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RNF11 (ring finger protein 11)

Written2013-07Elena Santonico, Anna Mattioni, Alberto Calderone
Department of Biology, University of Rome Tor Vergata, Rome, Italy

(Note : for Links provided by Atlas : click)

Identity

Alias_symbol (synonym)CGI-123
Sid1669p
MGC51169
Other aliasSID1669
HGNC (Hugo) RNF11
LocusID (NCBI) 26994
Atlas_Id 44143
Location 1p32.3  [Link to chromosome band 1p32]
Location_base_pair Starts at 51701945 and ends at 51739119 bp from pter ( according to hg19-Feb_2009)  [Mapping RNF11.png]
Local_order According to NCBI Map Viewer, RNF11 gene is located between: C1orf185 (chromosome 1 open reading frame 185), CFL1P2 (cofilin1 pseudogene 2) (in telomeric position); LOC100422413, EPS15 (epidermal growth factor receptor pathway substrate 15) TTC39A (tetratricopeptide repeat domain 39A) (in centromeric position); the RPS2P8 (ribosomal protein S2 pseudogene 8) sequence maps to the minus strand of the RNF11 gene in opposite transcriptional orientation.
 
  Analysis of the RNF11 genomic context. Adapted from NCBI.
Fusion genes
(updated 2016)
ANKRD11 (16q24.3) / RNF11 (1p32.3)RNF11 (1p32.3) / C8A (1p32.2)RNF11 (1p32.3) / CHD2 (15q26.1)
RNF11 (1p32.3) / FAF1 (1p32.3)RNF11 (1p32.3) / NLRP7 (19q13.42)RNF11 (1p32.3) / RNF11 (1p32.3)
RNF11 (1p32.3) / TMEM61 (1p32.3)STC2 (5q35.1) / RNF11 (1p32.3)XPO5 (6p21.1) / RNF11 (1p32.3)

DNA/RNA

Note According to NCBI Map Viewer, RNF11 gene is located at 51701945 - 51739119 (37175 bp) in human chromosome 1p32.3, plus strand. Unigene cluster Hs.309641, Entrez Gene ID: 26994. The human RNF11 gene is located in a genomic region where frequent alterations, deletions and chromosomal translocations, have been observed in T-cell acute lymphoblastic leukemia (Raimondi, 1993; Seki et al., 1999).
 
  DNA diagram of RNF11 gene. RNF11, Gene ID: 26994, chr: 51701945-51739119. Three exons.
Description In humans, RNF11, the gene coding for RNF11, is located on human chromosome 1p32.3. The coding sequence spans more than 37 kb of genomic DNA, in the telomere-to-centromere orientation.
Transcription The coding region of RNF11 is subdivided in 3 exons and includes additional 0,5 and 2,2 kb of 5' and 3' UTR regions, respectively. The open reading frame includes 465 bp and codes for a protein of 154 amino acids. A very rare transcript encoding a sequence lacking exon 2 has been identified (Kitching et al., 2003). RNA is expressed at low levels in lung, liver, kidney, pancreas, colon, spleen, prostate, thymus, ovary, small intestine and peripheral blood lymphocytes; stronger expression is observed in testes, heart, brain and placenta, while the highest level of RNF11 mRNA is in the skeletal muscle (Kitching et al., 2003). In tumor cell lines the strongest expression of the RNF11 transcript was reported in LnCAP prostate and HTB126 breast tumor cells (Kitching et al., 2003). In human brain RNF11 mRNA is detectable at similar levels in frontal cortex, striatum, hippocampus, pons and medulla (Pranski et al., 2012b). A functional consensus Ets1 transcription factor binding site (EBS) is conserved in the human and mouse RNF11 promoter and data suggest a role of Ets1 factor in RNF11 expression during embryonic bone formation (Gao et al., 2005). The presence of a miR-19 target site in 3' UTR of RNF11 mRNA has been reported. Moreover, it has been demonstrated that miR-19b levels are inversely related with endogenous RNF11 mRNA levels (Gantier et al., 2012; Kumps et al., 2013), clearly indicating an important role for RNF11 in the effect of miR-19b on NF-κB signaling.
Pseudogene No human pseudogene for RNF11 has been identified.

Protein

 
  Cartoon representation of domain organization of RNF11. The WW-binding motif (PPPY) and the RING domain are shown. The asterisks (*) represent the acylated residues, Gly2 and Cys4 respectively.
Description The RNF11 gene encodes for a 154 amino acid 17444 kDa protein (Uniprot Q9Y3C5) that is ubiquitously expressed in human tissues. RNF11 amino acid sequence is strongly evolutionarily conserved. It contains a WW domain binding PPPY motif and a carboxy-terminal RING-H2 domain (C3H2C3-type RING finger), a variant RING finger motif carrying two histidines in place of cysteines. It binds two zinc atoms. The PY motif and the RING-H2 domain mediate protein-protein interactions involved in ubiquitin-mediated pathways. RNF11 interacts with the WW domains of the E3 ubiquitin-ligases NEDD4, ITCH, SMURF2 and WWP1 and it's ubiquitinated by Itch, Smurf2, UBE2D1 and WWP1 (Connor and Seth, 2004; Santonico et al., 2010; Scheper et al., 2009; Subramaniam et al., 2003). The mature protein is anchored to intracellular membranes of the early endosome and the endosome recycling compartments (Santonico et al., 2010). Membrane binding requires two acylation motifs driving the myristoylation of Gly2 and the S-palmitoylation of Cys4. Membrane anchoring via acylation is necessary in order for RNF11 to be post-translationally modified by the addition of several ubiquitin moieties (Santonico et al., 2010). Four serine (Ser) residues have been identified as murine RNF11 phosphorylation sites (Ser7, Ser14, Ser25, Ser54) with differences between different tissues (Phosphomouse database). RNF11 is also phosphorylated on Threonine 135 by PKB/AKT1, promoting degradation by the proteasome (Connor et al., 2005).
Expression The expression of this gene has been shown to be induced by mutant RET proteins (MEN2A/MEN2B). The germline mutations in RET gene are known to be responsible for the development of multiple endocrine neoplasia (MEN). The expression of RNF11 was also induced in TGW human neuroblastoma cells in response to glial cell line-derived neurotrophic factor stimulation (Watanabe et al., 2002). RNF11 is overexpressed in invasive breast cancers, in adenocarcinomas of the pancreas, colon cancer and in bladder tumors (Subramaniam et al., 2003). Intense RNF11 expression was observed in osteoblasts in the mandible, calvarial bones and in the periosteal layer of developing endochondral bones of mouse embrios, while was undetectable in cartilage tissue at any stage of development. The expression of both the RNF11 mRNA and protein was higher in the immature osteoblast than in the mature osteoblast (Gao et al., 2005). RNF11 is variably expressed in neurons and excluded from white matter (Anderson et al., 2007).
Localisation RNF11 is primarly cytoplasmic (early endosome, recycling endosome). Nuclear localization has been detected following phosphorylation by PKB/AKT1 (Connor et al., 2005). The intracellular localization is dependent on the interaction of RNF11 with the GGA protein family of clathrin adaptors, involving the recognition of an N-terminal di-leucine motif in RNF11 by the VHS domain of GGA1 (Santonico et al., 2010).
Function Belongs to the RING E3-ligase protein family. RNF11 interacts with UbcH5 a, b and c, and with Smurf2. The interaction causes ubiquitination of both RNF11 and Smurf2. RNF11 bound to Smurf2 can prevent Smurf2-mediated ubiquitination of the TGFbeta receptor (Azmi and Seth, 2005); accordingly, the overexpression of RNF11 in transfected tumor cells can restore TGFbeta responsiveness (Subramaniam et al., 2003) while RNF11 knock-down abrogates the TGFbeta signal (Colland et al., 2004). RNF11 directly enhances TGF-beta signalling by binding Smad4, the common Smad for TGF-beta, activin and BMP signalling and increasing and/or stabilizing Smad4 steady-state levels (Azmi and Seth, 2009). RNF11 binds WWP1, interfering with its function, and it cooperates with Smurf2 to degrade the de-ubiquitinating enzyme AMSH thus up-regulating EGFR and TGF-beta signalling (Chen et al., 2008; Li and Seth, 2004). RNF11 is an essential component of the A20 ubiquitin-editing complex, comprising also RIP1, ITCH and TAX1BP1, which ensures the transient nature of inflammatory signaling pathways (Jacque and Ley, 2009; Shembade et al., 2009; Verstrepen et al., 2010). RNF11 promotes the association of A20 to RIP1 in a TNF-dependent manner, leading to the inactivation of key signaling molecules. A20 deubiquitinates 'Lys-63' polyubiquitin chains on RIP1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIP1 proteosomal degradation and consequently termination of the TNF- or LPS-mediated activation of NF-kappa-B (Jacque and Ley, 2009; Shembade et al., 2009). RNF11 has been shown to be involved in the regulation of EGFR degradation in the lysosomal compartment, by interacting with SARA and Hrs, both reported to be regulators of endocytic trafficking, on early-, late- and recycling endosome compartments. Data demonstrate that RNF11 and SARA participate structurally and functionally in the ESCRT-dependent lysosomal degradation of EGF receptor (Kostaras et al., 2012).

Mutations

Note An A to G transition (c124-2A>G) mutating the intron 1 acceptor splice site of the RNF11 gene has been identified in bovine RNF11 gene. The RNA product corresponds to a transcript skipping exon 2 and with a frameshift appending illegitimate residues. The protein product is severely truncated (41/154 amino acids) and misses the RING-finger domain (Sartelet et al., 2012).

Implicated in

Note
  
Entity Various cancers
Note RNF11 is overexpressed in invasive breast cancers, in adenocarcinomas of the pancreas, colon cancer and in bladder tumors (Burger et al., 2006; Subramaniam et al., 2003).
  
  
Entity Breast cancer
Note A direct involvement of RNF11 in oncogenesis has not been clearly established. Nevertheless, it has been shown that RNF11 competes with Smad7 in the interaction with Smurf2. Smurf2/Smad7 complex ubiquitinates TβRI leading to degradation of the receptor and TGFβ resistance in cancer cells, thus the interaction of RNF11 with Smurf2 could be important to restore TGFβ signalling. Furthermore, RNF11 also directly interacts with Smad4 and enhances its trans-activation potential (Azmi and Seth, 2005). On the other side, it has also been suggested that RNF11 could stimulate the positive effects of the TGFβ signalling on later tumor progression and metastasis (Subramaniam et al., 2003). Other evidences of a putative function of RNF11 in oncogenesis come from the observation that RNF11 interacts with several proteins, such as E3 ubiquitin ligases and deubiquitinating enzymes, that are involved in oncogenesis. Among them, AMSH (associated moleculate with the SH3 domain of STAM) interacts with RNF11 and has been shown to upregulate BMP/ TGFβ signalling pathway by binding to Smad6 and Smad7. The interaction with RNF11 promotes AMSH degradation, probably mediated by Smurf2/RNF11 complex and therefore abrogates the positive effects of AMSH on TGFβ signalling, leading to cell proliferation and malignant progression.
 
The RNF11 human interactome. RNF11 is involved in direct/enzymatic or indirect interactions with several proteins. The RNF11 human interactome is drawn according to MINT database. RNF11 interactors are clustered according to common biological function. The table below shows the Uniprot code and protein name of each RNF11 binding partner in the interaction network and the PubMed identifier (PMID) describing the interaction. The interactome browser mentha has been used to obtain the graphical representation (mentha: a resource to browse integrated protein interaction networks. In press; http://mentha.uniroma2.it/browser/index.html?ids=Q9Y3C5&org=9606).
  
  
Entity Parkinson's disease (PD)
Note The gene RNF11 is contained within PARK10 and produced a signal of altered expression in PD brains (Noureddine et al., 2005). Moreover, in Parkinson disease, RNF11 is sequestered in Lewy bodies and neuritis. RNF11 is expressed by vulnerable neurons of the substantia nigra and it is involved in the protein degradation pathway mediated by the ubiquitin-proteasome system (UPS), which has been repeatedly suggested as relevant in the etiology of PD (Anderson et al., 2007). RNF11 has been shown to modulate NF-κB signaling in neuroblastoma cells and in primary cortical neurons, indicating a critical role in the regulation of regulating the inflammatory signaling in the central nervous system. Accordingly, depletion of RNF11 increases production of the inflammatory cytokine MCP-1 following TNF-α; activation, resulting in aberrant regulation of inflammatory signaling (Pranski et al., 2012a). Moreover, RNF11 has been shown to be a negative regulator of NF-κB signaling in microglial cell lines and confers protection against LPS-induced cell cytotoxicity (Dalal et al., 2012). Finally, loss of RNF11-mediated inhibition of NF-κB signaling in dopaminergic cells is protective against 6-OHDA toxicity and promotes neuronal survival (Pranski et al., 2013). The effects observed following the reduced expression of RNF11 or the expression of functionally compromised mutants suggest that RNF11 may have a role in neurodegenerative disease pathogenesis and progression.
  
  
Entity Alzheimer disease
Note RNF11 is sequestered in Lewy bodies in human brains with Alzheimer disease with Lewy pathology.
  
  
Entity Regulation of the inflammatory response
Note The splice site variant caused by the A to G transition c124-2A>G has been shown to compromise growth and regulation of the inflammatory response in Belgian Blue Cattle (Sartelet et al., 2012). RNF11 has been shown to negatively regulate NF-κB signaling in human monocytic cell lines by interacting with the A20 ubiquitin-editing complex. Accordingly, depletion of RNF11 causes aberrant regulation of inflammatory signaling (Shembade et al., 2009). Endogenous RNF11 mRNA levels have been reported to be inversely related with miR-19b levels (Gantier et al., 2012; Kumps et al., 2013), clearly indicating an important role for RNF11 in the effect of miR-19b on NF-κB signaling. Finally, RNF11 has been shown to act as negative regulator of the RIG-I/MDA5 pathway and virus-induced IFN-beta production (Charoenthongtrakul et al., 2013).
  

Bibliography

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Kumps C, Fieuw A, Mestdagh P, Menten B, Lefever S, Pattyn F, De Brouwer S, Sante T, Schulte JH, Schramm A, Van Roy N, Van Maerken T, Noguera R, Combaret V, Devalck C, Westermann F, Laureys G, Eggert A, Vandesompele J, De Preter K, Speleman F.
PLoS One. 2013;8(1):e52321. doi: 10.1371/journal.pone.0052321. Epub 2013 Jan 4.
PMID 23308108
 
PARK10 candidate RNF11 is expressed by vulnerable neurons and localizes to Lewy bodies in Parkinson disease brain.
Anderson LR, Betarbet R, Gearing M, Gulcher J, Hicks AA, Stefnsson K, Lah JJ, Levey AI.
J Neuropathol Exp Neurol. 2007 Oct;66(10):955-64.
PMID 17917589
 
RNF11 is a multifunctional modulator of growth factor receptor signalling and transcriptional regulation.
Azmi P, Seth A.
Eur J Cancer. 2005 Nov;41(16):2549-60. Epub 2005 Oct 13. (REVIEW)
PMID 16226459
 
The RING finger protein11 binds to Smad4 and enhances Smad4-dependant TGF-beta signalling.
Azmi PB, Seth AK.
Anticancer Res. 2009 Jun;29(6):2253-63.
PMID 19528490
 
Novel RING E3 ubiquitin ligases in breast cancer.
Burger A, Amemiya Y, Kitching R, Seth AK.
Neoplasia. 2006 Aug;8(8):689-95. (REVIEW)
PMID 16925951
 
RING finger protein 11 targets TBK1/IKKi kinases to inhibit antiviral signaling.
Charoenthongtrakul S, Gao L, Parvatiyar K, Lee D, Harhaj EW.
PLoS One. 2013;8(1):e53717. doi: 10.1371/journal.pone.0053717. Epub 2013 Jan 7.
PMID 23308279
 
The WW domain containing E3 ubiquitin protein ligase 1 upregulates ErbB2 and EGFR through RING finger protein 11.
Chen C, Zhou Z, Liu R, Li Y, Azmi PB, Seth AK.
Oncogene. 2008 Nov 20;27(54):6845-55. doi: 10.1038/onc.2008.288. Epub 2008 Aug 25.
PMID 18724389
 
Functional proteomics mapping of a human signaling pathway.
Colland F, Jacq X, Trouplin V, Mougin C, Groizeleau C, Hamburger A, Meil A, Wojcik J, Legrain P, Gauthier JM.
Genome Res. 2004 Jul;14(7):1324-32.
PMID 15231748
 
Molecular characterization of ring finger protein 11.
Connor MK, Azmi PB, Subramaniam V, Li H, Seth A.
Mol Cancer Res. 2005 Aug;3(8):453-61.
PMID 16123141
 
A central role for the ring finger protein RNF11 in ubiquitin-mediated proteolysis via interactions with E2s and E3s.
Connor MK, Seth A.
Oncogene. 2004 Mar 15;23(11):2089-95. (REVIEW)
PMID 15021896
 
RNF11 modulates microglia activation through NF-kB signalling cascade.
Dalal NV, Pranski EL, Tansey MG, Lah JJ, Levey AI, Betarbet RS.
Neurosci Lett. 2012 Oct 24;528(2):174-9. doi: 10.1016/j.neulet.2012.08.060. Epub 2012 Sep 11.
PMID 22975135
 
A miR-19 regulon that controls NF-kB signaling.
Gantier MP, Stunden HJ, McCoy CE, Behlke MA, Wang D, Kaparakis-Liaskos M, Sarvestani ST, Yang YH, Xu D, Corr SC, Morand EF, Williams BR.
Nucleic Acids Res. 2012 Sep;40(16):8048-58. Epub 2012 Jun 7.
PMID 22684508
 
The RING finger protein RNF11 is expressed in bone cells during osteogenesis and is regulated by Ets1.
Gao Y, Ganss BW, Wang H, Kitching RE, Seth A.
Exp Cell Res. 2005 Mar 10;304(1):127-35. Epub 2004 Dec 13.
PMID 15707580
 
RNF11, a new piece in the A20 puzzle.
Jacque E, Ley SC.
EMBO J. 2009 Mar 4;28(5):455-6. doi: 10.1038/emboj.2009.18.
PMID 19262463
 
The RING-H2 protein RNF11 is differentially expressed in breast tumours and interacts with HECT-type E3 ligases.
Kitching R, Wong MJ, Koehler D, Burger AM, Landberg G, Gish G, Seth A.
Biochim Biophys Acta. 2003 Oct 15;1639(2):104-12.
PMID 14559117
 
SARA and RNF11 interact with each other and ESCRT-0 core proteins and regulate degradative EGFR trafficking.
Kostaras E, Sflomos G, Pedersen NM, Stenmark H, Fotsis T, Murphy C.
Oncogene. 2012 Dec 10. doi: 10.1038/onc.2012.554. [Epub ahead of print]
PMID 23222715
 
Focal DNA copy number changes in neuroblastoma target MYCN regulated genes.
Kumps C, Fieuw A, Mestdagh P, Menten B, Lefever S, Pattyn F, De Brouwer S, Sante T, Schulte JH, Schramm A, Van Roy N, Van Maerken T, Noguera R, Combaret V, Devalck C, Westermann F, Laureys G, Eggert A, Vandesompele J, De Preter K, Speleman F.
PLoS One. 2013;8(1):e52321. doi: 10.1371/journal.pone.0052321. Epub 2013 Jan 4.
PMID 23308108
 
An RNF11: Smurf2 complex mediates ubiquitination of the AMSH protein.
Li H, Seth A.
Oncogene. 2004 Mar 11;23(10):1801-8.
PMID 14755250
 
RING finger protein 11 (RNF11) modulates susceptibility to 6-OHDA-induced nigral degeneration and behavioral deficits through NF-kB signaling in dopaminergic cells.
Pranski EL, Dalal NV, Sanford CV, Herskowitz JH, Gearing M, Lazo C, Miller GW, Lah JJ, Levey AI, Betarbet RS.
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Current status of cytogenetic research in childhood acute lymphoblastic leukemia.
Raimondi SC.
Blood. 1993 May 1;81(9):2237-51. (REVIEW)
PMID 8481506
 
Multiple modification and protein interaction signals drive the Ring finger protein 11 (RNF11) E3 ligase to the endosomal compartment.
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Oncogene. 2010 Oct 14;29(41):5604-18. doi: 10.1038/onc.2010.294. Epub 2010 Aug 2.
PMID 20676133
 
A splice site variant in the bovine RNF11 gene compromises growth and regulation of the inflammatory response.
Sartelet A, Druet T, Michaux C, Fasquelle C, Géron S, Tamma N, Zhang Z, Coppieters W, Georges M, Charlier C.
PLoS Genet. 2012;8(3):e1002581. doi: 10.1371/journal.pgen.1002581. Epub 2012 Mar 15.
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Analysis of electrostatic contributions to the selectivity of interactions between RING-finger domains and ubiquitin-conjugating enzymes.
Scheper J, Oliva B, Vill-Freixa J, Thomson TM.
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Cloning and expression profile of mouse and human genes, Rnf11/RNF11, encoding a novel RING-H2 finger protein.
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Biochim Biophys Acta. 1999 Dec 23;1489(2-3):421-7.
PMID 10673045
 
The ubiquitin-editing enzyme A20 requires RNF11 to downregulate NF-kappaB signalling.
Shembade N, Parvatiyar K, Harhaj NS, Harhaj EW.
EMBO J. 2009 Mar 4;28(5):513-22. doi: 10.1038/emboj.2008.285. Epub 2009 Jan 8.
PMID 19131965
 
The RING-H2 protein RNF11 is overexpressed in breast cancer and is a target of Smurf2 E3 ligase.
Subramaniam V, Li H, Wong M, Kitching R, Attisano L, Wrana J, Zubovits J, Burger AM, Seth A.
Br J Cancer. 2003 Oct 20;89(8):1538-44.
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PMID 20599425
 
Characterization of gene expression induced by RET with MEN2A or MEN2B mutation.
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Am J Pathol. 2002 Jul;161(1):249-56.
PMID 12107109
 

Citation

This paper should be referenced as such :
Santonico, E ; Mattioni, A ; Calderone, A
RNF11 (ring finger protein 11)
Atlas Genet Cytogenet Oncol Haematol. 2014;18(2):112-116.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/RNF11ID44143ch1p32.html


External links

Nomenclature
HGNC (Hugo)RNF11   10056
Cards
AtlasRNF11ID44143ch1p32
Entrez_Gene (NCBI)RNF11  26994  ring finger protein 11
AliasesCGI-123; SID1669
GeneCards (Weizmann)RNF11
Ensembl hg19 (Hinxton)ENSG00000123091 [Gene_View]  chr1:51701945-51739119 [Contig_View]  RNF11 [Vega]
Ensembl hg38 (Hinxton)ENSG00000123091 [Gene_View]  chr1:51701945-51739119 [Contig_View]  RNF11 [Vega]
ICGC DataPortalENSG00000123091
TCGA cBioPortalRNF11
AceView (NCBI)RNF11
Genatlas (Paris)RNF11
WikiGenes26994
SOURCE (Princeton)RNF11
Genetics Home Reference (NIH)RNF11
Genomic and cartography
GoldenPath hg19 (UCSC)RNF11  -     chr1:51701945-51739119 +  1p32   [Description]    (hg19-Feb_2009)
GoldenPath hg38 (UCSC)RNF11  -     1p32   [Description]    (hg38-Dec_2013)
EnsemblRNF11 - 1p32 [CytoView hg19]  RNF11 - 1p32 [CytoView hg38]
Mapping of homologs : NCBIRNF11 [Mapview hg19]  RNF11 [Mapview hg38]
OMIM612598   
Gene and transcription
Genbank (Entrez)AA224090 AB024703 AF151881 AI817633 AK293047
RefSeq transcript (Entrez)NM_014372
RefSeq genomic (Entrez)NC_000001 NC_018912 NT_032977 NW_004929290
Consensus coding sequences : CCDS (NCBI)RNF11
Cluster EST : UnigeneHs.309641 [ NCBI ]
CGAP (NCI)Hs.309641
Alternative Splicing GalleryENSG00000123091
Gene ExpressionRNF11 [ NCBI-GEO ]   RNF11 [ EBI - ARRAY_EXPRESS ]   RNF11 [ SEEK ]   RNF11 [ MEM ]
Gene Expression Viewer (FireBrowse)RNF11 [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)26994
GTEX Portal (Tissue expression)RNF11
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ9Y3C5   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ9Y3C5  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ9Y3C5
Splice isoforms : SwissVarQ9Y3C5
PhosPhoSitePlusQ9Y3C5
Domaine pattern : Prosite (Expaxy)ZF_RING_2 (PS50089)   
Domains : Interpro (EBI)Znf_RING    Znf_RING/FYVE/PHD   
Domain families : Pfam (Sanger)zf-RING_2 (PF13639)   
Domain families : Pfam (NCBI)pfam13639   
Domain families : Smart (EMBL)RING (SM00184)  
Conserved Domain (NCBI)RNF11
DMDM Disease mutations26994
Blocks (Seattle)RNF11
SuperfamilyQ9Y3C5
Human Protein AtlasENSG00000123091
Peptide AtlasQ9Y3C5
HPRD09955
IPIIPI00003894   
Protein Interaction databases
DIP (DOE-UCLA)Q9Y3C5
IntAct (EBI)Q9Y3C5
FunCoupENSG00000123091
BioGRIDRNF11
STRING (EMBL)RNF11
ZODIACRNF11
Ontologies - Pathways
QuickGOQ9Y3C5
Ontology : AmiGOubiquitin ligase complex  DNA binding  ubiquitin-protein transferase activity  protein binding  nucleus  early endosome  zinc ion binding  protein ubiquitination involved in ubiquitin-dependent protein catabolic process  protein autoubiquitination  recycling endosome  extracellular exosome  
Ontology : EGO-EBIubiquitin ligase complex  DNA binding  ubiquitin-protein transferase activity  protein binding  nucleus  early endosome  zinc ion binding  protein ubiquitination involved in ubiquitin-dependent protein catabolic process  protein autoubiquitination  recycling endosome  extracellular exosome  
NDEx NetworkRNF11
Atlas of Cancer Signalling NetworkRNF11
Wikipedia pathwaysRNF11
Orthology - Evolution
OrthoDB26994
GeneTree (enSembl)ENSG00000123091
Phylogenetic Trees/Animal Genes : TreeFamRNF11
HOVERGENQ9Y3C5
HOGENOMQ9Y3C5
Homologs : HomoloGeneRNF11
Homology/Alignments : Family Browser (UCSC)RNF11
Gene fusions - Rearrangements
Fusion : MitelmanRNF11/C8A [1p32.3/1p32.2]  
Fusion : MitelmanRNF11/TMEM61 [1p32.3/1p32.3]  [t(1;1)(p32;p32)]  
Fusion : MitelmanSTC2/RNF11 [5q35.1/1p32.3]  [t(1;5)(p32;q35)]  
Fusion: TCGARNF11 1p32.3 C8A 1p32.2 OV
Fusion: TCGARNF11 1p32.3 TMEM61 1p32.3 BRCA
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerRNF11 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)RNF11
dbVarRNF11
ClinVarRNF11
1000_GenomesRNF11 
Exome Variant ServerRNF11
ExAC (Exome Aggregation Consortium)RNF11 (select the gene name)
Genetic variants : HAPMAP26994
Genomic Variants (DGV)RNF11 [DGVbeta]
DECIPHER (Syndromes)1:51701945-51739119  ENSG00000123091
CONAN: Copy Number AnalysisRNF11 
Mutations
ICGC Data PortalRNF11 
TCGA Data PortalRNF11 
Broad Tumor PortalRNF11
OASIS PortalRNF11 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICRNF11  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDRNF11
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch RNF11
DgiDB (Drug Gene Interaction Database)RNF11
DoCM (Curated mutations)RNF11 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)RNF11 (select a term)
intoGenRNF11
NCG5 (London)RNF11
Cancer3DRNF11(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM612598   
Orphanet
MedgenRNF11
Genetic Testing Registry RNF11
NextProtQ9Y3C5 [Medical]
TSGene26994
GENETestsRNF11
Huge Navigator RNF11 [HugePedia]
snp3D : Map Gene to Disease26994
BioCentury BCIQRNF11
ClinGenRNF11
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD26994
Chemical/Pharm GKB GenePA34420
Clinical trialRNF11
Miscellaneous
canSAR (ICR)RNF11 (select the gene name)
Probes
Litterature
PubMed38 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineRNF11
EVEXRNF11
GoPubMedRNF11
iHOPRNF11
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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