NUDT21

Functionⁱ

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).By similarity14 Publications

Caution

Lacks the conserved metal-binding residues in the NUDIX motif and does not have hydrolase activity.Curated

GO - Molecular functionⁱ

AU-rich element binding
Source: UniProtKB
Inferred from direct assayⁱ
- 20479262
- 21295486
chromatin binding Source: Ensembl
histone deacetylase binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 17172643
hydrolase activity Source: InterPro
identical protein binding
Source: UniProtKB
Inferred from direct assayⁱ
- 20695905
mRNA binding
Source: UniProtKB
Inferred from direct assayⁱ
- 21295486
protein homodimerization activity
Source: UniProtKB
Inferred from physical interactionⁱ
- 20479262
- 21295486
RNA binding
Source: UniProtKB
Inferred from high throughput direct assayⁱ
- 22658674
- 22681889

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cell differentiation Source: UniProtKB-KW
messenger ribonucleoprotein complex assembly
Source: UniProtKB
Inferred from direct assayⁱ
- 29276085
mRNA 3'-end processing Source: Reactome
mRNA alternative polyadenylation
Source: UniProtKB
Inferred from mutant phenotypeⁱ
mRNA polyadenylation Source: InterPro
mRNA processing
Source: UniProtKB
Inferred from direct assayⁱ
- 8626397
mRNA splicing, via spliceosome Source: Reactome
positive regulation of mRNA cleavage
Source: UniProtKB
Inferred from direct assayⁱ
- 15937220
positive regulation of mRNA polyadenylation
Source: UniProtKB
Inferred from direct assayⁱ
- 15937220
positive regulation of pro-B cell differentiation Source: UniProtKB
positive regulation of stem cell differentiation Source: UniProtKB
posttranscriptional regulation of gene expression Source: UniProtKB
pre-mRNA cleavage required for polyadenylation
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 20695905
protein heterotetramerization
Source: UniProtKB
Inferred from direct assayⁱ
- 23187700
protein tetramerization
Source: UniProtKB
Inferred from direct assayⁱ
- 21295486
termination of RNA polymerase II transcription Source: Reactome

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	RNA-binding
Biological process	Differentiation, mRNA processing

Enzyme and pathway databases

Reactomeⁱ	R-HSA-109688 Cleavage of Growing Transcript in the Termination Region R-HSA-72163 mRNA Splicing - Major Pathway R-HSA-72187 mRNA 3'-end processing R-HSA-77595 Processing of Intronless Pre-mRNAs

Reactomeⁱ

R-HSA-109688 Cleavage of Growing Transcript in the Termination Region
R-HSA-72163 mRNA Splicing - Major Pathway
R-HSA-72187 mRNA 3'-end processing
R-HSA-77595 Processing of Intronless Pre-mRNAs

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Cleavage and polyadenylation specificity factor subunit 51 Publication Alternative name(s): Cleavage and polyadenylation specificity factor 25 kDa subunit Short name: CPSF 25 kDa subunit Cleavage factor Im complex 25 kDa subunit1 Publication Short name: CFIm251 Publication Nucleoside diphosphate-linked moiety X motif 21 Short name: Nudix motif 21 Nudix hydrolase 21Curated Pre-mRNA cleavage factor Im 68 kDa subunit
Gene namesⁱ	Name:NUDT21Imported Synonyms:CFIM251 Publication, CPSF25, CPSF51 Publication
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 16

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000167005.13
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:13870 NUDT21
MIMⁱ	604978 gene
neXtProtⁱ	NX_O43809

Keywords - Cellular componentⁱ

Cytoplasm, Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	23	K → R: Abolishes acetylation. 1 Publication	1
Mutagenesisⁱ	29	K → R: No effect on acetylation. 1 Publication	1
Mutagenesisⁱ	55	E → A: Reduces affinity for UGUA RNA by 88%. 2 Publications	1
Mutagenesisⁱ	63	R → S: Reduces affinity for UGUA RNA by 99%. 2 Publications	1
Mutagenesisⁱ	81	E → A: Reduces affinity for UGUA RNA by 12%. 1 Publication	1
Mutagenesisⁱ	103	F → A: Reduces affinity for UGUA RNA by 99%. 2 Publications	1
Mutagenesisⁱ	103	F → W: Reduces affinity for UGUA RNA by over 90%. 2 Publications	1
Mutagenesisⁱ	154	E → A: Reduces affinity for UGUA RNA by 50%.	1
Mutagenesisⁱ	158	Y → A: Abolishes interaction with CPSF6; when associated with A-160. 1 Publication	1
Mutagenesisⁱ	160	Y → A: Abolishes interaction with CPSF6; when associated with A-158. 1 Publication	1
Mutagenesisⁱ	218	L → R: Reduces interactions with CPSF6 and CPSF7 and deacreases mRNA 3'-processing activity. 1 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	11051
Open Targets More...OpenTargetsⁱ	ENSG00000167005
PharmGKBⁱ	PA26845

Polymorphism and mutation databases

BioMutaⁱ	NUDT21

BioMutaⁱ

NUDT21

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		Removed1 Publication
ChainⁱPRO_0000057150	2 – 227	Cleavage and polyadenylation specificity factor subunit 5Add BLAST		226

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	2	N-acetylserine1 Publication	1
Modified residueⁱ	15	Omega-N-methylarginineCombined sources	1
Modified residueⁱ	23	N6-acetyllysineCombined sources1 Publication	1
Modified residueⁱ	29	N6-acetyllysineCombined sources	1
Modified residueⁱ	40	PhosphotyrosineCombined sources	1
Modified residueⁱ	56	N6-acetyllysineCombined sources	1

Post-translational modificationⁱ

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 SIRT2.1 Publication

Keywords - PTMⁱ

Acetylation, Methylation, Phosphoprotein

Proteomic databases

EPDⁱ	O43809
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	O43809
PaxDbⁱ	O43809
PeptideAtlas More...PeptideAtlasⁱ	O43809
PRIDEⁱ	O43809
ProteomicsDBⁱ	49176
TopDownProteomicsⁱ	O43809

2D gel databases

UCD-2DPAGEⁱ	O43809

UCD-2DPAGEⁱ

O43809

PTM databases

iPTMnetⁱ	O43809
PhosphoSitePlusⁱ	O43809
SwissPalmⁱ	O43809

Expressionⁱ

Tissue specificityⁱ

Expressed in the heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.1 Publication

Gene expression databases

Bgeeⁱ	ENSG00000167005 Expressed in 229 organ(s), highest expression level in testis
CleanExⁱ	HS_NUDT21
ExpressionAtlasⁱ	O43809 baseline and differential
Genevisibleⁱ	O43809 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA019863 HPA074228

HPAⁱ

HPA019863
HPA074228

Interactionⁱ

Subunit structureⁱ

Homodimer (via N- and C-terminus); binds RNA as homodimer (PubMed:20695905, PubMed:18445629, PubMed:20479262). Component of the cleavage factor Im (CFIm) complex which is an heterotetramer composed of two subunits of NUDT21/CPSF5 and two subunits of CPSF6 or CPSF7 or an heterodimer of CPSF6 and CPSF7 (PubMed:9659921, PubMed:8626397, PubMed:14561889, PubMed:20695905, PubMed:23187700, PubMed:21295486). The cleavage factor Im (CFIm) complex associates with the CPSF and CSTF complexes to promote the assembly of the core mRNA 3'-processing machinery (PubMed:29276085). Interacts with CPSF6 (via the RRM domain); this interaction is direct and enhances binding to RNA (PubMed:14561889, PubMed:15169763, PubMed:17172643, PubMed:19864460, PubMed:29276085). Interacts with CPSF7 (PubMed:29276085, Ref. 30). Interacts with FIP1L1; this interaction occurs in a RNA sequence-specific manner (PubMed:15937220). Interacts with PABPN1 (PubMed:15169763). Interacts (via N-terminus) with PAPOLA (via C-terminus); this interaction is direct and diminished by acetylation (PubMed:15169763, PubMed:17172643). Interacts with SNRNP70 (PubMed:14561889). Interacts with VIRMA (PubMed:29507755).15 Publications

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Siteⁱ	55	Interaction with RNA1 PublicationImported		1
Siteⁱ	63	Interaction with RNA1 PublicationImported		1

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
itself		5	EBI-355720,EBI-355720
ATXN1	P54253	2	EBI-355720,EBI-930964
CARM1	Q86X55	2	EBI-355720,EBI-2339854
CPSF6	Q16630	5	EBI-355720,EBI-358410
CPSF6	Q16630-1	4	EBI-355720,EBI-1019636
CPSF6	Q16630-2	3	EBI-355720,EBI-11088043
CPSF7	Q8N684	5	EBI-355720,EBI-746909
GOLGA2	Q08379	5	EBI-355720,EBI-618309
MYL6	P60660	3	EBI-355720,EBI-300817
TRIM27	P14373	5	EBI-355720,EBI-719493

GO - Molecular functionⁱ

histone deacetylase binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 17172643
identical protein binding
Source: UniProtKB
Inferred from direct assayⁱ
- 20695905
protein homodimerization activity
Source: UniProtKB
Inferred from physical interactionⁱ
- 20479262
- 21295486

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	116237, 183 interactors
CORUMⁱ	O43809
Database of interacting proteins More...DIPⁱ	DIP-42502N
IntActⁱ	O43809, 92 interactors
Molecular INTeraction database More...MINTⁱ	O43809
STRINGⁱ	9606.ENSP00000300291

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Turnⁱ	31 – 33	Combined sources	3
Beta strandⁱ	36 – 39	Combined sources	4
Helixⁱ	42 – 44	Combined sources	3
Beta strandⁱ	45 – 50	Combined sources	6
Helixⁱ	60 – 74	Combined sources	15
Beta strandⁱ	76 – 88	Combined sources	13
Beta strandⁱ	91 – 100	Combined sources	10
Beta strandⁱ	103 – 105	Combined sources	3
Beta strandⁱ	107 – 110	Combined sources	4
Helixⁱ	117 – 129	Combined sources	13
Beta strandⁱ	132 – 134	Combined sources	3
Beta strandⁱ	140 – 150	Combined sources	11
Beta strandⁱ	152 – 155	Combined sources	4
Beta strandⁱ	158 – 160	Combined sources	3
Beta strandⁱ	169 – 178	Combined sources	10
Beta strandⁱ	181 – 188	Combined sources	8
Beta strandⁱ	192 – 197	Combined sources	6
Helixⁱ	198 – 201	Combined sources	4
Helixⁱ	205 – 212	Combined sources	8
Helixⁱ	215 – 219	Combined sources	5
Beta strandⁱ	223 – 226	Combined sources	4

Show more details

3D structure databases

ProteinModelPortalⁱ	O43809
SMRⁱ	O43809
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	O43809

EvolutionaryTraceⁱ

O43809

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	76 – 201	Nudix hydrolasePROSITE-ProRule annotationAdd BLAST		126

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	2 – 147	Necessary for RNA-binding1 PublicationAdd BLAST	146
Regionⁱ	81 – 160	Necessary for interactions with PAPOLA and PABPN11 PublicationAdd BLAST	80
Regionⁱ	102 – 104	Interaction with RNA2 PublicationsImported	3

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	109 – 130	Nudix boxAdd BLAST		22

Sequence similaritiesⁱ

Belongs to the Nudix hydrolase family. CPSF5 subfamily.Curated

Phylogenomic databases

eggNOGⁱ	KOG1689 Eukaryota ENOG410XS8Z LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000015814
HOGENOMⁱ	HOG000161320
HOVERGENⁱ	HBG052968
InParanoidⁱ	O43809
KEGG Orthology (KO) More...KOⁱ	K14397
OMAⁱ	SRYNFIY
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0HGL
PhylomeDBⁱ	O43809
TreeFamⁱ	TF106356

Family and domain databases

InterProⁱ	View protein in InterPro IPR016706 Cleav_polyA_spec_factor_su5 IPR015797 NUDIX_hydrolase-like_dom_sf IPR000086 NUDIX_hydrolase_dom
PANTHERⁱ	PTHR13047 PTHR13047, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF13869 NUDIX_2, 1 hit
PIRSFⁱ	PIRSF017888 CPSF-25, 1 hit
SUPFAMⁱ	SSF55811 SSF55811, 1 hit
PROSITEⁱ	View protein in PROSITE PS51462 NUDIX, 1 hit

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show all Align All

O43809-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MSVVPPNRSQ TGWPRGVTQF GNKYIQQTKP LTLERTINLY PLTNYTFGTK 
        60         70         80         90        100
EPLYEKDSSV AARFQRMREE FDKIGMRRTV EGVLIVHEHR LPHVLLLQLG 
       110        120        130        140        150
TTFFKLPGGE LNPGEDEVEG LKRLMTEILG RQDGVLQDWV IDDCIGNWWR 
       160        170        180        190        200
PNFEPPQYPY IPAHITKPKE HKKLFLVQLQ EKALFAVPKN YKLVAAPLFE 
       210        220 
LYDNAPGYGP IISSLPQLLS RFNFIYN

Length:227

Mass (Da):26,227

Last modified:June 1, 1998 - v1

Checksum:ⁱD204243E57F1CCC5

GO

Computationally mapped potential isoform sequencesⁱ

There are 2 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

H3BND3	H3BND3_HUMAN	Cleavage and polyadenylation-specif... Cleavage and polyadenylation-specificity factor subunit 5	NUDT21	149	Annotation score:
H3BV41	H3BV41_HUMAN	Cleavage and polyadenylation-specif... Cleavage and polyadenylation-specificity factor subunit 5	NUDT21	71	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	57	D → G in CAG33200 (Ref. 2) Curated	1
Sequence conflictⁱ	112	N → D in CAD97606 (PubMed:17974005).Curated	1
Sequence conflictⁱ	218	L → P in CAD97606 (PubMed:17974005).Curated	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AJ001810 mRNA Translation: CAA05026.1 CR456919 mRNA Translation: CAG33200.1 BX537360 mRNA Translation: CAD97606.1 AC092140 Genomic DNA No translation available. BC001403 mRNA Translation: AAH01403.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS10760.1
NCBI Reference Sequences More...RefSeqⁱ	NP_008937.1, NM_007006.2
UniGeneⁱ	Hs.528834

Genome annotation databases

Ensemblⁱ	ENST00000300291; ENSP00000300291; ENSG00000167005
GeneIDⁱ	11051
KEGGⁱ	hsa:11051
UCSC genome browser More...UCSCⁱ	uc002eja.4 human

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
O43809	Cleavage and polyadenylation specificity factor subunit 5		BOVIN		227	UniRef100_O43809
Cleavage and polyadenylation specificity factor subunit 5		PONAB		227
Nudix (Nucleoside diphosphate linked moiety X)-type motif 21, isoform CRA_a		HUMAN		227
Cleavage and polyadenylation specificity factor subunit 5		CALJA		227
NUDT21 isoform 2		PANTR		227
+19

Protein	Similar proteins		Species	Score	Length	Source
O43809	Cleavage and polyadenylation specificity factor subunit 5		BOVIN		227	UniRef90_O43809
Cleavage and polyadenylation specificity factor subunit 5		PONAB		227
Cleavage and polyadenylation specificity factor subunit 5		DANRE		228
Cleavage and polyadenylation specificity factor subunit 5		MOUSE		227
Cleavage and polyadenylation specificity factor subunit 5		RAT		227
+162

Protein	Similar proteins		Species	Score	Length	Source
O43809	Cleavage and polyadenylation specificity factor subunit 5		BOVIN		227	UniRef50_O43809
Cleavage and polyadenylation specificity factor subunit 5		PONAB		227
Cleavage and polyadenylation specificity factor subunit 5		DANRE		228
Cleavage and polyadenylation specificity factor subunit 5		MOUSE		227
Cleavage and polyadenylation specificity factor subunit 5		RAT		227
+172

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AJ001810 mRNA Translation: CAA05026.1 CR456919 mRNA Translation: CAG33200.1 BX537360 mRNA Translation: CAD97606.1 AC092140 Genomic DNA No translation available. BC001403 mRNA Translation: AAH01403.1
CCDSⁱ	CCDS10760.1
RefSeqⁱ	NP_008937.1, NM_007006.2
UniGeneⁱ	Hs.528834

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	2CL3	X-ray	1.90	A	21-227	[»]
	2J8Q	X-ray	2.30	A/B	24-227	[»]
	3BAP	X-ray	1.85	A	1-227	[»]
	3BHO	X-ray	1.80	A	20-227	[»]
	3MDG	X-ray	2.22	A/B	1-227	[»]
	3MDI	X-ray	2.07	A/B	1-227	[»]
	3N9U	X-ray	1.92	A/B	21-227	[»]
	3P5T	X-ray	2.70	A/B/C/D/E/F	34-227	[»]
	3P6Y	X-ray	2.90	A/B/E/F/I/J/M/N	34-227	[»]
	3Q2S	X-ray	2.90	A/B	21-227	[»]
	3Q2T	X-ray	3.06	A/B	21-227	[»]
ProteinModelPortalⁱ	O43809
SMRⁱ	O43809
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	116237, 183 interactors
CORUMⁱ	O43809
DIPⁱ	DIP-42502N
IntActⁱ	O43809, 92 interactors
MINTⁱ	O43809
STRINGⁱ	9606.ENSP00000300291

PTM databases

iPTMnetⁱ	O43809
PhosphoSitePlusⁱ	O43809
SwissPalmⁱ	O43809

Polymorphism and mutation databases

BioMutaⁱ	NUDT21

BioMutaⁱ

NUDT21

2D gel databases

UCD-2DPAGEⁱ	O43809

UCD-2DPAGEⁱ

O43809

Proteomic databases

EPDⁱ	O43809
MaxQBⁱ	O43809
PaxDbⁱ	O43809
PeptideAtlasⁱ	O43809
PRIDEⁱ	O43809
ProteomicsDBⁱ	49176
TopDownProteomicsⁱ	O43809

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	11051
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000300291; ENSP00000300291; ENSG00000167005
GeneIDⁱ	11051
KEGGⁱ	hsa:11051
UCSCⁱ	uc002eja.4 human

Organism-specific databases

CTDⁱ	11051
DisGeNETⁱ	11051
EuPathDBⁱ	HostDB:ENSG00000167005.13
GeneCardsⁱ	NUDT21
HGNCⁱ	HGNC:13870 NUDT21
HPAⁱ	HPA019863 HPA074228
MIMⁱ	604978 gene
neXtProtⁱ	NX_O43809
OpenTargetsⁱ	ENSG00000167005
PharmGKBⁱ	PA26845
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG1689 Eukaryota ENOG410XS8Z LUCA
GeneTreeⁱ	ENSGT00390000015814
HOGENOMⁱ	HOG000161320
HOVERGENⁱ	HBG052968
InParanoidⁱ	O43809
KOⁱ	K14397
OMAⁱ	SRYNFIY
OrthoDBⁱ	EOG091G0HGL
PhylomeDBⁱ	O43809
TreeFamⁱ	TF106356

Enzyme and pathway databases

Reactomeⁱ	R-HSA-109688 Cleavage of Growing Transcript in the Termination Region R-HSA-72163 mRNA Splicing - Major Pathway R-HSA-72187 mRNA 3'-end processing R-HSA-77595 Processing of Intronless Pre-mRNAs

Reactomeⁱ

R-HSA-109688 Cleavage of Growing Transcript in the Termination Region
R-HSA-72163 mRNA Splicing - Major Pathway
R-HSA-72187 mRNA 3'-end processing
R-HSA-77595 Processing of Intronless Pre-mRNAs

Miscellaneous databases

ChiTaRSⁱ	NUDT21 human
EvolutionaryTraceⁱ	O43809
GeneWikiⁱ	NUDT21
GenomeRNAiⁱ	11051
Protein Ontology More...PROⁱ	PR:O43809
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000167005 Expressed in 229 organ(s), highest expression level in testis
CleanExⁱ	HS_NUDT21
ExpressionAtlasⁱ	O43809 baseline and differential
Genevisibleⁱ	O43809 HS

Family and domain databases

InterProⁱ	View protein in InterPro IPR016706 Cleav_polyA_spec_factor_su5 IPR015797 NUDIX_hydrolase-like_dom_sf IPR000086 NUDIX_hydrolase_dom
PANTHERⁱ	PTHR13047 PTHR13047, 1 hit
Pfamⁱ	View protein in Pfam PF13869 NUDIX_2, 1 hit
PIRSFⁱ	PIRSF017888 CPSF-25, 1 hit
SUPFAMⁱ	SSF55811 SSF55811, 1 hit
PROSITEⁱ	View protein in PROSITE PS51462 NUDIX, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	CPSF5_HUMAN
Accessionⁱ	O43809Primary (citable) accession number: O43809 Secondary accession number(s): Q6IB85, Q6NE84
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	February 7, 2006
	Last sequence update:	June 1, 1998
	Last modified:	November 7, 2018
	This is version 171 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
Human chromosome 16
Human chromosome 16: entries, gene names and cross-references to MIM
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - O43809 (CPSF5_HUMAN)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Cleavage and polyadenylation specificity factor subunit 5

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Caution

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Nucleus

Other locations

Cytoskeleton

Nucleus

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Organism-specific databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

2D gel databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Sites

GO - Molecular functioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

Motif

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism and mutation databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

UniProt is an ELIXIR core data resource

Your basket is currently empty. ⁱ

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ