Search Results
Overview
| Uniprot ID | Q9UKV3 |
|---|---|
| Protein Name | Apoptotic chromatin condensation inducer in the nucleus |
| Gene Name | ACIN1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 103 | SALVKRLKGALMLEN |
| 143 | FIKQYLEKQQELLRQ |
| 238 | VRQARAAKLSEGSQP |
| 302 | SREAPILKEFKEEGE |
| 349 | RSQEEARKSHLARQQ |
| 398 | RLTEDRKKASLVALP |
| 506 | SVLPLVQKSTLADYS |
| 516 | LADYSAQKDLEPESD |
| 532 | SAQPLPLKIEELALA |
| 548 | GITEECLKQPSLEQK |
| 81 | ALRVTDLKAALEQRG |
| 818 | KKESSLPKSFKRKIS |
| 823 | LPKSFKRKISVVSAT |
| 831 | ISVVSATKGVPAGNS |
| 860 | ASTATTQKKPSISIT |
| 861 | STATTQKKPSISITT |
| 970 | PAEHEVKKVTLGDTL |
| 986 | RRSISQQKSGVSITI |
Function
Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Component of the ASAP complexes which bind RNA in a sequence-independent manner and are proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets; ACIN1 confers RNA-binding to the complex. The ASAP complex can inhibit RNA processing during in vitro splicing reactions. The ASAP complex promotes apoptosis and is disassembled after induction of apoptosis. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the activity is different from the established EJC assembly and function. Induces apoptotic chromatin condensation after activation by CASP3. Regulates cyclin A1, but not cyclin A2, expression in leukemia cells
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0061574 | ASAP complex |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0016607 | nuclear speck |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Molecular Function | GO:0016887 | ATP hydrolysis activity |
| Molecular Function | GO:0019899 | enzyme binding |
| Molecular Function | GO:0003676 | nucleic acid binding |
| Molecular Function | GO:0003723 | RNA binding |
| Biological Process | GO:0030263 | apoptotic chromosome condensation |
| Biological Process | GO:0030218 | erythrocyte differentiation |
| Biological Process | GO:0006397 | mRNA processing |
| Biological Process | GO:0048025 | negative regulation of mRNA splicing, via spliceosome |
| Biological Process | GO:0043065 | positive regulation of apoptotic process |
| Biological Process | GO:0045657 | positive regulation of monocyte differentiation |
| Biological Process | GO:0050684 | regulation of mRNA processing |
| Biological Process | GO:0008380 | RNA splicing |
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] 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.
[4] 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.
[5] 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.
[6] 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.
[7] 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.
[8] 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.
[9] 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.