CPSF7_HUMAN
ID CPSF7_HUMAN Reviewed; 471 AA.
AC Q8N684; B3KU04; C9K0Q4; Q7Z3H9; Q9H025; Q9H9V1;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Cleavage and polyadenylation specificity factor subunit 7 {ECO:0000305};
DE AltName: Full=Cleavage and polyadenylation specificity factor 59 kDa subunit;
DE Short=CPSF 59 kDa subunit;
DE AltName: Full=Cleavage factor Im complex 59 kDa subunit {ECO:0000303|PubMed:8626397};
DE Short=CFIm59 {ECO:0000303|PubMed:8626397};
DE AltName: Full=Pre-mRNA cleavage factor Im 59 kDa subunit;
GN Name=CPSF7 {ECO:0000312|HGNC:HGNC:30098};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cervix carcinoma;
RA Rueegsegger U., Blank D., Dettwiler S., Keller W.;
RT "Cloning of a second SR protein related subunit of human pre-mRNA cleavage
RT factor I.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Bone marrow, and Embryonic brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
RP PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, IDENTIFICATION IN A CLEAVAGE FACTOR IM COMPLEX, AND RNA-BINDING.
RX PubMed=8626397; DOI=10.1074/jbc.271.11.6107;
RA Rueegsegger U., Beyer K., Keller W.;
RT "Purification and characterization of human cleavage factor Im involved in
RT the 3' end processing of messenger RNA precursors.";
RL J. Biol. Chem. 271:6107-6113(1996).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP FUNCTION, INTERACTION WITH U2AF2, AND RNA-BINDING.
RX PubMed=17024186; DOI=10.1038/sj.emboj.7601331;
RA Millevoi S., Loulergue C., Dettwiler S., Karaa S.Z., Keller W.,
RA Antoniou M., Vagner S.;
RT "An interaction between U2AF 65 and CF I(m) links the splicing and 3' end
RT processing machineries.";
RL EMBO J. 25:4854-4864(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203 AND SER-413, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=19864460; DOI=10.1091/mbc.e09-05-0389;
RA Ruepp M.D., Aringhieri C., Vivarelli S., Cardinale S., Paro S.,
RA Schuemperli D., Barabino S.M.;
RT "Mammalian pre-mRNA 3' end processing factor CF I m 68 functions in mRNA
RT export.";
RL Mol. Biol. Cell 20:5211-5223(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP FUNCTION, IDENTIFICATION IN A CLEAVAGE FACTOR IM COMPLEX, AND SUBCELLULAR
RP LOCATION.
RX PubMed=20695905; DOI=10.1111/j.1365-2443.2010.01436.x;
RA Kim S., Yamamoto J., Chen Y., Aida M., Wada T., Handa H., Yamaguchi Y.;
RT "Evidence that cleavage factor Im is a heterotetrameric protein complex
RT controlling alternative polyadenylation.";
RL Genes Cells 15:1003-1013(2010).
RN [15]
RP METHYLATION.
RX PubMed=20562214; DOI=10.1261/rna.2164210;
RA Martin G., Ostareck-Lederer A., Chari A., Neuenkirchen N., Dettwiler S.,
RA Blank D., Rueegsegger U., Fischer U., Keller W.;
RT "Arginine methylation in subunits of mammalian pre-mRNA cleavage factor
RT I.";
RL RNA 16:1646-1659(2010).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP FUNCTION, AND IDENTIFICATION IN A CLEAVAGE FACTOR IM COMPLEX.
RX PubMed=23187700; DOI=10.4161/rna.22570;
RA Gruber A.R., Martin G., Keller W., Zavolan M.;
RT "Cleavage factor Im is a key regulator of 3' UTR length.";
RL RNA Biol. 9:1405-1412(2012).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-354, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [21]
RP FUNCTION, INTERACTION WITH NUDT21/CPSF5 AND FIP1L1, IDENTIFICATION IN THE
RP MRNA 3'-PROCESSING COMPLEX, PHOSPHORYLATION, AND DOMAIN.
RX PubMed=29276085; DOI=10.1016/j.molcel.2017.11.031;
RA Zhu Y., Wang X., Forouzmand E., Jeong J., Qiao F., Sowd G.A.,
RA Engelman A.N., Xie X., Hertel K.J., Shi Y.;
RT "Molecular mechanisms for CFIm-mediated regulation of mRNA alternative
RT polyadenylation.";
RL Mol. Cell 69:62-74(2018).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 50-182 IN COMPLEX WITH
RP NUDT21/CPSF5, AND IDENTIFICATION IN THE MRNA 3'-PROCESSING COMPLEX.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the complex between the 25 kDA subunit and the 59 kDA
RT subunit (RRM domain) of human cleavage factor Im.";
RL Submitted (JUL-2010) to the PDB data bank.
CC -!- FUNCTION: Component of the cleavage factor Im (CFIm) complex that
CC functions as an activator of the pre-mRNA 3'-end cleavage and
CC polyadenylation processing required for the maturation of pre-mRNA into
CC functional mRNAs (PubMed:8626397, PubMed:17024186, PubMed:29276085).
CC CFIm contributes to the recruitment of multiprotein complexes on
CC specific sequences on the pre-mRNA 3'-end, so called cleavage and
CC polyadenylation signals (pA signals) (PubMed:8626397, PubMed:17024186).
CC Most pre-mRNAs contain multiple pA signals, resulting in alternative
CC cleavage and polyadenylation (APA) producing mRNAs with variable 3'-end
CC formation (PubMed:23187700, PubMed:29276085). The CFIm complex acts as
CC a key regulator of cleavage and polyadenylation site choice during APA
CC through its binding to 5'-UGUA-3' elements localized in the 3'-
CC untranslated region (UTR) for a huge number of pre-mRNAs
CC (PubMed:20695905, PubMed:29276085). CPSF7 activates directly the mRNA
CC 3'-processing machinery (PubMed:29276085). Binds to pA signals in RNA
CC substrates (PubMed:8626397, PubMed:17024186).
CC {ECO:0000269|PubMed:17024186, ECO:0000269|PubMed:20695905,
CC ECO:0000269|PubMed:23187700, ECO:0000269|PubMed:29276085,
CC ECO:0000269|PubMed:8626397}.
CC -!- SUBUNIT: Component of the cleavage factor Im (CFIm) complex which is a
CC heterotetramer composed of two subunits of NUDT21/CPSF5 and two
CC subunits of CPSF6 or CPSF7 or a heterodimer of CPSF6 and CPSF7
CC (PubMed:8626397, PubMed:20695905, PubMed:23187700, Ref.22). The
CC cleavage factor Im (CFIm) complex associates with the CPSF and CSTF
CC complexes to promote the assembly of the core mRNA 3'-processing
CC machinery (PubMed:29276085). Interacts with NUDT21/CPSF5
CC (PubMed:29276085). Interacts (via Arg/Ser-rich domain) with FIP1L1
CC (preferentially via unphosphorylated form and Arg/Glu/Asp-rich region);
CC this interaction mediates, at least in part, the interaction between
CC the CFIm and CPSF complexes and may be inhibited by CPSF7 hyper-
CC phosphorylation (PubMed:29276085). {ECO:0000269|PubMed:20695905,
CC ECO:0000269|PubMed:23187700, ECO:0000269|PubMed:29276085,
CC ECO:0000269|PubMed:8626397, ECO:0000269|Ref.22}.
CC -!- INTERACTION:
CC Q8N684; Q9H6L4: ARMC7; NbExp=3; IntAct=EBI-746909, EBI-742909;
CC Q8N684; P54253: ATXN1; NbExp=2; IntAct=EBI-746909, EBI-930964;
CC Q8N684; P49760: CLK2; NbExp=3; IntAct=EBI-746909, EBI-750020;
CC Q8N684; Q7L775: EPM2AIP1; NbExp=3; IntAct=EBI-746909, EBI-6255981;
CC Q8N684; O43639: NCK2; NbExp=4; IntAct=EBI-746909, EBI-713635;
CC Q8N684; O43809: NUDT21; NbExp=5; IntAct=EBI-746909, EBI-355720;
CC Q8N684; Q06455-4: RUNX1T1; NbExp=3; IntAct=EBI-746909, EBI-10224192;
CC Q8N684; Q15437: SEC23B; NbExp=3; IntAct=EBI-746909, EBI-742673;
CC Q8N684; P84022: SMAD3; NbExp=3; IntAct=EBI-746909, EBI-347161;
CC Q8N684; Q9BV90: SNRNP25; NbExp=3; IntAct=EBI-746909, EBI-9675976;
CC Q8N684; Q08117: TLE5; NbExp=3; IntAct=EBI-746909, EBI-717810;
CC Q8N684; P26368: U2AF2; NbExp=2; IntAct=EBI-746909, EBI-742339;
CC Q8N684-3; Q9H6L4: ARMC7; NbExp=3; IntAct=EBI-11523759, EBI-742909;
CC Q8N684-3; P54253: ATXN1; NbExp=6; IntAct=EBI-11523759, EBI-930964;
CC Q8N684-3; Q8NEC5: CATSPER1; NbExp=3; IntAct=EBI-11523759, EBI-744545;
CC Q8N684-3; Q8IYR0: CFAP206; NbExp=3; IntAct=EBI-11523759, EBI-749051;
CC Q8N684-3; O95995: GAS8; NbExp=3; IntAct=EBI-11523759, EBI-1052570;
CC Q8N684-3; P62993: GRB2; NbExp=3; IntAct=EBI-11523759, EBI-401755;
CC Q8N684-3; Q96NT3-2: GUCD1; NbExp=3; IntAct=EBI-11523759, EBI-11978177;
CC Q8N684-3; P49773: HINT1; NbExp=3; IntAct=EBI-11523759, EBI-1054330;
CC Q8N684-3; P52597: HNRNPF; NbExp=3; IntAct=EBI-11523759, EBI-352986;
CC Q8N684-3; Q96PV6: LENG8; NbExp=3; IntAct=EBI-11523759, EBI-739546;
CC Q8N684-3; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-11523759, EBI-739832;
CC Q8N684-3; O43639: NCK2; NbExp=3; IntAct=EBI-11523759, EBI-713635;
CC Q8N684-3; O43809: NUDT21; NbExp=3; IntAct=EBI-11523759, EBI-355720;
CC Q8N684-3; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-11523759, EBI-11022007;
CC Q8N684-3; Q7Z2X4-3: PID1; NbExp=3; IntAct=EBI-11523759, EBI-11953174;
CC Q8N684-3; P54646: PRKAA2; NbExp=3; IntAct=EBI-11523759, EBI-1383852;
CC Q8N684-3; P98175: RBM10; NbExp=6; IntAct=EBI-11523759, EBI-721525;
CC Q8N684-3; Q06455-2: RUNX1T1; NbExp=3; IntAct=EBI-11523759, EBI-11984663;
CC Q8N684-3; P84022: SMAD3; NbExp=3; IntAct=EBI-11523759, EBI-347161;
CC Q8N684-3; Q9BV90: SNRNP25; NbExp=3; IntAct=EBI-11523759, EBI-9675976;
CC Q8N684-3; Q96RF0: SNX18; NbExp=3; IntAct=EBI-11523759, EBI-298169;
CC Q8N684-3; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-11523759, EBI-742688;
CC Q8N684-3; Q08117-2: TLE5; NbExp=3; IntAct=EBI-11523759, EBI-11741437;
CC Q8N684-3; Q63HR2: TNS2; NbExp=3; IntAct=EBI-11523759, EBI-949753;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19864460,
CC ECO:0000305|PubMed:20695905}. Cytoplasm {ECO:0000269|PubMed:19864460}.
CC Note=Shuttles between the nucleus and the cytoplasm in a
CC transcription- and XPO1/CRM1-independent manner, most probably in
CC complex with the cleavage factor Im complex (CFIm) (PubMed:19864460).
CC {ECO:0000269|PubMed:19864460}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8N684-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N684-2; Sequence=VSP_017194;
CC Name=3;
CC IsoId=Q8N684-3; Sequence=VSP_038975;
CC -!- DOMAIN: Contains an Arg/Ser-rich domain composed of arginine-serine
CC dipeptide repeats within the C-terminal region that is necessary and
CC sufficient for activating mRNA 3'-processing (PubMed:29276085).
CC {ECO:0000269|PubMed:29276085}.
CC -!- PTM: Phosphorylated (PubMed:29276085). {ECO:0000269|PubMed:29276085}.
CC -!- PTM: Asymmetrically dimethylated on arginine residues by PRMT1
CC (PubMed:20562214). {ECO:0000269|PubMed:20562214}.
CC -!- SIMILARITY: Belongs to the RRM CPSF6/7 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH18135.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14118.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAD97884.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ275970; CAC81661.1; -; mRNA.
DR EMBL; AK022591; BAB14118.1; ALT_INIT; mRNA.
DR EMBL; AK096343; BAG53266.1; -; mRNA.
DR EMBL; AL512759; CAC21678.1; -; mRNA.
DR EMBL; BX537888; CAD97884.1; ALT_INIT; mRNA.
DR EMBL; AP003108; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC018135; AAH18135.1; ALT_INIT; mRNA.
DR CCDS; CCDS44619.1; -. [Q8N684-1]
DR CCDS; CCDS44620.1; -. [Q8N684-2]
DR CCDS; CCDS8006.2; -. [Q8N684-3]
DR RefSeq; NP_001129512.1; NM_001136040.2. [Q8N684-1]
DR RefSeq; NP_001136037.1; NM_001142565.1. [Q8N684-2]
DR RefSeq; NP_079087.3; NM_024811.3. [Q8N684-3]
DR RefSeq; XP_005274356.1; XM_005274299.4. [Q8N684-1]
DR RefSeq; XP_011543560.1; XM_011545258.2. [Q8N684-1]
DR RefSeq; XP_011543561.1; XM_011545259.2. [Q8N684-2]
DR PDB; 3N9U; X-ray; 1.92 A; C/I=50-182.
DR PDBsum; 3N9U; -.
DR AlphaFoldDB; Q8N684; -.
DR SMR; Q8N684; -.
DR BioGRID; 122957; 326.
DR ComplexPortal; CPX-951; mRNA cleavage factor I(m) complex, CPSF7 variant.
DR CORUM; Q8N684; -.
DR IntAct; Q8N684; 81.
DR MINT; Q8N684; -.
DR STRING; 9606.ENSP00000345412; -.
DR GlyGen; Q8N684; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8N684; -.
DR PhosphoSitePlus; Q8N684; -.
DR SwissPalm; Q8N684; -.
DR BioMuta; CPSF7; -.
DR DMDM; 74759932; -.
DR EPD; Q8N684; -.
DR jPOST; Q8N684; -.
DR MassIVE; Q8N684; -.
DR MaxQB; Q8N684; -.
DR PaxDb; Q8N684; -.
DR PeptideAtlas; Q8N684; -.
DR PRIDE; Q8N684; -.
DR ProteomicsDB; 72138; -. [Q8N684-1]
DR ProteomicsDB; 72139; -. [Q8N684-2]
DR ProteomicsDB; 72140; -. [Q8N684-3]
DR Antibodypedia; 14651; 138 antibodies from 24 providers.
DR DNASU; 79869; -.
DR Ensembl; ENST00000340437.8; ENSP00000345412.4; ENSG00000149532.16. [Q8N684-3]
DR Ensembl; ENST00000394888.8; ENSP00000378352.4; ENSG00000149532.16. [Q8N684-1]
DR Ensembl; ENST00000439958.8; ENSP00000397203.3; ENSG00000149532.16. [Q8N684-2]
DR Ensembl; ENST00000448745.5; ENSP00000407394.1; ENSG00000149532.16. [Q8N684-2]
DR GeneID; 79869; -.
DR KEGG; hsa:79869; -.
DR MANE-Select; ENST00000439958.8; ENSP00000397203.3; NM_001142565.3; NP_001136037.1. [Q8N684-2]
DR UCSC; uc001nrp.4; human. [Q8N684-1]
DR CTD; 79869; -.
DR DisGeNET; 79869; -.
DR GeneCards; CPSF7; -.
DR HGNC; HGNC:30098; CPSF7.
DR HPA; ENSG00000149532; Low tissue specificity.
DR neXtProt; NX_Q8N684; -.
DR OpenTargets; ENSG00000149532; -.
DR PharmGKB; PA165543380; -.
DR VEuPathDB; HostDB:ENSG00000149532; -.
DR eggNOG; KOG4849; Eukaryota.
DR GeneTree; ENSGT00730000110905; -.
DR HOGENOM; CLU_025289_1_0_1; -.
DR InParanoid; Q8N684; -.
DR OMA; YGDERCQ; -.
DR OrthoDB; 1016696at2759; -.
DR PhylomeDB; Q8N684; -.
DR TreeFam; TF316430; -.
DR PathwayCommons; Q8N684; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72187; mRNA 3'-end processing.
DR Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-HSA-77595; Processing of Intronless Pre-mRNAs.
DR Reactome; R-HSA-9013422; RHOBTB1 GTPase cycle.
DR SignaLink; Q8N684; -.
DR SIGNOR; Q8N684; -.
DR BioGRID-ORCS; 79869; 21 hits in 1087 CRISPR screens.
DR ChiTaRS; CPSF7; human.
DR EvolutionaryTrace; Q8N684; -.
DR GeneWiki; FLJ12529; -.
DR GenomeRNAi; 79869; -.
DR Pharos; Q8N684; Tbio.
DR PRO; PR:Q8N684; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q8N684; protein.
DR Bgee; ENSG00000149532; Expressed in adenohypophysis and 192 other tissues.
DR ExpressionAtlas; Q8N684; baseline and differential.
DR Genevisible; Q8N684; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IDA:UniProtKB.
DR GO; GO:0005849; C:mRNA cleavage factor complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:1990120; P:messenger ribonucleoprotein complex assembly; IDA:UniProtKB.
DR GO; GO:0031124; P:mRNA 3'-end processing; IDA:ComplexPortal.
DR GO; GO:0110104; P:mRNA alternative polyadenylation; IMP:UniProtKB.
DR GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IDA:ComplexPortal.
DR GO; GO:0051290; P:protein heterotetramerization; IDA:UniProtKB.
DR GO; GO:0051262; P:protein tetramerization; IDA:UniProtKB.
DR CDD; cd12644; RRM_CFIm59; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR034772; CPSF6/7.
DR InterPro; IPR034770; CPSF7.
DR InterPro; IPR034773; CPSF7_RRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR23204; PTHR23204; 1.
DR PANTHER; PTHR23204:SF2; PTHR23204:SF2; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Isopeptide bond;
KW Methylation; mRNA processing; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding; Ubl conjugation.
FT CHAIN 1..471
FT /note="Cleavage and polyadenylation specificity factor
FT subunit 7"
FT /id="PRO_0000081527"
FT DOMAIN 82..162
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 33..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..469
FT /note="Arg/Ser-rich domain"
FT /evidence="ECO:0000269|PubMed:29276085"
FT COMPBIAS 33..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 203
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BTV2"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT CROSSLNK 354
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1
FT /note="M -> MGRPESAGGGSRGPFEGGGRARRAGGIFLTLSILRTRDLPSGAM
FT (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_038975"
FT VAR_SEQ 176..184
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_017194"
FT CONFLICT 335
FT /note="A -> V (in Ref. 3; CAD97884)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="S -> F (in Ref. 3; CAD97884)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="E -> D (in Ref. 2; BAB14118)"
FT /evidence="ECO:0000305"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:3N9U"
FT HELIX 95..104
FT /evidence="ECO:0007829|PDB:3N9U"
FT STRAND 110..117
FT /evidence="ECO:0007829|PDB:3N9U"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:3N9U"
FT STRAND 124..133
FT /evidence="ECO:0007829|PDB:3N9U"
FT HELIX 135..144
FT /evidence="ECO:0007829|PDB:3N9U"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:3N9U"
FT HELIX 162..176
FT /evidence="ECO:0007829|PDB:3N9U"
SQ SEQUENCE 471 AA; 52050 MW; 69529E441D742CF9 CRC64;
MSEGVDLIDI YADEEFNQDP EFNNTDQIDL YDDVLTATSQ PSDDRSSSTE PPPPVRQEPS
PKPNNKTPAI LYTYSGLRNR RAAVYVGSFS WWTTDQQLIQ VIRSIGVYDV VELKFAENRA
NGQSKGYAEV VVASENSVHK LLELLPGKVL NGEKVDVRPA TRQNLSQFEA QARKRECVRV
PRGGIPPRAH SRDSSDSADG RATPSENLVP SSARVDKPPS VLPYFNRPPS ALPLMGLPPP
PIPPPPPLSS SFGVPPPPPG IHYQHLMPPP PRLPPHLAVP PPGAIPPALH LNPAFFPPPN
ATVGPPPDTY MKASAPYNHH GSRDSGPPPS TVSEAEFEDI MKRNRAISSS AISKAVSGAS
AGDYSDAIET LLTAIAVIKQ SRVANDERCR VLISSLKDCL HGIEAKSYSV GASGSSSRKR
HRSRERSPSR SRESSRRHRD LLHNEDRHDD YFQERNREHE RHRDRERDRH H
