Mouse Anti-NUDT21 Recombinant Antibody (F-5) (CBMAB-N3903-WJ)

nudix (nucleoside diphosphate linked moiety X)-type motif 21

The protein encoded by this gene is one subunit of a cleavage factor required for 3' RNA cleavage and polyadenylation processing. The interaction of the protein with the RNA is one of the earliest steps in the assembly of the 3' end processing complex and facilitates the recruitment of other processing factors. This gene encodes the 25kD subunit of the protein complex, which is composed of four polypeptides. [provided by RefSeq, Jul 2008]

Nudix Hydrolase 21; Cleavage And Polyadenylation Specificity Factor 25 KDa Subunit; Cleavage And Polyadenylation Specific Factor 5, 25 KD Subunit; Nudix (Nucleoside Diphosphate Linked Moiety X)-Type Motif 21; Cleavage And Polyadenylation Specific Factor 5, 25 KDa; Nucleoside Diphosphate-Linked Moiety X Motif 21; Pre-MRNA Cleavage Factor Im 25 KDa Subunit; Cleavage Factor Im Complex 25 KDa Subunit; CPSF 25 KDa Subunit;

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 (PubMed:9659921, PubMed:8626397, PubMed:14690600, PubMed:15937220, PubMed:17024186, PubMed:17098938, PubMed:29276085).
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) (PubMed:9659921, PubMed:8626397, PubMed:14690600, PubMed:17024186).
Most pre-mRNAs contain multiple pA signals, resulting in alternative cleavage and polyadenylation (APA) producing mRNAs with variable 3'-end formation (PubMed:17098938, PubMed:23187700, PubMed:29276085).
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 (PubMed:17098938, PubMed:20695905, PubMed:29276085).
NUDT21/CPSF5 activates indirectly the mRNA 3'-processing machinery by recruiting CPSF6 and/or CPSF7 (PubMed:29276085).
Binds to 5'-UGUA-3' elements localized upstream of pA signals that act as enhancers of pre-mRNA 3'-end processing (PubMed:8626397, PubMed:14690600, PubMed:15169763, PubMed:17024186, PubMed:22813749, PubMed:20479262).
The homodimer mediates simultaneous sequence-specific recognition of two 5'-UGUA-3' elements within the pre-mRNA (PubMed:20479262, PubMed:21295486).
Plays a role in somatic cell fate transitions and pluripotency by regulating widespread changes in gene expression through an APA-dependent function (By similarity).
Binds to chromatin (By similarity).
Binds to, but does not hydrolyze mono- and di-adenosine nucleotides (PubMed:18445629).

Cell differentiationIEA:UniProtKB-KW
Messenger ribonucleoprotein complex assemblyManual Assertion Based On ExperimentIDA:UniProtKB
mRNA 3'-end processingManual Assertion Based On ExperimentIDA:ComplexPortal
mRNA alternative polyadenylationManual Assertion Based On ExperimentIMP:UniProtKB
mRNA polyadenylationIEA:InterPro
mRNA processingManual Assertion Based On ExperimentIDA:UniProtKB
Positive regulation of mRNA cleavageManual Assertion Based On ExperimentIDA:UniProtKB
Positive regulation of mRNA polyadenylationManual Assertion Based On ExperimentIDA:UniProtKB
Positive regulation of pro-B cell differentiationISS:UniProtKB
Positive regulation of stem cell differentiationISS:UniProtKB
Posttranscriptional regulation of gene expressionISS:UniProtKB
Pre-mRNA cleavage required for polyadenylationManual Assertion Based On ExperimentIDA:ComplexPortal
Protein heterotetramerizationManual Assertion Based On ExperimentIDA:UniProtKB
Protein tetramerizationManual Assertion Based On ExperimentIDA:UniProtKB

Nucleus
Cytoplasm
Shuttles between the nucleus and the cytoplasm in a transcription- and XPO1/CRM1-independent manner, most probably in complex with the cleavage factor Im complex (CFIm) (PubMed:19864460).
In punctate subnuclear structures localized adjacent to nuclear speckles, called paraspeckles (PubMed:15169763).

Acetylated mainly by p300/CBP, recruited to the complex by CPSF6. Acetylation decreases interaction with PAPAO. Deacetylated by the class I/II HDACs, HDAC1, HDAC3 and HDAC10, and by the class III HDACs, SIRT1 AND SIRT2.