SND1

Staphylococcal nuclease and tudor domain containing 1

PDB rendering based on 2hqx.
Identifiers
Symbols SND1; TDRD11; p100
External IDs OMIM: 602181 MGI: 1929266 HomoloGene: 8665 GeneCards: SND1 Gene
Orthologs
Species Human Mouse
Entrez 27044 56463
Ensembl ENSG00000197157 ENSMUSG00000001424
UniProt Q7KZF4 Q3TJ56
RefSeq (mRNA) NM_014390 NM_019776.2
RefSeq (protein) NP_055205 NP_062750.2
Location (UCSC) Chr 7:
127.29 – 127.73 Mb		 Chr 6:
28.43 – 28.89 Mb
PubMed search [1] [2]

Staphylococcal nuclease domain-containing protein 1 also known as 100 kDa coactivator or Tudor domain-containing protein 11 (TDRD11) is a protein that in humans is encoded by the SND1 gene.[1][2][3][4] SND1 is a main component of RISC complex[5] and plays an important role in miRNA function.[6][7]

Contents

Clinical significance

SND1 acts as oncogene in many cancers[8][9][10] and in hepatocellular carcinoma progression.[6][7]

Interactions

SND1 has been shown to interact with PIM1,[11] STAT6,[12] RBPJ,[13][14] POLR2A[12] and MYB.[15]

SND1 also interacts with G3BP (stress granule protein)[16] and AEG-1.[6][7]

References

  1. ^ Tong X, Drapkin R, Yalamanchili R, Mosialos G, Kieff E (Sep 1995). "The Epstein-Barr virus nuclear protein 2 acidic domain forms a complex with a novel cellular coactivator that can interact with TFIIE". Mol Cell Biol 15 (9): 4735–44. PMC 230717. PMID 7651391. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=230717. 
  2. ^ Callebaut I, Mornon JP (Feb 1997). "The human EBNA-2 coactivator p100: multidomain organization and relationship to the staphylococcal nuclease fold and to the tudor protein involved in Drosophila melanogaster development". Biochem J 321 ( Pt 1): 125–32. PMC 1218045. PMID 9003410. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1218045. 
  3. ^ Paukku K, Yang J, Silvennoinen O (Aug 2003). "Tudor and nuclease-like domains containing protein p100 function as coactivators for signal transducer and activator of transcription 5". Mol Endocrinol 17 (9): 1805–14. doi:10.1210/me.2002-0256. PMID 12819296. 
  4. ^ "Entrez Gene: SND1 staphylococcal nuclease and tudor domain containing 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=27044. 
  5. ^ Tsuchiya N, Ochiai M, Nakashima K, Ubagai T, Sugimura T, Nakagama H (October 2007). "SND1, a component of RNA-induced silencing complex, is up-regulated in human colon cancers and implicated in early stage colon carcinogenesis". Cancer Res. 67 (19): 9568–76. doi:10.1158/0008-5472.CAN-06-2707. PMID 17909068. 
  6. ^ a b c Yoo BK, Santhekadur PK, Gredler R, Chen D, Emdad L, Bhutia SK, Pannell L, Fisher PB, Sarkar D (2011). "Increased RNA-induced silencing complex (RISC) activity contributes to hepatocellular carcinoma". Hepatology 53 (5): 1538–1548. doi:10.1002/hep.24216. PMC 3081619. PMID 21520169. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3081619. 
  7. ^ a b c Yoo BK, Emdad L, Lee SG, Su ZZ, Santhekadur P, Chen D, Gredler R, Fisher PB, Sarkar D (January 2011). "Astrocyte elevated gene-1 (AEG-1): A multifunctional regulator of normal and abnormal physiology". Pharmacol Ther 130 (1): 1–8. doi:10.1016/j.pharmthera.2011.01.008. PMC 3043119. PMID 21256156. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3043119. 
  8. ^ Tsuchiya N, Nakagama H (September 2010). "MicroRNA, SND1, and alterations in translational regulation in colon carcinogenesis". Mutat Res 693 (1–2): 94–100. doi:10.1016/j.mrfmmm.2010.09.001. PMID 20883704. 
  9. ^ Kuruma H, Kamata Y, Takahashi H, Igarashi K, Kimura T, Miki K, Miki J, Sasaki H, Hayashi N, Egawa S (June 2009). "Staphylococcal nuclease domain-containing protein 1 as a potential tissue marker for prostate cancer". Am. J. Pathol. 174 (6): 2044–50. doi:10.2353/ajpath.2009.080776. PMC 2684170. PMID 19435788. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2684170. 
  10. ^ Ho J, Kong JW, Choong LY, Loh MC, Toy W, Chong PK, Wong CH, Wong CY, Shah N, Lim YP (February 2009). "Novel breast cancer metastasis-associated proteins". J. Proteome Res. 8 (2): 583–94. doi:10.1021/pr8007368. PMID 19086899. 
  11. ^ Leverson JD, Koskinen PJ, Orrico FC, Rainio EM, Jalkanen KJ, Dash AB, Eisenman RN, Ness SA (October 1998). "Pim-1 kinase and p100 cooperate to enhance c-Myb activity". Mol. Cell 2 (4): 417–25. doi:10.1016/S1097-2765(00)80141-0. PMID 9809063. 
  12. ^ a b Yang J, Aittomäki S, Pesu M, Carter K, Saarinen J, Kalkkinen N, Kieff E, Silvennoinen O (September 2002). "Identification of p100 as a coactivator for STAT6 that bridges STAT6 with RNA polymerase II". EMBO J. 21 (18): 4950–8. doi:10.1093/emboj/cdf463. PMC 126276. PMID 12234934. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=126276. 
  13. ^ Zhou S, Fujimuro M, Hsieh JJ, Chen L, Hayward SD (February 2000). "A role for SKIP in EBNA2 activation of CBF1-repressed promoters". J. Virol. 74 (4): 1939–47. doi:10.1128/JVI.74.4.1939-1947.2000. PMC 111672. PMID 10644367. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=111672. 
  14. ^ Hsieh JJ, Zhou S, Chen L, Young DB, Hayward SD (January 1999). "CIR, a corepressor linking the DNA binding factor CBF1 to the histone deacetylase complex". Proc. Natl. Acad. Sci. U.S.A. 96 (1): 23–8. doi:10.1073/pnas.96.1.23. PMC 15086. PMID 9874765. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=15086. 
  15. ^ Dash AB, Orrico FC, Ness SA (August 1996). "The EVES motif mediates both intermolecular and intramolecular regulation of c-Myb". Genes Dev. 10 (15): 1858–69. doi:10.1101/gad.10.15.1858. PMID 8756344. 
  16. ^ Gao X, Ge L, Shao J, Su C, Zhao H, Saarikettu J, Yao X, Yao Z, Silvennoinen O, Yang J (August 2010). "Tudor-SN interacts with and co-localizes with G3BP in stress granules under stress conditions". FEBS Lett. 584 (16): 3525–32. doi:10.1016/j.febslet.2010.07.022. PMID 20643132. 

Further reading