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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.
23-MAY-2018, entry version 166.
RecName: Full=Cleavage and polyadenylation specificity factor subunit 5 {ECO:0000303|PubMed:23187700};
AltName: Full=Cleavage and polyadenylation specificity factor 25 kDa subunit;
Short=CPSF 25 kDa subunit;
AltName: Full=Cleavage factor Im complex 25 kDa subunit {ECO:0000303|PubMed:9659921};
Short=CFIm25 {ECO:0000303|PubMed:9659921};
AltName: Full=Nucleoside diphosphate-linked moiety X motif 21;
Short=Nudix motif 21;
AltName: Full=Nudix hydrolase 21 {ECO:0000305};
AltName: Full=Pre-mRNA cleavage factor Im 68 kDa subunit;
Name=NUDT21 {ECO:0000312|HGNC:HGNC:13870};
Synonyms=CFIM25 {ECO:0000303|PubMed:9659921}, CPSF25,
CPSF5 {ECO:0000303|PubMed:23187700};
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, SUBCELLULAR LOCATION, AND
DOMAIN.
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]
FUNCTION, AND INTERACTION WITH FIP1L1.
PubMed=15937220; DOI=10.1101/gad.1298605;
Venkataraman K., Brown K.M., Gilmartin G.M.;
"Analysis of a noncanonical poly(A) site reveals a tripartite
mechanism for vertebrate poly(A) site recognition.";
Genes Dev. 19:1315-1327(2005).
[12]
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).
[13]
FUNCTION.
PubMed=17024186; DOI=10.1038/sj.emboj.7601331;
Millevoi S., Loulergue C., Dettwiler S., Karaa S.Z., Keller W.,
Antoniou M., Vagner S.;
"An interaction between U2AF 65 and CF I(m) links the splicing and 3'
end processing machineries.";
EMBO J. 25:4854-4864(2006).
[14]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=17098938; DOI=10.1093/nar/gkl794;
Kubo T., Wada T., Yamaguchi Y., Shimizu A., Handa H.;
"Knock-down of 25 kDa subunit of cleavage factor Im in Hela cells
alters alternative polyadenylation within 3'-UTRs.";
Nucleic Acids Res. 34:6264-6271(2006).
[15]
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).
[16]
SUBCELLULAR LOCATION, AND INTERACTION WITH CPSF6.
PubMed=19864460; DOI=10.1091/mbc.E09-05-0389;
Ruepp M.D., Aringhieri C., Vivarelli S., Cardinale S., Paro S.,
Schuemperli D., Barabino S.M.;
"Mammalian pre-mRNA 3' end processing factor CF I m 68 functions in
mRNA export.";
Mol. Biol. Cell 20:5211-5223(2009).
[17]
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).
[18]
FUNCTION, IDENTIFICATION IN THE CLEAVAGE FACTOR IM COMPLEX, SUBUNIT,
SUBSTRATE SPECIFICITY, 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).
[19]
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).
[20]
RNA-BINDING.
PubMed=22813749; DOI=10.1016/j.celrep.2012.05.003;
Martin G., Gruber A.R., Keller W., Zavolan M.;
"Genome-wide analysis of pre-mRNA 3' end processing reveals a decisive
role of human cleavage factor I in the regulation of 3' UTR length.";
Cell Rep. 1:753-763(2012).
[21]
FUNCTION, AND SUBUNIT.
PubMed=23187700; DOI=10.4161/rna.22570;
Gruber A.R., Martin G., Keller W., Zavolan M.;
"Cleavage factor Im is a key regulator of 3' UTR length.";
RNA Biol. 9:1405-1412(2012).
[22]
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).
[23]
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).
[24]
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).
[25]
FUNCTION, INTERACTION WITH CPSF6 AND CPSF7, IDENTIFICATION IN THE MRNA
3'-PROCESSING COMPLEX, AND MUTAGENESIS OF LEU-218.
PubMed=29276085; DOI=10.1016/j.molcel.2017.11.031;
Zhu Y., Wang X., Forouzmand E., Jeong J., Qiao F., Sowd G.A.,
Engelman A.N., Xie X., Hertel K.J., Shi Y.;
"Molecular mechanisms for CFIm-mediated regulation of mRNA alternative
polyadenylation.";
Mol. Cell 69:62-74(2018).
[26]
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).
[27]
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).
[28]
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).
[29]
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.
[30]
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
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). {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}.
-!- SUBUNIT: 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.29). 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). {ECO:0000269|PubMed:14561889,
ECO:0000269|PubMed:15169763, ECO:0000269|PubMed:15937220,
ECO:0000269|PubMed:17172643, ECO:0000269|PubMed:18445629,
ECO:0000269|PubMed:19864460, ECO:0000269|PubMed:20479262,
ECO:0000269|PubMed:20695905, ECO:0000269|PubMed:21295486,
ECO:0000269|PubMed:23187700, ECO:0000269|PubMed:29276085,
ECO:0000269|PubMed:8626397, ECO:0000269|PubMed:9659921,
ECO:0000269|Ref.29}.
-!- 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: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}.
-!- TISSUE SPECIFICITY: Expressed in the heart, brain, placenta, lung,
liver, skeletal muscle, kidney and pancreas.
{ECO:0000269|PubMed:17098938}.
-!- 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}.
-!- 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; 124.
CORUM; O43809; -.
DIP; DIP-42502N; -.
IntAct; O43809; 84.
MINT; O43809; -.
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:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005815; C:microtubule organizing center; IDA:HPA.
GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IDA:UniProtKB.
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:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:1990120; P:messenger ribonucleoprotein complex assembly; 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:0031442; P:positive regulation of mRNA 3'-end processing; IMP:UniProtKB.
GO; GO:0031439; P:positive regulation of mRNA cleavage; IDA:UniProtKB.
GO; GO:1900365; P:positive regulation of mRNA polyadenylation; IDA:UniProtKB.
GO; GO:2000975; P:positive regulation of pro-B cell differentiation; ISS:UniProtKB.
GO; GO:2000738; P:positive regulation of stem cell differentiation; ISS:UniProtKB.
GO; GO:0010608; P:posttranscriptional regulation of gene expression; ISS:UniProtKB.
GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IMP:UniProtKB.
GO; GO:0051290; P:protein heterotetramerization; IDA:UniProtKB.
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; Cytoplasm;
Differentiation; 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.
{ECO:0000269|PubMed:15169763}.
REGION 81 160 Necessary for interactions with PAPOLA
and PABPN1.
{ECO:0000269|PubMed:15169763}.
REGION 102 104 Interaction with RNA.
{ECO:0000269|PubMed:20479262,
ECO:0000269|PubMed:21295486,
ECO:0000312|PDB:3MDG,
ECO:0000312|PDB:3MDI,
ECO:0000312|PDB:3Q2T}.
MOTIF 109 130 Nudix box.
SITE 55 55 Interaction with RNA.
{ECO:0000269|PubMed:20479262,
ECO:0000312|PDB:3MDG,
ECO:0000312|PDB:3MDI}.
SITE 63 63 Interaction with RNA.
{ECO:0000269|PubMed:20479262,
ECO:0000312|PDB:3MDG,
ECO:0000312|PDB:3MDI}.
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}.
MUTAGEN 218 218 L->R: Reduces interactions with CPSF6 and
CPSF7 and deacreases mRNA 3'-processing
activity. {ECO:0000269|PubMed:29276085}.
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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