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Cleavage and polyadenylation specificity factor subunit 5 (Cleavage and polyadenylation specificity factor 25 kDa subunit) (CFIm25) (CPSF 25 kDa subunit) (Nucleoside diphosphate-linked moiety X motif 21) (Nudix motif 21) (Pre-mRNA cleavage factor Im 25 kDa subunit)

 CPSF5_HUMAN             Reviewed;         227 AA.
O43809; Q6IB85; Q6NE84;
07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
22-NOV-2017, entry version 162.
RecName: Full=Cleavage and polyadenylation specificity factor subunit 5;
AltName: Full=Cleavage and polyadenylation specificity factor 25 kDa subunit;
Short=CFIm25;
Short=CPSF 25 kDa subunit;
AltName: Full=Nucleoside diphosphate-linked moiety X motif 21;
Short=Nudix motif 21;
AltName: Full=Pre-mRNA cleavage factor Im 25 kDa subunit;
Name=NUDT21; Synonyms=CFIM25, CPSF25, CPSF5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 60-73 AND 183-189,
FUNCTION, IDENTIFICATION IN THE CLEAVAGE FACTOR IM COMPLEX, AND
SUBCELLULAR LOCATION.
TISSUE=Brain;
PubMed=9659921; DOI=10.1016/S1097-2765(00)80025-8;
Rueegsegger U., Blank D., Keller W.;
"Human pre-mRNA cleavage factor Im is related to spliceosomal SR
proteins and can be reconstituted in vitro from recombinant
subunits.";
Mol. Cell 1:243-253(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Retina;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 2-15; 24-50 AND 79-131, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Ovarian carcinoma;
Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[7]
FUNCTION, IDENTIFICATION IN A CLEAVAGE FACTOR IM COMPLEX, AND
RNA-BINDING.
PubMed=8626397; DOI=10.1074/jbc.271.11.6107;
Rueegsegger U., Beyer K., Keller W.;
"Purification and characterization of human cleavage factor Im
involved in the 3' end processing of messenger RNA precursors.";
J. Biol. Chem. 271:6107-6113(1996).
[8]
FUNCTION, AND RNA-BINDING.
PubMed=14690600; DOI=10.1016/S1097-2765(03)00453-2;
Brown K.M., Gilmartin G.M.;
"A mechanism for the regulation of pre-mRNA 3' processing by human
cleavage factor Im.";
Mol. Cell 12:1467-1476(2003).
[9]
IDENTIFICATION IN A CLEAVAGE FACTOR IM COMPLEX, INTERACTION WITH CPSF6
AND SNRNP70, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=14561889; DOI=10.1261/rna.5104603;
Awasthi S., Alwine J.C.;
"Association of polyadenylation cleavage factor I with U1 snRNP.";
RNA 9:1400-1409(2003).
[10]
IDENTIFICATION IN A CLEAVAGE FACTOR IM COMPLEX, INTERACTION WITH
CPSF6; PAPOLA AND PABPN1, RNA-BINDING, AND SUBCELLULAR LOCATION.
PubMed=15169763; DOI=10.1074/jbc.M403927200;
Dettwiler S., Aringhieri C., Cardinale S., Keller W., Barabino S.M.;
"Distinct sequence motifs within the 68-kDa subunit of cleavage factor
Im mediate RNA binding, protein-protein interactions, and subcellular
localization.";
J. Biol. Chem. 279:35788-35797(2004).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-40, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
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.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[12]
ACETYLATION AT LYS-23, INTERACTION WITH PAPOLA AND CPSF6,
IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF LYS-23 AND
LYS-29.
PubMed=17172643; DOI=10.1074/jbc.M609745200;
Shimazu T., Horinouchi S., Yoshida M.;
"Multiple histone deacetylases and the CREB-binding protein regulate
pre-mRNA 3'-end processing.";
J. Biol. Chem. 282:4470-4478(2007).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-23; LYS-29 AND LYS-56, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[14]
FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=20695905; DOI=10.1111/j.1365-2443.2010.01436.x;
Kim S., Yamamoto J., Chen Y., Aida M., Wada T., Handa H.,
Yamaguchi Y.;
"Evidence that cleavage factor Im is a heterotetrameric protein
complex controlling alternative polyadenylation.";
Genes Cells 15:1003-1013(2010).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-15, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[19]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF APO FORM AND IN COMPLEX WITH
BETA DIADENOSINE TETRAPHOSPHATE, LACK OF METAL-BINDING, AND
HOMODIMERIZATION.
PubMed=18445629; DOI=10.1093/nar/gkn079;
Coseno M., Martin G., Berger C., Gilmartin G., Keller W., Doublie S.;
"Crystal structure of the 25 kDa subunit of human cleavage factor
Im.";
Nucleic Acids Res. 36:3474-3483(2008).
[20]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF APO FORM AND IN COMPLEX WITH
SULFATE.
PubMed=18767156; DOI=10.1002/prot.22198;
Tresaugues L., Stenmark P., Schaeler H., Flodin S., Welin M.,
Nyman T., Hammarstroem M., Moche M., Graeslund S., Nordlund P.;
"The crystal structure of human cleavage and polyadenylation specific
factor-5 reveals a dimeric Nudix protein with a conserved catalytic
site.";
Proteins 73:1047-1052(2008).
[21]
X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) IN COMPLEXES WITH RNA UGUAAA
AND UUGUAU, FUNCTION, SUBUNIT, AND MUTAGENESIS OF GLU-55; ARG-63;
GLU-81 AND PHE-103.
PubMed=20479262; DOI=10.1073/pnas.1000848107;
Yang Q., Gilmartin G.M., Doublie S.;
"Structural basis of UGUA recognition by the Nudix protein CFI(m)25
and implications for a regulatory role in mRNA 3' processing.";
Proc. Natl. Acad. Sci. U.S.A. 107:10062-10067(2010).
[22]
X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 21-227 IN COMPLEX WITH
CPSF7, AND SUBUNIT.
Structural genomics consortium (SGC);
"Crystal structure of the complex between the 25 kDA subunit and the
59 kDA subunit (RRM domain) of human cleavage factor Im.";
Submitted (JUL-2010) to the PDB data bank.
[23]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 21-227 IN COMPLEX WITH CPSF6
AND RNA, FUNCTION, SUBUNIT, AND MUTAGENESIS OF GLU-55; ARG-63;
PHE-103; TYR-158 AND TYR-160.
PubMed=21295486; DOI=10.1016/j.str.2010.12.021;
Yang Q., Coseno M., Gilmartin G.M., Doublie S.;
"Crystal structure of a human cleavage factor CFI(m)25/CFI(m)68/RNA
complex provides an insight into poly(A) site recognition and RNA
looping.";
Structure 19:368-377(2011).
-!- FUNCTION: Component of the cleavage factor Im (CFIm) complex that
plays a key role in pre-mRNA 3'-processing. Involved in
association with CPSF6 or CPSF7 in pre-MRNA 3'-end poly(A) site
cleavage and poly(A) addition. NUDT21/CPSF5 binds to cleavage and
polyadenylation RNA substrates. The homodimer mediates
simultaneous sequence-specific recognition of two 5'-UGUA-3'
elements within the pre-mRNA. Binds to, but does not hydrolyze
mono- and di-adenosine nucleotides. May have a role in mRNA
export. {ECO:0000269|PubMed:14690600, ECO:0000269|PubMed:20479262,
ECO:0000269|PubMed:20695905, ECO:0000269|PubMed:21295486,
ECO:0000269|PubMed:8626397, ECO:0000269|PubMed:9659921}.
-!- SUBUNIT: Homodimer. Component of the cleavage factor Im (CFIm)
complex, composed of, at least, NUDT21/CPSF5 and CPSF6 or CPSF7.
Within the cleavage factor Im complex, the NUDT21/CPSF5 homodimer
is at the core of a heterotetramer, and is clasped by two
additional subunits (CPSF6 or CPSF7). Interacts with CPSF6, CPSF7,
PABPN1 and SNRNP70. Interacts with PAPOLA; the interaction is
diminished by acetylation. {ECO:0000269|PubMed:14561889,
ECO:0000269|PubMed:15169763, ECO:0000269|PubMed:17172643,
ECO:0000269|PubMed:18445629, ECO:0000269|PubMed:18767156,
ECO:0000269|PubMed:20479262, ECO:0000269|PubMed:20695905,
ECO:0000269|PubMed:21295486, ECO:0000269|PubMed:8626397,
ECO:0000269|PubMed:9659921, ECO:0000269|Ref.22}.
-!- INTERACTION:
Self; NbExp=5; IntAct=EBI-355720, EBI-355720;
P54253:ATXN1; NbExp=2; IntAct=EBI-355720, EBI-930964;
Q86X55:CARM1; NbExp=2; IntAct=EBI-355720, EBI-2339854;
Q16630:CPSF6; NbExp=5; IntAct=EBI-355720, EBI-358410;
Q16630-1:CPSF6; NbExp=4; IntAct=EBI-355720, EBI-1019636;
Q16630-2:CPSF6; NbExp=3; IntAct=EBI-355720, EBI-11088043;
Q8N684:CPSF7; NbExp=5; IntAct=EBI-355720, EBI-746909;
Q08379:GOLGA2; NbExp=7; IntAct=EBI-355720, EBI-618309;
P60660:MYL6; NbExp=3; IntAct=EBI-355720, EBI-300817;
P14373:TRIM27; NbExp=5; IntAct=EBI-355720, EBI-719493;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15169763,
ECO:0000269|PubMed:20695905, ECO:0000269|PubMed:9659921}. Note=In
punctate subnuclear structures localized adjacent to nuclear
speckles, called paraspeckles.
-!- 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,
ECO:0000269|Ref.6}.
-!- SIMILARITY: Belongs to the Nudix hydrolase family. CPSF5
subfamily. {ECO:0000305}.
-!- CAUTION: Lacks the conserved metal-binding residues in the NUDIX
motif and does not have hydrolase activity. {ECO:0000305}.
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EMBL; AJ001810; CAA05026.1; -; mRNA.
EMBL; CR456919; CAG33200.1; -; mRNA.
EMBL; BX537360; CAD97606.1; -; mRNA.
EMBL; AC092140; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC001403; AAH01403.1; -; mRNA.
CCDS; CCDS10760.1; -.
RefSeq; NP_008937.1; NM_007006.2.
UniGene; Hs.528834; -.
PDB; 2CL3; X-ray; 1.90 A; A=21-227.
PDB; 2J8Q; X-ray; 2.30 A; A/B=24-227.
PDB; 3BAP; X-ray; 1.85 A; A=1-227.
PDB; 3BHO; X-ray; 1.80 A; A=20-227.
PDB; 3MDG; X-ray; 2.22 A; A/B=1-227.
PDB; 3MDI; X-ray; 2.07 A; A/B=1-227.
PDB; 3N9U; X-ray; 1.92 A; A/B=21-227.
PDB; 3P5T; X-ray; 2.70 A; A/B/C/D/E/F=34-227.
PDB; 3P6Y; X-ray; 2.90 A; A/B/E/F/I/J/M/N=34-227.
PDB; 3Q2S; X-ray; 2.90 A; A/B=21-227.
PDB; 3Q2T; X-ray; 3.06 A; A/B=21-227.
PDBsum; 2CL3; -.
PDBsum; 2J8Q; -.
PDBsum; 3BAP; -.
PDBsum; 3BHO; -.
PDBsum; 3MDG; -.
PDBsum; 3MDI; -.
PDBsum; 3N9U; -.
PDBsum; 3P5T; -.
PDBsum; 3P6Y; -.
PDBsum; 3Q2S; -.
PDBsum; 3Q2T; -.
ProteinModelPortal; O43809; -.
SMR; O43809; -.
BioGrid; 116237; 122.
CORUM; O43809; -.
DIP; DIP-42502N; -.
IntAct; O43809; 83.
MINT; MINT-5002263; -.
STRING; 9606.ENSP00000300291; -.
iPTMnet; O43809; -.
PhosphoSitePlus; O43809; -.
SwissPalm; O43809; -.
BioMuta; NUDT21; -.
UCD-2DPAGE; O43809; -.
EPD; O43809; -.
MaxQB; O43809; -.
PaxDb; O43809; -.
PeptideAtlas; O43809; -.
PRIDE; O43809; -.
TopDownProteomics; O43809; -.
DNASU; 11051; -.
Ensembl; ENST00000300291; ENSP00000300291; ENSG00000167005.
GeneID; 11051; -.
KEGG; hsa:11051; -.
UCSC; uc002eja.4; human.
CTD; 11051; -.
DisGeNET; 11051; -.
EuPathDB; HostDB:ENSG00000167005.13; -.
GeneCards; NUDT21; -.
HGNC; HGNC:13870; NUDT21.
HPA; HPA019863; -.
HPA; HPA074228; -.
MIM; 604978; gene.
neXtProt; NX_O43809; -.
OpenTargets; ENSG00000167005; -.
PharmGKB; PA26845; -.
eggNOG; KOG1689; Eukaryota.
eggNOG; ENOG410XS8Z; LUCA.
GeneTree; ENSGT00390000015814; -.
HOGENOM; HOG000161320; -.
HOVERGEN; HBG052968; -.
InParanoid; O43809; -.
KO; K14397; -.
OMA; CLAQWWR; -.
OrthoDB; EOG091G0HGL; -.
PhylomeDB; O43809; -.
TreeFam; TF106356; -.
Reactome; R-HSA-109688; Cleavage of Growing Transcript in the Termination Region.
Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
Reactome; R-HSA-72187; mRNA 3'-end processing.
Reactome; R-HSA-77595; Processing of Intronless Pre-mRNAs.
ChiTaRS; NUDT21; human.
EvolutionaryTrace; O43809; -.
GeneWiki; NUDT21; -.
GenomeRNAi; 11051; -.
PRO; PR:O43809; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000167005; -.
CleanEx; HS_NUDT21; -.
ExpressionAtlas; O43809; baseline and differential.
Genevisible; O43809; HS.
GO; GO:0005813; C:centrosome; IDA:LIFEdb.
GO; GO:0005815; C:microtubule organizing center; IDA:HPA.
GO; GO:0005849; C:mRNA cleavage factor complex; IDA:UniProtKB.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0042382; C:paraspeckles; IDA:UniProtKB.
GO; GO:0017091; F:AU-rich element binding; IDA:UniProtKB.
GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0031124; P:mRNA 3'-end processing; TAS:Reactome.
GO; GO:0006378; P:mRNA polyadenylation; IMP:UniProtKB.
GO; GO:0006397; P:mRNA processing; IDA:UniProtKB.
GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
GO; GO:0051262; P:protein tetramerization; IDA:UniProtKB.
GO; GO:0006369; P:termination of RNA polymerase II transcription; TAS:Reactome.
InterPro; IPR016706; Cleav_polyA_spec_factor_su5.
InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
InterPro; IPR000086; NUDIX_hydrolase_dom.
PANTHER; PTHR13047; PTHR13047; 1.
Pfam; PF13869; NUDIX_2; 1.
PIRSF; PIRSF017888; CPSF-25; 1.
SUPFAM; SSF55811; SSF55811; 1.
PROSITE; PS51462; NUDIX; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome;
Direct protein sequencing; Methylation; mRNA processing; Nucleus;
Phosphoprotein; Reference proteome; RNA-binding.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.6}.
CHAIN 2 227 Cleavage and polyadenylation specificity
factor subunit 5.
/FTId=PRO_0000057150.
DOMAIN 76 201 Nudix hydrolase. {ECO:0000255|PROSITE-
ProRule:PRU00794}.
REGION 2 147 Necessary for RNA-binding.
REGION 81 160 Necessary for interactions with PAPOLA
and PABPN1.
REGION 102 104 Interaction with RNA.
MOTIF 109 130 Nudix box.
SITE 55 55 Interaction with RNA.
SITE 63 63 Interaction with RNA.
SITE 208 208 Interaction with RNA.
MOD_RES 2 2 N-acetylserine. {ECO:0000269|Ref.6}.
MOD_RES 15 15 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 23 23 N6-acetyllysine.
{ECO:0000244|PubMed:19608861,
ECO:0000269|PubMed:17172643}.
MOD_RES 29 29 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 40 40 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
MOD_RES 56 56 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MUTAGEN 23 23 K->R: Abolishes acetylation.
{ECO:0000269|PubMed:17172643}.
MUTAGEN 29 29 K->R: No effect on acetylation.
{ECO:0000269|PubMed:17172643}.
MUTAGEN 55 55 E->A: Reduces affinity for UGUA RNA by
88%. {ECO:0000269|PubMed:20479262,
ECO:0000269|PubMed:21295486}.
MUTAGEN 63 63 R->S: Reduces affinity for UGUA RNA by
99%. {ECO:0000269|PubMed:20479262,
ECO:0000269|PubMed:21295486}.
MUTAGEN 81 81 E->A: Reduces affinity for UGUA RNA by
12%. {ECO:0000269|PubMed:20479262}.
MUTAGEN 103 103 F->A: Reduces affinity for UGUA RNA by
99%. {ECO:0000269|PubMed:20479262,
ECO:0000269|PubMed:21295486}.
MUTAGEN 103 103 F->W: Reduces affinity for UGUA RNA by
over 90%. {ECO:0000269|PubMed:20479262,
ECO:0000269|PubMed:21295486}.
MUTAGEN 154 154 E->A: Reduces affinity for UGUA RNA by
50%.
MUTAGEN 158 158 Y->A: Abolishes interaction with CPSF6;
when associated with A-160.
{ECO:0000269|PubMed:21295486}.
MUTAGEN 160 160 Y->A: Abolishes interaction with CPSF6;
when associated with A-158.
{ECO:0000269|PubMed:21295486}.
CONFLICT 57 57 D -> G (in Ref. 2; CAG33200).
{ECO:0000305}.
CONFLICT 112 112 N -> D (in Ref. 3; CAD97606).
{ECO:0000305}.
CONFLICT 218 218 L -> P (in Ref. 3; CAD97606).
{ECO:0000305}.
TURN 31 33 {ECO:0000244|PDB:3BHO}.
STRAND 36 39 {ECO:0000244|PDB:3BHO}.
HELIX 42 44 {ECO:0000244|PDB:3BHO}.
STRAND 45 50 {ECO:0000244|PDB:3BHO}.
HELIX 60 74 {ECO:0000244|PDB:3BHO}.
STRAND 76 88 {ECO:0000244|PDB:3BHO}.
STRAND 91 100 {ECO:0000244|PDB:3BHO}.
STRAND 103 105 {ECO:0000244|PDB:3BHO}.
STRAND 107 110 {ECO:0000244|PDB:3BHO}.
HELIX 117 129 {ECO:0000244|PDB:3BHO}.
STRAND 132 134 {ECO:0000244|PDB:3N9U}.
STRAND 140 150 {ECO:0000244|PDB:3BHO}.
STRAND 152 155 {ECO:0000244|PDB:3BHO}.
STRAND 158 160 {ECO:0000244|PDB:3BHO}.
STRAND 169 178 {ECO:0000244|PDB:3BHO}.
STRAND 181 188 {ECO:0000244|PDB:3BHO}.
STRAND 192 197 {ECO:0000244|PDB:3BHO}.
HELIX 198 201 {ECO:0000244|PDB:3BHO}.
HELIX 205 212 {ECO:0000244|PDB:3BHO}.
HELIX 215 219 {ECO:0000244|PDB:3BHO}.
STRAND 223 226 {ECO:0000244|PDB:3BHO}.
SEQUENCE 227 AA; 26227 MW; D204243E57F1CCC5 CRC64;
MSVVPPNRSQ TGWPRGVTQF GNKYIQQTKP LTLERTINLY PLTNYTFGTK EPLYEKDSSV
AARFQRMREE FDKIGMRRTV EGVLIVHEHR LPHVLLLQLG TTFFKLPGGE LNPGEDEVEG
LKRLMTEILG RQDGVLQDWV IDDCIGNWWR PNFEPPQYPY IPAHITKPKE HKKLFLVQLQ
EKALFAVPKN YKLVAAPLFE LYDNAPGYGP IISSLPQLLS RFNFIYN


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