CSTF2_HUMAN
ID CSTF2_HUMAN Reviewed; 577 AA.
AC P33240; Q5H951; Q6LA74; Q8N502;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Cleavage stimulation factor subunit 2;
DE AltName: Full=CF-1 64 kDa subunit;
DE AltName: Full=Cleavage stimulation factor 64 kDa subunit;
DE Short=CSTF 64 kDa subunit;
DE Short=CstF-64;
GN Name=CSTF2;
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 [MRNA] (ISOFORM 1), PHOSPHORYLATION, AND RNA-BINDING.
RX PubMed=1741396; DOI=10.1073/pnas.89.4.1403;
RA Takagaki Y., Macdonald C.C., Shenk T., Manley J.L.;
RT "The human 64-kDa polyadenylylation factor contains a ribonucleoprotein-
RT type RNA binding domain and unusual auxiliary motifs.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:1403-1407(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney, and Ovary;
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 [5]
RP RNA-BINDING, AND FUNCTION.
RX PubMed=9199325; DOI=10.1128/mcb.17.7.3907;
RA Takagaki Y., Manley J.L.;
RT "RNA recognition by the human polyadenylation factor CstF.";
RL Mol. Cell. Biol. 17:3907-3914(1997).
RN [6]
RP INDUCTION.
RX PubMed=9736695; DOI=10.1073/pnas.95.19.11095;
RA Martincic K., Campbell R., Edwalds-Gilbert G., Souan L., Lotze M.T.,
RA Milcarek C.;
RT "Increase in the 64-kDa subunit of the polyadenylation/cleavage stimulatory
RT factor during the G0 to S phase transition.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:11095-11100(1998).
RN [7]
RP INTERACTION WITH CSTF3 AND SYMPK.
RX PubMed=10669729; DOI=10.1128/mcb.20.5.1515-1525.2000;
RA Takagaki Y., Manley J.L.;
RT "Complex protein interactions within the human polyadenylation machinery
RT identify a novel component.";
RL Mol. Cell. Biol. 20:1515-1525(2000).
RN [8]
RP INTERACTION WITH RPO2TC1.
RX PubMed=11389848; DOI=10.1016/s1097-2765(01)00236-2;
RA Calvo O., Manley J.L.;
RT "Evolutionarily conserved interaction between CstF-64 and PC4 links
RT transcription, polyadenylation, and termination.";
RL Mol. Cell 7:1013-1023(2001).
RN [9]
RP INTERACTION WITH DDX1, AND SUBCELLULAR LOCATION.
RX PubMed=11598190; DOI=10.1091/mbc.12.10.3046;
RA Bleoo S., Sun X., Hendzel M.J., Rowe J.M., Packer M., Godbout R.;
RT "Association of human DEAD box protein DDX1 with a cleavage stimulation
RT factor involved in 3'-end processing of pre-MRNA.";
RL Mol. Biol. Cell 12:3046-3059(2001).
RN [10]
RP INTERACTION WITH FIP1L1.
RX PubMed=14749727; DOI=10.1038/sj.emboj.7600070;
RA Kaufmann I., Martin G., Friedlein A., Langen H., Keller W.;
RT "Human Fip1 is a subunit of CPSF that binds to U-rich RNA elements and
RT stimulates poly(A) polymerase.";
RL EMBO J. 23:616-626(2004).
RN [11]
RP INTERACTION WITH HSF1.
RX PubMed=14707147; DOI=10.1074/jbc.m311719200;
RA Xing H., Mayhew C.N., Cullen K.E., Park-Sarge O.-K., Sarge K.D.;
RT "HSF1 modulation of Hsp70 mRNA polyadenylation via interaction with
RT symplekin.";
RL J. Biol. Chem. 279:10551-10555(2004).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [13]
RP INTERACTION WITH CPSF2 AND CPSF3.
RX PubMed=18688255; DOI=10.1038/embor.2008.146;
RA Kolev N.G., Yario T.A., Benson E., Steitz J.A.;
RT "Conserved motifs in both CPSF73 and CPSF100 are required to assemble the
RT active endonuclease for histone mRNA 3'-end maturation.";
RL EMBO Rep. 9:1013-1018(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524, AND IDENTIFICATION BY
RP 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524, 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 [16]
RP IDENTIFICATION IN THE CPSF COMPLEX.
RX PubMed=21102410; DOI=10.1038/emboj.2010.287;
RA Laishram R.S., Anderson R.A.;
RT "The poly A polymerase Star-PAP controls 3'-end cleavage by promoting CPSF
RT interaction and specificity toward the pre-mRNA.";
RL EMBO J. 29:4132-4145(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
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 [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [21]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-308; ARG-468 AND ARG-475, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-189, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [23]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-189, 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 [24]
RP STRUCTURE BY NMR OF 8-111.
RX PubMed=12773396; DOI=10.1093/emboj/cdg259;
RA Perez Canadillas J.M., Varani G.;
RT "Recognition of GU-rich polyadenylation regulatory elements by human CstF-
RT 64 protein.";
RL EMBO J. 22:2821-2830(2003).
RN [25]
RP STRUCTURE BY NMR OF 531-577.
RX PubMed=17116658; DOI=10.1074/jbc.m609981200;
RA Qu X., Perez-Canadillas J.M., Agrawal S., De Baecke J., Cheng H.,
RA Varani G., Moore C.;
RT "The C-terminal domains of vertebrate CstF-64 and its yeast orthologue
RT Rna15 form a new structure critical for mRNA 3'-end processing.";
RL J. Biol. Chem. 282:2101-2115(2007).
CC -!- FUNCTION: One of the multiple factors required for polyadenylation and
CC 3'-end cleavage of mammalian pre-mRNAs. This subunit is directly
CC involved in the binding to pre-mRNAs (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:9199325}.
CC -!- SUBUNIT: The CSTF complex is composed of CSTF1 (50 kDa subunit), CSTF2
CC (64 kDa subunit) and CSTF3 (77 kDa subunit). CSTF2 directly interacts
CC with CSTF3, SYMPK and RPO2TC1. Interacts with HSF1 in heat-stressed
CC cells. Interacts with CPSF2, CPSF3 and FIP1L1. Interacts with DDX1.
CC {ECO:0000269|PubMed:10669729, ECO:0000269|PubMed:11389848,
CC ECO:0000269|PubMed:11598190, ECO:0000269|PubMed:14707147,
CC ECO:0000269|PubMed:14749727, ECO:0000269|PubMed:18688255,
CC ECO:0000269|PubMed:21102410}.
CC -!- INTERACTION:
CC P33240; Q8NFV4-4: ABHD11; NbExp=3; IntAct=EBI-711360, EBI-12318443;
CC P33240; Q9ULX6: AKAP8L; NbExp=3; IntAct=EBI-711360, EBI-357530;
CC P33240; Q9NXR5-2: ANKRD10; NbExp=3; IntAct=EBI-711360, EBI-12102070;
CC P33240; Q9Y6H3: ATP23; NbExp=3; IntAct=EBI-711360, EBI-12811889;
CC P33240; Q99728: BARD1; NbExp=8; IntAct=EBI-711360, EBI-473181;
CC P33240; Q6P1J9: CDC73; NbExp=5; IntAct=EBI-711360, EBI-930143;
CC P33240; P40199: CEACAM6; NbExp=3; IntAct=EBI-711360, EBI-4314501;
CC P33240; Q9NZN8: CNOT2; NbExp=3; IntAct=EBI-711360, EBI-743033;
CC P33240; Q9P2I0: CPSF2; NbExp=2; IntAct=EBI-711360, EBI-1043224;
CC P33240; P56545-3: CTBP2; NbExp=3; IntAct=EBI-711360, EBI-10171902;
CC P33240; A1KXE4-2: FAM168B; NbExp=3; IntAct=EBI-711360, EBI-12193763;
CC P33240; Q9BSH5: HDHD3; NbExp=3; IntAct=EBI-711360, EBI-745201;
CC P33240; O14964: HGS; NbExp=6; IntAct=EBI-711360, EBI-740220;
CC P33240; Q0VD86: INCA1; NbExp=3; IntAct=EBI-711360, EBI-6509505;
CC P33240; A6NJ78-4: METTL15; NbExp=3; IntAct=EBI-711360, EBI-10174029;
CC P33240; Q8N6F8: METTL27; NbExp=3; IntAct=EBI-711360, EBI-8487781;
CC P33240; O95453: PARN; NbExp=5; IntAct=EBI-711360, EBI-372832;
CC P33240; P78424: POU6F2; NbExp=3; IntAct=EBI-711360, EBI-12029004;
CC P33240; Q7Z5V6-2: PPP1R32; NbExp=3; IntAct=EBI-711360, EBI-12000762;
CC P33240; Q9NQX0: PRDM6; NbExp=3; IntAct=EBI-711360, EBI-11320284;
CC P33240; Q8HWS3: RFX6; NbExp=3; IntAct=EBI-711360, EBI-746118;
CC P33240; Q99932: SPAG8; NbExp=3; IntAct=EBI-711360, EBI-954419;
CC P33240; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-711360, EBI-11959123;
CC P33240; O75177: SS18L1; NbExp=3; IntAct=EBI-711360, EBI-744674;
CC P33240; Q8IWL8: STH; NbExp=3; IntAct=EBI-711360, EBI-12843506;
CC P33240; Q92734: TFG; NbExp=6; IntAct=EBI-711360, EBI-357061;
CC P33240; Q04726-4: TLE3; NbExp=3; IntAct=EBI-711360, EBI-12014388;
CC P33240; Q08117-2: TLE5; NbExp=3; IntAct=EBI-711360, EBI-11741437;
CC P33240; Q86WV8: TSC1; NbExp=3; IntAct=EBI-711360, EBI-12806590;
CC P33240; Q9UMX0: UBQLN1; NbExp=7; IntAct=EBI-711360, EBI-741480;
CC P33240; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-711360, EBI-10173939;
CC P33240; Q9UHD9: UBQLN2; NbExp=5; IntAct=EBI-711360, EBI-947187;
CC P33240; Q6NVU6: UFSP1; NbExp=3; IntAct=EBI-711360, EBI-12068150;
CC P33240; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-711360, EBI-11975223;
CC P33240; Q9BYN7: ZNF341; NbExp=3; IntAct=EBI-711360, EBI-9089622;
CC P33240; A0A1U9X8X8; NbExp=3; IntAct=EBI-711360, EBI-17234977;
CC P33240-1; P53999: SUB1; NbExp=3; IntAct=EBI-711374, EBI-998260;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11598190}.
CC Note=Localized with DDX1 in cleavage bodies.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P33240-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P33240-2; Sequence=VSP_014841;
CC -!- INDUCTION: Up-regulated during the G0 to S phase transition.
CC {ECO:0000269|PubMed:9736695}.
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DR EMBL; M85085; AAA35724.1; -; mRNA.
DR EMBL; BT009778; AAP88780.1; -; mRNA.
DR EMBL; Z83819; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z95327; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017712; AAH17712.1; -; mRNA.
DR EMBL; BC033135; AAH33135.1; -; mRNA.
DR CCDS; CCDS14473.1; -. [P33240-1]
DR PIR; A40220; A40220.
DR RefSeq; NP_001293138.1; NM_001306209.1. [P33240-2]
DR RefSeq; NP_001316.1; NM_001325.2. [P33240-1]
DR PDB; 1P1T; NMR; -; A=8-111.
DR PDB; 2J8P; NMR; -; A=531-577.
DR PDB; 6Q2I; NMR; -; A=1-107.
DR PDB; 6TZE; NMR; -; A=1-107.
DR PDBsum; 1P1T; -.
DR PDBsum; 2J8P; -.
DR PDBsum; 6Q2I; -.
DR PDBsum; 6TZE; -.
DR AlphaFoldDB; P33240; -.
DR BMRB; P33240; -.
DR SMR; P33240; -.
DR BioGRID; 107860; 148.
DR CORUM; P33240; -.
DR DIP; DIP-36129N; -.
DR IntAct; P33240; 66.
DR MINT; P33240; -.
DR STRING; 9606.ENSP00000362063; -.
DR GlyGen; P33240; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P33240; -.
DR MetOSite; P33240; -.
DR PhosphoSitePlus; P33240; -.
DR SwissPalm; P33240; -.
DR BioMuta; CSTF2; -.
DR DMDM; 461847; -.
DR EPD; P33240; -.
DR jPOST; P33240; -.
DR MassIVE; P33240; -.
DR MaxQB; P33240; -.
DR PaxDb; P33240; -.
DR PeptideAtlas; P33240; -.
DR PRIDE; P33240; -.
DR ProteomicsDB; 54902; -. [P33240-1]
DR ProteomicsDB; 54903; -. [P33240-2]
DR Antibodypedia; 411; 349 antibodies from 33 providers.
DR DNASU; 1478; -.
DR Ensembl; ENST00000372972.7; ENSP00000362063.2; ENSG00000101811.14. [P33240-1]
DR GeneID; 1478; -.
DR KEGG; hsa:1478; -.
DR MANE-Select; ENST00000372972.7; ENSP00000362063.2; NM_001325.3; NP_001316.1.
DR UCSC; uc004egh.4; human. [P33240-1]
DR CTD; 1478; -.
DR DisGeNET; 1478; -.
DR GeneCards; CSTF2; -.
DR HGNC; HGNC:2484; CSTF2.
DR HPA; ENSG00000101811; Low tissue specificity.
DR MIM; 300907; gene.
DR neXtProt; NX_P33240; -.
DR OpenTargets; ENSG00000101811; -.
DR PharmGKB; PA26986; -.
DR VEuPathDB; HostDB:ENSG00000101811; -.
DR eggNOG; KOG0108; Eukaryota.
DR GeneTree; ENSGT00940000158987; -.
DR InParanoid; P33240; -.
DR OMA; CEPEDAP; -.
DR PhylomeDB; P33240; -.
DR TreeFam; TF314948; -.
DR PathwayCommons; P33240; -.
DR Reactome; R-HSA-6784531; tRNA processing in the nucleus.
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 SignaLink; P33240; -.
DR SIGNOR; P33240; -.
DR BioGRID-ORCS; 1478; 36 hits in 706 CRISPR screens.
DR ChiTaRS; CSTF2; human.
DR EvolutionaryTrace; P33240; -.
DR GeneWiki; CSTF2; -.
DR GenomeRNAi; 1478; -.
DR Pharos; P33240; Tbio.
DR PRO; PR:P33240; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P33240; protein.
DR Bgee; ENSG00000101811; Expressed in oocyte and 171 other tissues.
DR ExpressionAtlas; P33240; baseline and differential.
DR Genevisible; P33240; HS.
DR GO; GO:0071920; C:cleavage body; IDA:UniProtKB.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IDA:GO_Central.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEA:Ensembl.
DR GO; GO:0006378; P:mRNA polyadenylation; IEA:InterPro.
DR GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IBA:GO_Central.
DR Gene3D; 1.10.20.70; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR033105; CSTF2.
DR InterPro; IPR025742; CSTF2_hinge.
DR InterPro; IPR026896; CSTF_C.
DR InterPro; IPR038192; CSTF_C_sf.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR45735:SF6; PTHR45735:SF6; 1.
DR Pfam; PF14327; CSTF2_hinge; 1.
DR Pfam; PF14304; CSTF_C; 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; Isopeptide bond; Methylation;
KW mRNA processing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Ubl conjugation.
FT CHAIN 1..577
FT /note="Cleavage stimulation factor subunit 2"
FT /id="PRO_0000081531"
FT DOMAIN 16..94
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REPEAT 410..414
FT /note="1; approximate"
FT REPEAT 415..419
FT /note="2"
FT REPEAT 420..424
FT /note="3"
FT REPEAT 425..429
FT /note="4; approximate"
FT REPEAT 430..434
FT /note="5; approximate"
FT REPEAT 435..439
FT /note="6"
FT REPEAT 440..444
FT /note="7"
FT REPEAT 445..449
FT /note="8"
FT REPEAT 450..454
FT /note="9"
FT REPEAT 455..459
FT /note="10; approximate"
FT REPEAT 460..464
FT /note="11"
FT REPEAT 465..469
FT /note="12; approximate"
FT REGION 108..248
FT /note="Interactions with CSTF3 and SYMPK"
FT REGION 206..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..469
FT /note="12 X 5 AA tandem repeats of M-E-A-R-[AG]"
FT REGION 508..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..577
FT /note="Interaction with RPO2TC1"
FT /evidence="ECO:0000269|PubMed:11389848"
FT COMPBIAS 211..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..385
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 308
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 468
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 475
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT CROSSLNK 189
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 235..251
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014841"
FT HELIX 12..15
FT /evidence="ECO:0007829|PDB:1P1T"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:1P1T"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:6Q2I"
FT HELIX 29..37
FT /evidence="ECO:0007829|PDB:1P1T"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:1P1T"
FT TURN 51..54
FT /evidence="ECO:0007829|PDB:1P1T"
FT STRAND 55..63
FT /evidence="ECO:0007829|PDB:1P1T"
FT HELIX 67..76
FT /evidence="ECO:0007829|PDB:1P1T"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:1P1T"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:1P1T"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:1P1T"
FT HELIX 97..104
FT /evidence="ECO:0007829|PDB:1P1T"
FT HELIX 532..535
FT /evidence="ECO:0007829|PDB:2J8P"
FT HELIX 537..545
FT /evidence="ECO:0007829|PDB:2J8P"
FT HELIX 549..553
FT /evidence="ECO:0007829|PDB:2J8P"
FT HELIX 557..560
FT /evidence="ECO:0007829|PDB:2J8P"
FT HELIX 562..571
FT /evidence="ECO:0007829|PDB:2J8P"
SQ SEQUENCE 577 AA; 60959 MW; B76595E9BF8FABBD CRC64;
MAGLTVRDPA VDRSLRSVFV GNIPYEATEE QLKDIFSEVG PVVSFRLVYD RETGKPKGYG
FCEYQDQETA LSAMRNLNGR EFSGRALRVD NAASEKNKEE LKSLGTGAPV IESPYGETIS
PEDAPESISK AVASLPPEQM FELMKQMKLC VQNSPQEARN MLLQNPQLAY ALLQAQVVMR
IVDPEIALKI LHRQTNIPTL IAGNPQPVHG AGPGSGSNVS MNQQNPQAPQ AQSLGGMHVN
GAPPLMQASM QGGVPAPGQM PAAVTGPGPG SLAPGGGMQA QVGMPGSGPV SMERGQVPMQ
DPRAAMQRGS LPANVPTPRG LLGDAPNDPR GGTLLSVTGE VEPRGYLGPP HQGPPMHHVP
GHESRGPPPH ELRGGPLPEP RPLMAEPRGP MLDQRGPPLD GRGGRDPRGI DARGMEARAM
EARGLDARGL EARAMEARAM EARAMEARAM EARAMEVRGM EARGMDTRGP VPGPRGPIPS
GMQGPSPINM GAVVPQGSRQ VPVMQGTGMQ GASIQGGSQP GGFSPGQNQV TPQDHEKAAL
IMQVLQLTAD QIAMLPPEQR QSILILKEQI QKSTGAP
