BOP1_MOUSE
ID BOP1_MOUSE Reviewed; 732 AA.
AC P97452; Q3TK87; Q6ZQI9; Q91X31;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 170.
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; Synonyms=Kiaa0124;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=SWR/J;
RX PubMed=9872334; DOI=10.1038/sj.onc.1202260;
RA Pestov D.G., Grzeszkiewicz T.M., Lau L.F.;
RT "Isolation of growth suppressors from a cDNA expression library.";
RL Oncogene 17:3187-3197(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Salivary gland;
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 [GENOMIC DNA] OF 1-89.
RC STRAIN=129/SvJ; TISSUE=Liver;
RA Zhang Y., Koushik S., Dai R., Mivechi N.F.;
RT "Sequence of the bidirectional promoter mouse heat shock transcription
RT factor I and Bop1.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=10891491; DOI=10.1128/mcb.20.15.5516-5528.2000;
RA Strezoska Z., Pestov D.G., Lau L.F.;
RT "Bop1 is a mouse WD40 repeat nucleolar protein involved in 28S and 5. 8S
RT rRNA processing and 60S ribosome biogenesis.";
RL Mol. Cell. Biol. 20:5516-5528(2000).
RN [7]
RP FUNCTION.
RX PubMed=11390653; DOI=10.1128/mcb.21.13.4246-4255.2001;
RA Pestov D.G., Strezoska Z., Lau L.F.;
RT "Evidence of p53-dependent cross-talk between ribosome biogenesis and the
RT cell cycle: effects of nucleolar protein Bop1 on G(1)/S transition.";
RL Mol. Cell. Biol. 21:4246-4255(2001).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12048210; DOI=10.1074/jbc.m204381200;
RA Strezoska Z., Pestov D.G., Lau L.F.;
RT "Functional inactivation of the mouse nucleolar protein Bop1 inhibits
RT multiple steps in pre-rRNA processing and blocks cell cycle progression.";
RL J. Biol. Chem. 277:29617-29625(2002).
RN [9]
RP INTERACTION WITH PES1.
RX PubMed=15225545; DOI=10.1016/j.molcel.2004.05.020;
RA Lapik Y.R., Fernandes C.J., Lau L.F., Pestov D.G.;
RT "Physical and functional interaction between Pes1 and Bop1 in mammalian
RT ribosome biogenesis.";
RL Mol. Cell 15:17-29(2004).
RN [10]
RP INTERACTION WITH PES1 AND WDR12, AND SUBCELLULAR LOCATION.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112 AND SER-113, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112 AND SER-113, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:10891491, ECO:0000269|PubMed:11390653,
CC ECO:0000269|PubMed:12048210}.
CC -!- SUBUNIT: Component of the PeBoW complex, composed of BOP1, PES1 and
CC WDR12 (PubMed:15225545, ECO:0000269|PubMed:17353269). The complex is
CC held together by BOP1, which interacts with PES1 via its N-terminal
CC domain and with WDR12 via a high-affinity interaction between the
CC seven-bladed beta-propeller domains of the 2 proteins. The NOP7 complex
CC associates with the 66S pre-ribosome. The PeBoW complex associates with
CC DDX27, BOP1 interacts directly with DDX27 (By similarity).
CC {ECO:0000255|HAMAP-Rule:MF_03027, ECO:0000269|PubMed:15225545,
CC ECO:0000269|PubMed:17353269}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus, nucleoplasm.
CC -!- TISSUE SPECIFICITY: Expressed in brain, gut, heart, kidney, liver,
CC lung, muscle, ovary, skin, spleen and testis.
CC -!- INDUCTION: Expression in quiescent fibroblasts is induced by serum
CC stimulation. {ECO:0000269|PubMed:10891491}.
CC -!- SIMILARITY: Belongs to the WD repeat BOP1/ERB1 family.
CC {ECO:0000255|HAMAP-Rule:MF_03027}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC97868.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U77415; AAB19223.1; -; mRNA.
DR EMBL; AK129058; BAC97868.1; ALT_INIT; mRNA.
DR EMBL; AK079627; BAC37708.1; -; mRNA.
DR EMBL; AK167110; BAE39258.1; -; mRNA.
DR EMBL; BC012693; AAH12693.1; -; mRNA.
DR EMBL; AF061503; AAC80429.1; -; Genomic_DNA.
DR CCDS; CCDS27570.1; -.
DR RefSeq; NP_038509.1; NM_013481.1.
DR AlphaFoldDB; P97452; -.
DR SMR; P97452; -.
DR BioGRID; 198380; 5.
DR CORUM; P97452; -.
DR IntAct; P97452; 1.
DR MINT; P97452; -.
DR STRING; 10090.ENSMUSP00000023217; -.
DR iPTMnet; P97452; -.
DR PhosphoSitePlus; P97452; -.
DR SwissPalm; P97452; -.
DR EPD; P97452; -.
DR jPOST; P97452; -.
DR MaxQB; P97452; -.
DR PaxDb; P97452; -.
DR PeptideAtlas; P97452; -.
DR PRIDE; P97452; -.
DR ProteomicsDB; 273759; -.
DR Antibodypedia; 59721; 152 antibodies from 22 providers.
DR DNASU; 12181; -.
DR Ensembl; ENSMUST00000023217; ENSMUSP00000023217; ENSMUSG00000022557.
DR GeneID; 12181; -.
DR KEGG; mmu:12181; -.
DR UCSC; uc007wkf.1; mouse.
DR CTD; 23246; -.
DR MGI; MGI:1334460; Bop1.
DR VEuPathDB; HostDB:ENSMUSG00000022557; -.
DR eggNOG; KOG0650; Eukaryota.
DR GeneTree; ENSGT00390000018422; -.
DR HOGENOM; CLU_011390_1_0_1; -.
DR InParanoid; P97452; -.
DR OMA; MRPAKGE; -.
DR OrthoDB; 759498at2759; -.
DR PhylomeDB; P97452; -.
DR TreeFam; TF300437; -.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 12181; 26 hits in 76 CRISPR screens.
DR ChiTaRS; Bop1; mouse.
DR PRO; PR:P97452; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P97452; protein.
DR Bgee; ENSMUSG00000022557; Expressed in otic placode and 275 other tissues.
DR Genevisible; P97452; MM.
DR GO; GO:0005694; C:chromosome; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0070545; C:PeBoW complex; ISS:UniProtKB.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IBA:GO_Central.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:MGI.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IDA:MGI.
DR GO; GO:0008283; P:cell population proliferation; IMP:UniProtKB.
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); IMP:UniProtKB.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); ISS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; ISO:MGI.
DR GO; GO:0000027; P:ribosomal large subunit assembly; ISO:MGI.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IMP:MGI.
DR GO; GO:0006364; P:rRNA processing; IMP:MGI.
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; 4.
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; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Ribosome biogenesis;
KW rRNA processing; WD repeat.
FT CHAIN 1..732
FT /note="Ribosome biogenesis protein BOP1"
FT /id="PRO_0000050886"
FT REPEAT 397..436
FT /note="WD 1"
FT REPEAT 438..478
FT /note="WD 2"
FT REPEAT 518..560
FT /note="WD 3"
FT REPEAT 563..601
FT /note="WD 4"
FT REPEAT 604..643
FT /note="WD 5"
FT REPEAT 647..686
FT /note="WD 6"
FT REPEAT 702..732
FT /note="WD 7"
FT REGION 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..413
FT /note="Sufficient for nucleolar localization"
FT COMPBIAS 34..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 108
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q14137"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT CONFLICT 56
FT /note="L -> S (in Ref. 2; BAC97868 and 4; AAH12693)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="P -> L (in Ref. 2; BAC97868)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 732 AA; 82546 MW; 48939C86071A84A9 CRC64;
MAGACGKPHM SPASLPGKRR LEPDQELQIQ EPPLLSDPDS SLSDSEESVF SGLEDLGSDS
SEEDTEGVAG SSGDEDNHRA EETSEELAQA APLCSRTEEA GALAQDEYEE DSSDEEDIRN
TVGNVPLAWY DEFPHVGYDL DGKRIYKPLR TRDELDQFLD KMDDPDFWRT VQDKMTGRDL
RLTDEQVALV HRLQRGQFGD SGFNPYEPAV DFFSGDIMIH PVTNRPADKR SFIPSLVEKE
KVSRMVHAIK MGWIKPRRPH DPTPSFYDLW AQEDPNAVLG RHKMHVPAPK LALPGHAESY
NPPPEYLPTE EERSAWMQQE PVERKLNFLP QKFPSLRTVP AYSRFIQERF ERCLDLYLCP
RQRKMRVNVD PEDLIPKLPR PRDLQPFPVC QALVYRGHSD LVRCLSVSPG GQWLASGSDD
GTLKLWEVAT ARCMKTVHVG GVVRSIAWNP NPTICLVAAA MDDAVLLLNP ALGDRLLVGS
TDQLLEAFTP PEEPALQPAR WLEVSEEEHQ RGLRLRICHS KPVTQVTWHG RGDYLAVVLS
SQEHTQVLLH QVSRRRSQSP FRRSHGQVQC VAFHPSRPFL LVASQRSIRI YHLLRQELTK
KLMPNCKWVS SMAVHPAGDN IICGSYDSKL VWFDLDLSTK PYKVLRHHKK ALRAVAFHPR
YPLFASGSDD GSVIVCHGMV YNDLLQNPLL VPVKVLKGHT LTRDLGVLDV AFHPTQPWVF
SSGADGTIRL FS
