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PTBP1 (polypyrimidine tract binding protein 1)

Written2012-02Laura Fontana
Department of Medicine, Surgery, Dentistry, Medical Genetics, Universita degli Studi di Milano, Italy

(Note : for Links provided by Atlas : click)


HGNC Alias symbHNRPI
HGNC Alias nameheterogeneous nuclear ribonucleoprotein I
HGNC Previous namePTB
HGNC Previous namepolypyrimidine tract binding protein (heterogeneous nuclear ribonucleoprotein I)
LocusID (NCBI) 5725
Atlas_Id 46504
Location 19p13.3  [Link to chromosome band 19p13]
Location_base_pair Starts at 797452 and ends at 812312 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping PTBP1.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)
PLEKHH3 (17q21.2)::PTBP1 (19p13.3)PTBP1 (19p13.3)::MALAT1 (11q13.1)PTBP1 (19p13.3)::PTBP1 (19p13.3)
PTBP1 (19p13.3)::TMEM259 (19p13.3)PTBP1 (19p13.3)::UBE3C (7q36.3)


  Shematic representation of PTB mRNA alternative splicing. Alternative splicing of PTB mRNA, as described below, originates four isoforms. Green boxes represent exons and thin black lines represent introns (not to scale).
Description The PTBP1 locus spans 14936 bases on the short arm of chromosome 19 and is composed of 14 exons.
Transcription PTBP1 results from skipping of exon 9 (3203 bp mRNA and 531 amino acid protein). Three additional isoforms are generated by alternative splicing: PTBP2 (3260 bp mRNA and 550 amino acid protein) and PTBP4 (3281 mRNA protein and 557 amino acid protein) derive from exon 9 inclusion using two alternative 3' splice sites, while PTB-T has been reported to result from alternative splicing of exons 2-10 (Sawicka et al., 2004).
Pseudogene PTBP1P (polypyrimidine tract binding protein 1 pseudogene), chromosome location 14q23.3, starts at 65745938 and ends at 65748375 bp from pter (according to hg19-Feb_2009).


  Schematic representation of PTBP1 protein structure. Each RNA recognition motif (RRM) has different binding affinity for pyrimidine-rich sequences on mRNA. The N-terminal domain encloses partially overlapping nuclear localisation (NLS) and export signals (NES). Blue boxes representing RRMs are not drawn to scale.
Description 57 kDa protein belonging to the heterogeneous nuclear ribonucleoprotein family (hnRNP). PTBP1 has four RNA recognition motifs (RRMs) and a conserved N-terminal domain that harbors both nuclear localisation and export signals (NLS and NES). Through the RRMs, PTBP1 binds to the transcript at multiple sites within large pyrimidine tracts leading to conformational changes suitable for functional mRNA processing (Sawicka et al., 2004).
Expression PTBP1 is ubiquitously expressed in human tissues emerging as a pleiotropic splicing regulator. PTBP1 expression levels have been associated with myoblast and neural precursor differentiation through specific modulation of the splicing pattern (Clower et al., 2010). In the brain, in particular, the switch from PTBP1 to nPTB expression drives the differentiation towards the neuronal lineage: PTBP1 is expressed in neural precursors and glial cells, while post-mitotic neurons express only nPTB (Boutz et al., 2007). Recently a strong PTBP1 expression has been found in embryonic stem cells, particularly those in the brain cortex and subventricular zone, where PTBP1 appears essential for cell division after implantation (Shibayama et al., 2009; Suckale et al., 2011).
Localisation PTBP1 shuttles between the nucleus and the cytoplasm. Cytoplasmic localisation is mainly achieved by PKA-mediated phosphorylation of a specific serine residue (Ser-16) within the nuclear localisation signal. Cytoplasmic accumulation of PTB occurs during cell stress (Sawicka et al., 2008). PTBP1 has also been identified as a key component in maintaining the integrity of the perinucleolar compartment, a sub-nuclear structure predominantly found in transformed cells (Wang et al., 2003).
Function PTB was originally identified as a regulator of alternative splicing (Garcia-Blanco et al., 1989) but other roles in mRNA processing have been described (Sawicka et al., 2008).
Alternative splicing regulation: PTBP1 commonly acts as repressor of alternative splicing favouring skipping of alternative exons. Different models of PTBP1 activity have been proposed (Spellman and Smith, 2006): 1) binding competition with the splicing factor U2AF65 at the 3' splice site of alternative exons; 2) polymerization of PTBP1 molecules on the alternative exon masking splicing enhancer sequences; and 3) looping out of alternative exon by PTBP1 binding of flanking intronic sequences. Targets of PTBP1-mediated repression of exon inclusion comprise α-tropomiosin, α-actinin, GABAAγ2 (gamma-aminobutyric acid Aγ2), c-src and FGFR2 (fibroblast growth factor receptor 2) (Li et al., 2007; Spellman et al., 2005). Recent evidences indicate that PTBP1 may also favour exon inclusion depending on the position of its binding sites relative to the target exon. Upon binding to the upstream intron and/or within the exon, PTBP1 represses exon inclusion, while by binding to the downstream intron, it activates exon inclusion. The PTBP1 position-dependent activity relies on the splice site features: in particular included exons show weaker 5' splice sites, whereas skipped exons have longer polypyrimidine tracts (Llorian et al., 2010).
PTBP1 pre-mRNA undergoes PTBP1-mediated alternative splicing too, as part of an autoregulatory feedback loop: high levels of PTBP1 induce skipping of exon 11 and hence mRNA degradation via the nonsense-mediated mRNA decay (Spellman et al., 2005).
3'-end processing: PTBP1 both promotes and inhibits the mRNA 3'-end cleavage required for polyadenylation. PTBP1 may prevent mRNA polyadenylation through competition with the cleavage stimulating factor (CstF), or stimulate polyadenylation by binding to pyrimidine-rich upstream elements (USEs).
mRNA transport: evidences for a role of PTBP1 in mRNA transport come from experiments in Xenopus, where the PTBP1 homologue (VgRBP60) is involved in the localisation of the Vg1 mRNA. In vertebrates PKA-activated PTBP1 is involved in α-actin mRNA localisation at neurite terminals.
mRNA stability: PTBP1 increases the stability of specific transcript by binding to the untraslated regions of mRNA and consequently competing with factors involved in mRNA degradation. Transcripts with PTB-mediated increased stability include those of insulin, VEGF (vascular endothelial growth factor), CD154 (cluster of differentiation 154) and iNOS (inducible nitric oxide synthase).
Viral translation and replication: PTBP1 acts as an ITAF (IRES -internal ribosomal entry site- trans-acting factor) for mRNA translation of virus belonging to the Picornaviridae family and lacking cap structure. PTBP1 seems to have a role as a viral RNA chaperone that stabilizes or alters IRES structure to direct ribosomes to the correct start codon.
IRES-mediated translation: PTBP1 favours cap-independent translation of few cellular RNAs under cell stress, apoptosis or infection through ribosome recruitment to IRES. In this case, PTBP1 cytoplasmic relocalisation is required.
Homology PTBP1 shares 70-80% homology with other two proteins: nPTB (neural PTB), expressed in adult brain, muscle and testis, and ROD1 (regulator of differentiation 1) only expressed in hematopoietic cells. PTB also regulates alternative splicing of its homologues, in particular the nonsense-mediated decay of nPTB transcripts and the non-productive splicing of ROD1 (Sawicka et al., 2008).


Somatic Three synonymous mutations have been reported in cancer samples: c.510C>T (p.A170A) in kidney carcinoma (Dalgliesh et al., 2010), c.1416C>T (p.F472F) in melanoma (Wei et al., 2011) and c.501G>A (p.S167S) in squamous cell carcinoma of the mouth (Stransky et al., 2011). Moreover five missense mutations have been identified in other cancer samples: c.932C>T (p.A311V) in ovarian carcinoma (Cancer Genome Atlas Research Network, 2011), c.413C>T (p.T138I) in skin squamous cell carcinoma (Durinck et al., 2011), c.212C>T (p.T71M), c.666C>G (p.F222L) and c.928G>A (p.G310R) in squamous cell carcinomas of the mouth and larynx (Durinck et al., 2011; Stransky et al., 2011).

Implicated in

Entity Glioma
Note PTBP1 is aberrantly overexpressed in glioma with expression levels correlated with glial cell transformation. The increased expression of PTBP1 contributes to gliomagenesis by deregulating the alternative splicing of genes involved in cell proliferation and migration (McCutcheon et al., 2004; Cheung et al., 2006; Cheung et al., 2009).
FGFR-1 (fibroblast growth factor receptor-1): PTBP1 overexpression increases FGFR-1 α-exon skipping and hence the synthesis of a receptor with higher affinity for fibroblast growth factor, favouring transformed cell growth (Jin et al., 2000).
PKM (pyruvate kinase): PTBP1 overexpression leads to the re-expression of the embryonic pyruvate kinase isoform, PKM2, in transformed glial cells. The switch from PKM1, normally expressed in terminally differentiated cells, to PKM2 is achieved through the PTBP1-mediated inclusion in the PKM mRNA of exon 10, instead of exon 9. In transformed cells PKM2 promotes aerobic glycolysis and proliferation. Recently c-Myc overexpression has been demonstrated to upregulate PTBP1 transcription in transformed glial cells (David et al., 2010).
USP5 (ubiquitin specific peptidase 5): PTBP1 overexpression in GBM forces the expression of USP5 isoform 2, a protein involved in ubiquitination. USP5 isoform 2 has a low activity and favours cell growth and migration (Izaguirre et al., 2011).
Entity Ovarian tumour
Note PTBP1 is overexpressed in the majority of epithelial ovarian tumours and deregulates cell proliferation, anchorage-dependent growth and invasiveness. PTBP1 targets in ovarian transformed cells have not yet been identified (He et al., 2007).
Entity Alzheimer's disease (AD)
Note Recent evidences delineate PTBP1 as a regulator of the amyloid precursor protein (APP) in neurons. In particular, PTBP1 altered expression in neuronal cells, likely mediated by miR-124, enhances the expression of APP isoforms including exon 7 and/or 8. These isoforms have been found enriched in AD patients and associated with β-amyloid production (Smith et al., 2011).


A post-transcriptional regulatory switch in polypyrimidine tract-binding proteins reprograms alternative splicing in developing neurons.
Boutz PL, Stoilov P, Li Q, Lin CH, Chawla G, Ostrow K, Shiue L, Ares M Jr, Black DL.
Genes Dev. 2007 Jul 1;21(13):1636-52.
PMID 17606642
Integrated genomic analyses of ovarian carcinoma.
Cancer Genome Atlas Research Network.
Nature. 2011 Jun 29;474(7353):609-15. doi: 10.1038/nature10166.
PMID 21720365
Polypyrimidine tract binding protein and Notch1 are independently re-expressed in glioma.
Cheung HC, Corley LJ, Fuller GN, McCutcheon IE, Cote GJ.
Mod Pathol. 2006 Aug;19(8):1034-41. Epub 2006 May 26.
PMID 16729017
Splicing factors PTBP1 and PTBP2 promote proliferation and migration of glioma cell lines.
Cheung HC, Hai T, Zhu W, Baggerly KA, Tsavachidis S, Krahe R, Cote GJ.
Brain. 2009 Aug;132(Pt 8):2277-88. Epub 2009 Jun 8.
PMID 19506066
The alternative splicing repressors hnRNP A1/A2 and PTB influence pyruvate kinase isoform expression and cell metabolism.
Clower CV, Chatterjee D, Wang Z, Cantley LC, Vander Heiden MG, Krainer AR.
Proc Natl Acad Sci U S A. 2010 Feb 2;107(5):1894-9. Epub 2010 Jan 19.
PMID 20133837
HnRNP proteins controlled by c-Myc deregulate pyruvate kinase mRNA splicing in cancer.
David CJ, Chen M, Assanah M, Canoll P, Manley JL.
Nature. 2010 Jan 21;463(7279):364-8. Epub 2009 Dec 13.
PMID 20010808
Temporal dissection of tumorigenesis in primary cancers.
Durinck S, Ho C, Wang NJ, Liao W, Jakkula LR, Collisson EA, Pons J, Chan SW, Lam ET, Chu C, Park K, Hong SW, Hur JS, Huh N, Neuhaus IM, Yu SS, Grekin RT, Mauro TM, Cleaver JE, Kwok PY, Leboit PE, Getz G, Cibulskis K, Aster JC, Huang H, Purdom E, Li J, Bolund L, Arron ST, Gray JW, Spellman PT, Cho RJ.
Cancer Discov. 2011 Jul 1;1(2):137-143.
PMID 21984974
Identification and purification of a 62,000-dalton protein that binds specifically to the polypyrimidine tract of introns.
Garcia-Blanco MA, Jamison SF, Sharp PA.
Genes Dev. 1989 Dec;3(12A):1874-86.
PMID 2533575
Knockdown of polypyrimidine tract-binding protein suppresses ovarian tumor cell growth and invasiveness in vitro.
He X, Pool M, Darcy KM, Lim SB, Auersperg N, Coon JS, Beck WT.
Oncogene. 2007 Jul 26;26(34):4961-8. Epub 2007 Feb 19.
PMID 17310993
PTBP1-dependent regulation of USP5 alternative RNA splicing plays a role in glioblastoma tumorigenesis.
Izaguirre DI, Zhu W, Hai T, Cheung HC, Krahe R, Cote GJ.
Mol Carcinog. 2011 Oct 4. doi: 10.1002/mc.20859. [Epub ahead of print]
PMID 21976412
Fibroblast growth factor receptor-1 alpha-exon exclusion and polypyrimidine tract-binding protein in glioblastoma multiforme tumors.
Jin W, McCutcheon IE, Fuller GN, Huang ES, Cote GJ.
Cancer Res. 2000 Mar 1;60(5):1221-4.
PMID 10728679
Neuronal regulation of alternative pre-mRNA splicing.
Li Q, Lee JA, Black DL.
Nat Rev Neurosci. 2007 Nov;8(11):819-31. (REVIEW)
PMID 17895907
Position-dependent alternative splicing activity revealed by global profiling of alternative splicing events regulated by PTB.
Llorian M, Schwartz S, Clark TA, Hollander D, Tan LY, Spellman R, Gordon A, Schweitzer AC, de la Grange P, Ast G, Smith CW.
Nat Struct Mol Biol. 2010 Sep;17(9):1114-23. Epub 2010 Aug 15.
PMID 20711188
Expression of the splicing regulator polypyrimidine tract-binding protein in normal and neoplastic brain.
McCutcheon IE, Hentschel SJ, Fuller GN, Jin W, Cote GJ.
Neuro Oncol. 2004 Jan;6(1):9-14.
PMID 14769134
Polypyrimidine-tract-binding protein: a multifunctional RNA-binding protein.
Sawicka K, Bushell M, Spriggs KA, Willis AE.
Biochem Soc Trans. 2008 Aug;36(Pt 4):641-7. (REVIEW)
PMID 18631133
Polypyrimidine tract-binding protein is essential for early mouse development and embryonic stem cell proliferation.
Shibayama M, Ohno S, Osaka T, Sakamoto R, Tokunaga A, Nakatake Y, Sato M, Yoshida N.
FEBS J. 2009 Nov;276(22):6658-68. Epub 2009 Oct 16.
PMID 19843185
In vivo regulation of amyloid precursor protein neuronal splicing by microRNAs.
Smith P, Al Hashimi A, Girard J, Delay C, Hebert SS.
J Neurochem. 2011 Jan;116(2):240-7. doi: 10.1111/j.1471-4159.2010.07097.x. Epub 2010 Dec 2.
PMID 21062284
Novel modes of splicing repression by PTB.
Spellman R, Smith CW.
Trends Biochem Sci. 2006 Feb;31(2):73-6. Epub 2006 Jan 5.
PMID 16403634
The mutational landscape of head and neck squamous cell carcinoma.
Stransky N, Egloff AM, Tward AD, Kostic AD, Cibulskis K, Sivachenko A, Kryukov GV, Lawrence MS, Sougnez C, McKenna A, Shefler E, Ramos AH, Stojanov P, Carter SL, Voet D, Cortes ML, Auclair D, Berger MF, Saksena G, Guiducci C, Onofrio RC, Parkin M, Romkes M, Weissfeld JL, Seethala RR, Wang L, Rangel-Escareno C, Fernandez-Lopez JC, Hidalgo-Miranda A, Melendez-Zajgla J, Winckler W, Ardlie K, Gabriel SB, Meyerson M, Lander ES, Getz G, Golub TR, Garraway LA, Grandis JR.
Science. 2011 Aug 26;333(6046):1157-60. Epub 2011 Jul 28.
PMID 21798893
PTBP1 is required for embryonic development before gastrulation.
Suckale J, Wendling O, Masjkur J, Jager M, Munster C, Anastassiadis K, Stewart AF, Solimena M.
PLoS One. 2011 Feb 17;6(2):e16992.
PMID 21423341
RNA polymerase III transcripts and the PTB protein are essential for the integrity of the perinucleolar compartment.
Wang C, Politz JC, Pederson T, Huang S.
Mol Biol Cell. 2003 Jun;14(6):2425-35.
PMID 12808040


This paper should be referenced as such :
Fontana, L
PTBP1 (polypyrimidine tract binding protein 1)
Atlas Genet Cytogenet Oncol Haematol. 2012;16(7):492-495.
Free journal version : [ pdf ]   [ DOI ]

Other Leukemias implicated (Data extracted from papers in the Atlas) [ 1 ]
  t(19;19)(p13;p13) PTBP1::TMEM259

External links


HGNC (Hugo)PTBP1   9583
Atlas Explorer : (Salamanque)PTBP1
Entrez_Gene (NCBI)PTBP1    polypyrimidine tract binding protein 1
GeneCards (Weizmann)PTBP1
Ensembl hg19 (Hinxton)ENSG00000011304 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000011304 [Gene_View]  ENSG00000011304 [Sequence]  chr19:797452-812312 [Contig_View]  PTBP1 [Vega]
ICGC DataPortalENSG00000011304
TCGA cBioPortalPTBP1
Genatlas (Paris)PTBP1
SOURCE (Princeton)PTBP1
Genetics Home Reference (NIH)PTBP1
Genomic and cartography
GoldenPath hg38 (UCSC)PTBP1  -     chr19:797452-812312 +  19p13.3   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)PTBP1  -     19p13.3   [Description]    (hg19-Feb_2009)
GoldenPathPTBP1 - 19p13.3 [CytoView hg19]  PTBP1 - 19p13.3 [CytoView hg38]
Genome Data Viewer NCBIPTBP1 [Mapview hg19]  
Gene and transcription
Genbank (Entrez)AB208910 BC002397 BC004383 BC013694 BC023219
RefSeq transcript (Entrez)NM_002819 NM_031990 NM_031991 NM_175847
Consensus coding sequences : CCDS (NCBI)PTBP1
Gene ExpressionPTBP1 [ NCBI-GEO ]   PTBP1 [ EBI - ARRAY_EXPRESS ]   PTBP1 [ SEEK ]   PTBP1 [ MEM ]
Gene Expression Viewer (FireBrowse)PTBP1 [ Firebrowse - Broad ]
GenevisibleExpression of PTBP1 in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)5725
GTEX Portal (Tissue expression)PTBP1
Human Protein AtlasENSG00000011304-PTBP1 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP26599   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP26599  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP26599
Domaine pattern : Prosite (Expaxy)RRM (PS50102)   
Domains : Interpro (EBI)HnRNP-L/PTB    Nucleotide-bd_a/b_plait_sf    PTBP1/2/3_RRM2    PTBP1_RRM    PTBP1_RRM1    PTBP1_RRM3    RBD_domain_sf    RRM_dom   
Domain families : Pfam (Sanger)RRM_1 (PF00076)    RRM_8 (PF11835)   
Domain families : Pfam (NCBI)pfam00076    pfam11835   
Domain families : Smart (EMBL)RRM (SM00360)  
Conserved Domain (NCBI)PTBP1
PDB (RSDB)1QM9    1SJQ    1SJR    2AD9    2ADB    2ADC    2EVZ    2N3O    3ZZY    3ZZZ   
PDB Europe1QM9    1SJQ    1SJR    2AD9    2ADB    2ADC    2EVZ    2N3O    3ZZY    3ZZZ   
PDB (PDBSum)1QM9    1SJQ    1SJR    2AD9    2ADB    2ADC    2EVZ    2N3O    3ZZY    3ZZZ   
PDB (IMB)1QM9    1SJQ    1SJR    2AD9    2ADB    2ADC    2EVZ    2N3O    3ZZY    3ZZZ   
Structural Biology KnowledgeBase1QM9    1SJQ    1SJR    2AD9    2ADB    2ADC    2EVZ    2N3O    3ZZY    3ZZZ   
SCOP (Structural Classification of Proteins)1QM9    1SJQ    1SJR    2AD9    2ADB    2ADC    2EVZ    2N3O    3ZZY    3ZZZ   
CATH (Classification of proteins structures)1QM9    1SJQ    1SJR    2AD9    2ADB    2ADC    2EVZ    2N3O    3ZZY    3ZZZ   
AlphaFold pdb e-kbP26599   
Human Protein Atlas [tissue]ENSG00000011304-PTBP1 [tissue]
Protein Interaction databases
IntAct (EBI)P26599
Ontologies - Pathways
Ontology : AmiGOregulation of alternative mRNA splicing, via spliceosome  RNA binding  mRNA binding  protein binding  nucleus  nucleoplasm  nucleolus  mRNA processing  poly-pyrimidine tract binding  RNA splicing  membrane  negative regulation of RNA splicing  positive regulation of protein dephosphorylation  pre-mRNA binding  regulation of RNA splicing  regulation of cell differentiation  negative regulation of mRNA splicing, via spliceosome  negative regulation of muscle cell differentiation  extracellular exosome  positive regulation of calcineurin-NFAT signaling cascade  IRES-dependent viral translational initiation  IRES-dependent viral translational initiation  
Ontology : EGO-EBIregulation of alternative mRNA splicing, via spliceosome  RNA binding  mRNA binding  protein binding  nucleus  nucleoplasm  nucleolus  mRNA processing  poly-pyrimidine tract binding  RNA splicing  membrane  negative regulation of RNA splicing  positive regulation of protein dephosphorylation  pre-mRNA binding  regulation of RNA splicing  regulation of cell differentiation  negative regulation of mRNA splicing, via spliceosome  negative regulation of muscle cell differentiation  extracellular exosome  positive regulation of calcineurin-NFAT signaling cascade  IRES-dependent viral translational initiation  IRES-dependent viral translational initiation  
REACTOMEP26599 [protein]
REACTOME PathwaysR-HSA-72203 [pathway]   
NDEx NetworkPTBP1
Atlas of Cancer Signalling NetworkPTBP1
Wikipedia pathwaysPTBP1
Orthology - Evolution
GeneTree (enSembl)ENSG00000011304
Phylogenetic Trees/Animal Genes : TreeFamPTBP1
Homologs : HomoloGenePTBP1
Homology/Alignments : Family Browser (UCSC)PTBP1
Gene fusions - Rearrangements
Fusion : MitelmanPTBP1::UBE3C [19p13.3/7q36.3]  
Fusion : FusionHubACTB--PTBP1    ARHGEF18--PTBP1    BSG--PTBP1    C20ORF166--PTBP1    CLK3--PTBP1    CYTH1--PTBP1    DOT1L--PTBP1    EIF2A--PTBP1    ELANE--PTBP1    GALNS--PTBP1   
KDM4B--PTBP1    MCF2L--PTBP1    MUC5AC--PTBP1    OAZ1--PTBP1    PLEKHH3--PTBP1    PNKP--PTBP1    PTBP1--AP3D1    PTBP1--CDC34    PTBP1--COL6A2    PTBP1--D2HGDH   
PTBP1--PER1    PTBP1--PLEKHM3    PTBP1--PPP1R12C    PTBP1--PTBP1    PTBP1--RBBP6    PTBP1--RND3    PTBP1--RNF126    PTBP1--RNF135    PTBP1--SBNO2    PTBP1--SCGB1C1   
PTBP1--SH3GL1    PTBP1--SPOP    PTBP1--UBE3C    SBNO2--PTBP1    SHC2--PTBP1    TPM2--PTBP1    VGLL4--PTBP1   
Fusion : QuiverPTBP1
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerPTBP1 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)PTBP1
Exome Variant ServerPTBP1
GNOMAD BrowserENSG00000011304
Varsome BrowserPTBP1
ACMGPTBP1 variants
Genomic Variants (DGV)PTBP1 [DGVbeta]
DECIPHERPTBP1 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisPTBP1 
ICGC Data PortalPTBP1 
TCGA Data PortalPTBP1 
Broad Tumor PortalPTBP1
OASIS PortalPTBP1 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICPTBP1  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DPTBP1
Mutations and Diseases : HGMDPTBP1
LOVD (Leiden Open Variation Database)[gene] [transcripts] [variants]
DgiDB (Drug Gene Interaction Database)PTBP1
DoCM (Curated mutations)PTBP1
CIViC (Clinical Interpretations of Variants in Cancer)PTBP1
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry PTBP1
NextProtP26599 [Medical]
Target ValidationPTBP1
Huge Navigator PTBP1 [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTDPTBP1
Pharm GKB GenePA33934
Clinical trialPTBP1
DataMed IndexPTBP1
PubMed337 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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