UTP20_HUMAN
ID UTP20_HUMAN Reviewed; 2785 AA.
AC O75691; Q9H3H4;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Small subunit processome component 20 homolog;
DE AltName: Full=Down-regulated in metastasis protein;
DE AltName: Full=Novel nucleolar protein 73;
DE Short=NNP73;
DE AltName: Full=Protein Key-1A6;
GN Name=UTP20; Synonyms=DRIM;
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], TISSUE SPECIFICITY, AND VARIANT GLN-1882.
RX PubMed=9673349;
RA Schwirzke M., Gnirke A., Bork P., Tarin D., Weidle U.H.;
RT "Differential gene expression in mammary carcinoma cell lines:
RT identification of DRIM, a new gene down-regulated in metastasis.";
RL Anticancer Res. 18:1409-1421(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1883-2785.
RA Ke Y., Hagiwara K., Zhao H., Ning T., Su X.L., Mcmenamin H., Lu G.R.,
RA Wang B., Harris C.C.;
RT "Key-1A6.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=11790298; DOI=10.1016/s0960-9822(01)00650-9;
RA Andersen J.S., Lyon C.E., Fox A.H., Leung A.K.L., Lam Y.W., Steen H.,
RA Mann M., Lamond A.I.;
RT "Directed proteomic analysis of the human nucleolus.";
RL Curr. Biol. 12:1-11(2002).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [6]
RP INTERACTION WITH PPP1R26.
RX PubMed=16053918; DOI=10.1016/j.bbrc.2005.06.179;
RA Yang L., Zhao J., Lu W., Li Y., Du X., Ning T., Lu G., Ke Y.;
RT "KIAA0649, a 1A6/DRIM-interacting protein with the oncogenic potential.";
RL Biochem. Biophys. Res. Commun. 334:884-890(2005).
RN [7]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF 2744-LYS--LYS-2746; LYS-2744;
RP LYS-2745; LYS-2746; 2748-LYS-LYS-2749; LYS-2748; LYS-2749; LYS-2751;
RP LYS-2753; 2757-LYS--LYS-2760; LYS-2757; LYS-2758 AND LYS-2760.
RX PubMed=16458307; DOI=10.1016/j.febslet.2006.01.064;
RA Liu J., Du X., Ke Y.;
RT "Mapping nucleolar localization sequences of 1A6/DRIM.";
RL FEBS Lett. 580:1405-1410(2006).
RN [8]
RP FUNCTION, AND INTERACTION WITH FBL.
RX PubMed=17498821; DOI=10.1016/j.bbamcr.2007.04.002;
RA Wang Y., Liu J., Zhao H., Lue W., Zhao J., Yang L., Li N., Du X., Ke Y.;
RT "Human 1A6/DRIM, the homolog of yeast Utp20, functions in the 18S rRNA
RT processing.";
RL Biochim. Biophys. Acta 1773:863-868(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-788 AND THR-1741, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1741, 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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1741, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2601, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1741 AND SER-2601, AND
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1741 AND SER-2637, AND
RP IDENTIFICATION BY 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 [17]
RP VARIANTS [LARGE SCALE ANALYSIS] ILE-1645 AND PHE-2452.
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: Involved in 18S pre-rRNA processing. Associates with U3
CC snoRNA. {ECO:0000269|PubMed:17498821}.
CC -!- SUBUNIT: Interacts with FBL and PPP1R26. {ECO:0000269|PubMed:16053918,
CC ECO:0000269|PubMed:17498821}.
CC -!- INTERACTION:
CC O75691; Q5T8A7: PPP1R26; NbExp=4; IntAct=EBI-356062, EBI-308500;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11790298,
CC ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:16458307}.
CC Note=Colocalizes with NCL in the nucleolus.
CC -!- TISSUE SPECIFICITY: Expressed in appendix, brain, colon, fetal liver,
CC heart, ovary, pancreas, placenta, prostate, skeletal muscle, small
CC intestine, spleen, testis and thymus. {ECO:0000269|PubMed:9673349}.
CC -!- SIMILARITY: Belongs to the UTP20 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG35208.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ006778; CAA07243.1; -; mRNA.
DR EMBL; AC063948; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC063951; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF072718; AAG35208.1; ALT_INIT; mRNA.
DR CCDS; CCDS9081.1; -.
DR RefSeq; NP_055318.2; NM_014503.2.
DR PDB; 7MQ8; EM; 3.60 A; SP=1-2785.
DR PDB; 7MQ9; EM; 3.87 A; SP=1-2785.
DR PDB; 7MQA; EM; 2.70 A; SP=1-2785.
DR PDBsum; 7MQ8; -.
DR PDBsum; 7MQ9; -.
DR PDBsum; 7MQA; -.
DR SMR; O75691; -.
DR BioGRID; 118152; 189.
DR IntAct; O75691; 24.
DR MINT; O75691; -.
DR STRING; 9606.ENSP00000261637; -.
DR CarbonylDB; O75691; -.
DR iPTMnet; O75691; -.
DR MetOSite; O75691; -.
DR PhosphoSitePlus; O75691; -.
DR SwissPalm; O75691; -.
DR BioMuta; UTP20; -.
DR SWISS-2DPAGE; O75691; -.
DR EPD; O75691; -.
DR jPOST; O75691; -.
DR MassIVE; O75691; -.
DR MaxQB; O75691; -.
DR PaxDb; O75691; -.
DR PeptideAtlas; O75691; -.
DR PRIDE; O75691; -.
DR ProteomicsDB; 50164; -.
DR Antibodypedia; 30370; 49 antibodies from 16 providers.
DR DNASU; 27340; -.
DR Ensembl; ENST00000261637.5; ENSP00000261637.4; ENSG00000120800.5.
DR GeneID; 27340; -.
DR KEGG; hsa:27340; -.
DR MANE-Select; ENST00000261637.5; ENSP00000261637.4; NM_014503.3; NP_055318.2.
DR UCSC; uc001tia.2; human.
DR CTD; 27340; -.
DR DisGeNET; 27340; -.
DR GeneCards; UTP20; -.
DR HGNC; HGNC:17897; UTP20.
DR HPA; ENSG00000120800; Low tissue specificity.
DR MIM; 612822; gene.
DR neXtProt; NX_O75691; -.
DR OpenTargets; ENSG00000120800; -.
DR PharmGKB; PA143485666; -.
DR VEuPathDB; HostDB:ENSG00000120800; -.
DR eggNOG; KOG1823; Eukaryota.
DR GeneTree; ENSGT00390000016813; -.
DR HOGENOM; CLU_000327_0_1_1; -.
DR InParanoid; O75691; -.
DR OMA; LAWIFKF; -.
DR OrthoDB; 674160at2759; -.
DR PhylomeDB; O75691; -.
DR TreeFam; TF105652; -.
DR PathwayCommons; O75691; -.
DR Reactome; R-HSA-6790901; rRNA modification in the nucleus and cytosol.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR SignaLink; O75691; -.
DR BioGRID-ORCS; 27340; 765 hits in 1084 CRISPR screens.
DR ChiTaRS; UTP20; human.
DR GeneWiki; UTP20; -.
DR GenomeRNAi; 27340; -.
DR Pharos; O75691; Tbio.
DR PRO; PR:O75691; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; O75691; protein.
DR Bgee; ENSG00000120800; Expressed in tendon of biceps brachii and 137 other tissues.
DR Genevisible; O75691; HS.
DR GO; GO:0030686; C:90S preribosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0030688; C:preribosome, small subunit precursor; ISS:UniProtKB.
DR GO; GO:0032040; C:small-subunit processome; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000480; P:endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); ISS:UniProtKB.
DR GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); ISS:UniProtKB.
DR GO; GO:0000472; P:endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0006364; P:rRNA processing; IMP:UniProtKB.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR011430; DRIM.
DR Pfam; PF07539; DRIM; 1.
DR SUPFAM; SSF48371; SSF48371; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; rRNA processing.
FT CHAIN 1..2785
FT /note="Small subunit processome component 20 homolog"
FT /id="PRO_0000080011"
FT REPEAT 165..202
FT /note="HEAT 1"
FT REPEAT 1841..1878
FT /note="HEAT 2"
FT REGION 880..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1720..1760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2688..2765
FT /evidence="ECO:0000255"
FT MOTIF 2744..2775
FT /note="Nuclear localization signal"
FT MOTIF 2744..2761
FT /note="Nucleolar localization signal"
FT COMPBIAS 880..896
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 788
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 1741
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 2601
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 2637
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 120
FT /note="M -> T (in dbSNP:rs2290723)"
FT /id="VAR_055135"
FT VARIANT 502
FT /note="S -> C (in dbSNP:rs4764643)"
FT /id="VAR_022162"
FT VARIANT 1645
FT /note="K -> I (in a breast cancer sample; somatic mutation;
FT dbSNP:rs140657361)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036274"
FT VARIANT 1882
FT /note="L -> Q (in dbSNP:rs10082778)"
FT /evidence="ECO:0000269|PubMed:9673349"
FT /id="VAR_055136"
FT VARIANT 2452
FT /note="I -> F (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036275"
FT VARIANT 2612
FT /note="E -> Q (in dbSNP:rs1061436)"
FT /id="VAR_022163"
FT MUTAGEN 2744..2746
FT /note="KKK->AAA: Inhibits nucleolar but not nuclear
FT localization."
FT /evidence="ECO:0000269|PubMed:16458307"
FT MUTAGEN 2744
FT /note="K->A: Does not decrease nucleolar localization."
FT /evidence="ECO:0000269|PubMed:16458307"
FT MUTAGEN 2745
FT /note="K->A: Does not decrease nucleolar localization."
FT /evidence="ECO:0000269|PubMed:16458307"
FT MUTAGEN 2746
FT /note="K->A: Decreases nucleolar localization."
FT /evidence="ECO:0000269|PubMed:16458307"
FT MUTAGEN 2748..2749
FT /note="KK->AA: Inhibits nucleolar but not nuclear
FT localization."
FT /evidence="ECO:0000269|PubMed:16458307"
FT MUTAGEN 2748
FT /note="K->A: Does not decrease nucleolar localization."
FT /evidence="ECO:0000269|PubMed:16458307"
FT MUTAGEN 2749
FT /note="K->A: Decreases nucleolar localization."
FT /evidence="ECO:0000269|PubMed:16458307"
FT MUTAGEN 2751
FT /note="K->A: Does not decrease nucleolar localization."
FT /evidence="ECO:0000269|PubMed:16458307"
FT MUTAGEN 2753
FT /note="K->A: Does not decrease nucleolar localization."
FT /evidence="ECO:0000269|PubMed:16458307"
FT MUTAGEN 2757..2760
FT /note="KKRK->AAAA: Inhibits nucleolar localization and
FT decreases nuclear localization."
FT /evidence="ECO:0000269|PubMed:16458307"
FT MUTAGEN 2757
FT /note="K->A: Does not decrease nucleolar localization."
FT /evidence="ECO:0000269|PubMed:16458307"
FT MUTAGEN 2758
FT /note="K->A: Does not decrease nucleolar localization."
FT /evidence="ECO:0000269|PubMed:16458307"
FT MUTAGEN 2760
FT /note="K->A: Does not decrease nucleolar localization."
FT /evidence="ECO:0000269|PubMed:16458307"
FT CONFLICT 1505
FT /note="A -> P (in Ref. 1; CAA07243)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2785 AA; 318385 MW; 0CE63611C8440E0D CRC64;
MKTKPVSHKT ENTYRFLTFA ERLGNVNIDI IHRIDRTASY EEEVETYFFE GLLKWRELNL
TEHFGKFYKE VIDKCQSFNQ LVYHQNEIVQ SLKTHLQVKN SFAYQPLLDL VVQLARDLQM
DFYPHFPEFF LTITSILETQ DTELLEWAFT SLSYLYKYLW RLMVKDMSSI YSMYSTLLAH
KKLHIRNFAA ESFTFLMRKV SDKNALFNLM FLDLDKHPEK VEGVGQLLFE MCKGVRNMFH
SCTGQAVKLI LRKLGPVTET ETQLPWMLIG ETLKNMVKST VSYISKEHFG TFFECLQESL
LDLHTKVTKT NCCESSEQIK RLLETYLILV KHGSGTKIPT PADVCKVLSQ TLQVASLSTS
CWETLLDVIS ALILGENVSL PETLIKETIE KIFESRFEKR LIFSFSEVMF AMKQFEQLFL
PSFLSYIVNC FLIDDAVVKD EALAILAKLI LNKAAPPTAG SMAIEKYPLV FSPQMVGFYI
KQKKTRSKGR NEQFPVLDHL LSIIKLPPNK DTTYLSQSWA ALVVLPHIRP LEKEKVIPLV
TGFIEALFMT VDKGSFGKGN LFVLCQAVNT LLSLEESSEL LHLVPVERVK NLVLTFPLEP
SVLLLTDLYY QRLALCGCKG PLSQEALMEL FPKLQANIST GVSKIRLLTI RILNHFDVQL
PESMEDDGLS ERQSVFAILR QAELVPATVN DYREKLLHLR KLRHDVVQTA VPDGPLQEVP
LRYLLGMLYI NFSALWDPVI ELISSHAHEM ENKQFWKVYY EHLEKAATHA EKELQNDMTD
EKSVGDESWE QTQEGDVGAL YHEQLALKTD CQERLDHTNF RFLLWRALTK FPERVEPRSR
ELSPLFLRFI NNEYYPADLQ VAPTQDLRRK GKGMVAEEIE EEPAAGDDEE LEEEAVPQDE
SSQKKKTRRA AAKQLIAHLQ VFSKFSNPRA LYLESKLYEL YLQLLLHQDQ MVQKITLDCI
MTYKHPHVLP YRENLQRLLE DRSFKEEIVH FSISEDNAVV KTAHRADLFP ILMRILYGRM
KNKTGSKTQG KSASGTRMAI VLRFLAGTQP EEIQIFLDLL FEPVRHFKNG ECHSAVIQAV
EDLDLSKVLP LGRQHGILNS LEIVLKNISH LISAYLPKIL QILLCMTATV SHILDQREKI
QLRFINPLKN LRRLGIKMVT DIFLDWESYQ FRTEEIDAVF HGAVWPQISR LGSESQYSPT
PLLKLISIWS RNARYFPLLA KQKPGHPECD ILTNVFAILS AKNLSDATAS IVMDIVDDLL
NLPDFEPTET VLNLLVTGCV YPGIAENIGE SITIGGRLIL PHVPAILQYL SKTTISAEKV
KKKKNRAQVS KELGILSKIS KFMKDKEQSS VLITLLLPFL HRGNIAEDTE VDILVTVQNL
LKHCVDPTSF LKPIAKLFSV IKNKLSRKLL CTVFETLSDF ESGLKYITDV VKLNAFDQRH
LDDINFDVRF ETFQTITSYI KEMQIVDVNY LIPVMHNCFY NLELGDMSLS DNASMCLMSI
IKKLAALNVT EKDYREIIHR SLLEKLRKGL KSQTESIQQD YTTILSCLIQ TFPNQLEFKD
LVQLTHYHDP EMDFFENMKH IQIHRRARAL KKLAKQLMEG KVVLSSKSLQ NYIMPYAMTP
IFDEKMLKHE NITTAATEII GAICKHLSWS AYMYYLKHFI HVLQTGQINQ KLGVSLLVIV
LEAFHFDHKT LEEQMGKIEN EENAIEAIEL PEPEAMELER VDEEEKEYTC KSLSDNGQPG
TPDPADSGGT SAKESECITK PVSFLPQNKE EIERTIKNIQ GTITGDILPR LHKCLASTTK
REEEHKLVKS KVVNDEEVVR VPLAFAMVKL MQSLPQEVME ANLPSILLKV CALLKNRAQE
IRDIARSTLA KIIEDLGVHF LLYVLKELQT TLVRGYQVHV LTFTVHMLLQ GLTNKLQVGD
LDSCLDIMIE IFNHELFGAV AEEKEVKQIL SKVMEARRSK SYDSYEILGK FVGKDQVTKL
ILPLKEILQN TTSLKLARKV HETLRRITVG LIVNQEMTAE SILLLSYGLI SENLPLLTEK
EKNPVAPAPD PRLPPQSCLL LPPTPVRGGQ KAVVSRKTNM HIFIESGLRL LHLSLKTSKI
KSSGECVLEM LDPFVSLLID CLGSMDVKVI TGALQCLIWV LRFPLPSIET KAEQLTKHLF
LLLKDYAKLG AARGQNFHLV VNCFKCVTIL VKKVKSYQIT EKQLQVLLAY AEEDIYDTSR
QATAFGLLKA ILSRKLLVPE IDEVMRKVSK LAVSAQSEPA RVQCRQVFLK YILDYPLGDK
LRPNLEFMLA QLNYEHETGR ESTLEMIAYL FDTFPQGLLH ENCGMFFIPL CLMTINDDSA
TCKKMASMTI KSLLGKISLE KKDWLFDMVT TWFGAKKRLN RQLAALICGL FVESEGVDFE
KRLGTVLPVI EKEIDPENFK DIMEETEEKA ADRLLFSFLT LITKLIKECN IIQFTKPAET
LSKIWSHVHS HLRHPHNWVW LTAAQIFGLL FASCQPEELI QKWNTKKTKK HLPEPVAIKF
LASDLDQKMK SISLASCHQL HSKFLDQSLG EQVVKNLLFA AKVLYLLELY CEDKQSKIKE
DLEEQEALED GVACADEKAE SDGEEKEEVK EELGRPATLL WLIQKLSRIA KLEAAYSPRN
PLKRTCIFKF LGAVAMDLGI DKVKPYLPMI IAPLFRELNS TYSEQDPLLK NLSQEIIELL
KKLVGLESFS LAFASVQKQA NEKRALRKKR KALEFVTNPD IAAKKKMKKH KNKSEAKKRK
IEFLRPGYKA KRQKSHSLKD LAMVE
