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Cleavage and polyadenylation specificity factor subunit 6 (Cleavage and polyadenylation specificity factor 68 kDa subunit) (CFIm68) (CPSF 68 kDa subunit) (Pre-mRNA cleavage factor Im 68 kDa subunit) (Protein HPBRII-4/7)

 CPSF6_HUMAN             Reviewed;         551 AA.
Q16630; A8K7K9; Q53ES1; Q9BSJ7; Q9BW18;
07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
07-FEB-2006, sequence version 2.
12-SEP-2018, entry version 168.
RecName: Full=Cleavage and polyadenylation specificity factor subunit 6 {ECO:0000305};
AltName: Full=Cleavage and polyadenylation specificity factor 68 kDa subunit;
Short=CPSF 68 kDa subunit;
AltName: Full=Cleavage factor Im complex 68 kDa subunit {ECO:0000303|PubMed:9659921};
Short=CFIm68 {ECO:0000303|PubMed:9659921};
AltName: Full=Pre-mRNA cleavage factor Im 68 kDa subunit;
AltName: Full=Protein HPBRII-4/7;
Name=CPSF6 {ECO:0000312|HGNC:HGNC:13871};
Synonyms=CFIM68 {ECO:0000303|PubMed:9659921};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 125-138
AND 162-168, FUNCTION, IDENTIFICATION IN THE CLEAVAGE FACTOR IM
COMPLEX, AND SUBCELLULAR LOCATION.
TISSUE=Leukemia;
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 [GENOMIC DNA / MRNA] (ISOFORM 1).
TISSUE=Leukemia;
Fleischhauer K.L.;
Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Spleen;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Heart;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Kidney;
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).
[7]
FUNCTION, AND IDENTIFICATION IN A CLEAVAGE FACTOR IM COMPLEX.
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.
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, AND INTERACTION WITH
NUDT21/CPSF5 AND SNRNP70.
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]
FUNCTION, IDENTIFICATION IN A CLEAVAGE FACTOR IM COMPLEX, INTERACTION
WITH NUDT21/CPSF5; SRSF3; SRSF7 AND TRA2B, RNA-BINDING, MUTAGENESIS OF
GLY-86 AND ASN-87, 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]
SUBCELLULAR LOCATION, AND DOMAIN.
PubMed=17267687; DOI=10.1091/mbc.E06-09-0846;
Cardinale S., Cisterna B., Bonetti P., Aringhieri C., Biggiogera M.,
Barabino S.M.;
"Subnuclear localization and dynamics of the pre-mRNA 3' end
processing factor mammalian cleavage factor I 68-kDa subunit.";
Mol. Biol. Cell 18:1282-1292(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-404, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NXF1; NUDT21/CPSF5;
UPF1 AND UPF3B, ASSOCIATION WITH THE EXON JUNCTION COMPLEX AND 80S
RIBOSOME PARTICLE, AND DOMAIN.
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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-407, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[16]
FUNCTION, IDENTIFICATION IN THE CLEAVAGE FACTOR IM COMPLEX, 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).
[17]
METHYLATION, AND MUTAGENESIS OF ARG-202; ARG-204 AND ARG-206.
PubMed=20562214; DOI=10.1261/rna.2164210;
Martin G., Ostareck-Lederer A., Chari A., Neuenkirchen N.,
Dettwiler S., Blank D., Rueegsegger U., Fischer U., Keller W.;
"Arginine methylation in subunits of mammalian pre-mRNA cleavage
factor I.";
RNA 16:1646-1659(2010).
[18]
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).
[19]
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).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-404 AND THR-407, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[21]
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).
[22]
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).
[23]
INTERACTION WITH VIRMA.
PubMed=29507755; DOI=10.1038/s41421-018-0019-0;
Yue Y., Liu J., Cui X., Cao J., Luo G., Zhang Z., Cheng T., Gao M.,
Shu X., Ma H., Wang F., Wang X., Shen B., Wang Y., Feng X., He C.,
Liu J.;
"VIRMA mediates preferential m6A mRNA methylation in 3'UTR and near
stop codon and associates with alternative polyadenylation.";
Cell Discov. 4:10-10(2018).
[24]
FUNCTION, INTERACTION WITH NUDT21/CPSF5 AND FIP1L1, IDENTIFICATION IN
THE MRNA 3'-PROCESSING COMPLEX, PHOSPHORYLATION, AND DOMAIN.
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).
[25]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 13-235 IN COMPLEX WITH
NUDT21/CPSF5 AND RNA, FUNCTION, SUBUNIT, AND MUTAGENESIS OF TYR-84;
90-TRP-TRP-91; ASP-94; GLU-111; PHE-126 AND LEU-128.
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: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).
Most pre-mRNAs contain multiple pA signals, resulting in
alternative cleavage and polyadenylation (APA) producing mRNAs
with variable 3'-end formation (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:20695905, PubMed:29276085).
CPSF6 enhances NUDT21/CPSF5 binding to 5'-UGUA-3' elements
localized upstream of pA signals and promotes RNA looping, and
hence activates directly the mRNA 3'-processing machinery
(PubMed:15169763, PubMed:29276085, PubMed:21295486). Plays a role
in mRNA export (PubMed:19864460). {ECO:0000269|PubMed:14690600,
ECO:0000269|PubMed:15169763, ECO:0000269|PubMed:19864460,
ECO:0000269|PubMed:20695905, ECO:0000269|PubMed:21295486,
ECO:0000269|PubMed:23187700, ECO:0000269|PubMed:29276085,
ECO:0000269|PubMed:8626397, ECO:0000269|PubMed:9659921}.
-!- SUBUNIT: 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). 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). Associates with the exon junction complex (EJC)
(PubMed:19864460). Associates with the 80S ribosome particle
(PubMed:19864460). Interacts (via the RRM domain) with
NUDT21/CPSF5; this interaction is direct and enhances binding to
RNA (PubMed:14561889, PubMed:15169763, PubMed:19864460,
PubMed:29276085, PubMed:21295486). Interacts (via Arg/Ser-rich
domain) with FIP1L1 (preferentially via unphosphorylated form and
Arg/Glu/Asp-rich domain); this interaction mediates, at least in
part, the interaction between the CFIm and CPSF complexes and may
be inhibited by CPSF6 hyper-phosphorylation (PubMed:29276085).
Interacts (via N-terminus) with NXF1; this interaction is direct
(PubMed:19864460). Interacts with SRSF3 (PubMed:15169763).
Interacts with SRSF7 (PubMed:15169763). Interacts with SNRNP70
(PubMed:14561889). Interacts with TRA2B/SFRS10 (PubMed:15169763).
Interacts with UPF1 (PubMed:19864460). Interacts with UPF3B
(PubMed:19864460). Interacts with VIRMA (PubMed:29507755).
{ECO:0000269|PubMed:14561889, ECO:0000269|PubMed:15169763,
ECO:0000269|PubMed:19864460, ECO:0000269|PubMed:20695905,
ECO:0000269|PubMed:21295486, ECO:0000269|PubMed:23187700,
ECO:0000269|PubMed:29276085, ECO:0000269|PubMed:29507755,
ECO:0000269|PubMed:8626397, ECO:0000269|PubMed:9659921}.
-!- INTERACTION:
Q9H6L4:ARMC7; NbExp=4; IntAct=EBI-358410, EBI-742909;
O43809:NUDT21; NbExp=5; IntAct=EBI-358410, EBI-355720;
Q96DC9:OTUB2; NbExp=3; IntAct=EBI-358410, EBI-746259;
O15162:PLSCR1; NbExp=2; IntAct=EBI-358410, EBI-740019;
Q9Y3C6:PPIL1; NbExp=3; IntAct=EBI-358410, EBI-2557649;
Q6FIE9:TOLLIP; NbExp=3; IntAct=EBI-358410, EBI-10249783;
Q9H0M0:WWP1; NbExp=3; IntAct=EBI-358410, EBI-742157;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15169763,
ECO:0000269|PubMed:19864460, ECO:0000269|PubMed:20695905,
ECO:0000269|PubMed:9659921}. Nucleus, nucleoplasm
{ECO:0000269|PubMed:17267687}. Nucleus speckle
{ECO:0000269|PubMed:17267687}. 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). Colocalizes with PSPC1 in
punctate subnuclear structures often located adjacent to nuclear
speckles, called paraspeckles, and corresponding to interchromatin
granules-associated zones (IGAZs) (PubMed:17267687). Distribution
in speckles and paraspeckles varies during the cell cycle
(PubMed:17267687). Associates at sites of active transcription on
nascent perichromatin fibrils (PFs) and perichromatin granules
(PubMed:17267687). {ECO:0000269|PubMed:15169763,
ECO:0000269|PubMed:17267687, ECO:0000269|PubMed:19864460}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q16630-1; Sequence=Displayed;
Name=2;
IsoId=Q16630-2; Sequence=VSP_017192;
Name=3;
IsoId=Q16630-3; Sequence=VSP_017191;
-!- DOMAIN: Contains an Arg/Ser-rich domain composed of arginine-
serine dipeptide repeats within the C-terminal region that is
necessary and sufficient for activating mRNA 3'-processing and
alternative polyadenylation (APA). {ECO:0000269|PubMed:29276085}.
-!- PTM: Phosphorylated (PubMed:29276085). Phosphorylated in the
Arg/Ser-rich domain by SRPK1, in vitro (PubMed:29276085).
{ECO:0000269|PubMed:29276085}.
-!- PTM: Symmetrically dimethylated on arginine residues in the GAR
motif by PRMT5 in a WDR77- and CLNS1A-dependent manner
(PubMed:20562214). Asymmetrically dimethylated on arginine
residues in the GAR motif by PRMT1 (PubMed:20562214).
{ECO:0000269|PubMed:20562214}.
-!- SIMILARITY: Belongs to the RRM CPSF6/7 family. {ECO:0000305}.
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EMBL; X67336; CAA47751.1; -; Genomic_DNA.
EMBL; X67337; CAA47752.1; -; mRNA.
EMBL; AK223568; BAD97288.1; -; mRNA.
EMBL; AK292024; BAF84713.1; -; mRNA.
EMBL; CH471054; EAW97215.1; -; Genomic_DNA.
EMBL; BC000714; AAH00714.1; -; mRNA.
EMBL; BC005000; AAH05000.1; -; mRNA.
CCDS; CCDS73494.1; -. [Q16630-2]
CCDS; CCDS8988.1; -. [Q16630-1]
PIR; S57447; S57447.
RefSeq; NP_001287876.1; NM_001300947.1. [Q16630-2]
RefSeq; NP_008938.2; NM_007007.2. [Q16630-1]
UniGene; Hs.369606; -.
PDB; 3P5T; X-ray; 2.70 A; L/M/N/O/P/Q=80-161.
PDB; 3P6Y; X-ray; 2.90 A; C/D/G/H/K/L/O/P=80-161.
PDB; 3Q2S; X-ray; 2.90 A; C/D=13-235.
PDB; 3Q2T; X-ray; 3.06 A; C/D=13-235.
PDB; 4B4N; X-ray; 1.81 A; B=276-290.
PDB; 4U0A; X-ray; 2.05 A; B=276-290.
PDB; 4U0B; X-ray; 2.80 A; M/N/O/P/Q/R/S/T/U/V/W/X=276-290.
PDB; 4WYM; X-ray; 2.60 A; M/N/O/P/Q/R/S/T/U/V/W=276-290.
PDBsum; 3P5T; -.
PDBsum; 3P6Y; -.
PDBsum; 3Q2S; -.
PDBsum; 3Q2T; -.
PDBsum; 4B4N; -.
PDBsum; 4U0A; -.
PDBsum; 4U0B; -.
PDBsum; 4WYM; -.
ProteinModelPortal; Q16630; -.
SMR; Q16630; -.
BioGrid; 116238; 123.
CORUM; Q16630; -.
DIP; DIP-34501N; -.
IntAct; Q16630; 49.
MINT; Q16630; -.
STRING; 9606.ENSP00000391774; -.
iPTMnet; Q16630; -.
PhosphoSitePlus; Q16630; -.
SwissPalm; Q16630; -.
BioMuta; CPSF6; -.
DMDM; 88909266; -.
EPD; Q16630; -.
MaxQB; Q16630; -.
PaxDb; Q16630; -.
PeptideAtlas; Q16630; -.
PRIDE; Q16630; -.
ProteomicsDB; 60979; -.
ProteomicsDB; 60980; -. [Q16630-2]
ProteomicsDB; 60981; -. [Q16630-3]
DNASU; 11052; -.
Ensembl; ENST00000266679; ENSP00000266679; ENSG00000111605. [Q16630-2]
Ensembl; ENST00000435070; ENSP00000391774; ENSG00000111605. [Q16630-1]
GeneID; 11052; -.
KEGG; hsa:11052; -.
UCSC; uc001sut.4; human. [Q16630-1]
CTD; 11052; -.
DisGeNET; 11052; -.
EuPathDB; HostDB:ENSG00000111605.16; -.
GeneCards; CPSF6; -.
HGNC; HGNC:13871; CPSF6.
HPA; HPA039973; -.
MIM; 604979; gene.
neXtProt; NX_Q16630; -.
OpenTargets; ENSG00000111605; -.
PharmGKB; PA26846; -.
eggNOG; KOG4849; Eukaryota.
eggNOG; ENOG410Y0H0; LUCA.
GeneTree; ENSGT00730000110905; -.
HOGENOM; HOG000111137; -.
InParanoid; Q16630; -.
KO; K14398; -.
OMA; MGNQQPP; -.
OrthoDB; EOG091G0CVC; -.
PhylomeDB; Q16630; -.
TreeFam; TF316430; -.
Reactome; R-HSA-1839117; Signaling by cytosolic FGFR1 fusion mutants.
Reactome; R-HSA-5655302; Signaling by FGFR1 in disease.
ChiTaRS; CPSF6; human.
GeneWiki; CPSF6; -.
GenomeRNAi; 11052; -.
PRO; PR:Q16630; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000111605; Expressed in 228 organ(s), highest expression level in lung.
CleanEx; HS_CPSF6; -.
ExpressionAtlas; Q16630; baseline and differential.
Genevisible; Q16630; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0035061; C:interchromatin granule; IDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
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:0016607; C:nuclear speck; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0042382; C:paraspeckles; IDA:UniProtKB.
GO; GO:0005726; C:perichromatin fibrils; IDA:UniProtKB.
GO; GO:1990904; C:ribonucleoprotein complex; IDA:MGI.
GO; GO:1990448; F:exon-exon junction complex binding; IDA:UniProtKB.
GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
GO; GO:0043023; F:ribosomal large subunit binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:1990120; P:messenger ribonucleoprotein complex assembly; IDA:UniProtKB.
GO; GO:0110104; P:mRNA alternative polyadenylation; IMP:UniProtKB.
GO; GO:0006397; P:mRNA processing; IDA:UniProtKB.
GO; GO:0046833; P:positive regulation of RNA export from nucleus; IMP: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.
Gene3D; 3.30.70.330; -; 1.
InterPro; IPR034769; CPSF6.
InterPro; IPR034772; CPSF6/7.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
PANTHER; PTHR23204; PTHR23204; 1.
PANTHER; PTHR23204:SF3; PTHR23204:SF3; 1.
Pfam; PF00076; RRM_1; 1.
SMART; SM00360; RRM; 1.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50102; RRM; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Direct protein sequencing; Methylation; mRNA processing; Nucleus;
Phosphoprotein; Reference proteome; RNA-binding.
CHAIN 1 551 Cleavage and polyadenylation specificity
factor subunit 6.
/FTId=PRO_0000081521.
DOMAIN 81 161 RRM. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
REGION 1 213 Necessary for interaction with NXF1.
{ECO:0000269|PubMed:19864460}.
REGION 81 161 Necessary for interaction with
NUDT21/CPSF5.
{ECO:0000269|PubMed:15169763}.
REGION 81 161 Necessary for nuclear paraspeckles
localization.
{ECO:0000269|PubMed:17267687}.
REGION 404 551 Sufficient for nuclear speckle
localization.
{ECO:0000269|PubMed:17267687}.
REGION 405 551 Necessary for RNA-binding.
{ECO:0000269|PubMed:15169763}.
REGION 481 551 Necessary for interaction with SRSF3,
SRSF7 and TRA2B/SFRS10.
{ECO:0000269|PubMed:15169763}.
REGION 490 551 Arg/Ser-rich domain.
{ECO:0000269|PubMed:29276085}.
REGION 510 551 Sufficient for nuclear targeting.
{ECO:0000269|PubMed:15169763}.
MOTIF 202 206 GAR. {ECO:0000269|PubMed:20562214}.
COMPBIAS 208 398 Pro-rich.
COMPBIAS 490 551 Arg-rich.
MOD_RES 404 404 Phosphothreonine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:23186163}.
MOD_RES 407 407 Phosphothreonine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 188 260 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_017191.
VAR_SEQ 231 231 P -> PGNLIKHLVKGTRPLFLETRIPWHMGHSIEEIPIFG
LK (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_017192.
MUTAGEN 84 84 Y->A: Reduces affinity for UGUA RNA by
40%; when associated with A-128.
{ECO:0000269|PubMed:21295486}.
MUTAGEN 86 86 G->V: Abolishes interaction with
NUDT21/CPSF5; when associated with V-87.
{ECO:0000269|PubMed:15169763}.
MUTAGEN 87 87 N->V: Abolishes interaction with
NUDT21/CPSF5; when associated with V-86.
{ECO:0000269|PubMed:15169763}.
MUTAGEN 90 91 WW->AA: Reduces affinity for UGUA RNA by
70%. Strongly reduced affinity for UGUA
RNA; when associated with A-94.
{ECO:0000269|PubMed:21295486}.
MUTAGEN 94 94 D->A: Strongly reduced affinity for UGUA
RNA; when associated with 90-A-A-91.
{ECO:0000269|PubMed:21295486}.
MUTAGEN 111 111 E->A: Reduces affinity for UGUA RNA by
85%. {ECO:0000269|PubMed:21295486}.
MUTAGEN 126 126 F->A: Increases affinity for UGUA RNA by
40%. {ECO:0000269|PubMed:21295486}.
MUTAGEN 128 128 L->A: Reduces affinity for UGUA RNA by
40%; when associated with A-84.
{ECO:0000269|PubMed:21295486}.
MUTAGEN 202 202 R->A: Decreased methylation in presence
of PRMT5/WDR77. Loss of methylation in
presence of PRMT5/WDR77 or PRMT1; when
associated with A-204 and A-206.
{ECO:0000269|PubMed:20562214}.
MUTAGEN 204 204 R->A: Decreased methylation in presence
of PRMT5/WDR77. Loss of methylation in
presence of PRMT5/WDR77 or PRMT1; when
associated with A-202 and A-206.
{ECO:0000269|PubMed:20562214}.
MUTAGEN 206 206 R->A: Loss of methylation in presence of
PRMT5/WDR77 or PRMT1.
{ECO:0000269|PubMed:20562214}.
CONFLICT 9 9 D -> N (in Ref. 2; CAA47751/CAA47752).
{ECO:0000305}.
STRAND 84 87 {ECO:0000244|PDB:3P5T}.
HELIX 94 102 {ECO:0000244|PDB:3P5T}.
TURN 103 105 {ECO:0000244|PDB:3P5T}.
STRAND 112 116 {ECO:0000244|PDB:3P5T}.
TURN 118 120 {ECO:0000244|PDB:3P5T}.
STRAND 123 129 {ECO:0000244|PDB:3P5T}.
HELIX 134 143 {ECO:0000244|PDB:3P5T}.
HELIX 144 146 {ECO:0000244|PDB:3P5T}.
STRAND 149 151 {ECO:0000244|PDB:3P5T}.
STRAND 155 158 {ECO:0000244|PDB:3P6Y}.
HELIX 161 170 {ECO:0000244|PDB:3Q2S}.
SEQUENCE 551 AA; 59210 MW; 721A5DA1B456AA79 CRC64;
MADGVDHIDI YADVGEEFNQ EAEYGGHDQI DLYDDVISPS ANNGDAPEDR DYMDTLPPTV
GDDVGKGAAP NVVYTYTGKR IALYIGNLTW WTTDEDLTEA VHSLGVNDIL EIKFFENRAN
GQSKGFALVG VGSEASSKKL MDLLPKRELH GQNPVVTPCN KQFLSQFEMQ SRKTTQSGQM
SGEGKAGPPG GSSRAAFPQG GRGRGRFPGA VPGGDRFPGP AGPGGPPPPF PAGQTPPRPP
LGPPGPPGPP GPPPPGQVLP PPLAGPPNRG DRPPPPVLFP GQPFGQPPLG PLPPGPPPPV
PGYGPPPGPP PPQQGPPPPP GPFPPRPPGP LGPPLTLAPP PHLPGPPPGA PPPAPHVNPA
FFPPPTNSGM PTSDSRGPPP TDPYGRPPPY DRGDYGPPGR EMDTARTPLS EAEFEEIMNR
NRAISSSAIS RAVSDASAGD YGSAIETLVT AISLIKQSKV SADDRCKVLI SSLQDCLHGI
ESKSYGSGSR RERSRERDHS RSREKSRRHK SRSRDRHDDY YRERSRERER HRDRDRDRDR
ERDREREYRH R


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