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Reviewed, UniProtKB/Swiss-Prot Q14137 (BOP1_HUMAN)

Last modified November 3, 2009. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Ribosome biogenesis protein BOP1
Alternative name(s):
    Block of proliferation 1 protein
Gene names
Name: BOP1
Synonyms: KIAA0124
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length746 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Component of the PeBoW complex, which is required for maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S ribosome. Ref.9

Subunit structure

Component of the PeBoW complex, composed of BOP1, PES1 and WDR12. Within the PeBoW complex BOP1 interacts directly with PES1 and WDR12. The PeBoW complex also associates with the 66S pre-ribosome. Ref.9 Ref.4 Ref.7 Ref.10

Subcellular location

Nucleusnucleolus. Nucleusnucleoplasm. Ref.3

Induction

By MYC. Ref.4

Sequence similarities

Belongs to the WD repeat BOP1/ERB1 family.

Contains 7 WD repeats.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 746746Ribosome biogenesis protein BOP1
PRO_0000050885

Regions

Repeat411 – 45040WD 1
Repeat452 – 49241WD 2
Repeat532 – 57645WD 3
Repeat577 – 61539WD 4
Repeat618 – 65740WD 5
Repeat661 – 70040WD 6
Repeat716 – 74631WD 7
Region265 – 427163Sufficient for nucleolar localization By similarity

Amino acid modifications

Modified residue1061Phosphothreonine Ref.6 Ref.11 Ref.12 Ref.14
Modified residue1261Phosphoserine Ref.14 Ref.5 Ref.8 Ref.13 Ref.15
Modified residue1271Phosphoserine Ref.14 Ref.5 Ref.8 Ref.13 Ref.15
Modified residue1971Phosphothreonine Ref.14

Experimental info

Sequence conflict5771R → H in BAA09473. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q14137-1 [UniParc].

Last modified October 10, 2002. Version 2.
Checksum: 49A97BE21B0EB3DD

FASTA74683,630
        10         20         30         40         50         60 
MAGSRGAGRT AAPSVRPEKR RSEPELEPEP EPEPPLLCTS PLSHSTGSDS GVSDSEESVF 

        70         80         90        100        110        120 
SGLEDSGSDS SEDDDEGDEE GEDGALDDEG HSGIKKTTEE QVQASTPCPR TEMASARIGD 

       130        140        150        160        170        180 
EYAEDSSDEE DIRNTVGNVP LEWYDDFPHV GYDLDGRRIY KPLRTRDELD QFLDKMDDPD 

       190        200        210        220        230        240 
YWRTVQDPMT GRDLRLTDEQ VALVRRLQSG QFGDVGFNPY EPAVDFFSGD VMIHPVTNRP 

       250        260        270        280        290        300 
ADKRSFIPSL VEKEKVSRMV HAIKMGWIQP RRPRDPTPSF YDLWAQEDPN AVLGRHKMHV 

       310        320        330        340        350        360 
PAPKLALPGH AESYNPPPEY LLSEEERLAW EQQEPGERKL SFLPRKFPSL RAVPAYGRFI 

       370        380        390        400        410        420 
QERFERCLDL YLCPRQRKMR VNVDPEDLIP KLPRPRDLQP FPTCQALVYR GHSDLVRCLS 

       430        440        450        460        470        480 
VSPGGQWLVS GSDDGSLRLW EVATARCVRT VPVGGVVKSV AWNPSPAVCL VAAAVEDSVL 

       490        500        510        520        530        540 
LLNPALGDRL VAGSTDQLLS AFVPPEEPPL QPARWLEASE EERQVGLRLR ICHGKPVTQV 

       550        560        570        580        590        600 
TWHGRGDYLA VVLATQGHTQ VLIHQLSRRR SQSPFRRSHG QVQRVAFHPA RPFLLVASQR 

       610        620        630        640        650        660 
SVRLYHLLRQ ELTKKLMPNC KWVSSLAVHP AGDNVICGSY DSKLVWFDLD LSTKPYRMLR 

       670        680        690        700        710        720 
HHKKALRAVA FHPRYPLFAS GSDDGSVIVC HGMVYNDLLQ NPLLVPVKVL KGHVLTRDLG 

       730        740 
VLDVIFHPTQ PWVFSSGADG TVRLFT 

« Hide

References

« Hide 'large scale' references
[1]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain, Eye, Lymph, Muscle and Pancreas.
[2]"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."
Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.
DNA Res. 2:167-174(1995) [PubMed: 8590280] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 65-746.
Tissue: Bone marrow.
[3]"Functional proteomic analysis of human nucleolus."
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J.
Mol. Biol. Cell 13:4100-4109(2002) [PubMed: 12429849] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[4]"Mammalian WDR12 is a novel member of the Pes1-Bop1 complex and is required for ribosome biogenesis and cell proliferation."
Hoelzel M., Rohrmoser M., Schlee M., Grimm T., Harasim T., Malamoussi A., Gruber-Eber A., Kremmer E., Hiddemann W., Bornkamm G.W., Eick D.
J. Cell Biol. 170:367-378(2005) [PubMed: 16043514] [Abstract]
Cited for: INTERACTION WITH PES1 AND WDR12, INDUCTION.
[5]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126 AND SER-127, MASS SPECTROMETRY.
Tissue: Epithelium.
[6]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-106, MASS SPECTROMETRY.
Tissue: Epithelium.
[7]"Dominant-negative Pes1 mutants inhibit ribosomal RNA processing and cell proliferation via incorporation into the PeBoW-complex."
Grimm T., Hoelzel M., Rohrmoser M., Harasim T., Malamoussi A., Gruber-Eber A., Kremmer E., Eick D.
Nucleic Acids Res. 34:3030-3043(2006) [PubMed: 16738141] [Abstract]
Cited for: INTERACTION WITH PES1 AND WDR12.
[8]"Phosphoproteome analysis of the human mitotic spindle."
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126 AND SER-127, MASS SPECTROMETRY.
Tissue: Epithelium.
[9]"Interdependence of Pes1, Bop1, and WDR12 controls nucleolar localization and assembly of the PeBoW complex required for maturation of the 60S ribosomal subunit."
Rohrmoser M., Hoelzel M., Grimm T., Malamoussi A., Harasim T., Orban M., Pfisterer I., Gruber-Eber A., Kremmer E., Eick D.
Mol. Cell. Biol. 27:3682-3694(2007) [PubMed: 17353269] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PES1 AND WDR12.
[10]"The BRCT domain of mammalian Pes1 is crucial for nucleolar localization and rRNA processing."
Hoelzel M., Grimm T., Rohrmoser M., Malamoussi A., Harasim T., Gruber-Eber A., Kremmer E., Eick D.
Nucleic Acids Res. 35:789-800(2007) [PubMed: 17189298] [Abstract]
Cited for: INTERACTION WITH PES1 AND WDR12.
[11]"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-106, MASS SPECTROMETRY.
[12]"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis."
Wang B., Malik R., Nigg E.A., Korner R.
Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-106, MASS SPECTROMETRY.
[13]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126 AND SER-127, MASS SPECTROMETRY.
[14]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-106; SER-126; SER-127 AND THR-197, MASS SPECTROMETRY.
[15]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed: 18318008] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126 AND SER-127, MASS SPECTROMETRY.
Tissue: Liver.
[16]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

BC001086 mRNA. Translation: AAH01086.2.
BC005160 mRNA. Translation: AAH05160.2.
BC007274 mRNA. Translation: AAH07274.1.
BC013787 mRNA. Translation: AAH13787.1.
BC013980 mRNA. Translation: AAH13980.1.
BC017674 mRNA. Translation: AAH17674.1.
D50914 mRNA. Translation: BAA09473.1.
IPIIPI00028955.
RefSeqNP_056016.1.
UniGeneHs.535901
Hs.645279

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ14137. 2 interactions.
STRINGQ14137.

PTM databases

PhosphoSiteQ14137.

2-D gel databases

SWISS-2DPAGEQ14137.

Proteomic databases

PeptideAtlasQ14137.
PRIDEQ14137.

Genome annotation databases

EnsemblENST00000307404; ENSP00000304151; ENSG00000170727; Homo sapiens. [Genome view]
GeneID23246.
KEGGhsa:23246.
UCSCuc003zbr.1. human.

Organism-specific databases

CTD23246.
GeneCardsGC08M145456.
H-InvDBHIX0007848.
HIX0034600.
HGNCHGNC:15519. BOP1.
MIM610596. gene.
PharmGKBPA25398.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ14137.
HOVERGENQ14137.
OMAMASARIG.

Gene expression databases

CleanExHS_BOP1.
GenevestigatorQ14137.
GermOnlineENSG00000170727. Homo sapiens.

Family and domain databases

InterProIPR012953. BOP1_N.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019782. WD40_repeat_2.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
IPR019781. WD40_repeat_sg.
[Graphical view]
Gene3DG3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.
PfamPF08145. BOP1NT. 1 hit.
PF00400. WD40. 4 hits.
[Graphical view]
ProDomPD000018. WD40. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00320. WD40. 7 hits.
[Graphical view]
PROSITEPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 2 hits.
PS50294. WD_REPEATS_REGION. 2 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio44934.
SOURCESearch...

Entry information

Entry nameBOP1_HUMAN
AccessionPrimary (citable) accession number: Q14137
Secondary accession number(s): Q969Z6 expand/collapse secondary AC list , Q96IS8, Q9BSA7, Q9BVM0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 10, 2002
Last modified: November 3, 2009
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents