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TRIM27 (tripartite motif containing 27)

Written2014-07Georgia Zoumpoulidou, Sibylle Mittnacht
UCL Cancer Institute, University College London, 72 Huntley Street, WC1E 6DD, London, UK

(Note : for Links provided by Atlas : click)

Identity

Alias_namesRFP
ret finger protein
tripartite motif-containing 27
Alias_symbol (synonym)RNF76
Other alias
HGNC (Hugo) TRIM27
LocusID (NCBI) 5987
Atlas_Id 42092
Location 6p22.1  [Link to chromosome band 6p22]
Location_base_pair Starts at 28903002 and ends at 28923991 bp from pter ( according to hg19-Feb_2009)  [Mapping TRIM27.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)
RET (10q11.21) / TRIM27 (6p22.1)TRIM27 (6p22.1) / MDM2 (12q15)TRIM27 (6p22.1) / RET (10q11.21)

DNA/RNA

Description The unprocessed TRIM27 transcript spans 20.990 kb and is organised in 8 exons. Reporter construct studies suggest the presence of elements between -365 and -68 relative to the transcription start point to be sufficient to drive basal gene transcription. This promoter region is GC rich and has no typical TATA and CAAT boxes (Iwata et al., 1999).
Transcription Alternative splicing of the human locus may generate 7 or more processed alternative transcripts. Three of these transcripts contain open reading frames and presumably give rise to protein products (Ensembl).
Transcript 1: 2969 bps (transcript ID ENST00000377199, protein encoding, protein ID ENSP00000366404);
Transcript 2: 2704 bps (transcript ID ENST00000377194, protein encoding, protein ID ENSP00000366399);
Transcript 3: 1813 bps (transcript ID ENST00000414543, protein encoding, protein ID ENSP00000400058);
Transcript 4: 7006 bps (transcript ID ENST00000481474, processed transcript without open reading frame);
Transcript 5: 687 bps (transcript ID ENST00000496091, processed transcript without open reading frame);
Transcript 6: 541 bps (transcript ID ENST00000467742, processed transcripts without open reading frame);
Transcript 7: 7006 bps (transcript ID ENST00000481474, retains intronic sequence relative to other coding transcripts, without open reading frame).
Pseudogene There are no reported pseudogenes of TRIM27.

Protein

 
  Schematic diagram of TRIM27 protein. The domain structure of the three TRIM27 protein isoforms (i-iii) and a ribbon diagram of the structure of TRIM27 domains which represents a high confidence model generated by Phyre2 (http://www.sbg.bio.ic.ac.uk/phyre2/html/page.cgi?id=index). NH2, Amino-terminal region; COOH, Carboxyl-terminal region.
Description The longest isoform 1 of TRIM27 (protein ID ENSP00000366404) encodes a 513 amino acids protein with a molecular weight of 58 KDa; displaying the so-called tripartite/RBCC motif within its N-terminal region, composed of a RING type zinc finger (InterPro ID IPR001841) (aa 16-57), a B-box type zinc finger (InterPro ID001841) (aa 96-127) and coiled-coil domains (aa 132-172 and aa 282-311), and a B30.2/PRY-SPRY domain (InterPro ID IPR001870) within its C-terminal region (aa 298-492). The RING finger may be involved in mediating protein-protein interactions and may confer ubiquitin family ligase activity. TRIM27 can form homo and hetero-oligomeric assemblies mediated by the centrally located coiled-coil domain (Cao et al., 1997). Isoform 2 (protein ID ENSP00000366399) lacks the C-terminal SPRY domain. Isoform 3 (protein ID ENSP00000400058) encodes the B30.2/PRY-SPRY domain only. The diagram above is a scheme of the protein isoforms and their domains.
Expression TRIM27 transcripts and protein is ubiquitous in day 10.5-13.5 mouse embryos. Expression is restricted in adult mice, with the highest level of expression in pachytene spermatocytes and round spermatids of differentiating sperm (Cao et al., 1996; Tezel et al., 1999). TRIM27 is also expressed in mouse spleen, thymus, cerebrum and cerebellum. TRIM27 is expressed in various human and rodent cell lines. Based on RNAseq., TRIM27 mRNA is detected widely in human tissues, with no evidence for absence. Expression levels between tissues are similar, including testes, with comparative expression rating of low to medium across tissues (Human Protein Atlas).
Localisation The protein localizes to the nucleus, cytoplasm and in nuclear bodies (NB) associated with the nuclear matrix (Isomura et al., 1992). Nuclear export of RFP is dependent on a functional NES, which can be activated by protein kinase C (PKC) (Harbers et al., 2001). Hetero-oligomerization has been observed between TRIM27 and TRIM19 with the recruitment of TRIM27 to the promyelocytic leukaemia nuclear bodies (PMLs) (Cao et al., 1998). Furthermore, interaction with members of the protein inhibitors of activated STAT (PIAS) family targets TRIM27 to subnuclear compartments/NBs, involving TRIM27 sumoylation (Matsuura et al., 2005). Nuclear or cytoplasmic localisation depends on the cell type or tissue.
Function A role for TRIM27 has been reported in transcriptional regulation through interaction with retinoblastoma protein (RB1) and the Mi-2b-containing histone deacetylase complex in the nucleus (Krutzfeldt et al., 2005; Shimono et al., 2005), in transcriptional repression through interaction with the enhancer of polycomb protein (EPC) (Shimono et al., 2000; Bloor et al., 2005) and MBD proteins (Fukushige et al., 2006), in the negative regulation of NF-kB and IFN-signaling pathways (Zha et al., 2006), in the positive regulation of apoptosis through activation of Jun N-terminal kinase (JNK) (Dho and Kwon, 2003) and augmentation of TNF alpha receptor activation (Zaman et al., 2013), and in cell cycle regulation (Patel and Ghiselli, 2005) suggesting that TRIM27 is involved in the control of multiple cellular processes. TRIM27 has been shown to confer E3 ubiquitin ligase activity with the enzymes UBE2D1 and UBE2D3 (Napolitano et al., 2011) and to possess SUMO E3 ligase activity (Chu and Yang, 2011). TRIM27 regulates innate immune responses by physical interaction with NOD2. So, TRIM27 mediates K48-linked ubiquitination and subsequent proteasomal degradation of NOD2 (Zurek et al., 2012). TRIM27 has a critical role in regulating PTEN phosphatase activity through ubiquitination which inhibits PTEN increasing AKT signalling (Lee et al., 2013). TRIM27 functions as an E3 ligase to ubiquitinate and inhibit PI3K-C2beta's kinase activity and negatively regulates CD4 T cells (Cai et al., 2011). TRIM27 also negatively regulates IgE receptor activation and downstream signalling by the same mechanism (Srivastava et al., 2012). TRIM27 interacts with MAGE-L2 protein and ubiquitination of WASH K220 by MAGE-L2-TRIM27 is required for endosomal F-actin nucleation and retrograde transport (Hao et al., 2013). MRTF-B/TRIM27 complex plays a role in the regulation of integrin b1 expression via Rho and miR-124 in Leading Cells (LCs) among migrating cancer cell groups following loss of intracellular adhension (Kato et al., 2014).
Homology H. sapiens, TRIM27 tripartite motif containing 27, 513 aa.
P. troglodytes (chimpanzee), TRIM27 tripartite motif containing 27, 513 aa (XP_001140726.2).
M. mulatta, TRIM27 tripartite motif containing 27, 513 aa (XP_001094465.2).
C. lupus, TRIM27 tripartite motif containing 27, 487 aa (XP_005642504.1).
B. taurus, TRIM27 tripartite motif containing 27, 513 aa (XP_001069267.1).
M. musculus, Trim27 tripartite motif containing 27, 513 aa (NP_033080.2).
R. norvegicus, Trim27 tripartite motif containing 27, 513 aa (NP_001128446.1).
G. gallus, TRIM27 tripartite motif containing 27, 505 aa (NP_001092824.1).
With other RING finger/B box proteins.

Mutations

 
  TRIM27 mutations identified in cancer.
Germinal No germinal mutations described for TRIM27.
Somatic TRIM27 have been identified in cancer tissues by large scale tumour genome sequencing at low frequency (see table above). COSMIC lists 26 mutations from sequence analysis of 8960 cancers (mutation rate 0.29%). Mutation spectrum: one nonrecurrent, 8 synonymous substitutions, one nonsense mutation, 16 nonsynonymous missense substitutions mostly leading to conservative aminoacid changes. Evidence is not available at present whether these observed mutations affect function of TRIM27 or confer selective advantage to tumour cells (COSMIC).

Implicated in

Note
  
Entity Thyroid papillary carcinoma (TPC)
Disease A chromosomal translocation involving TRIM27/RFP is found in human thyroid papillary carcinomas. TPC is the most common cancer of the thyroid gland that usually begins as a small irregular solid lump (nodule) in the thyroid gland. Classical papillary carcinoma is characterised by the formation of papillae and a set of distinctive nuclear features (optically clear appearance, overlapping, pseudo-inclusions and nuclear grooves) (Rosai et al., 1992).
Cytogenetics t(6;10)(p21.3;q11.2)
Hybrid/Mutated Gene TRIM27-RET; deltaTRIM27-RET.
Abnormal Protein Fusion of the N-terminus tripartite motif of TRIM27 with the truncated C-terminus tyrosine kinase domain of the c-ret proto-oncogene result in production of the ret transforming protein (Hasegawa et al., 1996; Saenko et al., 2003). The level of catalytic activity of the hybrid TRIM27-RET protein is higher than that of RET alone (Kato et al., 2000).
  
  
Entity Lung cancer
Note TRIM27 mRNA or protein is highly expressed in human lung cancers. In a study that uses a cancer-profiling array containing tumour cRNA alongside cRNA from paired tissue, TRIM27 expression was found to be significantly increased in lung cancers versus normal tissue (Zoumpoulidou et al., 2012). TRIM27 expression is associated with poor prognosis of lung cancers with EGFR mutations suggesting that TRIM27 status might be associated with response to anticancer therapy in EGFR-mutated lung cancers (Iwakoshi et al., 2012).
  
  
Entity Endometrial cancer
Note Positive TRIM27 expression in human endometrial cancer cells is correlated with poor clinical outcome in patients (Tsukamoto et al., 2009). Immunohistochemical analysis of TRIM27 expression in non-neoplastic endometrium samples as well as type I endometrial cancer in comparison to type II endometrial cancer has shown that TRIM27 positive expression was strongly correlated with serous carcinoma morphology (Tezel et al., 2012).
  
  
Entity Breast cancer
Note Analysis of TRIM27 expression by Townson et al. revealed TRIM27 is expressed in breast cancer derived cell lines regardless of estrogen receptor (ER) status. However, it is not clear to what extend TRIM27 is involved in breast tumorigenesis (Townson et al., 2006). In a tissue microarray (TMA) study, TRIM27 protein expression was found in breast carcinomas but not in benign breast tissues. TRIM27 expression also correlates with ERBB2 protein expression and ERBB2 gene amplification, which is a marker for poor prognosis in breast cancer (Tezel et al., 2009). However, the biological significance of this correlation is not known.
  
  
Entity Ovarian cancer
Note Immunohistochemical analysis of TRIM27 expression in epithelial ovarian cancer shows that TRIM27 expression significantly correlates with chemoresistance in ovarian cancer patients. In addition, positive TRIM27 staining was increased in recurrent ovarian cancer, correlating with a poor outcome of the patients. TRIM27 protein expression was significantly higher in platinum-resistant than in platinum-sensitive patients (Horio et al., 2012). Recombinant TRIM27 expression enhances chemoresistance of ovarian cancer cells to carboplatin and paclitaxel in culture and xenografts (Horio et al., 2012).
  
  
Entity Murine squamous carcinoma of the skin
Note TRIM27 is highly expressed in chemically induced squamous cell carcinomas (SCC) in the mouse after exposure of the skin to the carcinogen 7, 12-dimethylbenzanthracene (DMBA)/12-O-tetradecanoylphorbol-13-acetate (TPA), as part of a two-step carcinogenesis model. Trim27 expression peaks in early mouse cancer development (Zoumpoulidou et al., 2012). Moreover, mice with TRIM27 deletion are resistant to development of chemically induced SSC (Zoumpoulidou et al., 2012).
  

Bibliography

RFP represses transcriptional activation by bHLH transcription factors.
Bloor AJ, Kotsopoulou E, Hayward P, Champion BR, Green AR.
Oncogene. 2005 Oct 13;24(45):6729-36.
PMID 16007160
 
Tripartite motif containing protein 27 negatively regulates CD4 T cells by ubiquitinating and inhibiting the class II PI3K-C2beta.
Cai X, Srivastava S, Sun Y, Li Z, Wu H, Zuvela-Jelaska L, Li J, Salamon RS, Backer JM, Skolnik EY.
Proc Natl Acad Sci U S A. 2011 Dec 13;108(50):20072-7. doi: 10.1073/pnas.1111233109. Epub 2011 Nov 29.
PMID 22128329
 
Involvement of the rfp tripartite motif in protein-protein interactions and subcellular distribution.
Cao T, Borden KL, Freemont PS, Etkin LD.
J Cell Sci. 1997 Jul;110 ( Pt 14):1563-71.
PMID 9247190
 
Ret finger protein is a normal component of PML nuclear bodies and interacts directly with PML.
Cao T, Duprez E, Borden KL, Freemont PS, Etkin LD.
J Cell Sci. 1998 May;111 ( Pt 10):1319-29.
PMID 9570750
 
Mouse ret finger protein (rfp) proto-oncogene is expressed at specific stages of mouse spermatogenesis.
Cao T, Shannon M, Handel MA, Etkin LD.
Dev Genet. 1996;19(4):309-20.
PMID 9023983
 
SUMO E3 ligase activity of TRIM proteins.
Chu Y, Yang X.
Oncogene. 2011 Mar 3;30(9):1108-16. doi: 10.1038/onc.2010.462. Epub 2010 Oct 25.
PMID 20972456
 
The Ret finger protein induces apoptosis via its RING finger-B box-coiled-coil motif.
Dho SH, Kwon KS.
J Biol Chem. 2003 Aug 22;278(34):31902-8. Epub 2003 Jun 13.
PMID 12807881
 
RET finger protein enhances MBD2- and MBD4-dependent transcriptional repression.
Fukushige S, Kondo E, Gu Z, Suzuki H, Horii A.
Biochem Biophys Res Commun. 2006 Dec 8;351(1):85-92. Epub 2006 Oct 10.
PMID 17049487
 
Regulation of WASH-dependent actin polymerization and protein trafficking by ubiquitination.
Hao YH, Doyle JM, Ramanathan S, Gomez TS, Jia D, Xu M, Chen ZJ, Billadeau DD, Rosen MK, Potts PR.
Cell. 2013 Feb 28;152(5):1051-64. doi: 10.1016/j.cell.2013.01.051.
PMID 23452853
 
Intracellular localization of the Ret finger protein depends on a functional nuclear export signal and protein kinase C activation.
Harbers M, Nomura T, Ohno S, Ishii S.
J Biol Chem. 2001 Dec 21;276(51):48596-607. Epub 2001 Oct 8.
PMID 11591718
 
A RING finger motif regulates transforming activity of the rfp/ret fusion gene.
Hasegawa N, Iwashita T, Asai N, Murakami H, Iwata Y, Isomura T, Goto H, Hayakawa T, Takahashi M.
Biochem Biophys Res Commun. 1996 Aug 14;225(2):627-31.
PMID 8753810
 
Expression of RET finger protein predicts chemoresistance in epithelial ovarian cancer.
Horio M, Kato T, Mii S, Enomoto A, Asai M, Asai N, Murakumo Y, Shibata K, Kikkawa F, Takahashi M.
Cancer Med. 2012 Oct;1(2):218-29. doi: 10.1002/cam4.32. Epub 2012 Sep 13.
PMID 23342271
 
RFP is a DNA binding protein associated with the nuclear matrix.
Isomura T, Tamiya-Koizumi K, Suzuki M, Yoshida S, Taniguchi M, Matsuyama M, Ishigaki T, Sakuma S, Takahashi M.
Nucleic Acids Res. 1992 Oct 25;20(20):5305-10.
PMID 1437549
 
RET finger protein expression is associated with prognosis in lung cancer with epidermal growth factor receptor mutations.
Iwakoshi A, Murakumo Y, Kato T, Kitamura A, Mii S, Saito S, Yatabe Y, Takahashi M.
Pathol Int. 2012 May;62(5):324-30. doi: 10.1111/j.1440-1827.2012.02797.x. Epub 2012 Mar 27.
PMID 22524660
 
Characterization of the promoter region of the human RFP gene.
Iwata Y, Nakayama A, Murakami H, Iida K, Iwashita T, Asai N, Takahashi M.
Biochem Biophys Res Commun. 1999 Aug 2;261(2):381-4.
PMID 10425194
 
Molecular mechanism of activation and superactivation of Ret tyrosine kinases by ultraviolet light irradiation.
Kato M, Iwashita T, Akhand AA, Liu W, Takeda K, Takeuchi K, Yoshihara M, Hossain K, Wu J, Du J, Oh C, Kawamoto Y, Suzuki H, Takahashi M, Nakashima I.
Antioxid Redox Signal. 2000 Winter;2(4):841-9. (REVIEW)
PMID 11213488
 
TRIM27/MRTF-B-dependent integrin beta1 expression defines leading cells in cancer cell collectives.
Kato T, Enomoto A, Watanabe T, Haga H, Ishida S, Kondo Y, Furukawa K, Urano T, Mii S, Weng L, Ishida-Takagishi M, Asai M, Asai N, Kaibuchi K, Murakumo Y, Takahashi M.
Cell Rep. 2014 May 22;7(4):1156-67. doi: 10.1016/j.celrep.2014.03.068. Epub 2014 May 1.
PMID 24794433
 
Selective ablation of retinoblastoma protein function by the RET finger protein.
Krutzfeldt M, Ellis M, Weekes DB, Bull JJ, Eilers M, Vivanco MD, Sellers WR, Mittnacht S.
Mol Cell. 2005 Apr 15;18(2):213-24.
PMID 15837424
 
RFP-mediated ubiquitination of PTEN modulates its effect on AKT activation.
Lee JT, Shan J, Zhong J, Li M, Zhou B, Zhou A, Parsons R, Gu W.
Cell Res. 2013 Apr;23(4):552-64. doi: 10.1038/cr.2013.27. Epub 2013 Feb 19.
PMID 23419514
 
PIAS proteins are involved in the SUMO-1 modification, intracellular translocation and transcriptional repressive activity of RET finger protein.
Matsuura T, Shimono Y, Kawai K, Murakami H, Urano T, Niwa Y, Goto H, Takahashi M.
Exp Cell Res. 2005 Aug 1;308(1):65-77.
PMID 15907835
 
Functional interactions between ubiquitin E2 enzymes and TRIM proteins.
Napolitano LM, Jaffray EG, Hay RT, Meroni G.
Biochem J. 2011 Mar 1;434(2):309-19. doi: 10.1042/BJ20101487.
PMID 21143188
 
The RET finger protein interacts with the hinge region of SMC3.
Patel CA, Ghiselli G.
Biochem Biophys Res Commun. 2005 Apr 29;330(1):333-40.
PMID 15781269
 
Tumors of the Thyroid Gland.
Rosai J, Carcangiu ML, DeLellis RA.
Atlas of Tumor Pathology, Armed Forces Institute of Pathology, Washington, D.C. 1992;183-93.
 
Novel tumorigenic rearrangement, Delta rfp/ret, in a papillary thyroid carcinoma from externally irradiated patient.
Saenko V, Rogounovitch T, Shimizu-Yoshida Y, Abrosimov A, Lushnikov E, Roumiantsev P, Matsumoto N, Nakashima M, Meirmanov S, Ohtsuru A, Namba H, Tsyb A, Yamashita S.
Mutat Res. 2003 Jun 19;527(1-2):81-90.
PMID 12787916
 
Microspherule protein 1, Mi-2beta, and RET finger protein associate in the nucleolus and up-regulate ribosomal gene transcription.
Shimono K, Shimono Y, Shimokata K, Ishiguro N, Takahashi M.
J Biol Chem. 2005 Nov 25;280(47):39436-47. Epub 2005 Sep 26.
PMID 16186106
 
RET finger protein is a transcriptional repressor and interacts with enhancer of polycomb that has dual transcriptional functions.
Shimono Y, Murakami H, Hasegawa Y, Takahashi M.
J Biol Chem. 2000 Dec 15;275(50):39411-9.
PMID 10976108
 
Phosphatidylinositol-3-kinase C2beta and TRIM27 function to positively and negatively regulate IgE receptor activation of mast cells.
Srivastava S, Cai X, Li Z, Sun Y, Skolnik EY.
Mol Cell Biol. 2012 Aug;32(15):3132-9. doi: 10.1128/MCB.00019-12. Epub 2012 May 29.
PMID 22645315
 
Differential expression of RET finger protein in testicular germ cell tumors.
Tezel G, Nagasaka T, Shimono Y, Takahashi M.
Pathol Int. 2002 Oct;52(10):623-7.
PMID 12445133
 
The selective expression of ret finger protein in endometrial cancer: can RFP be a marker of serous carcinomas?
Tezel GG, Ordulu Z, Himmetoglu C, Usubutun A.
Turk Patoloji Derg. 2012;28(3):213-9. doi: 10.5146/tjpath.2012.01127.
PMID 23011823
 
RET finger protein expression in invasive breast carcinoma: relationship between RFP and ErbB2 expression.
Tezel GG, Uner A, Yildiz I, Guler G, Takahashi M.
Pathol Res Pract. 2009;205(6):403-8. doi: 10.1016/j.prp.2008.12.014. Epub 2009 Feb 20.
PMID 19232840
 
Novel role of the RET finger protein in estrogen receptor-mediated transcription in MCF-7 cells.
Townson SM, Kang K, Lee AV, Oesterreich S.
Biochem Biophys Res Commun. 2006 Oct 20;349(2):540-8. Epub 2006 Aug 22.
PMID 16945332
 
Expression of Ret finger protein correlates with outcomes in endometrial cancer.
Tsukamoto H, Kato T, Enomoto A, Nakamura N, Shimono Y, Jijiwa M, Asai N, Murakumo Y, Shibata K, Kikkawa F, Takahashi M.
Cancer Sci. 2009 Oct;100(10):1895-901. doi: 10.1111/j.1349-7006.2009.01278.x. Epub 2009 Jul 10.
PMID 19650860
 
Ubiquitination-deubiquitination by the TRIM27-USP7 complex regulates tumor necrosis factor alpha-induced apoptosis.
Zaman MM, Nomura T, Takagi T, Okamura T, Jin W, Shinagawa T, Tanaka Y, Ishii S.
Mol Cell Biol. 2013 Dec;33(24):4971-84. doi: 10.1128/MCB.00465-13. Epub 2013 Oct 21.
PMID 24144979
 
The Ret finger protein inhibits signaling mediated by the noncanonical and canonical IkappaB kinase family members.
Zha J, Han KJ, Xu LG, He W, Zhou Q, Chen D, Zhai Z, Shu HB.
J Immunol. 2006 Jan 15;176(2):1072-80.
PMID 16393995
 
Role of the tripartite motif protein 27 in cancer development.
Zoumpoulidou G, Broceno C, Li H, Bird D, Thomas G, Mittnacht S.
J Natl Cancer Inst. 2012 Jun 20;104(12):941-52. doi: 10.1093/jnci/djs224. Epub 2012 May 3.
PMID 22556269
 
TRIM27 negatively regulates NOD2 by ubiquitination and proteasomal degradation.
Zurek B, Schoultz I, Neerincx A, Napolitano LM, Birkner K, Bennek E, Sellge G, Lerm M, Meroni G, Soderholm JD, Kufer TA.
PLoS One. 2012;7(7):e41255. doi: 10.1371/journal.pone.0041255. Epub 2012 Jul 19.
PMID 22829933
 

Citation

This paper should be referenced as such :
G Zoumpoulidou, S Mittnacht
TRIM27 (tripartite motif containing 27)
Atlas Genet Cytogenet Oncol Haematol. 2015;19(4):302-307.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/TRIM27ID42092ch6p22.html


External links

Nomenclature
HGNC (Hugo)TRIM27   9975
Cards
AtlasTRIM27ID42092ch6p22
Entrez_Gene (NCBI)TRIM27  5987  tripartite motif containing 27
AliasesRFP; RNF76
GeneCards (Weizmann)TRIM27
Ensembl hg19 (Hinxton)ENSG00000204713 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000204713 [Gene_View]  chr6:28903002-28923991 [Contig_View]  TRIM27 [Vega]
ICGC DataPortalENSG00000204713
TCGA cBioPortalTRIM27
AceView (NCBI)TRIM27
Genatlas (Paris)TRIM27
WikiGenes5987
SOURCE (Princeton)TRIM27
Genetics Home Reference (NIH)TRIM27
Genomic and cartography
GoldenPath hg38 (UCSC)TRIM27  -     chr6:28903002-28923991 -  6p22.1   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)TRIM27  -     6p22.1   [Description]    (hg19-Feb_2009)
EnsemblTRIM27 - 6p22.1 [CytoView hg19]  TRIM27 - 6p22.1 [CytoView hg38]
Mapping of homologs : NCBITRIM27 [Mapview hg19]  TRIM27 [Mapview hg38]
OMIM602165   
Gene and transcription
Genbank (Entrez)AB209885 AF230393 AF230394 AJ420519 AX776009
RefSeq transcript (Entrez)NM_006510 NM_030950
RefSeq genomic (Entrez)NC_000006 NC_018917 NT_113891 NT_167244 NT_167246 NT_167247 NT_167248 NT_167249
Consensus coding sequences : CCDS (NCBI)TRIM27
Cluster EST : UnigeneHs.440382 [ NCBI ]
CGAP (NCI)Hs.440382
Alternative Splicing GalleryENSG00000204713
Gene ExpressionTRIM27 [ NCBI-GEO ]   TRIM27 [ EBI - ARRAY_EXPRESS ]   TRIM27 [ SEEK ]   TRIM27 [ MEM ]
Gene Expression Viewer (FireBrowse)TRIM27 [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)5987
GTEX Portal (Tissue expression)TRIM27
Human Protein AtlasENSG00000204713-TRIM27 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP14373   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP14373  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP14373
Splice isoforms : SwissVarP14373
Catalytic activity : Enzyme2.3.2.27 [ Enzyme-Expasy ]   2.3.2.272.3.2.27 [ IntEnz-EBI ]   2.3.2.27 [ BRENDA ]   2.3.2.27 [ KEGG ]   
PhosPhoSitePlusP14373
Domaine pattern : Prosite (Expaxy)B302_SPRY (PS50188)    ZF_BBOX (PS50119)    ZF_RING_1 (PS00518)    ZF_RING_2 (PS50089)   
Domains : Interpro (EBI)B30.2/SPRY    Butyrophylin    ConA-like_dom    PRY    SPRY_dom    Znf_B-box    Znf_B-box_chordata    Znf_RING    Znf_RING/FYVE/PHD    Znf_RING_CS   
Domain families : Pfam (Sanger)PRY (PF13765)    SPRY (PF00622)    zf-B_box (PF00643)   
Domain families : Pfam (NCBI)pfam13765    pfam00622    pfam00643   
Domain families : Smart (EMBL)BBOX (SM00336)  PRY (SM00589)  RING (SM00184)  SPRY (SM00449)  
Conserved Domain (NCBI)TRIM27
DMDM Disease mutations5987
Blocks (Seattle)TRIM27
SuperfamilyP14373
Human Protein Atlas [tissue]ENSG00000204713-TRIM27 [tissue]
Peptide AtlasP14373
HPRD15996
IPIIPI00426252   IPI00412657   IPI00894328   IPI01012273   IPI00893697   IPI00892915   IPI00892816   IPI00892663   
Protein Interaction databases
DIP (DOE-UCLA)P14373
IntAct (EBI)P14373
FunCoupENSG00000204713
BioGRIDTRIM27
STRING (EMBL)TRIM27
ZODIACTRIM27
Ontologies - Pathways
QuickGOP14373
Ontology : AmiGOnegative regulation of transcription from RNA polymerase II promoter  fibrillar center  negative regulation of adaptive immune response  nucleic acid binding  DNA binding  transmembrane receptor protein tyrosine kinase activity  ubiquitin-protein transferase activity  ubiquitin-protein transferase activity  protein binding  nucleus  nucleoplasm  nucleolus  cytoplasm  endosome  early endosome  cytosol  integral component of plasma membrane  transcription, DNA-templated  negative regulation of protein kinase activity  spermatogenesis  zinc ion binding  cell proliferation  membrane  PML body  peptidyl-tyrosine phosphorylation  retromer complex  nuclear membrane  negative regulation of tumor necrosis factor production  negative regulation of viral transcription  Arp2/3 complex-mediated actin nucleation  retrograde transport, endosome to Golgi  identical protein binding  innate immune response  negative regulation of gene expression, epigenetic  metal ion binding  positive regulation of sequence-specific DNA binding transcription factor activity  positive regulation of actin nucleation  protein trimerization  protein K63-linked ubiquitination  interferon-gamma secretion  negative regulation of calcium ion import  negative regulation of interleukin-2 secretion  negative regulation of viral release from host cell  
Ontology : EGO-EBInegative regulation of transcription from RNA polymerase II promoter  fibrillar center  negative regulation of adaptive immune response  nucleic acid binding  DNA binding  transmembrane receptor protein tyrosine kinase activity  ubiquitin-protein transferase activity  ubiquitin-protein transferase activity  protein binding  nucleus  nucleoplasm  nucleolus  cytoplasm  endosome  early endosome  cytosol  integral component of plasma membrane  transcription, DNA-templated  negative regulation of protein kinase activity  spermatogenesis  zinc ion binding  cell proliferation  membrane  PML body  peptidyl-tyrosine phosphorylation  retromer complex  nuclear membrane  negative regulation of tumor necrosis factor production  negative regulation of viral transcription  Arp2/3 complex-mediated actin nucleation  retrograde transport, endosome to Golgi  identical protein binding  innate immune response  negative regulation of gene expression, epigenetic  metal ion binding  positive regulation of sequence-specific DNA binding transcription factor activity  positive regulation of actin nucleation  protein trimerization  protein K63-linked ubiquitination  interferon-gamma secretion  negative regulation of calcium ion import  negative regulation of interleukin-2 secretion  negative regulation of viral release from host cell  
NDEx NetworkTRIM27
Atlas of Cancer Signalling NetworkTRIM27
Wikipedia pathwaysTRIM27
Orthology - Evolution
OrthoDB5987
GeneTree (enSembl)ENSG00000204713
Phylogenetic Trees/Animal Genes : TreeFamTRIM27
HOVERGENP14373
HOGENOMP14373
Homologs : HomoloGeneTRIM27
Homology/Alignments : Family Browser (UCSC)TRIM27
Gene fusions - Rearrangements
Fusion : MitelmanTRIM27/RET [6p22.1/10q11.21]  
Fusion : COSMICTRIM27 [6p22.1]  -  RET [10q11.21]  [fusion_1519]  [fusion_1520]  
Fusion: TCGATRIM27 6p22.1 RET 10q11.21 THCA
Fusion : TICdbTRIM27 [6p22.1]  -  RET [10q11.21]
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerTRIM27 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)TRIM27
dbVarTRIM27
ClinVarTRIM27
1000_GenomesTRIM27 
Exome Variant ServerTRIM27
ExAC (Exome Aggregation Consortium)ENSG00000204713
GNOMAD BrowserENSG00000204713
Genetic variants : HAPMAP5987
Genomic Variants (DGV)TRIM27 [DGVbeta]
DECIPHERTRIM27 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisTRIM27 
Mutations
ICGC Data PortalTRIM27 
TCGA Data PortalTRIM27 
Broad Tumor PortalTRIM27
OASIS PortalTRIM27 [ Somatic mutations - Copy number]
Cancer Gene: CensusTRIM27 
Somatic Mutations in Cancer : COSMICTRIM27  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDTRIM27
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
BioMutasearch TRIM27
DgiDB (Drug Gene Interaction Database)TRIM27
DoCM (Curated mutations)TRIM27 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)TRIM27 (select a term)
intoGenTRIM27
NCG5 (London)TRIM27
Cancer3DTRIM27(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM602165   
Orphanet905   
MedgenTRIM27
Genetic Testing Registry TRIM27
NextProtP14373 [Medical]
TSGene5987
GENETestsTRIM27
Target ValidationTRIM27
Huge Navigator TRIM27 [HugePedia]
snp3D : Map Gene to Disease5987
BioCentury BCIQTRIM27
ClinGenTRIM27
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD5987
Chemical/Pharm GKB GenePA162406956
Clinical trialTRIM27
Miscellaneous
canSAR (ICR)TRIM27 (select the gene name)
Other databaseTRIM27 at canSAR
Probes
Litterature
PubMed80 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineTRIM27
EVEXTRIM27
GoPubMedTRIM27
iHOPTRIM27
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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indexed on : Thu Oct 12 16:36:03 CEST 2017

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