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TOPORS (topoisomerase I binding, arginine/serine-rich)

Identity

Other namesEC 6.3.2.-
LUN
OTTHUMP00000021182
OTTHUMP00000021184
OTTHUMP00000045227
P53BP3
RP31
TP53BPL
p53BP3
HGNC (Hugo) TOPORS
LocusID (NCBI) 10210
Location 9p21.1
Location_base_pair Starts at 32540542 and ends at 32552626 bp from pter ( according to hg19-Feb_2009)  [Mapping]

DNA/RNA

 
  The two splicing variants of TOPORS are shown. Transcript 1 (ENST00000360538) has three exons, the first one non-coding. Transcript 2 (ENST00000379858) has two exons, the first one non-coding. The coding regions are shown in yellow boxes and the non-coding regions (untranslated regions, UTRs) are shown in open boxes.
Description Spans approximately 8kbs of DNA in the reverse strand of chromosome 9.
Transcription Two splicing variants.
Transcript 1 (ENST00000360538): Transcript length 4145 bps, three exons, first one non-coding.
Transcript 2 (ENST00000379858): Transcript length 3,621 bps, two exons, first one non-coding.
Pseudogene None reported.

Protein

 
  Homology between murine Topors and human TOPORS is shown. The N-terminal Ring-finger (RF, red) and leucine zipper (LZ, green) domains show 93% homology and the C-terminal nuclear localization signal (NLS, blue) domain shows 90% homology between mouse and human. The P53 binding regions of TOPORS, located inside the NLS domain, are highlighted with red lines.
Description TOPORS transcript 1 encodes a protein containing 1,045 amino acids (ENSP00000353735).
TOPORS transcript 2 encodes a protein containing 980 amino acids (ENSP00000369187).
The 1045aa human TOPORS contains a RING family zinc-finger domain and a leucine zipper (LZ) domain in the N-terminal. It also possesses a C-terminal bipartite nuclear localization signal (NLS), five sequences rich in proline, glutamine, serine and threonine (PEST sequences) and an arginine rich domain.
Expression Widely expressed.
Localisation Nucleus.
Function The RING finger protein TOPORS contains a RING family zinc-finger domain, a putative leucine zipper (LZ) domain, five sequences rich in proline, glutamine, serine and threonine (PEST sequences), an arginine/serine (RS) domain and a bipartite nuclear localization signal (NLS).
TOPORS was first identified as a human topoisomerase I-interacting protein by yeast two-hybrid screening (Haluska et al., 1999). TOPORS is localized in the nucleus and has been reported to be closely associated with the PML bodies (Weger et al., 2003; Rasheed et al., 2002).
An important role of TOPORS is its ability to interact with the tumor suppressor protein P53 (Zhou et al., 1999). Forced expression of murine Topors during DNA damage stabilizes p53, enhances the p53-dependent transcriptional activities of p21waf1, MDM2 and Bax promoters and elevates the level of endogenous p21waf1 mRNA (Lin et al., 2005). These findings suggest an anti-oncogenic role for TOPORS. Indeed, it was shown that TOPORS expression is decreased or undetectable in colon adenocarcinomas relative to normal colon tissue, and the protein level of TOPORS is undetected in several colon cancer cell lines (Saleem et al., 2004). Repression of TOPORS expression was also reported in progression and development of non-small cell lung cancer (Oyanagi et al., 2004).
Furthermore, loss of heterozygosity in the region 9p21, the chromosomal locus harboring TOPORS, has been frequently associated with different malignancies (Puig et al., 2005). A high-resolution genomewide mapping study identified deletion of the TOPORS genomic locus in human glial tumors, suggesting a possible role for TOPORS in gliomagenesis (Bredel et al., 2005).
A missense mutation in the TOPORS gene was implicated in autosomal dominant pericentral retinal dystrophy, showing that mutations in the TOPORS gene can lead to genetic disorders (Selmer et al., 2009). Concomitant with these observations, point mutations and small insertions and deletions in the TOPORS gene was found to cause approximately 1% of autosomal dominant retinitis pigmentosa (Bowne et al., 2008). Another study reported that mutations in TOPORS cause autosomal dominant retinitis pigmentosa with perivascular retinal pigment epithelium atrophy (Chakarova et al., 2007).
Valuable information on the cellular roles for TOPORS came through several biochemical studies. It was shown that in the nucleus TOPORS undergoes SUMO-1 modifications (Weger et al., 2003). Interestingly, TOPORS itself has the ability to sumoylate other proteins by functioning as a SUMO-1 E3 ligase. For example, TOPORS can sumoylate p53 and the chromatin modifying protein Sin3A (Shinbo et al., 2005; Weger et al., 2005; Pungaliya et al., 2007). Furthermore, TOPORS induce the accumulation of polysumoylated forms of DNA topoisomerase I in vitro and in vivo (Hammer et al., 2007). Intriguingly, apart from its role as a SUMO-1 E3 ligase, TOPORS can also function as an E3 ubiquitin ligase. In fact, TOPORS was the first example of a protein that possesses dual-roles as an E3 ligase for sumoylation and ubiquitination of other proteins. It was reported that Topors works as an E3 ubiquitin ligase with specific E2 enzymes to ubiquitinate the p53 protein and the prostrate tumor suppressor protein NKX3.1 (Rajendra et al., 2004; Guan et al., 2008). Intense investigations have been undertaken in recent years to elucidate the mechanisms of molecules that have dual E3 ligase activities for sumoylation and ubiquitination such as TOPORS. These studies have discovered a new family of proteins, designated as the small ubiquitin-related modifier (SUMO)-targeted ubiquitin ligases (STUbLs), which directly links sumoylation and ubiquitination (Perry et al., 2008). It has been suggested that similar to STUbLs, TOPORS may be recruited to its targets through SUMO-associated interactions and stimulate their ubiquitination in a RING finger-dependent manner (Perry et al., 2008).
Furthermore, TOPORS has been connected with transcriptional regulation because of its role as an E3 ubiquitin ligase. In drosophila, the homolog of human TOPORS (dTopors) ubiquitinates the Hairy transcriptional repressor, suggesting that TOPORS could be involved in regulating other transcription factors as well (Secombe et al., 2004). Indeed, it was shown that TOPORS interacts with the adeno-associated virus type 2 (AAV-2) Rep78/68 proteins and enhances the expression of a Rep78/68 dependent AAV-2 gene in the absence of the helper virus (Weger et al., 2002). Finally, it was shown that drosophila dTopors was required for the nuclear organization of a chromatin insulator, suggesting a role for TOPORS in regulation of the chromatin (Capelson et al., 2005).
Homology Widely conserved among different species. Murine Topors shows high similarity with human TOPORS.

Mutations

Germinal TOPORS has been implicated in autosomal dominant pericentral retinal dystrophy (adPRD), an atypical form of retinitis pigmentosa. Retinitis pigmentosa is the collective name for a group of genetically induced eye disorders that are frequenctly associated with night blindness and tunnel vision. The TOPORS gene was sequenced in 19 affected members of a large Norwegian family. A novel missense mutation, c.1205a>c, resulting in an amino acid substitution p.Q402P, was found in all of the cases. Furthermore, the mutation showed complete co-segregation with the disease in the family, with the LOD score of 7.3. This mutation was not detected in 207 unrelated and healthy Norwegian subjects (Selmer et al., 2009). A separate study showed that mutations in the TOPORS gene is responsible for autosomal dominant retinitis pigmentosa (adRP). Mutations that included an insertion and a deletion was identified in two adRP-affected families (Chakarova et al., 2007). Finally, another recent study investigated whether mutation(s) in the TOPORS gene is associated with autosomal dominant retinitis pigmentosa (adRP). The frequency of TOPORS mutation was analyzed in an adRP cohort of 215 families and two different mutations, namely, p.Glu808X and p.Arg857GlyfsX9, were identified. This study concluded that point mutations and small insertions or deletions in TOPORS may cause approximately 1% of adRP (Bowne et al., 2008).

Implicated in

Entity Non-small cell lung cancer (NSCLC)
Disease Non-small cell lung cancer (NSCLC) is the major form of lung cancer, with a frequency of 80~90% of all lung carcinomas. NSCLCs are usually classified into three groups, namely, squamous cell carcinoma, adenocarcinoma and large-cell carcinoma. The squamous cell carcinoma is linked with smoking and accounts for approximately 25~30% of all lung cancers, which are usually found in the middle of the lungs or near a bronchus. Adenocarcinoma is frequently spotted in the outer part of the lungs and is thought to be responsible for ~40% of all lung cancers. About 10~15% of lung cancers are large-cell carcinomas, which can start in any part of the lung and has the ability to grow and spread quickly, making this type of lung cancers difficult to treat.
Oncogenesis Expression of TOPORS was found to be significantly repressed in lung cancer tissues compared to normal lung tissues. TOPORS gene expression was slightly down-regulated along with progression of primary tumors, and strongly downregulated along with nodal metastases. Interestingly, in normal tissues TOPORS gene expression was downregulated in smokers (Oyanagi et al., 2004). These findings show that there is a reverse correlation between NSCLC and TOPORS expression and suggest that TOPORS may act as a tumor suppressor gene for lung cancers.
  
Entity Glial brain tumor
Disease Glial brain tumors arise from glial cells and are highly lethal. Glial brain tumors include astrocytomas, oligodendrogliomas and oligoastrocytomas.
Oncogenesis A recent study investigated copy number alterations of 42,000 mapped human cDNA clones in a series of 54 gliomas of varying histogenesis and tumor grade by comparative genomic hybridization technology. This study reported a set of genetic alterations predominantly associated with either astrocytic or oligodendrocytic tumor phenotype. Among these genetic alterations, a minimally deleted region containing the TOPORS gene was identified, suggesting a role for TOPORS in gliomagenesis (Bredel et al., 2005).
  
Entity Colon cancer
Disease Cancerous growth in colon, rectum or the appendix are collectively addressed as colon cancer or colorectal cancer. This is the third most frequent form of cancer and a major cause of cancer-related death all over the world.
Oncogenesis TOPORS expression is decreased or undetected in colon adenocarcinomas compared to normal colon tissues. Furthermore, TOPORS protein is not detectable in several colon cancer cell lines, suggesting an anti-oncogenic role for TOPORS (Saleem et al., 2004).
  
Entity Autosomal dominant retinitis pigmentosa (adRP)
Disease Autosomal dominant retinitis pigmentosa (adRP) is a form of retinitis pigmentosa, a collective title for a group of genetically induced eye disorders that are frequenctly associated with night blindness and tunnel vision.
Prognosis Mutations and small insertions or deletions of the TOPORS gene have been associated with adRP. TOPORS has been associated with autosomal dominant pericentral retinal dystrophy (adPRD), which has a favorable prognosis compared to classical retinitis pigmentosa (RP). A novel missense mutation, c.1205a>c, resulting in an amino acid substitution p.Q402P, was observed in all affected members of a large Norweigian family (Selmer et al., 2009). In another study, an adRP cohort of 215 families was investigated and two different mutations, namely, p.Glu808X and p.Arg857GlyfsX9, were identified (Bowne at al., 2008). TOPORS has also been implicated in autosomal dominant retinitis pigmentosa with perivascular retinal pigment atrophy, a disorder that showed a distinct phenotype at the earlier stage of the disease, with an unusual perivascular cuff of retinal pigment epithelium atrophy, which was found surrounding the superior and inferior arcades in the retina. This study reported mutations in the TOPORS gene that included an insertion and a deletion was identified in two adRP-affected families (Chakarova et al., 2007).
  

External links

Nomenclature
HGNC (Hugo)TOPORS   21653
Cards
AtlasTOPORSID42663ch9p21
Entrez_Gene (NCBI)TOPORS  10210  topoisomerase I binding, arginine/serine-rich, E3 ubiquitin protein ligase
GeneCards (Weizmann)TOPORS
Ensembl (Hinxton)ENSG00000197579 [Gene_View]  chr9:32540542-32552626 [Contig_View]  TOPORS [Vega]
ICGC DataPortalENSG00000197579
AceView (NCBI)TOPORS
Genatlas (Paris)TOPORS
WikiGenes10210
SOURCE (Princeton)NM_001195622 NM_005802
Genomic and cartography
GoldenPath (UCSC)TOPORS  -  9p21.1   chr9:32540542-32552626 -  9p21   [Description]    (hg19-Feb_2009)
EnsemblTOPORS - 9p21 [CytoView]
Mapping of homologs : NCBITOPORS [Mapview]
OMIM609507   609923   
Gene and transcription
Genbank (Entrez)AB045732 AB045733 AF098300 AI934577 AU280552
RefSeq transcript (Entrez)NM_001195622 NM_005802
RefSeq genomic (Entrez)AC_000141 NC_000009 NC_018920 NG_017050 NT_008413 NW_001839149 NW_004929342
Consensus coding sequences : CCDS (NCBI)TOPORS
Cluster EST : UnigeneHs.589962 [ NCBI ]
CGAP (NCI)Hs.589962
Alternative Splicing : Fast-db (Paris)GSHG0030746
Alternative Splicing GalleryENSG00000197579
Gene ExpressionTOPORS [ NCBI-GEO ]     TOPORS [ SEEK ]   TOPORS [ MEM ]
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ9NS56 (Uniprot)
NextProtQ9NS56  [Medical]
With graphics : InterProQ9NS56
Splice isoforms : SwissVarQ9NS56 (Swissvar)
Catalytic activity : Enzyme6.3.2.- [ Enzyme-Expasy ]   6.3.2.-6.3.2.- [ IntEnz-EBI ]   6.3.2.- [ BRENDA ]   6.3.2.- [ KEGG ]   
Domaine pattern : Prosite (Expaxy)ZF_RING_1 (PS00518)    ZF_RING_2 (PS50089)   
Domains : Interpro (EBI)Znf_C3HC4_RING-type    Znf_RING    Znf_RING/FYVE/PHD    Znf_RING_CS   
Related proteins : CluSTrQ9NS56
Domain families : Pfam (Sanger)zf-C3HC4 (PF00097)   
Domain families : Pfam (NCBI)pfam00097   
Domain families : Smart (EMBL)RING (SM00184)  
DMDM Disease mutations10210
Blocks (Seattle)Q9NS56
Human Protein AtlasENSG00000197579
Peptide AtlasQ9NS56
HPRD11642
IPIIPI00396077   IPI00643426   
Protein Interaction databases
DIP (DOE-UCLA)Q9NS56
IntAct (EBI)Q9NS56
FunCoupENSG00000197579
BioGRIDTOPORS
IntegromeDBTOPORS
STRING (EMBL)TOPORS
Ontologies - Pathways
QuickGOQ9NS56
Ontology : AmiGOubiquitin ligase complex  spindle pole  gamma-tubulin complex  DNA binding  antigen binding  ubiquitin-protein transferase activity  ubiquitin-protein transferase activity  protein binding  nucleus  centriole  cytoplasmic dynein complex  transcription, DNA-templated  ubiquitin-dependent protein catabolic process  protein monoubiquitination  cellular response to DNA damage stimulus  zinc ion binding  intrinsic apoptotic signaling pathway in response to DNA damage  retina layer formation  PML body  PML body  nuclear speck  protein sumoylation  protein sumoylation  SUMO ligase activity  SUMO ligase activity  midbody  photoreceptor connecting cilium  protein localization to nucleus  photoreceptor cell outer segment organization  ciliary basal body  regulation of cell proliferation  intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator  negative regulation of apoptotic process  proteasome-mediated ubiquitin-dependent protein catabolic process  DNA topoisomerase binding  positive regulation of transcription, DNA-templated  retinal rod cell development  retinal cone cell development  positive regulation of ubiquitin-protein transferase activity  maintenance of protein location in nucleus  protein K48-linked ubiquitination  
Ontology : EGO-EBIubiquitin ligase complex  spindle pole  gamma-tubulin complex  DNA binding  antigen binding  ubiquitin-protein transferase activity  ubiquitin-protein transferase activity  protein binding  nucleus  centriole  cytoplasmic dynein complex  transcription, DNA-templated  ubiquitin-dependent protein catabolic process  protein monoubiquitination  cellular response to DNA damage stimulus  zinc ion binding  intrinsic apoptotic signaling pathway in response to DNA damage  retina layer formation  PML body  PML body  nuclear speck  protein sumoylation  protein sumoylation  SUMO ligase activity  SUMO ligase activity  midbody  photoreceptor connecting cilium  protein localization to nucleus  photoreceptor cell outer segment organization  ciliary basal body  regulation of cell proliferation  intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator  negative regulation of apoptotic process  proteasome-mediated ubiquitin-dependent protein catabolic process  DNA topoisomerase binding  positive regulation of transcription, DNA-templated  retinal rod cell development  retinal cone cell development  positive regulation of ubiquitin-protein transferase activity  maintenance of protein location in nucleus  protein K48-linked ubiquitination  
Protein Interaction DatabaseTOPORS
Wikipedia pathwaysTOPORS
Gene fusion - rearrangments
Polymorphisms : SNP, mutations, diseases
SNP Single Nucleotide Polymorphism (NCBI)TOPORS
SNP (GeneSNP Utah)TOPORS
SNP : HGBaseTOPORS
Genetic variants : HAPMAPTOPORS
1000_GenomesTOPORS 
ICGC programENSG00000197579 
CONAN: Copy Number AnalysisTOPORS 
Somatic Mutations in Cancer : COSMICTOPORS 
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
LOVD (Leiden Open Variation Database)Eye diseases - LOVD
DECIPHER (Syndromes)9:32540542-32552626
Mutations and Diseases : HGMDTOPORS
OMIM609507    609923   
MedgenTOPORS
GENETestsTOPORS
Disease Genetic AssociationTOPORS
Huge Navigator TOPORS [HugePedia]  TOPORS [HugeCancerGEM]
Genomic VariantsTOPORS  TOPORS [DGVbeta]
Exome VariantTOPORS
dbVarTOPORS
ClinVarTOPORS
snp3D : Map Gene to Disease10210
DGIdb (Curated mutations)TOPORS
DGIdb (Drug Gene Interaction db)TOPORS
General knowledge
Homologs : HomoloGeneTOPORS
Homology/Alignments : Family Browser (UCSC)TOPORS
Phylogenetic Trees/Animal Genes : TreeFamTOPORS
Chemical/Protein Interactions : CTD10210
Chemical/Pharm GKB GenePA134979531
Clinical trialTOPORS
Cancer Resource (Charite)ENSG00000197579
Other databases
Probes
Litterature
PubMed60 Pubmed reference(s) in Entrez
CoreMineTOPORS
GoPubMedTOPORS
iHOPTOPORS

Bibliography

Chromosome 9p deletions in cutaneous malignant melanoma tumors: the minimal deleted region involves markers outside the p16 (CDKN2) gene.
Puig S, Ruiz A, Lazaro C, Castel T, Lynch M, Palou J, Vilalta A, Weissenbach J, Mascaro JM, Estivill X.
Am J Hum Genet. 1995 Aug;57(2):395-402.
PMID 7668266
 
Interaction between human topoisomerase I and a novel RING finger/arginine-serine protein.
Haluska P Jr, Saleem A, Rasheed Z, Ahmed F, Su EW, Liu LF, Rubin EH.
Nucleic Acids Res. 1999 Jun 15;27(12):2538-44.
PMID 10352183
 
Identification of a novel gene encoding a p53-associated protein.
Zhou R, Wen H, Ao SZ.
Gene. 1999 Jul 22;235(1-2):93-101.
PMID 10415337
 
The topoisomerase I-binding RING protein, topors, is associated with promyelocytic leukemia nuclear bodies.
Rasheed ZA, Saleem A, Ravee Y, Pandolfi PP, Rubin EH.
Exp Cell Res. 2002 Jul 15;277(2):152-60.
PMID 12083797
 
Topors, a p53 and topoisomerase I binding protein, interacts with the adeno-associated virus (AAV-2) Rep78/68 proteins and enhances AAV-2 gene expression.
Weger S, Hammer E, Heilbronn R.
J Gen Virol. 2002 Mar;83(Pt 3):511-6.
PMID 11842245
 
Expression of LUN gene that encodes a novel RING finger protein is correlated with development and progression of non-small cell lung cancer.
Oyanagi H, Takenaka K, Ishikawa S, Kawano Y, Adachi Y, Ueda K, Wada H, Tanaka F.
Lung Cancer. 2004 Oct;46(1):21-8.
PMID 15364129
 
Topors functions as an E3 ubiquitin ligase with specific E2 enzymes and ubiquitinates p53.
Rajendra R, Malegaonkar D, Pungaliya P, Marshall H, Rasheed Z, Brownell J, Liu LF, Lutzker S, Saleem A, Rubin EH.
J Biol Chem. 2004 Aug 27;279(35):36440-4. Epub 2004 Jul 9.
PMID 15247280
 
The topoisomerase I- and p53-binding protein topors is differentially expressed in normal and malignant human tissues and may function as a tumor suppressor.
Saleem A, Dutta J, Malegaonkar D, Rasheed F, Rasheed Z, Rajendra R, Marshall H, Luo M, Li H, Rubin EH.
Oncogene. 2004 Jul 8;23(31):5293-300.
PMID 15107820
 
Drosophila Topors is a RING finger-containing protein that functions as a ubiquitin-protein isopeptide ligase for the hairy basic helix-loop-helix repressor protein.
Secombe J, Parkhurst SM.
J Biol Chem. 2004 Apr 23;279(17):17126-33. Epub 2004 Feb 9.
PMID 14871887
 
High-resolution genome-wide mapping of genetic alterations in human glial brain tumors.
Bredel M, Bredel C, Juric D, Harsh GR, Vogel H, Recht LD, Sikic BI.
Cancer Res. 2005 May 15;65(10):4088-96.
PMID 15899798
 
The ubiquitin ligase dTopors directs the nuclear organization of a chromatin insulator.
Capelson M, Corces VG.
Mol Cell. 2005 Oct 7;20(1):105-16.
PMID 16209949
 
topors, a p53 and topoisomerase I-binding RING finger protein, is a coactivator of p53 in growth suppression induced by DNA damage.
Lin L, Ozaki T, Takada Y, Kageyama H, Nakamura Y, Hata A, Zhang JH, Simonds WF, Nakagawara A, Koseki H.
Oncogene. 2005 May 12;24(21):3385-96.
PMID 15735665
 
DJ-1 restores p53 transcription activity inhibited by Topors/p53BP3.
Shinbo Y, Taira T, Niki T, Iguchi-Ariga SM, Ariga H.
Int J Oncol. 2005 Mar;26(3):641-8.
PMID 15703819
 
Topors acts as a SUMO-1 E3 ligase for p53 in vitro and in vivo.
Weger S, Hammer E, Heilbronn R.
FEBS Lett. 2005 Sep 12;579(22):5007-12.
PMID 16122737
 
Mutations in TOPORS cause autosomal dominant retinitis pigmentosa with perivascular retinal pigment epithelium atrophy.
Chakarova CF, Papaioannou MG, Khanna H, Lopez I, Waseem N, Shah A, Theis T, Friedman J, Maubaret C, Bujakowska K, Veraitch B, Abd El-Aziz MM, Prescott de Q, Parapuram SK, Bickmore WA, Munro PM, Gal A, Hamel CP, Marigo V, Ponting CP, Wissinger B, Zrenner E, Matter K, Swaroop A, Koenekoop RK, Bhattacharya SS.
Am J Hum Genet. 2007 Nov;81(5):1098-103. Epub 2007 Sep 26.
PMID 17924349
 
The E3 ligase Topors induces the accumulation of polysumoylated forms of DNA topoisomerase I in vitro and in vivo.
Hammer E, Heilbronn R, Weger S.
FEBS Lett. 2007 Nov 27;581(28):5418-24. Epub 2007 Oct 30.
PMID 17976381
 
TOPORS functions as a SUMO-1 E3 ligase for chromatin-modifying proteins.
Pungaliya P, Kulkarni D, Park HJ, Marshall H, Zheng H, Lackland H, Saleem A, Rubin EH.
J Proteome Res. 2007 Oct;6(10):3918-23. Epub 2007 Sep 6.
PMID 17803295
 
Mutations in the TOPORS gene cause 1% of autosomal dominant retinitis pigmentosa.
Bowne SJ, Sullivan LS, Gire AI, Birch DG, Hughbanks-Wheaton D, Heckenlively JR, Daiger SP.
Mol Vis. 2008 May 19;14:922-7.
PMID 18509552
 
Ubiquitination by TOPORS regulates the prostate tumor suppressor NKX3.1.
Guan B, Pungaliya P, Li X, Uquillas C, Mutton LN, Rubin EH, Bieberich CJ.
J Biol Chem. 2008 Feb 22;283(8):4834-40. Epub 2007 Dec 12.
PMID 18077445
 
A SIM-ultaneous role for SUMO and ubiquitin.
Perry JJ, Tainer JA, Boddy MN.
Trends Biochem Sci. 2008 May;33(5):201-8. Epub 2008 Apr 9. (REVIEW)
PMID 18403209
 
Autosomal dominant pericentral retinal dystrophy caused by a novel missense mutation in the TOPORS gene.
Selmer KK, Grondahl J, Riise R, Brandal K, Braaten O, Bragadottir R, Undlien DE.
Acta Ophthalmol. 2009 Jan 30. [Epub ahead of print]
PMID 19183411
 
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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Contributor(s)

Written03-2009Jafar Sharif, Asami Tsuboi, Haruhiko Koseki
Developmental Genetics Group, RIKEN Center for Allergy and Immunology (RCAI), Suehirocho 1-7-22, Tsurumi-ku, Yokohama-shi, Kanagawa-ken, Japan 230-0045

Citation

This paper should be referenced as such :
Sharif, J ; Tsuboi, A ; Koseki, H
TOPORS (topoisomerase I binding, arginine/serine-rich)
Atlas Genet Cytogenet Oncol Haematol. 2010;14(3):-.
Free online version   Free pdf version   [Bibliographic record ]
URL : http://AtlasGeneticsOncology.org/Genes/TOPORSID42663ch9p21.html

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