Cleavage and polyadenylation specificity factor subunit 5

Contribute

Send feedback

Reviewed, UniProtKB/Swiss-Prot O43809 (CPSF5_HUMAN)

Last modified December 16, 2008. Version 68. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein names

Recommended name:
    Cleavage and polyadenylation specificity factor subunit 5
Alternative name(s):
    Cleavage and polyadenylation specificity factor 25 kDa subunit
      Short name=CPSF 25 kDa subunit
    Pre-mRNA cleavage factor Im 25 kDa subunit
    Nucleoside diphosphate-linked moiety X motif 21
      Short name=Nudix motif 21

Gene names

Name:	NUDT21
Synonyms:	CFIM25, CPSF25, CPSF5

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Hide | Top

Protein attributes

Sequence length	227 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

Hide | Top

General annotation (Comments)

Function	Component of the cleavage factor Im (CFIm) complex that plays a key role in pre-mRNA 3'-processing. Involved in association with CPSF6 in pre-MRNA 3'-end poly(A) site cleavage and poly(A) addition. NUDT21/CPSF5 binds to cleavage and polyadenylation RNA substrates. Ref.1 Ref.5 Ref.6
Subunit structure	Component of the cleavage factor Im (CFIm) complex, composed at least of NUDT21/CPSF5 and CPSF6 or CPSF7. Interacts with CPSF6, PAPOLA, PABPN1 and SNRP70. Ref.7 Ref.8
Subcellular location	Nucleus. Note= In punctate subnuclear structures localized adjacent to nuclear speckles, called paraspeckles. Ref.1 Ref.8
Sequence similarities	Belongs to the Nudix hydrolase family. CPSF5 subfamily. Contains 1 nudix hydrolase domain.

Hide | Top

Ontologies

Keywords
Biological process	mRNA processing
Cellular component	Nucleus
Ligand	RNA-binding
PTM	Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	nuclear mRNA splicing, via spliceosome Inferred from Experiment. Source: Reactome
Cellular component	centrosome Inferred from direct assay. Source: LIFEdb paraspeckles Ref.8 Inferred from direct assay. Source: UniProtKB
Molecular function	RNA binding Ref.5 Inferred from electronic annotation. Source: UniProtKB-KW hydrolase activity Inferred from electronic annotation. Source: InterPro protein binding Ref.7 Ref.8 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Hide | Top

Binary interactions

With	Entry	#Exp.	IntAct
ATXN1	P54253	1	EBI-355720,EBI-930964
CD2BP2	O95400	1	EBI-355720,EBI-768015
RNPS1	Q15287	1	EBI-355720,EBI-395959

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 227

227

Cleavage and polyadenylation specificity factor subunit 5

PRO_0000057150

Regions

Domain

77 – 202

126

Nudix hydrolase

Region

1 – 147

147

Necessary for RNA-binding

Region

81 – 160

Necessary for interactions with PAPOLA and PABPN1

Amino acid modifications

Modified residue

Phosphotyrosine Ref.9

Experimental info

Sequence conflict

D → G in CAG33200. Ref.3

Sequence conflict

112

N → D in CAD97606. Ref.2

Sequence conflict

218

L → P in CAD97606. Ref.2

Secondary structure

227

Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

O43809-1 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: D204243E57F1CCC5
Show »

FASTA

227

26,227

        10         20         30         40         50         60 
MSVVPPNRSQ TGWPRGVTQF GNKYIQQTKP LTLERTINLY PLTNYTFGTK EPLYEKDSSV 

        70         80         90        100        110        120 
AARFQRMREE FDKIGMRRTV EGVLIVHEHR LPHVLLLQLG TTFFKLPGGE LNPGEDEVEG 

       130        140        150        160        170        180 
LKRLMTEILG RQDGVLQDWV IDDCIGNWWR PNFEPPQYPY IPAHITKPKE HKKLFLVQLQ 

       190        200        210        220 
EKALFAVPKN YKLVAAPLFE LYDNAPGYGP IISSLPQLLS RFNFIYN

« Hide

Hide | Top

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human pre-mRNA cleavage factor Im is related to spliceosomal SR proteins and can be reconstituted in vitro from recombinant subunits." Rueegsegger U., Blank D., Keller W. Mol. Cell 1:243-253(1998) [PubMed: 9659921] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 60-73 AND 183-189, FUNCTION, IDENTIFICATION IN THE CLEAVAGE FACTOR IM COMPLEX, SUBCELLULAR LOCATION. Tissue: Brain.
[2]	The German cDNA consortium Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Retina.
[3]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[5]	"Purification and characterization of human cleavage factor Im involved in the 3' end processing of messenger RNA precursors." Rueegsegger U., Beyer K., Keller W. J. Biol. Chem. 271:6107-6113(1996) [PubMed: 8626397] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN A CLEAVAGE FACTOR IM COMPLEX, RNA-BINDING.
[6]	"A mechanism for the regulation of pre-mRNA 3' processing by human cleavage factor Im." Brown K.M., Gilmartin G.M. Mol. Cell 12:1467-1476(2003) [PubMed: 14690600] [Abstract] Cited for: FUNCTION, RNA-BINDING.
[7]	"Association of polyadenylation cleavage factor I with U1 snRNP." Awasthi S., Alwine J.C. RNA 9:1400-1409(2003) [PubMed: 14561889] [Abstract] Cited for: IDENTIFICATION IN A CLEAVAGE FACTOR IM COMPLEX, INTERACTION WITH CPSF6 AND SNRP70, IDENTIFICATION BY MASS SPECTROMETRY.
[8]	"Distinct sequence motifs within the 68-kDa subunit of cleavage factor Im mediate RNA binding, protein-protein interactions, and subcellular localization." Dettwiler S., Aringhieri C., Cardinale S., Keller W., Barabino S.M. J. Biol. Chem. 279:35788-35797(2004) [PubMed: 15169763] [Abstract] Cited for: IDENTIFICATION IN A CLEAVAGE FACTOR IM COMPLEX, INTERACTION WITH CPSF6; PAPOLA AND PABPN1, RNA-BINDING, SUBCELLULAR LOCATION.
[9]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-40, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

AJ001810 mRNA. Translation: CAA05026.1.
BX537360 mRNA. Translation: CAD97606.1.
CR456919 mRNA. Translation: CAG33200.1.
BC001403 mRNA. Translation: AAH01403.1.

RefSeq

NP_008937.1.

UniGene

Hs.528834

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CL3	X-ray	1.90	A	21-227	[»]
2J8Q	X-ray	2.30	A/B	20-227	[»]
3BAP	X-ray	1.85	A	1-227	[»]
3BHO	X-ray	1.80	A	20-227	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

O43809. 21 interactions.

PTM databases

PhosphoSite

O43809.

Proteomic databases

PeptideAtlas

O43809.

PRIDE

O43809.

Genome annotation databases

Ensembl

ENSG00000167005. Homo sapiens. [Contig view]

GeneID

11051.

KEGG

hsa:11051.

Organism-specific databases

GeneCards

GC16M055021.

H-InvDB

HIX0013051.

HGNC

HGNC:13870. NUDT21.

MIM

604978. gene.

PharmGKB

PA26845.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

O43809.

HOVERGEN

O43809.

Enzyme and pathway databases

Reactome

REACT_1675. mRNA Processing.
REACT_1788. Transcription.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

O43809.

CleanEx

HS_NUDT21.

GermOnline

ENSG00000167005. Homo sapiens.

Family and domain databases

InterPro

IPR016706. Cleav_polyA_spec_factor_25kDa.
IPR000086. NUDIX_hydrolase_core.
[Graphical view]

Pfam

PF00293. NUDIX. 1 hit.
[Graphical view]

PIRSF

PIRSF017888. CPSF-25. 1 hit.

PROSITE

PS00893. NUDIX. False negative.
[Graphical view]

ProtoNet

Search...

Other Resources

LinkHub

O43809.

NextBio

41991.

SOURCE

Search...

Hide | Top

Entry information

Entry name

CPSF5_HUMAN

Accession

Primary (citable) accession number: O43809
Secondary accession number(s): Q6IB85, Q6NE84

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 7, 2006
Last sequence update:	June 1, 1998
Last modified:	December 16, 2008
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Hide | Top

Relevant documents

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

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents