CPSF3_HUMAN
ID CPSF3_HUMAN Reviewed; 684 AA.
AC Q9UKF6; O14769; Q53RS2; Q96F36;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Cleavage and polyadenylation specificity factor subunit 3;
DE EC=3.1.27.- {ECO:0000269|PubMed:15037765, ECO:0000269|PubMed:17128255};
DE AltName: Full=Cleavage and polyadenylation specificity factor 73 kDa subunit;
DE Short=CPSF 73 kDa subunit;
DE AltName: Full=mRNA 3'-end-processing endonuclease CPSF-73;
GN Name=CPSF3; Synonyms=CPSF73;
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].
RC TISSUE=Hepatoma;
RA Yu S., Chen W., Pang X., Dong X., Wang H.;
RT "Homo sapiens mRNA for CPSF (cleavage and polyadenylation specificity
RT factor) 73 kDa subunit.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-142.
RC TISSUE=Brain, and 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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 120-498.
RA Pusch W.;
RT "H. sapiens mRNA for the 73 kDa subunit of CPSF (cleavage and
RT polyadenylation specificity factor, partial cds).";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION IN PRE-MRNA 3'-END PROCESSING, AND IDENTIFICATION IN THE CPSF
RP COMPLEX.
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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
RX PubMed=15037765; DOI=10.1261/rna.5214404;
RA Ryan K., Calvo O., Manley J.L.;
RT "Evidence that polyadenylation factor CPSF-73 is the mRNA 3' processing
RT endonuclease.";
RL RNA 10:565-573(2004).
RN [8]
RP SUMOYLATION AT LYS-462; LYS-465 AND LYS-545, AND MUTAGENESIS OF LYS-462;
RP LYS-465 AND LYS-545.
RX PubMed=17923699; DOI=10.1128/mcb.01186-07;
RA Vethantham V., Rao N., Manley J.L.;
RT "Sumoylation modulates the assembly and activity of the pre-mRNA 3'
RT processing complex.";
RL Mol. Cell. Biol. 27:8848-8858(2007).
RN [9]
RP FUNCTION, INTERACTION WITH CPSF2; CSTF2 AND SYMPK, AND MUTAGENESIS OF
RP HIS-73; ASP-75; HIS-76; SER-334 AND HIS-396.
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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP INTERACTION WITH WDR33.
RX PubMed=19217410; DOI=10.1016/j.molcel.2008.12.028;
RA Shi Y., Di Giammartino D.C., Taylor D., Sarkeshik A., Rice W.J.,
RA Yates J.R. III, Frank J., Manley J.L.;
RT "Molecular architecture of the human pre-mRNA 3' processing complex.";
RL Mol. Cell 33:365-376(2009).
RN [12]
RP IDENTIFICATION IN THE CPSF COMPLEX, AND INTERACTION WITH TUT1.
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-681, AND IDENTIFICATION BY
RP 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 [14]
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 [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-681, 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 [17]
RP IDENTIFICATION BY 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 [18]
RP FUNCTION.
RX PubMed=30507380; DOI=10.7554/elife.39865;
RA Pettinati I., Grzechnik P., Ribeiro de Almeida C., Brem J., McDonough M.A.,
RA Dhir S., Proudfoot N.J., Schofield C.J.;
RT "Biosynthesis of histone messenger RNA employs a specific 3' end
RT endonuclease.";
RL Elife 7:0-0(2018).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-459 IN COMPLEX WITH ZINC IONS,
RP FUNCTION, MUTAGENESIS OF 75-ASP-HIS-76, COFACTOR, AND CATALYTIC ACTIVITY.
RX PubMed=17128255; DOI=10.1038/nature05363;
RA Mandel C.R., Kaneko S., Zhang H., Gebauer D., Vethantham V., Manley J.L.,
RA Tong L.;
RT "Polyadenylation factor CPSF-73 is the pre-mRNA 3'-end-processing
RT endonuclease.";
RL Nature 444:953-956(2006).
RN [20]
RP VARIANT [LARGE SCALE ANALYSIS] ASN-578.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Component of the cleavage and polyadenylation specificity
CC factor (CPSF) complex that plays a key role in pre-mRNA 3'-end
CC formation, recognizing the AAUAAA signal sequence and interacting with
CC poly(A) polymerase and other factors to bring about cleavage and
CC poly(A) addition. Has endonuclease activity, and functions as mRNA 3'-
CC end-processing endonuclease (PubMed:30507380). Also involved in the
CC histone 3'-end pre-mRNA processing (PubMed:30507380). U7 snRNP-
CC dependent protein that induces both the 3'-endoribonucleolytic cleavage
CC of histone pre-mRNAs and acts as a 5' to 3' exonuclease for degrading
CC the subsequent downstream cleavage product (DCP) of mature histone
CC mRNAs. Cleavage occurs after the 5'-ACCCA-3' sequence in the histone
CC pre-mRNA leaving a 3'hydroxyl group on the upstream fragment containing
CC the stem loop (SL) and 5' phosphate on the downstream cleavage product
CC (DCP) starting with CU nucleotides. The U7-dependent 5' to 3'
CC exonuclease activity is processive and degrades the DCP RNA substrate
CC even after complete removal of the U7-binding site. Binds to the
CC downstream cleavage product (DCP) of histone pre-mRNAs and the cleaved
CC DCP RNA substrate in a U7 snRNP dependent manner. Required for
CC entering/progressing through S-phase of the cell cycle
CC (PubMed:30507380). Required for the selective processing of microRNAs
CC (miRNAs) during embryonic stem cell differentiation via its interaction
CC with ISY1 (By similarity). Required for the biogenesis of all miRNAs
CC from the pri-miR-17-92 primary transcript except miR-92a (By
CC similarity). Only required for the biogenesis of miR-290 and miR-96
CC from the pri-miR-290-295 and pri-miR-96-183 primary transcripts,
CC respectively (By similarity). {ECO:0000250|UniProtKB:Q9QXK7,
CC ECO:0000269|PubMed:14749727, ECO:0000269|PubMed:15037765,
CC ECO:0000269|PubMed:17128255, ECO:0000269|PubMed:18688255,
CC ECO:0000269|PubMed:30507380}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:17128255};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:17128255};
CC -!- SUBUNIT: Component of the cleavage and polyadenylation specificity
CC factor (CPSF) complex, composed of CPSF1, CPSF2, CPSF3, CPSF4 and
CC FIP1L1. Interacts with CPSF2, CSTF2 and SYMPK. Interacts with TUT1; the
CC interaction is direct and mediates the recruitment of the CPSF complex
CC on the 3'UTR of pre-mRNAs. Interacts with WDR33. Interacts with ZC3H3
CC (By similarity). {ECO:0000250|UniProtKB:Q9QXK7,
CC ECO:0000269|PubMed:14749727, ECO:0000269|PubMed:17128255,
CC ECO:0000269|PubMed:18688255, ECO:0000269|PubMed:19217410,
CC ECO:0000269|PubMed:21102410}.
CC -!- INTERACTION:
CC Q9UKF6; P42858: HTT; NbExp=3; IntAct=EBI-1044699, EBI-466029;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15037765}.
CC -!- PTM: Sumoylated on Lys-462, Lys-465 and Lys-545, preferentially by
CC SUMO3. {ECO:0000269|PubMed:17923699}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA-
CC metabolizing metallo-beta-lactamase-like family. CPSF3 subfamily.
CC {ECO:0000305}.
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DR EMBL; AF171877; AAF00224.1; -; mRNA.
DR EMBL; AC080162; AAY14858.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00989.1; -; Genomic_DNA.
DR EMBL; BC011654; AAH11654.1; -; mRNA.
DR EMBL; BC020211; AAH20211.1; -; mRNA.
DR EMBL; AF017269; AAB70268.1; -; mRNA.
DR CCDS; CCDS1664.1; -.
DR RefSeq; NP_057291.1; NM_016207.3.
DR PDB; 2I7T; X-ray; 2.10 A; A=1-459.
DR PDB; 2I7V; X-ray; 2.10 A; A=1-459.
DR PDB; 6M8Q; X-ray; 2.49 A; A/B=1-459.
DR PDB; 6V4X; EM; 3.20 A; H=1-684.
DR PDBsum; 2I7T; -.
DR PDBsum; 2I7V; -.
DR PDBsum; 6M8Q; -.
DR PDBsum; 6V4X; -.
DR AlphaFoldDB; Q9UKF6; -.
DR SMR; Q9UKF6; -.
DR BioGRID; 119680; 101.
DR CORUM; Q9UKF6; -.
DR DIP; DIP-42501N; -.
DR IntAct; Q9UKF6; 53.
DR MINT; Q9UKF6; -.
DR STRING; 9606.ENSP00000238112; -.
DR GlyGen; Q9UKF6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UKF6; -.
DR PhosphoSitePlus; Q9UKF6; -.
DR BioMuta; CPSF3; -.
DR DMDM; 18203503; -.
DR EPD; Q9UKF6; -.
DR jPOST; Q9UKF6; -.
DR MassIVE; Q9UKF6; -.
DR MaxQB; Q9UKF6; -.
DR PaxDb; Q9UKF6; -.
DR PeptideAtlas; Q9UKF6; -.
DR PRIDE; Q9UKF6; -.
DR ProteomicsDB; 84782; -.
DR Antibodypedia; 12409; 231 antibodies from 27 providers.
DR DNASU; 51692; -.
DR Ensembl; ENST00000238112.8; ENSP00000238112.3; ENSG00000119203.14.
DR GeneID; 51692; -.
DR KEGG; hsa:51692; -.
DR MANE-Select; ENST00000238112.8; ENSP00000238112.3; NM_016207.4; NP_057291.1.
DR UCSC; uc002qzo.3; human.
DR CTD; 51692; -.
DR DisGeNET; 51692; -.
DR GeneCards; CPSF3; -.
DR HGNC; HGNC:2326; CPSF3.
DR HPA; ENSG00000119203; Low tissue specificity.
DR MIM; 606029; gene.
DR neXtProt; NX_Q9UKF6; -.
DR OpenTargets; ENSG00000119203; -.
DR PharmGKB; PA26843; -.
DR VEuPathDB; HostDB:ENSG00000119203; -.
DR eggNOG; KOG1137; Eukaryota.
DR GeneTree; ENSGT00940000155699; -.
DR HOGENOM; CLU_009673_2_3_1; -.
DR InParanoid; Q9UKF6; -.
DR OMA; TRSVECE; -.
DR OrthoDB; 218195at2759; -.
DR PhylomeDB; Q9UKF6; -.
DR TreeFam; TF105643; -.
DR PathwayCommons; Q9UKF6; -.
DR Reactome; R-HSA-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
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; Q9UKF6; -.
DR SIGNOR; Q9UKF6; -.
DR BioGRID-ORCS; 51692; 799 hits in 1080 CRISPR screens.
DR ChiTaRS; CPSF3; human.
DR EvolutionaryTrace; Q9UKF6; -.
DR GeneWiki; CPSF3; -.
DR GenomeRNAi; 51692; -.
DR Pharos; Q9UKF6; Tchem.
DR PRO; PR:Q9UKF6; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9UKF6; protein.
DR Bgee; ENSG00000119203; Expressed in ganglionic eminence and 184 other tissues.
DR ExpressionAtlas; Q9UKF6; baseline and differential.
DR Genevisible; Q9UKF6; HS.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0008409; F:5'-3' exonuclease activity; IBA:GO_Central.
DR GO; GO:0004534; F:5'-3' exoribonuclease activity; ISS:UniProtKB.
DR GO; GO:0004521; F:endoribonuclease activity; IMP:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IMP:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0031124; P:mRNA 3'-end processing; IMP:UniProtKB.
DR GO; GO:0006398; P:mRNA 3'-end processing by stem-loop binding and cleavage; IDA:UniProtKB.
DR GO; GO:0006379; P:mRNA cleavage; TAS:ProtInc.
DR GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IMP:UniProtKB.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR022712; Beta_Casp.
DR InterPro; IPR021718; CPSF73-100_C.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR011108; RMMBL.
DR Pfam; PF10996; Beta-Casp; 1.
DR Pfam; PF11718; CPSF73-100_C; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR Pfam; PF07521; RMMBL; 1.
DR SMART; SM01027; Beta-Casp; 1.
DR SMART; SM01098; CPSF73-100_C; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Endonuclease; Hydrolase; Isopeptide bond;
KW Metal-binding; mRNA processing; Nuclease; Nucleus; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; RNA-binding; Ubl conjugation; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..684
FT /note="Cleavage and polyadenylation specificity factor
FT subunit 3"
FT /id="PRO_0000074400"
FT ACT_SITE 396
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17128255,
FT ECO:0007744|PDB:2I7T, ECO:0007744|PDB:2I7V"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17128255,
FT ECO:0007744|PDB:2I7T, ECO:0007744|PDB:2I7V"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17128255,
FT ECO:0007744|PDB:2I7T, ECO:0007744|PDB:2I7V"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17128255,
FT ECO:0007744|PDB:2I7T, ECO:0007744|PDB:2I7V"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17128255,
FT ECO:0007744|PDB:2I7T, ECO:0007744|PDB:2I7V"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17128255,
FT ECO:0007744|PDB:2I7T, ECO:0007744|PDB:2I7V"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17128255,
FT ECO:0007744|PDB:2I7T, ECO:0007744|PDB:2I7V"
FT BINDING 418
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17128255,
FT ECO:0007744|PDB:2I7T, ECO:0007744|PDB:2I7V"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 659
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXK7"
FT MOD_RES 681
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 462
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:17923699"
FT CROSSLNK 465
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:17923699"
FT CROSSLNK 545
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:17923699"
FT VARIANT 142
FT /note="E -> G (in dbSNP:rs17850770)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_037646"
FT VARIANT 578
FT /note="D -> N (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035873"
FT MUTAGEN 73
FT /note="H->A: Inhibits histone 3'-end processing."
FT /evidence="ECO:0000269|PubMed:18688255"
FT MUTAGEN 75..76
FT /note="DH->KA: Loss of histone 3'-end processing."
FT /evidence="ECO:0000269|PubMed:17128255"
FT MUTAGEN 75
FT /note="D->A: Inhibits histone 3'-end processing."
FT /evidence="ECO:0000269|PubMed:18688255"
FT MUTAGEN 76
FT /note="H->A: Inhibits histone 3'-end processing."
FT /evidence="ECO:0000269|PubMed:18688255"
FT MUTAGEN 334
FT /note="S->A: Does not inhibit histone 3'-end processing."
FT /evidence="ECO:0000269|PubMed:18688255"
FT MUTAGEN 396
FT /note="H->A: Inhibits histone 3'-end processing."
FT /evidence="ECO:0000269|PubMed:18688255"
FT MUTAGEN 462
FT /note="K->R: Reduced sumoylation; when associated with R-
FT 465 and R-545."
FT /evidence="ECO:0000269|PubMed:17923699"
FT MUTAGEN 465
FT /note="K->R: Reduced sumoylation; when associated with R-
FT 462 and R-545."
FT /evidence="ECO:0000269|PubMed:17923699"
FT MUTAGEN 545
FT /note="K->R: Reduced sumoylation; when associated with R-
FT 462 and R-465."
FT /evidence="ECO:0000269|PubMed:17923699"
FT STRAND 10..25
FT /evidence="ECO:0007829|PDB:2I7T"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:2I7T"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:2I7T"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:2I7T"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:2I7T"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:2I7T"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:2I7T"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:2I7T"
FT HELIX 80..86
FT /evidence="ECO:0007829|PDB:2I7T"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:2I7T"
FT HELIX 97..110
FT /evidence="ECO:0007829|PDB:2I7T"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:6M8Q"
FT HELIX 125..131
FT /evidence="ECO:0007829|PDB:2I7T"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:2I7T"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:2I7T"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:2I7T"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:2I7T"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:2I7T"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:2I7T"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:2I7V"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:2I7T"
FT TURN 206..209
FT /evidence="ECO:0007829|PDB:2I7T"
FT HELIX 215..231
FT /evidence="ECO:0007829|PDB:2I7T"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:2I7T"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:2I7T"
FT HELIX 246..259
FT /evidence="ECO:0007829|PDB:2I7T"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:2I7T"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:2I7T"
FT HELIX 275..284
FT /evidence="ECO:0007829|PDB:2I7V"
FT TURN 285..287
FT /evidence="ECO:0007829|PDB:2I7V"
FT HELIX 291..296
FT /evidence="ECO:0007829|PDB:6M8Q"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:6M8Q"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:2I7T"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:2I7V"
FT STRAND 321..328
FT /evidence="ECO:0007829|PDB:2I7T"
FT HELIX 335..344
FT /evidence="ECO:0007829|PDB:2I7T"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:2I7T"
FT HELIX 363..367
FT /evidence="ECO:0007829|PDB:2I7T"
FT STRAND 372..375
FT /evidence="ECO:0007829|PDB:2I7T"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:6M8Q"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:2I7T"
FT STRAND 386..390
FT /evidence="ECO:0007829|PDB:2I7T"
FT HELIX 399..409
FT /evidence="ECO:0007829|PDB:2I7T"
FT STRAND 412..419
FT /evidence="ECO:0007829|PDB:2I7T"
FT HELIX 421..435
FT /evidence="ECO:0007829|PDB:2I7T"
FT STRAND 444..446
FT /evidence="ECO:0007829|PDB:2I7T"
FT STRAND 454..458
FT /evidence="ECO:0007829|PDB:2I7T"
FT STRAND 462..466
FT /evidence="ECO:0007829|PDB:6V4X"
FT HELIX 469..471
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 481..490
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 492..495
FT /evidence="ECO:0007829|PDB:6V4X"
FT TURN 499..503
FT /evidence="ECO:0007829|PDB:6V4X"
SQ SEQUENCE 684 AA; 77486 MW; F8AA24EA6FB78377 CRC64;
MSAIPAEESD QLLIRPLGAG QEVGRSCIIL EFKGRKIMLD CGIHPGLEGM DALPYIDLID
PAEIDLLLIS HFHLDHCGAL PWFLQKTSFK GRTFMTHATK AIYRWLLSDY VKVSNISADD
MLYTETDLEE SMDKIETINF HEVKEVAGIK FWCYHAGHVL GAAMFMIEIA GVKLLYTGDF
SRQEDRHLMA AEIPNIKPDI LIIESTYGTH IHEKREEREA RFCNTVHDIV NRGGRGLIPV
FALGRAQELL LILDEYWQNH PELHDIPIYY ASSLAKKCMA VYQTYVNAMN DKIRKQININ
NPFVFKHISN LKSMDHFDDI GPSVVMASPG MMQSGLSREL FESWCTDKRN GVIIAGYCVE
GTLAKHIMSE PEEITTMSGQ KLPLKMSVDY ISFSAHTDYQ QTSEFIRALK PPHVILVHGE
QNEMARLKAA LIREYEDNDE VHIEVHNPRN TEAVTLNFRG EKLAKVMGFL ADKKPEQGQR
VSGILVKRNF NYHILSPCDL SNYTDLAMST VKQTQAIPYT GPFNLLCYQL QKLTGDVEEL
EIQEKPALKV FKNITVIQEP GMVVLEWLAN PSNDMYADTV TTVILEVQSN PKIRKGAVQK
VSKKLEMHVY SKRLEIMLQD IFGEDCVSVK DDSILSVTVD GKTANLNLET RTVECEEGSE
DDESLREMVE LAAQRLYEAL TPVH
