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Cleavage stimulation factor subunit 2 (CF-1 64 kDa subunit) (Cleavage stimulation factor 64 kDa subunit) (CSTF 64 kDa subunit) (CstF-64)

 CSTF2_HUMAN             Reviewed;         577 AA.
P33240; Q5H951; Q6LA74; Q8N502;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
25-OCT-2017, entry version 175.
RecName: Full=Cleavage stimulation factor subunit 2;
AltName: Full=CF-1 64 kDa subunit;
AltName: Full=Cleavage stimulation factor 64 kDa subunit;
Short=CSTF 64 kDa subunit;
Short=CstF-64;
Name=CSTF2;
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), PHOSPHORYLATION, AND
RNA-BINDING.
PubMed=1741396; DOI=10.1073/pnas.89.4.1403;
Takagaki Y., Macdonald C.C., Shenk T., Manley J.L.;
"The human 64-kDa polyadenylylation factor contains a
ribonucleoprotein-type RNA binding domain and unusual auxiliary
motifs.";
Proc. Natl. Acad. Sci. U.S.A. 89:1403-1407(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Kidney, and Ovary;
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).
[5]
RNA-BINDING, AND FUNCTION.
PubMed=9199325; DOI=10.1128/MCB.17.7.3907;
Takagaki Y., Manley J.L.;
"RNA recognition by the human polyadenylation factor CstF.";
Mol. Cell. Biol. 17:3907-3914(1997).
[6]
INDUCTION.
PubMed=9736695; DOI=10.1073/pnas.95.19.11095;
Martincic K., Campbell R., Edwalds-Gilbert G., Souan L., Lotze M.T.,
Milcarek C.;
"Increase in the 64-kDa subunit of the polyadenylation/cleavage
stimulatory factor during the G0 to S phase transition.";
Proc. Natl. Acad. Sci. U.S.A. 95:11095-11100(1998).
[7]
INTERACTION WITH CSTF3 AND SYMPK.
PubMed=10669729; DOI=10.1128/MCB.20.5.1515-1525.2000;
Takagaki Y., Manley J.L.;
"Complex protein interactions within the human polyadenylation
machinery identify a novel component.";
Mol. Cell. Biol. 20:1515-1525(2000).
[8]
INTERACTION WITH RPO2TC1.
PubMed=11389848; DOI=10.1016/S1097-2765(01)00236-2;
Calvo O., Manley J.L.;
"Evolutionarily conserved interaction between CstF-64 and PC4 links
transcription, polyadenylation, and termination.";
Mol. Cell 7:1013-1023(2001).
[9]
INTERACTION WITH DDX1, AND SUBCELLULAR LOCATION.
PubMed=11598190; DOI=10.1091/mbc.12.10.3046;
Bleoo S., Sun X., Hendzel M.J., Rowe J.M., Packer M., Godbout R.;
"Association of human DEAD box protein DDX1 with a cleavage
stimulation factor involved in 3'-end processing of pre-MRNA.";
Mol. Biol. Cell 12:3046-3059(2001).
[10]
INTERACTION WITH FIP1L1.
PubMed=14749727; DOI=10.1038/sj.emboj.7600070;
Kaufmann I., Martin G., Friedlein A., Langen H., Keller W.;
"Human Fip1 is a subunit of CPSF that binds to U-rich RNA elements and
stimulates poly(A) polymerase.";
EMBO J. 23:616-626(2004).
[11]
INTERACTION WITH HSF1.
PubMed=14707147; DOI=10.1074/jbc.M311719200;
Xing H., Mayhew C.N., Cullen K.E., Park-Sarge O.-K., Sarge K.D.;
"HSF1 modulation of Hsp70 mRNA polyadenylation via interaction with
symplekin.";
J. Biol. Chem. 279:10551-10555(2004).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[13]
INTERACTION WITH CPSF2 AND CPSF3.
PubMed=18688255; DOI=10.1038/embor.2008.146;
Kolev N.G., Yario T.A., Benson E., Steitz J.A.;
"Conserved motifs in both CPSF73 and CPSF100 are required to assemble
the active endonuclease for histone mRNA 3'-end maturation.";
EMBO Rep. 9:1013-1018(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524, AND 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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524, 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]
IDENTIFICATION IN THE CPSF COMPLEX.
PubMed=21102410; DOI=10.1038/emboj.2010.287;
Laishram R.S., Anderson R.A.;
"The poly A polymerase Star-PAP controls 3'-end cleavage by promoting
CPSF interaction and specificity toward the pre-mRNA.";
EMBO J. 29:4132-4145(2010).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(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]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=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]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-308; ARG-468 AND ARG-475,
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).
[22]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-189, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[23]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-189, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[24]
STRUCTURE BY NMR OF 8-111.
PubMed=12773396; DOI=10.1093/emboj/cdg259;
Perez Canadillas J.M., Varani G.;
"Recognition of GU-rich polyadenylation regulatory elements by human
CstF-64 protein.";
EMBO J. 22:2821-2830(2003).
[25]
STRUCTURE BY NMR OF 531-577.
PubMed=17116658; DOI=10.1074/jbc.M609981200;
Qu X., Perez-Canadillas J.M., Agrawal S., De Baecke J., Cheng H.,
Varani G., Moore C.;
"The C-terminal domains of vertebrate CstF-64 and its yeast orthologue
Rna15 form a new structure critical for mRNA 3'-end processing.";
J. Biol. Chem. 282:2101-2115(2007).
-!- FUNCTION: One of the multiple factors required for polyadenylation
and 3'-end cleavage of mammalian pre-mRNAs. This subunit is
directly involved in the binding to pre-mRNAs (By similarity).
{ECO:0000250, ECO:0000269|PubMed:9199325}.
-!- SUBUNIT: The CSTF complex is composed of CSTF1 (50 kDa subunit),
CSTF2 (64 kDa subunit) and CSTF3 (77 kDa subunit). CSTF2 directly
interacts with CSTF3, SYMPK and RPO2TC1. Interacts with HSF1 in
heat-stressed cells. Interacts with CPSF2, CPSF3 and FIP1L1.
Interacts with DDX1. {ECO:0000269|PubMed:10669729,
ECO:0000269|PubMed:11389848, ECO:0000269|PubMed:11598190,
ECO:0000269|PubMed:14707147, ECO:0000269|PubMed:14749727,
ECO:0000269|PubMed:18688255, ECO:0000269|PubMed:21102410}.
-!- INTERACTION:
Q99728:BARD1; NbExp=8; IntAct=EBI-711360, EBI-473181;
Q6P1J9:CDC73; NbExp=5; IntAct=EBI-711360, EBI-930143;
Q9P2I0:CPSF2; NbExp=2; IntAct=EBI-711360, EBI-1043224;
O14964:HGS; NbExp=7; IntAct=EBI-711360, EBI-740220;
Q0VD86:INCA1; NbExp=4; IntAct=EBI-711360, EBI-6509505;
O95453:PARN; NbExp=5; IntAct=EBI-711360, EBI-372832;
Q99932:SPAG8; NbExp=3; IntAct=EBI-711360, EBI-954419;
O75177:SS18L1; NbExp=3; IntAct=EBI-711360, EBI-744674;
P53999:SUB1; NbExp=3; IntAct=EBI-711374, EBI-998260;
Q92734:TFG; NbExp=5; IntAct=EBI-711360, EBI-357061;
Q9UMX0:UBQLN1; NbExp=6; IntAct=EBI-711360, EBI-741480;
Q9UMX0-2:UBQLN1; NbExp=3; IntAct=EBI-711360, EBI-10173939;
Q70EL1-9:USP54; NbExp=4; IntAct=EBI-711360, EBI-11975223;
Q9BYN7:ZNF341; NbExp=3; IntAct=EBI-711360, EBI-9089622;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11598190}.
Note=Localized with DDX1 in cleavage bodies.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P33240-1; Sequence=Displayed;
Name=2;
IsoId=P33240-2; Sequence=VSP_014841;
Note=No experimental confirmation available.;
-!- INDUCTION: Up-regulated during the G0 to S phase transition.
{ECO:0000269|PubMed:9736695}.
-!- SEQUENCE CAUTION:
Sequence=CAI42681.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; M85085; AAA35724.1; -; mRNA.
EMBL; BT009778; AAP88780.1; -; mRNA.
EMBL; Z83819; CAB06072.2; -; Genomic_DNA.
EMBL; Z95327; CAB06072.2; JOINED; Genomic_DNA.
EMBL; Z95327; CAI42680.1; -; Genomic_DNA.
EMBL; Z83819; CAI42680.1; JOINED; Genomic_DNA.
EMBL; Z95327; CAI42681.1; ALT_SEQ; Genomic_DNA.
EMBL; BC017712; AAH17712.1; -; mRNA.
EMBL; BC033135; AAH33135.1; -; mRNA.
CCDS; CCDS14473.1; -. [P33240-1]
PIR; A40220; A40220.
RefSeq; NP_001293138.1; NM_001306209.1. [P33240-2]
RefSeq; NP_001316.1; NM_001325.2. [P33240-1]
UniGene; Hs.132370; -.
PDB; 1P1T; NMR; -; A=8-111.
PDB; 2J8P; NMR; -; A=531-577.
PDBsum; 1P1T; -.
PDBsum; 2J8P; -.
ProteinModelPortal; P33240; -.
SMR; P33240; -.
BioGrid; 107860; 78.
CORUM; P33240; -.
DIP; DIP-36129N; -.
IntAct; P33240; 53.
MINT; MINT-1375144; -.
STRING; 9606.ENSP00000362063; -.
iPTMnet; P33240; -.
PhosphoSitePlus; P33240; -.
SwissPalm; P33240; -.
BioMuta; CSTF2; -.
DMDM; 461847; -.
EPD; P33240; -.
MaxQB; P33240; -.
PaxDb; P33240; -.
PeptideAtlas; P33240; -.
PRIDE; P33240; -.
DNASU; 1478; -.
Ensembl; ENST00000372972; ENSP00000362063; ENSG00000101811. [P33240-1]
GeneID; 1478; -.
KEGG; hsa:1478; -.
UCSC; uc004egh.4; human. [P33240-1]
CTD; 1478; -.
DisGeNET; 1478; -.
EuPathDB; HostDB:ENSG00000101811.13; -.
GeneCards; CSTF2; -.
HGNC; HGNC:2484; CSTF2.
HPA; CAB004680; -.
HPA; HPA000427; -.
MIM; 300907; gene.
neXtProt; NX_P33240; -.
OpenTargets; ENSG00000101811; -.
PharmGKB; PA26986; -.
eggNOG; KOG0108; Eukaryota.
eggNOG; ENOG410XQBV; LUCA.
GeneTree; ENSGT00890000139457; -.
HOGENOM; HOG000214373; -.
HOVERGEN; HBG051145; -.
InParanoid; P33240; -.
KO; K14407; -.
PhylomeDB; P33240; -.
TreeFam; TF314948; -.
Reactome; R-HSA-109688; Cleavage of Growing Transcript in the Termination Region.
Reactome; R-HSA-6784531; tRNA processing in the nucleus.
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; CSTF2; human.
EvolutionaryTrace; P33240; -.
GeneWiki; CSTF2; -.
GenomeRNAi; 1478; -.
PRO; PR:P33240; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000101811; -.
CleanEx; HS_CSTF2; -.
ExpressionAtlas; P33240; baseline and differential.
Genevisible; P33240; HS.
GO; GO:0071920; C:cleavage body; IDA:UniProtKB.
GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IDA:UniProtKB.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0031124; P:mRNA 3'-end processing; TAS:Reactome.
GO; GO:0006378; P:mRNA polyadenylation; IEA:InterPro.
GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IBA:GO_Central.
GO; GO:0006369; P:termination of RNA polymerase II transcription; TAS:Reactome.
GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; TAS:Reactome.
InterPro; IPR033105; CSTF2.
InterPro; IPR025742; CSTF2_hinge.
InterPro; IPR026896; CSTF_C.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
PANTHER; PTHR23139:SF57; PTHR23139:SF57; 1.
Pfam; PF14327; CSTF2_hinge; 1.
Pfam; PF14304; CSTF_C; 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;
Isopeptide bond; Methylation; mRNA processing; Nucleus;
Phosphoprotein; Reference proteome; Repeat; RNA-binding;
Ubl conjugation.
CHAIN 1 577 Cleavage stimulation factor subunit 2.
/FTId=PRO_0000081531.
DOMAIN 16 94 RRM. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
REPEAT 410 414 1; approximate.
REPEAT 415 419 2.
REPEAT 420 424 3.
REPEAT 425 429 4; approximate.
REPEAT 430 434 5; approximate.
REPEAT 435 439 6.
REPEAT 440 444 7.
REPEAT 445 449 8.
REPEAT 450 454 9.
REPEAT 455 459 10; approximate.
REPEAT 460 464 11.
REPEAT 465 469 12; approximate.
REGION 108 248 Interactions with CSTF3 and SYMPK.
REGION 410 469 12 X 5 AA tandem repeats of M-E-A-R-[AG].
REGION 514 577 Interaction with RPO2TC1.
{ECO:0000269|PubMed:11389848}.
COMPBIAS 198 409 Gly/Pro-rich.
COMPBIAS 470 526 Gly/Pro-rich.
MOD_RES 14 14 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 308 308 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 468 468 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 475 475 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 518 518 Phosphoserine.
{ECO:0000244|PubMed:17525332}.
MOD_RES 524 524 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
CROSSLNK 189 189 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 235 251 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_014841.
HELIX 12 15 {ECO:0000244|PDB:1P1T}.
STRAND 18 22 {ECO:0000244|PDB:1P1T}.
HELIX 29 37 {ECO:0000244|PDB:1P1T}.
STRAND 43 50 {ECO:0000244|PDB:1P1T}.
TURN 51 54 {ECO:0000244|PDB:1P1T}.
STRAND 55 63 {ECO:0000244|PDB:1P1T}.
HELIX 67 76 {ECO:0000244|PDB:1P1T}.
STRAND 77 81 {ECO:0000244|PDB:1P1T}.
STRAND 83 85 {ECO:0000244|PDB:1P1T}.
STRAND 87 91 {ECO:0000244|PDB:1P1T}.
HELIX 97 104 {ECO:0000244|PDB:1P1T}.
HELIX 532 535 {ECO:0000244|PDB:2J8P}.
HELIX 537 545 {ECO:0000244|PDB:2J8P}.
HELIX 549 553 {ECO:0000244|PDB:2J8P}.
HELIX 557 560 {ECO:0000244|PDB:2J8P}.
HELIX 562 571 {ECO:0000244|PDB:2J8P}.
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


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