BOP1_HUMAN
ID BOP1_HUMAN Reviewed; 746 AA.
AC Q14137; Q969Z6; Q96IS8; Q96Q25; Q9BSA7; Q9BVM0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=Ribosome biogenesis protein BOP1 {ECO:0000255|HAMAP-Rule:MF_03027};
DE AltName: Full=Block of proliferation 1 protein {ECO:0000255|HAMAP-Rule:MF_03027};
GN Name=BOP1 {ECO:0000255|HAMAP-Rule:MF_03027}; Synonyms=KIAA0124;
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 2).
RX PubMed=11237751; DOI=10.1006/bbrc.2001.4377;
RA Nakatsura T., Senju S., Yamada K., Jotsuka T., Ogawa M., Nishimura Y.;
RT "Gene cloning of immunogenic antigens overexpressed in pancreatic cancer.";
RL Biochem. Biophys. Res. Commun. 281:936-944(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Eye, Lymph, Muscle, and Pancreas;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 65-746 (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=8590280; DOI=10.1093/dnares/2.4.167;
RA Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. IV. The
RT coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 2:167-174(1995).
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 PES1 AND WDR12, AND INDUCTION.
RX PubMed=16043514; DOI=10.1083/jcb.200501141;
RA Hoelzel M., Rohrmoser M., Schlee M., Grimm T., Harasim T., Malamoussi A.,
RA Gruber-Eber A., Kremmer E., Hiddemann W., Bornkamm G.W., Eick D.;
RT "Mammalian WDR12 is a novel member of the Pes1-Bop1 complex and is required
RT for ribosome biogenesis and cell proliferation.";
RL J. Cell Biol. 170:367-378(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-106, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [9]
RP INTERACTION WITH PES1 AND WDR12.
RX PubMed=16738141; DOI=10.1093/nar/gkl378;
RA Grimm T., Hoelzel M., Rohrmoser M., Harasim T., Malamoussi A.,
RA Gruber-Eber A., Kremmer E., Eick D.;
RT "Dominant-negative Pes1 mutants inhibit ribosomal RNA processing and cell
RT proliferation via incorporation into the PeBoW-complex.";
RL Nucleic Acids Res. 34:3030-3043(2006).
RN [10]
RP FUNCTION, AND INTERACTION WITH PES1 AND WDR12.
RX PubMed=17353269; DOI=10.1128/mcb.00172-07;
RA Rohrmoser M., Hoelzel M., Grimm T., Malamoussi A., Harasim T., Orban M.,
RA Pfisterer I., Gruber-Eber A., Kremmer E., Eick D.;
RT "Interdependence of Pes1, Bop1, and WDR12 controls nucleolar localization
RT and assembly of the PeBoW complex required for maturation of the 60S
RT ribosomal subunit.";
RL Mol. Cell. Biol. 27:3682-3694(2007).
RN [11]
RP INTERACTION WITH PES1 AND WDR12.
RX PubMed=17189298; DOI=10.1093/nar/gkl1058;
RA Hoelzel M., Grimm T., Rohrmoser M., Malamoussi A., Harasim T.,
RA Gruber-Eber A., Kremmer E., Eick D.;
RT "The BRCT domain of mammalian Pes1 is crucial for nucleolar localization
RT and rRNA processing.";
RL Nucleic Acids Res. 35:789-800(2007).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-106; SER-126 AND SER-127, AND
RP IDENTIFICATION BY 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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126 AND SER-127, AND
RP IDENTIFICATION BY 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126 AND SER-127, AND
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126 AND SER-127, 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 [20]
RP FUNCTION.
RX PubMed=24120868; DOI=10.1016/j.celrep.2013.08.049;
RA Sloan K.E., Bohnsack M.T., Watkins N.J.;
RT "The 5S RNP couples p53 homeostasis to ribosome biogenesis and nucleolar
RT stress.";
RL Cell Rep. 5:237-247(2013).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126 AND SER-127, 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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-122; SER-126 AND SER-127, AND
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 [23]
RP INTERACTION WITH DDX27.
RX PubMed=25825154; DOI=10.1016/j.yexcr.2015.03.017;
RA Kellner M., Rohrmoser M., Forne I., Voss K., Burger K., Muehl B.,
RA Gruber-Eber A., Kremmer E., Imhof A., Eick D.;
RT "DEAD-box helicase DDX27 regulates 3' end formation of ribosomal 47S RNA
RT and stably associates with the PeBoW-complex.";
RL Exp. Cell Res. 334:146-159(2015).
CC -!- FUNCTION: Component of the PeBoW complex, which is required for
CC maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S
CC ribosome. {ECO:0000255|HAMAP-Rule:MF_03027,
CC ECO:0000269|PubMed:17353269, ECO:0000269|PubMed:24120868}.
CC -!- SUBUNIT: Component of the PeBoW complex, composed of BOP1, PES1 and
CC WDR12 (PubMed:16043514, PubMed:16738141, PubMed:17189298,
CC PubMed:17353269). The complex is held together by BOP1, which interacts
CC with PES1 via its N-terminal domain and with WDR12 via a high-affinity
CC interaction between the seven-bladed beta-propeller domains of the 2
CC proteins. The NOP7 complex associates with the 66S pre-ribosome (By
CC similarity). The PeBoW complex associates with DDX27, BOP1 interacts
CC directly with DDX27 (PubMed:25825154). {ECO:0000255|HAMAP-
CC Rule:MF_03027, ECO:0000269|PubMed:16043514,
CC ECO:0000269|PubMed:16738141, ECO:0000269|PubMed:17189298,
CC ECO:0000269|PubMed:17353269, ECO:0000269|PubMed:25825154}.
CC -!- INTERACTION:
CC Q14137; O00541: PES1; NbExp=4; IntAct=EBI-1050828, EBI-1053271;
CC Q14137; Q9GZL7: WDR12; NbExp=3; IntAct=EBI-1050828, EBI-2490660;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-
CC Rule:MF_03027, ECO:0000269|PubMed:12429849}. Nucleus, nucleoplasm
CC {ECO:0000255|HAMAP-Rule:MF_03027, ECO:0000269|PubMed:12429849}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q14137-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14137-2; Sequence=VSP_056391;
CC -!- INDUCTION: By MYC. {ECO:0000269|PubMed:16043514}.
CC -!- SIMILARITY: Belongs to the WD repeat BOP1/ERB1 family.
CC {ECO:0000255|HAMAP-Rule:MF_03027}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/BOP1ID44348ch8q22.html";
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DR EMBL; AB060694; BAB70666.1; -; mRNA.
DR EMBL; AC145291; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC231662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001086; AAH01086.2; -; mRNA.
DR EMBL; BC005160; AAH05160.2; -; mRNA.
DR EMBL; BC007274; AAH07274.1; -; mRNA.
DR EMBL; BC013787; AAH13787.1; -; mRNA.
DR EMBL; BC013980; AAH13980.1; -; mRNA.
DR EMBL; BC017674; AAH17674.1; -; mRNA.
DR EMBL; D50914; BAA09473.1; -; mRNA.
DR CCDS; CCDS6418.2; -. [Q14137-1]
DR RefSeq; NP_056016.1; NM_015201.4. [Q14137-1]
DR AlphaFoldDB; Q14137; -.
DR SMR; Q14137; -.
DR BioGRID; 116850; 151.
DR CORUM; Q14137; -.
DR IntAct; Q14137; 44.
DR MINT; Q14137; -.
DR STRING; 9606.ENSP00000455106; -.
DR GlyGen; Q14137; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q14137; -.
DR PhosphoSitePlus; Q14137; -.
DR SwissPalm; Q14137; -.
DR BioMuta; BOP1; -.
DR DMDM; 23830903; -.
DR SWISS-2DPAGE; Q14137; -.
DR EPD; Q14137; -.
DR jPOST; Q14137; -.
DR MassIVE; Q14137; -.
DR MaxQB; Q14137; -.
DR PaxDb; Q14137; -.
DR PeptideAtlas; Q14137; -.
DR PRIDE; Q14137; -.
DR ProteomicsDB; 59839; -. [Q14137-1]
DR ProteomicsDB; 77815; -.
DR Antibodypedia; 59721; 152 antibodies from 22 providers.
DR DNASU; 23246; -.
DR Ensembl; ENST00000569669.6; ENSP00000455106.1; ENSG00000261236.8. [Q14137-1]
DR Ensembl; ENST00000642409.2; ENSP00000495401.1; ENSG00000285301.2. [Q14137-1]
DR GeneID; 23246; -.
DR KEGG; hsa:23246; -.
DR MANE-Select; ENST00000569669.6; ENSP00000455106.1; NM_015201.5; NP_056016.1.
DR UCSC; uc033ccj.2; human. [Q14137-1]
DR CTD; 23246; -.
DR DisGeNET; 23246; -.
DR GeneCards; BOP1; -.
DR HGNC; HGNC:15519; BOP1.
DR HPA; ENSG00000261236; Tissue enhanced (skeletal).
DR MIM; 610596; gene.
DR neXtProt; NX_Q14137; -.
DR OpenTargets; ENSG00000261236; -.
DR PharmGKB; PA25398; -.
DR VEuPathDB; HostDB:ENSG00000261236; -.
DR eggNOG; KOG0650; Eukaryota.
DR GeneTree; ENSGT00390000018422; -.
DR HOGENOM; CLU_011390_0_1_1; -.
DR InParanoid; Q14137; -.
DR OMA; MRPAKGE; -.
DR OrthoDB; 759498at2759; -.
DR PhylomeDB; Q14137; -.
DR TreeFam; TF300437; -.
DR PathwayCommons; Q14137; -.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR SignaLink; Q14137; -.
DR BioGRID-ORCS; 23246; 660 hits in 1083 CRISPR screens.
DR ChiTaRS; BOP1; human.
DR GeneWiki; BOP1; -.
DR GenomeRNAi; 23246; -.
DR Pharos; Q14137; Tbio.
DR PRO; PR:Q14137; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q14137; protein.
DR Bgee; ENSG00000261236; Expressed in right lobe of thyroid gland and 95 other tissues.
DR ExpressionAtlas; Q14137; baseline and differential.
DR Genevisible; Q14137; HS.
DR GO; GO:0005694; C:chromosome; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0070545; C:PeBoW complex; IDA:UniProtKB.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IBA:GO_Central.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:MGI.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:0000448; P:cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:Ensembl.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:UniProtKB.
DR GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; IMP:UniProtKB.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IMP:UniProtKB.
DR GO; GO:0042254; P:ribosome biogenesis; NAS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR HAMAP; MF_03027; BOP1; 1.
DR InterPro; IPR028598; BOP1/Erb1.
DR InterPro; IPR012953; BOP1_N_dom.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR17605; PTHR17605; 1.
DR Pfam; PF08145; BOP1NT; 1.
DR Pfam; PF00400; WD40; 3.
DR SMART; SM01035; BOP1NT; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ribosome biogenesis; rRNA processing; WD repeat.
FT CHAIN 1..746
FT /note="Ribosome biogenesis protein BOP1"
FT /id="PRO_0000050885"
FT REPEAT 411..450
FT /note="WD 1"
FT REPEAT 452..492
FT /note="WD 2"
FT REPEAT 532..576
FT /note="WD 3"
FT REPEAT 577..615
FT /note="WD 4"
FT REPEAT 618..657
FT /note="WD 5"
FT REPEAT 661..700
FT /note="WD 6"
FT REPEAT 716..746
FT /note="WD 7"
FT REGION 1..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..427
FT /note="Sufficient for nucleolar localization"
FT /evidence="ECO:0000250"
FT COMPBIAS 14..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..86
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 106
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 122
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..112
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11237751"
FT /id="VSP_056391"
FT CONFLICT 577
FT /note="R -> H (in Ref. 4; BAA09473)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 746 AA; 83630 MW; 49A97BE21B0EB3DD CRC64;
MAGSRGAGRT AAPSVRPEKR RSEPELEPEP EPEPPLLCTS PLSHSTGSDS GVSDSEESVF
SGLEDSGSDS SEDDDEGDEE GEDGALDDEG HSGIKKTTEE QVQASTPCPR TEMASARIGD
EYAEDSSDEE DIRNTVGNVP LEWYDDFPHV GYDLDGRRIY KPLRTRDELD QFLDKMDDPD
YWRTVQDPMT GRDLRLTDEQ VALVRRLQSG QFGDVGFNPY EPAVDFFSGD VMIHPVTNRP
ADKRSFIPSL VEKEKVSRMV HAIKMGWIQP RRPRDPTPSF YDLWAQEDPN AVLGRHKMHV
PAPKLALPGH AESYNPPPEY LLSEEERLAW EQQEPGERKL SFLPRKFPSL RAVPAYGRFI
QERFERCLDL YLCPRQRKMR VNVDPEDLIP KLPRPRDLQP FPTCQALVYR GHSDLVRCLS
VSPGGQWLVS GSDDGSLRLW EVATARCVRT VPVGGVVKSV AWNPSPAVCL VAAAVEDSVL
LLNPALGDRL VAGSTDQLLS AFVPPEEPPL QPARWLEASE EERQVGLRLR ICHGKPVTQV
TWHGRGDYLA VVLATQGHTQ VLIHQLSRRR SQSPFRRSHG QVQRVAFHPA RPFLLVASQR
SVRLYHLLRQ ELTKKLMPNC KWVSSLAVHP AGDNVICGSY DSKLVWFDLD LSTKPYRMLR
HHKKALRAVA FHPRYPLFAS GSDDGSVIVC HGMVYNDLLQ NPLLVPVKVL KGHVLTRDLG
VLDVIFHPTQ PWVFSSGADG TVRLFT
