NUDT21
entrez
11051
canonical
uniprot
O43809
canonical
ensembl
ENSG00000167005
resolver
ensp
ENSP00000300291
resolver
enst
ENST00000300291
resolver
genesymbol
NUDT21
resolver
genesymbol_syn
CFIM25
resolver
genesymbol_syn
CPSF25
resolver
genesymbol_syn
CPSF5
resolver
hgnc
HGNC:13870
resolver
uniprot
Q6IB85
resolver
uniprot
Q6NE84
resolver
uniprot_entry
CPSF5_HUMAN
resolver
uniprot_sec
Q6IB85
resolver
uniprot_sec
Q6NE84
resolver
amino_acid_sequence
MSVVPPNRSQTGWPRGVTQFGNKYIQQTKPLTLERTINLYPLTNYTFGTKEPLYEKDSSVAARFQRMREEFDKIGMRRTVEGVLIVHEHRLPHVLLLQLGTTFFKLPGGELNPGEDEVEGLKRLMTEILGRQDGVLQDWVIDDCIGNWWRPNFEPPQYPYIPAHITKPKEHKKLFLVQLQEKALFAVPKNYKLVAAPLFELYDNAPGYGPIISSLPQLLSRFNFIYN
uniprot
proteins
function
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 (PubMed:14690600, PubMed:15937220, PubMed:17024186, PubMed:17098938, PubMed:29276085, PubMed:8626397, PubMed:9659921). 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:14690600, PubMed:17024186, PubMed:8626397, PubMed:9659921). 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:14690600, PubMed:15169763, PubMed:17024186, PubMed:20479262, PubMed:22813749, PubMed:8626397). 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). {ECO:0000250|UniProtKB:Q9CQF3, ECO:0000269|PubMed:14690600, ECO:0000269|PubMed:15169763, ECO:0000269|PubMed:15937220, ECO:0000269|PubMed:17024186, ECO:0000269|PubMed:17098938, ECO:0000269|PubMed:18445629, ECO:0000269|PubMed:20479262, ECO:0000269|PubMed:20695905, ECO:0000269|PubMed:21295486, ECO:0000269|PubMed:22813749, ECO:0000269|PubMed:23187700, ECO:0000269|PubMed:29276085, ECO:0000269|PubMed:8626397, ECO:0000269|PubMed:9659921}.
uniprot
proteins
mass_dalton
26227
uniprot
proteins
mutagenesis
MUTAGEN 23; /note="K->R: Abolishes acetylation."; /evidence="ECO:0000269|PubMed:17172643"; MUTAGEN 29; /note="K->R: No effect on acetylation."; /evidence="ECO:0000269|PubMed:17172643"; MUTAGEN 55; /note="E->A: Reduces affinity for UGUARNA by 88%."; /evidence="ECO:0000269|PubMed:20479262, ECO:0000269|PubMed:21295486"; MUTAGEN 63; /note="R->S: Reduces affinity for UGUARNA by 99%."; /evidence="ECO:0000269|PubMed:20479262, ECO:0000269|PubMed:21295486"; MUTAGEN 81; /note="E->A: Reduces affinity for UGUARNA by 12%."; /evidence="ECO:0000269|PubMed:20479262"; MUTAGEN 103; /note="F->A: Reduces affinity for UGUARNA by 99%."; /evidence="ECO:0000269|PubMed:20479262, ECO:0000269|PubMed:21295486"; MUTAGEN 103; /note="F->W: Reduces affinity for UGUARNA by over 90%."; /evidence="ECO:0000269|PubMed:20479262, ECO:0000269|PubMed:21295486"; MUTAGEN 154; /note="E->A: Reduces affinity for UGUARNA by 50%."; MUTAGEN 158; /note="Y->A: Abolishes interaction with CPSF6; when associated with A-160."; /evidence="ECO:0000269|PubMed:21295486"; MUTAGEN 160; /note="Y->A: Abolishes interaction with CPSF6; when associated with A-158."; /evidence="ECO:0000269|PubMed:21295486"; MUTAGEN 218; /note="L->R: Reduces interactions with CPSF6 and CPSF7 and decreases mRNA 3'-processing activity."; /evidence="ECO:0000269|PubMed:29276085
uniprot
proteins
post_translational_modification
PTM: 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. {ECO:0000269|PubMed:17172643}.
uniprot
proteins
protein_family
CPSF5 subfamily
uniprot
proteins
protein_family
Nudix hydrolase family
uniprot
proteins
pubmed
14561889
uniprot
proteins
pubmed
14690600
uniprot
proteins
pubmed
15169763
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15592455
uniprot
proteins
pubmed
15616553
uniprot
proteins
pubmed
15937220
uniprot
proteins
pubmed
17024186
uniprot
proteins
pubmed
17098938
uniprot
proteins
pubmed
17172643
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18445629
uniprot
proteins
pubmed
18767156
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19864460
uniprot
proteins
pubmed
20479262
uniprot
proteins
pubmed
20695905
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21295486
uniprot
proteins
pubmed
22813749
uniprot
proteins
pubmed
23187700
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
29276085
uniprot
proteins
pubmed
29507755
uniprot
proteins
pubmed
8626397
uniprot
proteins
pubmed
9659921
uniprot
proteins
sequence_length
227
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15169763, ECO:0000269|PubMed:19864460, ECO:0000269|PubMed:20695905, ECO:0000269|PubMed:9659921}. Cytoplasm {ECO:0000269|PubMed:19864460}. Note=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). {ECO:0000269|PubMed:15169763, ECO:0000269|PubMed:19864460}.
uniprot
proteins