Search Results
Overview
| Uniprot ID | P52298 |
|---|---|
| Protein Name | Nuclear cap-binding protein subunit 2 |
| Gene Name | NCBP2 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 151 | AGRGGYGKLAQNQ** |
| 7 | *MSGGLLKALRSDSY |
| 75 | KIIMGLDKMKKTACG |
| 78 | MGLDKMKKTACGFCF |
Function
Component of the cap-binding complex (CBC), which binds co-transcriptionally to the 5' cap of pre-mRNAs and is involved in various processes such as pre-mRNA splicing, translation regulation, nonsense-mediated mRNA decay, RNA-mediated gene silencing (RNAi) by microRNAs (miRNAs) and mRNA export. The CBC complex is involved in mRNA export from the nucleus via its interaction with ALYREF/THOC4/ALY, leading to the recruitment of the mRNA export machinery to the 5' end of mRNA and to mRNA export in a 5' to 3' direction through the nuclear pore. The CBC complex is also involved in mediating U snRNA and intronless mRNAs export from the nucleus. The CBC complex is essential for a pioneer round of mRNA translation, before steady state translation when the CBC complex is replaced by cytoplasmic cap-binding protein eIF4E. The pioneer round of mRNA translation mediated by the CBC complex plays a central role in nonsense-mediated mRNA decay (NMD), NMD only taking place in mRNAs bound to the CBC complex, but not on eIF4E-bound mRNAs. The CBC complex enhances NMD in mRNAs containing at least one exon-junction complex (EJC) via its interaction with UPF1, promoting the interaction between UPF1 and UPF2. The CBC complex is also involved in 'failsafe' NMD, which is independent of the EJC complex, while it does not participate in Staufen-mediated mRNA decay (SMD). During cell proliferation, the CBC complex is also involved in microRNAs (miRNAs) biogenesis via its interaction with SRRT/ARS2, thereby being required for miRNA-mediated RNA interference. The CBC complex also acts as a negative regulator of PARN, thereby acting as an inhibitor of mRNA deadenylation. In the CBC complex, NCBP2/CBP20 recognizes and binds capped RNAs (m7GpppG-capped RNA) but requires NCBP1/CBP80 to stabilize the movement of its N-terminal loop and lock the CBC into a high affinity cap-binding state with the cap structure. The conventional cap-binding complex with NCBP2 binds both small nuclear RNA (snRNA) and messenger (mRNA) and is involved in their export from the nucleus (PubMed:26382858)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0034518 | RNA cap binding complex |
| Molecular Function | GO:0003677 | DNA binding |
| Molecular Function | GO:0003729 | mRNA binding |
| Molecular Function | GO:0000340 | RNA 7-methylguanosine cap binding |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0000339 | RNA cap binding |
| Molecular Function | GO:0017069 | snRNA binding |
| Biological Process | GO:0000380 | alternative mRNA splicing, via spliceosome |
| Biological Process | GO:0002191 | cap-dependent translational initiation |
| Biological Process | GO:0008334 | histone mRNA metabolic process |
| Biological Process | GO:0035195 | miRNA-mediated post-transcriptional gene silencing |
| Biological Process | GO:0031124 | mRNA 3'-end processing |
| Biological Process | GO:0045292 | mRNA cis splicing, via spliceosome |
| Biological Process | GO:0006406 | mRNA export from nucleus |
| Biological Process | GO:0016071 | mRNA metabolic process |
| Biological Process | GO:0000398 | mRNA splicing, via spliceosome |
| Biological Process | GO:0042789 | mRNA transcription by RNA polymerase II |
| Biological Process | GO:0000184 | nuclear-transcribed mRNA catabolic process, nonsense-mediated decay |
| Biological Process | GO:0031442 | positive regulation of mRNA 3'-end processing |
| Biological Process | GO:0046833 | positive regulation of RNA export from nucleus |
| Biological Process | GO:0032968 | positive regulation of transcription elongation by RNA polymerase II |
| Biological Process | GO:0031053 | primary miRNA processing |
| Biological Process | GO:0006446 | regulation of translational initiation |
| Biological Process | GO:0035194 | regulatory ncRNA-mediated post-transcriptional gene silencing |
| Biological Process | GO:0008380 | RNA splicing |
| Biological Process | GO:0006408 | snRNA export from nucleus |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005846 | nuclear cap binding complex |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
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] 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.
[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] 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.
[6] 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.