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Cleavage and polyadenylation specificity factor subunit 3 (EC 3.1.27.-) (Cleavage and polyadenylation specificity factor 73 kDa subunit) (CPSF 73 kDa subunit) (mRNA 3'-end-processing endonuclease CPSF-73)

 CPSF3_HUMAN             Reviewed;         684 AA.
Q9UKF6; O14769; Q53RS2; Q96F36;
18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-OCT-2017, entry version 150.
RecName: Full=Cleavage and polyadenylation specificity factor subunit 3;
EC=3.1.27.- {ECO:0000269|PubMed:15037765, ECO:0000269|PubMed:17128255};
AltName: Full=Cleavage and polyadenylation specificity factor 73 kDa subunit;
Short=CPSF 73 kDa subunit;
AltName: Full=mRNA 3'-end-processing endonuclease CPSF-73;
Name=CPSF3; Synonyms=CPSF73;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Hepatoma;
Yu S., Chen W., Pang X., Dong X., Wang H.;
"Homo sapiens mRNA for CPSF (cleavage and polyadenylation specificity
factor) 73 kDa subunit.";
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-142.
TISSUE=Brain, and Uterus;
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]
NUCLEOTIDE SEQUENCE [MRNA] OF 120-498.
Pusch W.;
"H. sapiens mRNA for the 73 kDa subunit of CPSF (cleavage and
polyadenylation specificity factor, partial cds).";
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
[6]
FUNCTION IN PRE-MRNA 3'-END PROCESSING, AND IDENTIFICATION IN THE CPSF
COMPLEX.
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).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
PubMed=15037765; DOI=10.1261/rna.5214404;
Ryan K., Calvo O., Manley J.L.;
"Evidence that polyadenylation factor CPSF-73 is the mRNA 3'
processing endonuclease.";
RNA 10:565-573(2004).
[8]
SUMOYLATION AT LYS-462; LYS-465 AND LYS-545, AND MUTAGENESIS OF
LYS-462; LYS-465 AND LYS-545.
PubMed=17923699; DOI=10.1128/MCB.01186-07;
Vethantham V., Rao N., Manley J.L.;
"Sumoylation modulates the assembly and activity of the pre-mRNA 3'
processing complex.";
Mol. Cell. Biol. 27:8848-8858(2007).
[9]
FUNCTION, INTERACTION WITH CPSF2; CSTF2 AND SYMPK, AND MUTAGENESIS OF
HIS-73; ASP-75; HIS-76; SER-334 AND HIS-396.
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).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[11]
INTERACTION WITH WDR33.
PubMed=19217410; DOI=10.1016/j.molcel.2008.12.028;
Shi Y., Di Giammartino D.C., Taylor D., Sarkeshik A., Rice W.J.,
Yates J.R. III, Frank J., Manley J.L.;
"Molecular architecture of the human pre-mRNA 3' processing complex.";
Mol. Cell 33:365-376(2009).
[12]
IDENTIFICATION IN THE CPSF COMPLEX, AND INTERACTION WITH TUT1.
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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-681, AND 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).
[14]
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).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-681, 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).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-459 IN COMPLEX WITH ZINC
IONS, FUNCTION, MUTAGENESIS OF 75-ASP-HIS-76, COFACTOR, AND CATALYTIC
ACTIVITY.
PubMed=17128255; DOI=10.1038/nature05363;
Mandel C.R., Kaneko S., Zhang H., Gebauer D., Vethantham V.,
Manley J.L., Tong L.;
"Polyadenylation factor CPSF-73 is the pre-mRNA 3'-end-processing
endonuclease.";
Nature 444:953-956(2006).
[19]
VARIANT [LARGE SCALE ANALYSIS] ASN-578.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Component of the cleavage and polyadenylation
specificity factor (CPSF) complex that play a key role in pre-mRNA
3'-end formation, recognizing the AAUAAA signal sequence and
interacting with poly(A) polymerase and other factors to bring
about cleavage and poly(A) addition. Has endonuclease activity,
and functions as mRNA 3'-end-processing endonuclease. Also
involved in the histone 3'-end pre-mRNA processing. U7 snRNP-
dependent protein that induces both the 3'-endoribonucleolytic
cleavage of histone pre-mRNAs and acts as a 5' to 3' exonuclease
for degrading the subsequent downstream cleavage product (DCP) of
mature histone mRNAs. Cleavage occurs after the 5'-ACCCA-3'
sequence in the histone pre-mRNA leaving a 3'hydroxyl group on the
upstream fragment containing the stem loop (SL) and 5' phosphate
on the downstream cleavage product (DCP) starting with CU
nucleotides. The U7-dependent 5' to 3' exonuclease activity is
processive and degrades the DCP RNA substrate even after complete
removal of the U7-binding site. Binds to the downstream cleavage
product (DCP) of histone pre-mRNAs and the cleaved DCP RNA
substrate in a U7 snRNP dependent manner.
{ECO:0000269|PubMed:14749727, ECO:0000269|PubMed:15037765,
ECO:0000269|PubMed:17128255, ECO:0000269|PubMed:18688255}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:17128255};
Note=Binds 2 Zn(2+) ions per subunit.
{ECO:0000269|PubMed:17128255};
-!- SUBUNIT: Component of the cleavage and polyadenylation specificity
factor (CPSF) complex, composed of CPSF1, CPSF2, CPSF3, CPSF4 and
FIP1L1. Interacts with CPSF2, CSTF2 and SYMPK. Interacts with
TUT1; the interaction is direct and mediates the recruitment of
the CPSF complex on the 3'UTR of pre-mRNAs. Interacts with WDR33.
Interacts with ZC3H3 (By similarity).
{ECO:0000250|UniProtKB:Q9QXK7, ECO:0000269|PubMed:14749727,
ECO:0000269|PubMed:17128255, ECO:0000269|PubMed:18688255,
ECO:0000269|PubMed:19217410, ECO:0000269|PubMed:21102410}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15037765}.
-!- PTM: Sumoylated on Lys-462, Lys-465 and Lys-545, preferentially by
SUMO3. {ECO:0000269|PubMed:17923699}.
-!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
RNA-metabolizing metallo-beta-lactamase-like family. CPSF3
subfamily. {ECO:0000305}.
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EMBL; AF171877; AAF00224.1; -; mRNA.
EMBL; AC080162; AAY14858.1; -; Genomic_DNA.
EMBL; CH471053; EAX00989.1; -; Genomic_DNA.
EMBL; BC011654; AAH11654.1; -; mRNA.
EMBL; BC020211; AAH20211.1; -; mRNA.
EMBL; AF017269; AAB70268.1; -; mRNA.
CCDS; CCDS1664.1; -.
RefSeq; NP_057291.1; NM_016207.3.
UniGene; Hs.515972; -.
PDB; 2I7T; X-ray; 2.10 A; A=1-459.
PDB; 2I7V; X-ray; 2.10 A; A=1-459.
PDBsum; 2I7T; -.
PDBsum; 2I7V; -.
ProteinModelPortal; Q9UKF6; -.
SMR; Q9UKF6; -.
BioGrid; 119680; 47.
CORUM; Q9UKF6; -.
DIP; DIP-42501N; -.
IntAct; Q9UKF6; 36.
MINT; MINT-1742891; -.
STRING; 9606.ENSP00000238112; -.
iPTMnet; Q9UKF6; -.
PhosphoSitePlus; Q9UKF6; -.
BioMuta; CPSF3; -.
DMDM; 18203503; -.
EPD; Q9UKF6; -.
MaxQB; Q9UKF6; -.
PaxDb; Q9UKF6; -.
PeptideAtlas; Q9UKF6; -.
PRIDE; Q9UKF6; -.
DNASU; 51692; -.
Ensembl; ENST00000238112; ENSP00000238112; ENSG00000119203.
GeneID; 51692; -.
KEGG; hsa:51692; -.
UCSC; uc002qzo.3; human.
CTD; 51692; -.
EuPathDB; HostDB:ENSG00000119203.13; -.
GeneCards; CPSF3; -.
HGNC; HGNC:2326; CPSF3.
HPA; HPA034657; -.
MIM; 606029; gene.
neXtProt; NX_Q9UKF6; -.
OpenTargets; ENSG00000119203; -.
PharmGKB; PA26843; -.
eggNOG; KOG1137; Eukaryota.
eggNOG; COG1236; LUCA.
GeneTree; ENSGT00890000139395; -.
HOGENOM; HOG000203394; -.
HOVERGEN; HBG051107; -.
InParanoid; Q9UKF6; -.
KO; K14403; -.
OMA; QMLYTEA; -.
OrthoDB; EOG091G03UN; -.
PhylomeDB; Q9UKF6; -.
TreeFam; TF105643; -.
Reactome; R-HSA-109688; Cleavage of Growing Transcript in the Termination Region.
Reactome; R-HSA-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
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; CPSF3; human.
EvolutionaryTrace; Q9UKF6; -.
GeneWiki; CPSF3; -.
GenomeRNAi; 51692; -.
PRO; PR:Q9UKF6; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000119203; -.
CleanEx; HS_CPSF3; -.
ExpressionAtlas; Q9UKF6; baseline and differential.
Genevisible; Q9UKF6; HS.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IEA:UniProtKB-KW.
GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0008409; F:5'-3' exonuclease activity; ISS:UniProtKB.
GO; GO:0004521; F:endoribonuclease activity; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
GO; GO:0031124; P:mRNA 3'-end processing; TAS:Reactome.
GO; GO:0006398; P:mRNA 3'-end processing by stem-loop binding and cleavage; IDA:UniProtKB.
GO; GO:0006379; P:mRNA cleavage; TAS:ProtInc.
GO; GO:0006406; P:mRNA export from nucleus; TAS:Reactome.
GO; GO:0006378; P:mRNA polyadenylation; TAS:ProtInc.
GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
GO; GO:0006369; P:termination of RNA polymerase II transcription; TAS:Reactome.
Gene3D; 3.60.15.10; -; 2.
InterPro; IPR022712; Beta_Casp.
InterPro; IPR021718; CPSF73-100_C.
InterPro; IPR001279; Metallo-B-lactamas.
InterPro; IPR036866; Metallo-hydrolase/OxRdtase.
InterPro; IPR011108; RMMBL.
Pfam; PF10996; Beta-Casp; 1.
Pfam; PF11718; CPSF73-100_C; 1.
Pfam; PF00753; Lactamase_B; 1.
Pfam; PF07521; RMMBL; 1.
SMART; SM01027; Beta-Casp; 1.
SMART; SM01098; CPSF73-100_C; 1.
SMART; SM00849; Lactamase_B; 1.
SUPFAM; SSF56281; SSF56281; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Endonuclease; Hydrolase;
Isopeptide bond; Metal-binding; mRNA processing; Nuclease; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Ribonucleoprotein;
RNA-binding; Ubl conjugation; Zinc.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895}.
CHAIN 2 684 Cleavage and polyadenylation specificity
factor subunit 3.
/FTId=PRO_0000074400.
ACT_SITE 396 396 Proton donor. {ECO:0000255}.
METAL 71 71 Zinc 1. {ECO:0000244|PDB:2I7T,
ECO:0000244|PDB:2I7V,
ECO:0000269|PubMed:17128255}.
METAL 73 73 Zinc 1. {ECO:0000244|PDB:2I7T,
ECO:0000244|PDB:2I7V,
ECO:0000269|PubMed:17128255}.
METAL 75 75 Zinc 2. {ECO:0000244|PDB:2I7T,
ECO:0000244|PDB:2I7V,
ECO:0000269|PubMed:17128255}.
METAL 76 76 Zinc 2. {ECO:0000244|PDB:2I7T,
ECO:0000244|PDB:2I7V,
ECO:0000269|PubMed:17128255}.
METAL 158 158 Zinc 1. {ECO:0000244|PDB:2I7T,
ECO:0000244|PDB:2I7V,
ECO:0000269|PubMed:17128255}.
METAL 179 179 Zinc 1. {ECO:0000244|PDB:2I7T,
ECO:0000244|PDB:2I7V,
ECO:0000269|PubMed:17128255}.
METAL 179 179 Zinc 2. {ECO:0000244|PDB:2I7T,
ECO:0000244|PDB:2I7V,
ECO:0000269|PubMed:17128255}.
METAL 418 418 Zinc 2. {ECO:0000244|PDB:2I7T,
ECO:0000244|PDB:2I7V,
ECO:0000269|PubMed:17128255}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895}.
MOD_RES 659 659 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QXK7}.
MOD_RES 681 681 Phosphothreonine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
CROSSLNK 462 462 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:17923699}.
CROSSLNK 465 465 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:17923699}.
CROSSLNK 545 545 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:17923699}.
VARIANT 142 142 E -> G (in dbSNP:rs17850770).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_037646.
VARIANT 578 578 D -> N (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035873.
MUTAGEN 73 73 H->A: Inhibits histone 3'-end processing.
{ECO:0000269|PubMed:18688255}.
MUTAGEN 75 76 DH->KA: Loss of histone 3'-end
processing.
{ECO:0000269|PubMed:17128255}.
MUTAGEN 75 75 D->A: Inhibits histone 3'-end processing.
{ECO:0000269|PubMed:18688255}.
MUTAGEN 76 76 H->A: Inhibits histone 3'-end processing.
{ECO:0000269|PubMed:18688255}.
MUTAGEN 334 334 S->A: Does not inhibit histone 3'-end
processing.
{ECO:0000269|PubMed:18688255}.
MUTAGEN 396 396 H->A: Inhibits histone 3'-end processing.
{ECO:0000269|PubMed:18688255}.
MUTAGEN 462 462 K->R: Reduced sumoylation; when
associated with R-465 and R-545.
{ECO:0000269|PubMed:17923699}.
MUTAGEN 465 465 K->R: Reduced sumoylation; when
associated with R-462 and R-545.
{ECO:0000269|PubMed:17923699}.
MUTAGEN 545 545 K->R: Reduced sumoylation; when
associated with R-462 and R-465.
{ECO:0000269|PubMed:17923699}.
STRAND 10 25 {ECO:0000244|PDB:2I7T}.
STRAND 27 32 {ECO:0000244|PDB:2I7T}.
STRAND 35 39 {ECO:0000244|PDB:2I7T}.
HELIX 49 52 {ECO:0000244|PDB:2I7T}.
HELIX 56 58 {ECO:0000244|PDB:2I7T}.
HELIX 61 63 {ECO:0000244|PDB:2I7T}.
STRAND 66 68 {ECO:0000244|PDB:2I7T}.
HELIX 74 77 {ECO:0000244|PDB:2I7T}.
HELIX 80 86 {ECO:0000244|PDB:2I7T}.
STRAND 91 96 {ECO:0000244|PDB:2I7T}.
HELIX 97 110 {ECO:0000244|PDB:2I7T}.
HELIX 125 131 {ECO:0000244|PDB:2I7T}.
HELIX 132 134 {ECO:0000244|PDB:2I7T}.
STRAND 135 138 {ECO:0000244|PDB:2I7T}.
STRAND 144 146 {ECO:0000244|PDB:2I7T}.
STRAND 149 155 {ECO:0000244|PDB:2I7T}.
STRAND 163 169 {ECO:0000244|PDB:2I7T}.
STRAND 172 176 {ECO:0000244|PDB:2I7T}.
STRAND 186 188 {ECO:0000244|PDB:2I7V}.
STRAND 199 204 {ECO:0000244|PDB:2I7T}.
TURN 206 209 {ECO:0000244|PDB:2I7T}.
HELIX 215 231 {ECO:0000244|PDB:2I7T}.
STRAND 235 239 {ECO:0000244|PDB:2I7T}.
STRAND 242 245 {ECO:0000244|PDB:2I7T}.
HELIX 246 259 {ECO:0000244|PDB:2I7T}.
HELIX 261 263 {ECO:0000244|PDB:2I7T}.
STRAND 268 271 {ECO:0000244|PDB:2I7T}.
HELIX 275 284 {ECO:0000244|PDB:2I7V}.
TURN 285 287 {ECO:0000244|PDB:2I7V}.
STRAND 307 310 {ECO:0000244|PDB:2I7T}.
HELIX 314 316 {ECO:0000244|PDB:2I7V}.
STRAND 321 328 {ECO:0000244|PDB:2I7T}.
HELIX 335 344 {ECO:0000244|PDB:2I7T}.
STRAND 351 354 {ECO:0000244|PDB:2I7T}.
HELIX 363 367 {ECO:0000244|PDB:2I7T}.
STRAND 372 375 {ECO:0000244|PDB:2I7T}.
STRAND 381 383 {ECO:0000244|PDB:2I7T}.
STRAND 386 390 {ECO:0000244|PDB:2I7T}.
HELIX 399 409 {ECO:0000244|PDB:2I7T}.
STRAND 412 419 {ECO:0000244|PDB:2I7T}.
HELIX 421 435 {ECO:0000244|PDB:2I7T}.
STRAND 444 446 {ECO:0000244|PDB:2I7T}.
STRAND 454 458 {ECO:0000244|PDB:2I7T}.
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


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