO:0006351	DNA-templated transcription
Biological Process	GO:0035556	intracellular signal transduction
Biological Process	GO:0006913	nucleocytoplasmic transport
Biological Process	GO:0042981	regulation of apoptotic 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] 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.

[3] 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.