Full text data of BOP1
BOP1
(KIAA0124)
[Confidence: low (only semi-automatic identification from reviews)]
Ribosome biogenesis protein BOP1 (Block of proliferation 1 protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Ribosome biogenesis protein BOP1 (Block of proliferation 1 protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q14137
ID BOP1_HUMAN Reviewed; 746 AA.
AC Q14137; Q969Z6; Q96IS8; Q9BSA7; Q9BVM0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 10-OCT-2002, sequence version 2.
DT 22-JAN-2014, entry version 144.
DE RecName: Full=Ribosome biogenesis protein BOP1;
DE AltName: Full=Block of proliferation 1 protein;
GN Name=BOP1; Synonyms=KIAA0124;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 65-746.
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.
RT The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by
RT analysis of cDNA clones from human cell line KG-1.";
RL DNA Res. 2:167-174(1995).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
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 [4]
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.,
RA Malamoussi A., Gruber-Eber A., Kremmer E., Hiddemann W.,
RA Bornkamm G.W., Eick D.;
RT "Mammalian WDR12 is a novel member of the Pes1-Bop1 complex and is
RT required for ribosome biogenesis and cell proliferation.";
RL J. Cell Biol. 170:367-378(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-106, AND MASS
RP SPECTROMETRY.
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
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [6]
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
RT cell proliferation via incorporation into the PeBoW-complex.";
RL Nucleic Acids Res. 34:3030-3043(2006).
RN [7]
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.,
RA Orban M., Pfisterer I., Gruber-Eber A., Kremmer E., Eick D.;
RT "Interdependence of Pes1, Bop1, and WDR12 controls nucleolar
RT localization and assembly of the PeBoW complex required for maturation
RT of the 60S ribosomal subunit.";
RL Mol. Cell. Biol. 27:3682-3694(2007).
RN [8]
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
RT localization and rRNA processing.";
RL Nucleic Acids Res. 35:789-800(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-106, AND MASS
RP SPECTROMETRY.
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).
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.
CC -!- SUBUNIT: Component of the PeBoW complex, composed of BOP1, PES1
CC and WDR12. Within the PeBoW complex BOP1 interacts directly with
CC PES1 and WDR12. The PeBoW complex also associates with the 66S
CC pre-ribosome.
CC -!- INTERACTION:
CC O00541:PES1; NbExp=3; IntAct=EBI-1050828, EBI-1053271;
CC Q9GZL7:WDR12; NbExp=3; IntAct=EBI-1050828, EBI-2490660;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus, nucleoplasm.
CC -!- INDUCTION: By MYC.
CC -!- SIMILARITY: Belongs to the WD repeat BOP1/ERB1 family.
CC -!- SIMILARITY: Contains 7 WD repeats.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/BOP1ID44348ch8q22.html";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 RefSeq; NP_056016.1; NM_015201.3.
DR UniGene; Hs.645279; -.
DR ProteinModelPortal; Q14137; -.
DR SMR; Q14137; 410-745.
DR IntAct; Q14137; 8.
DR MINT; MINT-3029124; -.
DR STRING; 9606.ENSP00000304151; -.
DR PhosphoSite; Q14137; -.
DR DMDM; 23830903; -.
DR SWISS-2DPAGE; Q14137; -.
DR PaxDb; Q14137; -.
DR PeptideAtlas; Q14137; -.
DR PRIDE; Q14137; -.
DR DNASU; 23246; -.
DR Ensembl; ENST00000307404; ENSP00000304151; ENSG00000170727.
DR Ensembl; ENST00000569669; ENSP00000455106; ENSG00000261236.
DR GeneID; 23246; -.
DR KEGG; hsa:23246; -.
DR UCSC; uc003zbm.3; human.
DR CTD; 23246; -.
DR GeneCards; GC08M145486; -.
DR H-InvDB; HIX0168814; -.
DR HGNC; HGNC:15519; BOP1.
DR MIM; 610596; gene.
DR neXtProt; NX_Q14137; -.
DR PharmGKB; PA25398; -.
DR eggNOG; COG2319; -.
DR HOGENOM; HOG000029368; -.
DR HOVERGEN; HBG008113; -.
DR InParanoid; Q14137; -.
DR KO; K14824; -.
DR OMA; QIFHGKV; -.
DR PhylomeDB; Q14137; -.
DR SignaLink; Q14137; -.
DR GeneWiki; BOP1; -.
DR GenomeRNAi; 23246; -.
DR NextBio; 44934; -.
DR PRO; PR:Q14137; -.
DR ArrayExpress; Q14137; -.
DR Bgee; Q14137; -.
DR CleanEx; HS_BOP1; -.
DR Genevestigator; Q14137; -.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070545; C:PeBoW complex; IDA:UniProtKB.
DR GO; GO:0008283; P:cell proliferation; NAS:UniProtKB.
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 Gene3D; 2.130.10.10; -; 2.
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.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR017986; WD40_repeat_dom.
DR Pfam; PF08145; BOP1NT; 1.
DR Pfam; PF00400; WD40; 3.
DR SMART; SM01035; BOP1NT; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 2.
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 Complete proteome; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Ribosome biogenesis; rRNA processing; WD repeat.
FT CHAIN 1 746 Ribosome biogenesis protein BOP1.
FT /FTId=PRO_0000050885.
FT REPEAT 411 450 WD 1.
FT REPEAT 452 492 WD 2.
FT REPEAT 532 576 WD 3.
FT REPEAT 577 615 WD 4.
FT REPEAT 618 657 WD 5.
FT REPEAT 661 700 WD 6.
FT REPEAT 716 746 WD 7.
FT REGION 265 427 Sufficient for nucleolar localization (By
FT similarity).
FT MOD_RES 106 106 Phosphothreonine.
FT MOD_RES 126 126 Phosphoserine (By similarity).
FT MOD_RES 127 127 Phosphoserine (By similarity).
FT CONFLICT 577 577 R -> H (in Ref. 2; BAA09473).
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
//
ID BOP1_HUMAN Reviewed; 746 AA.
AC Q14137; Q969Z6; Q96IS8; Q9BSA7; Q9BVM0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 10-OCT-2002, sequence version 2.
DT 22-JAN-2014, entry version 144.
DE RecName: Full=Ribosome biogenesis protein BOP1;
DE AltName: Full=Block of proliferation 1 protein;
GN Name=BOP1; Synonyms=KIAA0124;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 65-746.
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.
RT The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by
RT analysis of cDNA clones from human cell line KG-1.";
RL DNA Res. 2:167-174(1995).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
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 [4]
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.,
RA Malamoussi A., Gruber-Eber A., Kremmer E., Hiddemann W.,
RA Bornkamm G.W., Eick D.;
RT "Mammalian WDR12 is a novel member of the Pes1-Bop1 complex and is
RT required for ribosome biogenesis and cell proliferation.";
RL J. Cell Biol. 170:367-378(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-106, AND MASS
RP SPECTROMETRY.
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
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [6]
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
RT cell proliferation via incorporation into the PeBoW-complex.";
RL Nucleic Acids Res. 34:3030-3043(2006).
RN [7]
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.,
RA Orban M., Pfisterer I., Gruber-Eber A., Kremmer E., Eick D.;
RT "Interdependence of Pes1, Bop1, and WDR12 controls nucleolar
RT localization and assembly of the PeBoW complex required for maturation
RT of the 60S ribosomal subunit.";
RL Mol. Cell. Biol. 27:3682-3694(2007).
RN [8]
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
RT localization and rRNA processing.";
RL Nucleic Acids Res. 35:789-800(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-106, AND MASS
RP SPECTROMETRY.
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).
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.
CC -!- SUBUNIT: Component of the PeBoW complex, composed of BOP1, PES1
CC and WDR12. Within the PeBoW complex BOP1 interacts directly with
CC PES1 and WDR12. The PeBoW complex also associates with the 66S
CC pre-ribosome.
CC -!- INTERACTION:
CC O00541:PES1; NbExp=3; IntAct=EBI-1050828, EBI-1053271;
CC Q9GZL7:WDR12; NbExp=3; IntAct=EBI-1050828, EBI-2490660;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus, nucleoplasm.
CC -!- INDUCTION: By MYC.
CC -!- SIMILARITY: Belongs to the WD repeat BOP1/ERB1 family.
CC -!- SIMILARITY: Contains 7 WD repeats.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/BOP1ID44348ch8q22.html";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 RefSeq; NP_056016.1; NM_015201.3.
DR UniGene; Hs.645279; -.
DR ProteinModelPortal; Q14137; -.
DR SMR; Q14137; 410-745.
DR IntAct; Q14137; 8.
DR MINT; MINT-3029124; -.
DR STRING; 9606.ENSP00000304151; -.
DR PhosphoSite; Q14137; -.
DR DMDM; 23830903; -.
DR SWISS-2DPAGE; Q14137; -.
DR PaxDb; Q14137; -.
DR PeptideAtlas; Q14137; -.
DR PRIDE; Q14137; -.
DR DNASU; 23246; -.
DR Ensembl; ENST00000307404; ENSP00000304151; ENSG00000170727.
DR Ensembl; ENST00000569669; ENSP00000455106; ENSG00000261236.
DR GeneID; 23246; -.
DR KEGG; hsa:23246; -.
DR UCSC; uc003zbm.3; human.
DR CTD; 23246; -.
DR GeneCards; GC08M145486; -.
DR H-InvDB; HIX0168814; -.
DR HGNC; HGNC:15519; BOP1.
DR MIM; 610596; gene.
DR neXtProt; NX_Q14137; -.
DR PharmGKB; PA25398; -.
DR eggNOG; COG2319; -.
DR HOGENOM; HOG000029368; -.
DR HOVERGEN; HBG008113; -.
DR InParanoid; Q14137; -.
DR KO; K14824; -.
DR OMA; QIFHGKV; -.
DR PhylomeDB; Q14137; -.
DR SignaLink; Q14137; -.
DR GeneWiki; BOP1; -.
DR GenomeRNAi; 23246; -.
DR NextBio; 44934; -.
DR PRO; PR:Q14137; -.
DR ArrayExpress; Q14137; -.
DR Bgee; Q14137; -.
DR CleanEx; HS_BOP1; -.
DR Genevestigator; Q14137; -.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070545; C:PeBoW complex; IDA:UniProtKB.
DR GO; GO:0008283; P:cell proliferation; NAS:UniProtKB.
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 Gene3D; 2.130.10.10; -; 2.
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.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR017986; WD40_repeat_dom.
DR Pfam; PF08145; BOP1NT; 1.
DR Pfam; PF00400; WD40; 3.
DR SMART; SM01035; BOP1NT; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 2.
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 Complete proteome; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Ribosome biogenesis; rRNA processing; WD repeat.
FT CHAIN 1 746 Ribosome biogenesis protein BOP1.
FT /FTId=PRO_0000050885.
FT REPEAT 411 450 WD 1.
FT REPEAT 452 492 WD 2.
FT REPEAT 532 576 WD 3.
FT REPEAT 577 615 WD 4.
FT REPEAT 618 657 WD 5.
FT REPEAT 661 700 WD 6.
FT REPEAT 716 746 WD 7.
FT REGION 265 427 Sufficient for nucleolar localization (By
FT similarity).
FT MOD_RES 106 106 Phosphothreonine.
FT MOD_RES 126 126 Phosphoserine (By similarity).
FT MOD_RES 127 127 Phosphoserine (By similarity).
FT CONFLICT 577 577 R -> H (in Ref. 2; BAA09473).
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
//
MIM
610596
*RECORD*
*FIELD* NO
610596
*FIELD* TI
*610596 BLOCK OF PROLIFERATION 1; BOP1
;;KIAA0124
*FIELD* TX
CLONING
By sequencing clones obtained from a size-fractionated myeloid leukemia
read morecell line cDNA library, Nagase et al. (1995) cloned BOP1, which they
designated KIAA0124. The deduced 682-amino acid protein contains
beta-transducin repeats. Northern blot analysis detected BOP1 expression
in all tissues examined, with highest levels in skeletal muscle and
colon.
Strezoska et al. (2000) cloned mouse Bop1. The deduced 732-amino acid
protein has a calculated molecular mass of 83 kD. It has 2 PEST
sequences in its N-terminal half and 4 WD40 repeats in its C-terminal
half. Northern blot analysis detected Bop1 expression in all mouse
tissues examined. Immunofluorescence staining localized endogenous and
epitope-tagged Bop1 predominantly to nucleoli, although weak, diffuse
nucleoplasmic staining was also present. Western blot analysis detected
endogenous Bop1 at an apparent molecular mass of 100 kD.
GENE FUNCTION
By examining sucrose density gradients of mouse fibroblast nuclear
extracts, Strezoska et al. (2000) found that Bop1 cosedimented with the
50S to 80S ribonucleoprotein particles containing the 32S rRNA
precursor. RNase A treatment disrupted these particles and released Bop1
into a low molecular mass fraction. Expression of an N-terminally
truncated Bop1 protein (Bop1-delta) led to cell growth arrest in the G1
phase and specific inhibition of 28S and 5.8S rRNA synthesis without
affecting 18S rRNA formation. Pulse-chase analysis showed that
Bop1-delta expression partially inhibited conversion of 36S to 32S
pre-rRNA and completely inhibited processing of 32S pre-rRNA to form
mature 28S and 5.8S rRNAs. Bop1-delta expression also led to a deficit
in cytosolic 60S ribosomal subunits. Strezoska et al. (2000) concluded
that BOP1 is a nonribosomal protein that plays a key role in formation
of mature 28S and 5.8S rRNAs and in biogenesis of the 60S ribosomal
subunit.
Using dominant-negative mutants of mouse Bop1 and antisense
oligonucleotides, Strezoska et al. (2002) showed that Bop1 was required
for proper processing of pre-rRNA at distinct sites within the internal
transcribed spacers ITS1 and ITS2 and at the 3-prime external spacer.
Using small interfering RNA, Killian et al. (2004) found that
downregulation of BOP1 and other components of the pescadillo (PES1;
605819) complex involved in ribosome biogenesis altered chromosome
segregation and led to abnormal mitoses in a human colon carcinoma cell
line.
Killian et al. (2006) found that BOP1 gene dosage was increased in 39%
of 56 primary colorectal tumors. In some of these cancers, the dosage of
the MYC (190080) gene, which lies 16.6 Mb from the BOP1 gene, was also
increased. PCR analysis showed that increased BOP1 gene dosage resulted
in increased BOP1 mRNA in 6 of 6 cancers tested, and overexpression of
BOP1 in human cells increased the percentage of multipolar spindles.
Killian et al. (2006) concluded that deregulation of BOP1 can contribute
to colorectal tumorigenesis.
GENE STRUCTURE
Zhang et al. (1998) found that the first exon of the mouse Bop1 gene
lies on the opposite strand and just upstream of the Hsf1 (140580)
translation initiation site. Functional analysis showed that the region
of overlap behaves as a bidirectional promoter for transcription of both
genes.
MAPPING
By PCR of human/rodent hybrid panels, Nagase et al. (1995) mapped the
BOP1 gene to chromosome 8. Killian et al. (2006) stated that the BOP1
gene maps to chromosome 8q24.
*FIELD* RF
1. Killian, A.; Le Meur, N.; Sesboue, R.; Bourguignon, J.; Bougeard,
G.; Gautherot, J.; Bastard, C.; Frebourg, T.; Flaman, J.-M.: Inactivation
of the RRB1-pescadillo pathway involved in ribosome biogenesis induces
chromosomal instability. Oncogene 23: 8597-8602, 2004.
2. Killian, A.; Sarafan-Vasseur, N.; Sesboue, R.; Le Pessot, F.; Blanchard,
F.; Lamy, A.; Laurent, M.; Flaman, J.-M.; Frebourg, T.: Contribution
of the BOP1 gene, located on 8q24, to colorectal tumorigenesis. Genes
Chromosomes Cancer 45: 874-881, 2006.
3. Nagase, T.; Seki, N.; Tanaka, A.; Ishikawa, K.; Nomura, N.: Prediction
of the coding sequences of unidentified human genes. IV. The coding
sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis
of cDNA clones from human cell line KG-1. DNA Res. 2: 167-174, 1995.
4. Strezoska, Z.; Pestov, D. G.; Lau, L. F.: Functional inactivation
of the mouse nucleolar protein Bop1 inhibits multiple steps in pre-rRNA
processing and blocks cell cycle progression. J. Biol. Chem. 277:
29617-29625, 2002.
5. Strezoska, Z.; Pestov, D. G.; Lau, L. F.: Bop1 is a mouse WD40
repeat nucleolar protein involved in 28S and 5.8S rRNA processing
and 60S ribosome biogenesis. Molec. Cell. Biol. 20: 5516-5528, 2000.
6. Zhang, Y.; Koushik, S.; Dai, R.; Mivechi, N. F.: Structural organization
and promoter analysis of murine heat shock transcription factor-1
gene. J. Biol. Chem. 273: 32514-32521, 1998.
*FIELD* CD
Patricia A. Hartz: 11/22/2006
*FIELD* ED
mgross: 11/22/2006
*RECORD*
*FIELD* NO
610596
*FIELD* TI
*610596 BLOCK OF PROLIFERATION 1; BOP1
;;KIAA0124
*FIELD* TX
CLONING
By sequencing clones obtained from a size-fractionated myeloid leukemia
read morecell line cDNA library, Nagase et al. (1995) cloned BOP1, which they
designated KIAA0124. The deduced 682-amino acid protein contains
beta-transducin repeats. Northern blot analysis detected BOP1 expression
in all tissues examined, with highest levels in skeletal muscle and
colon.
Strezoska et al. (2000) cloned mouse Bop1. The deduced 732-amino acid
protein has a calculated molecular mass of 83 kD. It has 2 PEST
sequences in its N-terminal half and 4 WD40 repeats in its C-terminal
half. Northern blot analysis detected Bop1 expression in all mouse
tissues examined. Immunofluorescence staining localized endogenous and
epitope-tagged Bop1 predominantly to nucleoli, although weak, diffuse
nucleoplasmic staining was also present. Western blot analysis detected
endogenous Bop1 at an apparent molecular mass of 100 kD.
GENE FUNCTION
By examining sucrose density gradients of mouse fibroblast nuclear
extracts, Strezoska et al. (2000) found that Bop1 cosedimented with the
50S to 80S ribonucleoprotein particles containing the 32S rRNA
precursor. RNase A treatment disrupted these particles and released Bop1
into a low molecular mass fraction. Expression of an N-terminally
truncated Bop1 protein (Bop1-delta) led to cell growth arrest in the G1
phase and specific inhibition of 28S and 5.8S rRNA synthesis without
affecting 18S rRNA formation. Pulse-chase analysis showed that
Bop1-delta expression partially inhibited conversion of 36S to 32S
pre-rRNA and completely inhibited processing of 32S pre-rRNA to form
mature 28S and 5.8S rRNAs. Bop1-delta expression also led to a deficit
in cytosolic 60S ribosomal subunits. Strezoska et al. (2000) concluded
that BOP1 is a nonribosomal protein that plays a key role in formation
of mature 28S and 5.8S rRNAs and in biogenesis of the 60S ribosomal
subunit.
Using dominant-negative mutants of mouse Bop1 and antisense
oligonucleotides, Strezoska et al. (2002) showed that Bop1 was required
for proper processing of pre-rRNA at distinct sites within the internal
transcribed spacers ITS1 and ITS2 and at the 3-prime external spacer.
Using small interfering RNA, Killian et al. (2004) found that
downregulation of BOP1 and other components of the pescadillo (PES1;
605819) complex involved in ribosome biogenesis altered chromosome
segregation and led to abnormal mitoses in a human colon carcinoma cell
line.
Killian et al. (2006) found that BOP1 gene dosage was increased in 39%
of 56 primary colorectal tumors. In some of these cancers, the dosage of
the MYC (190080) gene, which lies 16.6 Mb from the BOP1 gene, was also
increased. PCR analysis showed that increased BOP1 gene dosage resulted
in increased BOP1 mRNA in 6 of 6 cancers tested, and overexpression of
BOP1 in human cells increased the percentage of multipolar spindles.
Killian et al. (2006) concluded that deregulation of BOP1 can contribute
to colorectal tumorigenesis.
GENE STRUCTURE
Zhang et al. (1998) found that the first exon of the mouse Bop1 gene
lies on the opposite strand and just upstream of the Hsf1 (140580)
translation initiation site. Functional analysis showed that the region
of overlap behaves as a bidirectional promoter for transcription of both
genes.
MAPPING
By PCR of human/rodent hybrid panels, Nagase et al. (1995) mapped the
BOP1 gene to chromosome 8. Killian et al. (2006) stated that the BOP1
gene maps to chromosome 8q24.
*FIELD* RF
1. Killian, A.; Le Meur, N.; Sesboue, R.; Bourguignon, J.; Bougeard,
G.; Gautherot, J.; Bastard, C.; Frebourg, T.; Flaman, J.-M.: Inactivation
of the RRB1-pescadillo pathway involved in ribosome biogenesis induces
chromosomal instability. Oncogene 23: 8597-8602, 2004.
2. Killian, A.; Sarafan-Vasseur, N.; Sesboue, R.; Le Pessot, F.; Blanchard,
F.; Lamy, A.; Laurent, M.; Flaman, J.-M.; Frebourg, T.: Contribution
of the BOP1 gene, located on 8q24, to colorectal tumorigenesis. Genes
Chromosomes Cancer 45: 874-881, 2006.
3. Nagase, T.; Seki, N.; Tanaka, A.; Ishikawa, K.; Nomura, N.: Prediction
of the coding sequences of unidentified human genes. IV. The coding
sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis
of cDNA clones from human cell line KG-1. DNA Res. 2: 167-174, 1995.
4. Strezoska, Z.; Pestov, D. G.; Lau, L. F.: Functional inactivation
of the mouse nucleolar protein Bop1 inhibits multiple steps in pre-rRNA
processing and blocks cell cycle progression. J. Biol. Chem. 277:
29617-29625, 2002.
5. Strezoska, Z.; Pestov, D. G.; Lau, L. F.: Bop1 is a mouse WD40
repeat nucleolar protein involved in 28S and 5.8S rRNA processing
and 60S ribosome biogenesis. Molec. Cell. Biol. 20: 5516-5528, 2000.
6. Zhang, Y.; Koushik, S.; Dai, R.; Mivechi, N. F.: Structural organization
and promoter analysis of murine heat shock transcription factor-1
gene. J. Biol. Chem. 273: 32514-32521, 1998.
*FIELD* CD
Patricia A. Hartz: 11/22/2006
*FIELD* ED
mgross: 11/22/2006