Search Results
Overview
| Uniprot ID | Q9CQF3 |
|---|---|
| Protein Name | Cleavage and polyadenylation specificity factor subunit 5 |
| Gene Name | Nudt21 |
| Organism | Mus musculus |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 23 | GVNQFGNKYIQQTKP |
Function
Component of the cleavage factor Im (CFIm) complex that functions as an activator of the pre-mRNA 3'-end cleavage and polyadenylation processing required for the maturation of pre-mRNA into functional mRNAs. CFIm contributes to the recruitment of multiprotein complexes on specific sequences on the pre-mRNA 3'-end, so called cleavage and polyadenylation signals (pA signals). Most pre-mRNAs contain multiple pA signals, resulting in alternative cleavage and polyadenylation (APA) producing mRNAs with variable 3'-end formation. The CFIm complex acts as a key regulator of cleavage and polyadenylation site choice during APA through its binding to 5'-UGUA-3' elements localized in the 3'-untranslated region (UTR) for a huge number of pre-mRNAs. NUDT21/CPSF5 activates indirectly the mRNA 3'-processing machinery by recruiting CPSF6 and/or CPSF7. Binds to 5'-UGUA-3' elements localized upstream of pA signals that act as enhancers of pre-mRNA 3'-end processing. The homodimer mediates simultaneous sequence-specific recognition of two 5'-UGUA-3' elements within the pre-mRNA (By similarity). Plays a role in somatic cell fate transitions and pluripotency by regulating widespread changes in gene expression through an APA-dependent function (PubMed:29249356). Binds to chromatin (PubMed:18032416). Binds to, but does not hydrolyze mono- and di-adenosine nucleotides (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0034451 | centriolar satellite |
| Cellular Component | GO:0005813 | centrosome |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005847 | mRNA cleavage and polyadenylation specificity factor complex |
| Cellular Component | GO:0005849 | mRNA cleavage factor complex |
| Cellular Component | GO:0016604 | nuclear body |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0042382 | paraspeckles |
| Molecular Function | GO:0003682 | chromatin binding |
| Molecular Function | GO:0042826 | histone deacetylase binding |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0035925 | mRNA 3'-UTR AU-rich region binding |
| Molecular Function | GO:0003729 | mRNA binding |
| Molecular Function | GO:0042803 | protein homodimerization activity |
| Biological Process | GO:0030154 | cell differentiation |
| Biological Process | GO:0180010 | co-transcriptional mRNA 3'-end processing, cleavage and polyadenylation pathway |
| Biological Process | GO:0031124 | mRNA 3'-end processing |
| Biological Process | GO:0110104 | mRNA alternative polyadenylation |
| Biological Process | GO:0006397 | mRNA processing |
| Biological Process | GO:2000975 | positive regulation of pro-B cell differentiation |
| Biological Process | GO:2000738 | positive regulation of stem cell differentiation |
| Biological Process | GO:0010608 | post-transcriptional regulation of gene expression |
| Biological Process | GO:0051290 | protein heterotetramerization |
| Biological Process | GO:0051262 | protein tetramerization |
Reference
[1] Sung E, Sim H, Cho YC, Lee W, Bae JS et al.. Global Profiling of Lysine Acetylation and Lactylation in Kupffer Cells.. J Proteome Res 22(12):3683-3691. 2023 Dec 1. PMID: 37897433.
[2] Wu D, Tang Y, Li X, Xiong S, Zhang Z et al.. Characterization of protein lactylation in healthy and ischemic mouse hearts.. Front Cardiovasc Med 12:1644886. 2025. PMID: 41089239.