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MYBBP1A (MYB binding protein (P160) 1a)

Written2011-01Claudia Perrera, Riccardo Colombo
Department of Cell Biology-Oncology, Nerviano Medical Sciences, Viale Pasteur 10, Nerviano 20014, Italy

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Alias (NCBI)FLJ37886
HGNC Alias symbP160
HGNC Alias namep53-activated protein-2
HGNC Previous nameMYB binding protein (P160) 1a
LocusID (NCBI) 10514
Atlas_Id 41467
Location 17p13.2  [Link to chromosome band 17p13]
Location_base_pair Starts at 4538904 and ends at 4555384 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping MYBBP1A.png]
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
MYBBP1A (17p13.2)::BAG6 (6p21.33)MYBBP1A (17p13.2)::EPC2 (2q23.1)


Note Total gene length 16491 bp, mRNA length 4122 bp, telomeric to SPNS2 and centromeric to GGT6. Two variants described. MYBBP1A gene is composed by 26 exones and 28 introns.
Description The human MYBBP1A gene is located on chromosome 17p13.3 (Keough et al., 1999).
Transcription The complete MYBBP1A cDNA is 4518 bp, including 25 bp of 5' UTR and 506 bp of 3' UTR up to the polyA tail.


  Schematic representation of Mybbp1A protein. aa 1-582 is the domain reported to interact in vitro with Myb. NLS: Nuclear and nucleolar localisation signal. The indicated S, T and Y are phosphorylated residues identified in several phospho-proteomic studies.
Description Human MYBBP1A is a 1328 aa long protein. Murine MYBBP1A was originally identified as a protein interacting with the leucine zipper of c-Myb (Favier et al., 1994). Subsequently, in 1998, the human gene homologue of MYBBP1A was cloned and its chromosomal location mapped to 17p13.3 (Keough et al., 1999).
Expression MYBBP1A is ubiquitously expressed (Tavner et al., 1998).
Localisation MYBBP1A is a nuclear protein, predominantly localized in the nucleolus (Keough et al., 2003). MYBBP1A has been confirmed as a resident protein of the nucleolus by three large-scale proteomic studies that have established a protein inventory of this sub-nuclear compartment (Andersen et al., 2002; Scherl et al., 2002; Andersen et al., 2005). The nuclear/nucleolar localization signals are present in the C-terminal tail of MYBBP1A.
Function MYBBP1A functions have not yet been completely clarified. It was originally identified as a protein able to interact with the negative regulatory domain (NRD) of c-Myb; however, it was later shown to lack any significant effect in a Myb-dependent transcription reporter assay (Favier et al., 1994). MYBBP1A has been found to interact with and regulate several transcription factors: it binds and represses both Prep1-Pbx1, involved in development and organogenesis, and also PGC-1a, a key regulator of metabolic processes such as mitochondrial biogenesis and respiration and gluconeogenesis in liver (Fan et al., 2004; Diaz et al., 2007). MYBBP1A acts as a co-repressor for RelA/p65, a member of the NFkB family, by competing with the co-activator p300 histone acetyltrasferase for interaction with the transcription activation domain (TAD) of RelA/p65. It is also a co-repressor on the Period2 promoter, repressing the expression of Per2, an essential gene in the regulation of the circadian clock (Owen et al., 2007; Hara et al., 2009). Conversely, MYBBP1A is a positive regulator of the aromatic hydrocarbon receptor (AhR) which mediates transcriptional responses to certain hydrophobic ligands, such as dioxin, by enhancing the ability of AhR to activate transcription (Jones et al., 2002).
MYBBP1A has also been reported to be a component of macromolecular complexes such as the B-WICH complex, a 3 MDa assembly made of proteins and RNAs, formed during active transcription (Cavellan et al., 2006) or part of large interactomes such as the SMN interactome (Fuller et al., 2010).
MYBBP1A can be post-translationally processed in some type of cells to generate an amino-terminal fragments of 67 kDa (p67). Ribosomal stress induced by Actinomycin D (an inhibitor of ribosome biogenesis) treatment causes MYBBP1A processing and translocation from the nucleolus to the nucloplasm (Diaz et al., 2007; Yamauchi et al., 2008), indicating a possible MYBBP1A role in ribosome biogenesis.
Several post-translational modifications have been described for MYBBP1A, even if their biological significance is not yet clarified. MYBBP1A is reported to be a heavily phosphorylated protein in cells, according to several large-scale mass spectrometry-based phosphoproteomic studies (Beausoleil et al., 2004; Beausoleil et al., 2006; Nousiainen et al., 2006; Olsen et al., 2006; Cantin et al., 2008; Daub et al., 2008; Dephoure et al., 2008; Imami et al., 2008). The majority of the phosphosites mapped in MYBBP1A in these studies (18 out of a total of 21) reside within the ~200 amino-acid long C-terminal portion of the protein, which has been shown to be relevant for its nuclear and nucleolar localization (Keough et al., 2003). Notably, MYBBP1A was also found to be also a component of the proteome as well as the phospho-proteome of the human mitotic spindle. MYBBP1A contains several consensus motifs for several kinases, but until now, only Ser1303 has been proven in vitro and in HeLa cells to be indeed phosphorylated by Aurora B kinase (Perrera et al., 2010). In this work, it has been shown that MYBBP1A depletion by RNAi causes a delay in progression through mitosis and defects in mitotic spindle assembly and stability, indicating that, like other nucleolar proteins, MYBBP1A may have a role in insuring correct mitotic progression (Perrera et al., 2010).
MYBBP1A has been reported to be also sumoylated upon MG132 treatment (Matafora et al., 2009).
Homology Orthologous genes for MYBBP1A sharing a high degree of similarity are present in rat and mice. Protein homologues have also been recognized in dog, bovine, and chicken and a MYBBP1A-like protein spanning 1269 residues and showing a 60% similarity to the human protein has been identified in zebrafish, suggesting that MYBBP1A is significantly conserved across vertebrate species (Amsterdam et al., 2004). MYBBP1A shares some homology to a yeast protein called POL5, reported to be an essential DNA polymerase in Saccharomyces cerevisiae (Yang et al., 2003).

Implicated in

Entity Various cancers
Disease MYBBP1A maps at 17p13.3, a region frequently lost in many solid and haematological tumors, such as breast and ovarian cancer, medulloblastoma, astrocytoma, leukemias, etc. This indicates that this chromosomal band contains one or more tumor suppressor genes. However, MYBBP1A is unlikely a candidate for being a tumor suppressor gene, as it lies centromeric to the regions of LOH described (Keough et al., 1999).


Identification of 315 genes essential for early zebrafish development.
Amsterdam A, Nissen RM, Sun Z, Swindell EC, Farrington S, Hopkins N.
Proc Natl Acad Sci U S A. 2004 Aug 31;101(35):12792-7. Epub 2004 Jul 15.
PMID 15256591
Nucleolar proteome dynamics.
Andersen JS, Lam YW, Leung AK, Ong SE, Lyon CE, Lamond AI, Mann M.
Nature. 2005 Jan 6;433(7021):77-83.
PMID 15635413
A probability-based approach for high-throughput protein phosphorylation analysis and site localization.
Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP.
Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10.
PMID 16964243
Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.
Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd.
J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26.
PMID 18220336
The WSTF-SNF2h chromatin remodeling complex interacts with several nuclear proteins in transcription.
Cavellan E, Asp P, Percipalle P, Farrants AK.
J Biol Chem. 2006 Jun 16;281(24):16264-71. Epub 2006 Apr 9.
PMID 16603771
Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.
Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M.
Mol Cell. 2008 Aug 8;31(3):438-48.
PMID 18691976
A quantitative atlas of mitotic phosphorylation.
Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP.
Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31.
PMID 18669648
p160 Myb-binding protein interacts with Prep1 and inhibits its transcriptional activity.
Diaz VM, Mori S, Longobardi E, Menendez G, Ferrai C, Keough RA, Bachi A, Blasi F.
Mol Cell Biol. 2007 Nov;27(22):7981-90. Epub 2007 Sep 17.
PMID 17875935
Suppression of mitochondrial respiration through recruitment of p160 myb binding protein to PGC-1alpha: modulation by p38 MAPK.
Fan M, Rhee J, St-Pierre J, Handschin C, Puigserver P, Lin J, Jaeger S, Erdjument-Bromage H, Tempst P, Spiegelman BM.
Genes Dev. 2004 Feb 1;18(3):278-89. Epub 2004 Jan 26.
PMID 14744933
Detection of proteins that bind to the leucine zipper motif of c-Myb.
Favier D, Gonda TJ.
Oncogene. 1994 Jan;9(1):305-11.
PMID 8302594
The SMN interactome includes Myb-binding protein 1a.
Fuller HR, Man NT, Lam le T, Thanh le T, Keough RA, Asperger A, Gonda TJ, Morris GE.
J Proteome Res. 2010 Jan;9(1):556-63.
PMID 19928837
Molecular characterization of Mybbp1a as a co-repressor on the Period2 promoter.
Hara Y, Onishi Y, Oishi K, Miyazaki K, Fukamizu A, Ishida N.
Nucleic Acids Res. 2009 Mar;37(4):1115-26. Epub 2009 Jan 7.
PMID 19129230
Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.
Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y.
Anal Sci. 2008 Jan;24(1):161-6.
PMID 18187866
Myb-binding protein 1a augments AhR-dependent gene expression.
Jones LC, Okino ST, Gonda TJ, Whitlock JP Jr.
J Biol Chem. 2002 Jun 21;277(25):22515-9. Epub 2002 Apr 15.
PMID 11956195
Molecular cloning and chromosomal mapping of the human homologue of MYB binding protein (P160) 1A (MYBBP1A) to 17p13.3.
Keough R, Woollatt E, Crawford J, Sutherland GR, Plummer S, Casey G, Gonda TJ.
Genomics. 1999 Dec 15;62(3):483-9.
PMID 10644447
Myb-binding protein 1a is a nucleocytoplasmic shuttling protein that utilizes CRM1-dependent and independent nuclear export pathways.
Keough RA, Macmillan EM, Lutwyche JK, Gardner JM, Tavner FJ, Jans DA, Henderson BR, Gonda TJ.
Exp Cell Res. 2003 Sep 10;289(1):108-23.
PMID 12941609
Proteomics analysis of nucleolar SUMO-1 target proteins upon proteasome inhibition.
Matafora V, D'Amato A, Mori S, Blasi F, Bachi A.
Mol Cell Proteomics. 2009 Oct;8(10):2243-55. Epub 2009 Jul 12.
PMID 19596686
Phosphoproteome analysis of the human mitotic spindle.
Nousiainen M, Sillje HH, Sauer G, Nigg EA, Korner R.
Proc Natl Acad Sci U S A. 2006 Apr 4;103(14):5391-6. Epub 2006 Mar 24.
PMID 16565220
Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.
Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M.
Cell. 2006 Nov 3;127(3):635-48.
PMID 17081983
MYBBP1a is a novel repressor of NF-kappaB.
Owen HR, Elser M, Cheung E, Gersbach M, Kraus WL, Hottiger MO.
J Mol Biol. 2007 Feb 23;366(3):725-36. Epub 2006 Dec 15.
PMID 17196614
Identification of Myb-binding protein 1A (MYBBP1A) as a novel substrate for aurora B kinase.
Perrera C, Colombo R, Valsasina B, Carpinelli P, Troiani S, Modugno M, Gianellini L, Cappella P, Isacchi A, Moll J, Rusconi L.
J Biol Chem. 2010 Apr 16;285(16):11775-85. Epub 2010 Feb 22.
PMID 20177074
Functional proteomic analysis of human nucleolus.
Scherl A, Coute Y, Deon C, Calle A, Kindbeiter K, Sanchez JC, Greco A, Hochstrasser D, Diaz JJ.
Mol Biol Cell. 2002 Nov;13(11):4100-9.
PMID 12429849
Molecular cloning reveals that the p160 Myb-binding protein is a novel, predominantly nucleolar protein which may play a role in transactivation by Myb.
Tavner FJ, Simpson R, Tashiro S, Favier D, Jenkins NA, Gilbert DJ, Copeland NG, Macmillan EM, Lutwyche J, Keough RA, Ishii S, Gonda TJ.
Mol Cell Biol. 1998 Feb;18(2):989-1002.
PMID 9447996
Ribosomal stress induces processing of Mybbp1a and its translocation from the nucleolus to the nucleoplasm.
Yamauchi T, Keough RA, Gonda TJ, Ishii S.
Genes Cells. 2008 Jan;13(1):27-39.
PMID 18173745
Yeast POL5 is an evolutionarily conserved regulator of rDNA transcription unrelated to any known DNA polymerases.
Yang W, Rogozin IB, Koonin EV.
Cell Cycle. 2003 Mar-Apr;2(2):120-2.
PMID 12695662


This paper should be referenced as such :
Perrera, C ; Colombo, R
MYBBP1A (MYB binding protein (P160) 1a)
Atlas Genet Cytogenet Oncol Haematol. 2011;15(8):667-669.
Free journal version : [ pdf ]   [ DOI ]

External links


HGNC (Hugo)MYBBP1A   7546
Atlas Explorer : (Salamanque)MYBBP1A
Entrez_Gene (NCBI)MYBBP1A    MYB binding protein 1a
AliasesP160; PAP2; Pol5
GeneCards (Weizmann)MYBBP1A
Ensembl hg19 (Hinxton)ENSG00000132382 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000132382 [Gene_View]  ENSG00000132382 [Sequence]  chr17:4538904-4555384 [Contig_View]  MYBBP1A [Vega]
ICGC DataPortalENSG00000132382
Genatlas (Paris)MYBBP1A
Genetics Home Reference (NIH)MYBBP1A
Genomic and cartography
GoldenPath hg38 (UCSC)MYBBP1A  -     chr17:4538904-4555384 -  17p13.2   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)MYBBP1A  -     17p13.2   [Description]    (hg19-Feb_2009)
GoldenPathMYBBP1A - 17p13.2 [CytoView hg19]  MYBBP1A - 17p13.2 [CytoView hg38]
Genome Data Viewer NCBIMYBBP1A [Mapview hg19]  
Gene and transcription
Genbank (Entrez)AF147709 AK095205 AK293458 AK301622 AK303150
RefSeq transcript (Entrez)NM_001105538 NM_014520
Consensus coding sequences : CCDS (NCBI)MYBBP1A
Gene Expression Viewer (FireBrowse)MYBBP1A [ Firebrowse - Broad ]
GenevisibleExpression of MYBBP1A in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)10514
GTEX Portal (Tissue expression)MYBBP1A
Human Protein AtlasENSG00000132382-MYBBP1A [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ9BQG0   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ9BQG0  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ9BQG0
Domains : Interpro (EBI)ARM-type_fold    DNA_pol_V/MYBBP1A   
Domain families : Pfam (Sanger)DNA_pol_phi (PF04931)   
Domain families : Pfam (NCBI)pfam04931   
Conserved Domain (NCBI)MYBBP1A
AlphaFold pdb e-kbQ9BQG0   
Human Protein Atlas [tissue]ENSG00000132382-MYBBP1A [tissue]
Protein Interaction databases
IntAct (EBI)Q9BQG0
Complex Portal (EBI)Q9BQG0 CPX-1099 B-WICH chromatin remodelling complex
Ontologies - Pathways
Ontology : AmiGOosteoblast differentiation  transcription corepressor activity  transcription corepressor activity  RNA binding  nucleus  nucleus  nucleoplasm  nucleolus  nucleolus  nucleolus  cytoplasm  regulation of transcription, DNA-templated  transcription factor binding  membrane  respiratory electron transport chain  circadian regulation of gene expression  cellular response to glucose starvation  ribosome biogenesis  NLS-dependent protein nuclear import complex  intracellular membrane-bounded organelle  sequence-specific DNA binding  negative regulation of transcription, DNA-templated  positive regulation of transcription by RNA polymerase III  E-box binding  intrinsic apoptotic signaling pathway by p53 class mediator  B-WICH complex  regulation of G1 to G0 transition  positive regulation of anoikis  
Ontology : EGO-EBIosteoblast differentiation  transcription corepressor activity  transcription corepressor activity  RNA binding  nucleus  nucleus  nucleoplasm  nucleolus  nucleolus  nucleolus  cytoplasm  regulation of transcription, DNA-templated  transcription factor binding  membrane  respiratory electron transport chain  circadian regulation of gene expression  cellular response to glucose starvation  ribosome biogenesis  NLS-dependent protein nuclear import complex  intracellular membrane-bounded organelle  sequence-specific DNA binding  negative regulation of transcription, DNA-templated  positive regulation of transcription by RNA polymerase III  E-box binding  intrinsic apoptotic signaling pathway by p53 class mediator  B-WICH complex  regulation of G1 to G0 transition  positive regulation of anoikis  
REACTOMEQ9BQG0 [protein]
REACTOME PathwaysR-HSA-5250924 [pathway]   
Atlas of Cancer Signalling NetworkMYBBP1A
Wikipedia pathwaysMYBBP1A
Orthology - Evolution
GeneTree (enSembl)ENSG00000132382
Phylogenetic Trees/Animal Genes : TreeFamMYBBP1A
Homologs : HomoloGeneMYBBP1A
Homology/Alignments : Family Browser (UCSC)MYBBP1A
Gene fusions - Rearrangements
Fusion : QuiverMYBBP1A
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerMYBBP1A [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)MYBBP1A
Exome Variant ServerMYBBP1A
GNOMAD BrowserENSG00000132382
Varsome BrowserMYBBP1A
ACMGMYBBP1A variants
Genomic Variants (DGV)MYBBP1A [DGVbeta]
DECIPHERMYBBP1A [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisMYBBP1A 
ICGC Data PortalMYBBP1A 
TCGA Data PortalMYBBP1A 
Broad Tumor PortalMYBBP1A
OASIS PortalMYBBP1A [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICMYBBP1A  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DMYBBP1A
Mutations and Diseases : HGMDMYBBP1A
LOVD (Leiden Open Variation Database)[gene] [transcripts] [variants]
DgiDB (Drug Gene Interaction Database)MYBBP1A
DoCM (Curated mutations)MYBBP1A
CIViC (Clinical Interpretations of Variants in Cancer)MYBBP1A
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry MYBBP1A
NextProtQ9BQG0 [Medical]
Target ValidationMYBBP1A
Huge Navigator MYBBP1A [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTDMYBBP1A
Pharm GKB GenePA31346
Clinical trialMYBBP1A
DataMed IndexMYBBP1A
PubMed189 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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