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Reliable, easy-to-read patient information on common medical conditions — written in plain language, free of jargon, and grounded in current evidence. Browse the most frequent diagnoses, understand what they mean for everyday life, and learn which steps and questions help you have a focused conversation with your doctor.

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RBM14

Introduction

RNA-binding protein 14 is a protein that in humans is encoded by the RBM14 gene.[1][2]

Interactions

Interactions

RBM14 has been shown to interact with TARBP2.[3]

Model organisms

Model organisms

Model organisms have been used in the study of RBM14 function. A conditional knockout mouse line called Rbm14tm1a(KOMP)Wtsi was generated at the Wellcome Trust Sanger Institute.[4] Male and female animals underwent a standardized phenotypic screen[5] to determine the effects of deletion.[6][7][8][9] Additional screens performed: – In-depth immunological phenotyping[10]

References

References

  1. ↑ Brett D, Whitehouse S, Antonson P, Shipley J, Cooper C, Goodwin G (Sep 1997). “The SYT protein involved in the t(X;18) synovial sarcoma translocation is a transcriptional activator localised in nuclear bodies”. Human Molecular Genetics. 6 (9): 1559–64. doi:10.1093/hmg/6.9.1559. PMID 9285794.
  2. ↑ “Entrez Gene: RBM14 RNA binding motif protein 14”.
  3. ↑ Iwasaki T, Chin WW, Ko L (Sep 2001). “Identification and characterization of RRM-containing coactivator activator (CoAA) as TRBP-interacting protein, and its splice variant as a coactivator modulator (CoAM)”. The Journal of Biological Chemistry. 276 (36): 33375–83. doi:10.1074/jbc.M101517200. PMID 11443112.
  4. ↑ Gerdin AK (2010). “The Sanger Mouse Genetics Programme: high throughput characterisation of knockout mice”. Acta Ophthalmologica. 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.
  5. ↑ 5.0 5.1 “International Mouse Phenotyping Consortium”.
  6. ↑ Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (Jun 2011). “A conditional knockout resource for the genome-wide study of mouse gene function”. Nature. 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
  7. ↑ Dolgin E (Jun 2011). “Mouse library set to be knockout”. Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
  8. ↑ Collins FS, Rossant J, Wurst W (Jan 2007). “A mouse for all reasons”. Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
  9. ↑ White JK, Gerdin AK, Karp NA, Ryder E, Buljan M, Bussell JN, Salisbury J, Clare S, Ingham NJ, Podrini C, Houghton R, Estabel J, Bottomley JR, Melvin DG, Sunter D, Adams NC, Tannahill D, Logan DW, Macarthur DG, Flint J, Mahajan VB, Tsang SH, Smyth I, Watt FM, Skarnes WC, Dougan G, Adams DJ, Ramirez-Solis R, Bradley A, Steel KP (Jul 2013). “Genome-wide generation and systematic phenotyping of knockout mice reveals new roles for many genes”. Cell. 154 (2): 452–64. doi:10.1016/j.cell.2013.06.022. PMC 3717207. PMID 23870131.
  10. ↑ 10.0 10.1 “Infection and Immunity Immunophenotyping (3i) Consortium”.
Further reading

Further reading

  • Maruyama K, Sugano S (Jan 1994). “Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides”. Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (Oct 1997). “Construction and characterization of a full length-enriched and a 5′-end-enriched cDNA library”. Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • Iwasaki T, Chin WW, Ko L (Sep 2001). “Identification and characterization of RRM-containing coactivator activator (CoAA) as TRBP-interacting protein, and its splice variant as a coactivator modulator (CoAM)”. The Journal of Biological Chemistry. 276 (36): 33375–83. doi:10.1074/jbc.M101517200. PMID 11443112.
  • Andersen JS, Lyon CE, Fox AH, Leung AK, Lam YW, Steen H, Mann M, Lamond AI (Jan 2002). “Directed proteomic analysis of the human nucleolus”. Current Biology. 12 (1): 1–11. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298.
  • Brill LM, Salomon AR, Ficarro SB, Mukherji M, Stettler-Gill M, Peters EC (May 2004). “Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry”. Analytical Chemistry. 76 (10): 2763–72. doi:10.1021/ac035352d. PMID 15144186.
  • Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (Aug 2004). “Large-scale characterization of HeLa cell nuclear phosphoproteins”. Proceedings of the National Academy of Sciences of the United States of America. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
  • Perani M, Antonson P, Hamoudi R, Ingram CJ, Cooper CS, Garrett MD, Goodwin GH (Dec 2005). “The proto-oncoprotein SYT interacts with SYT-interacting protein/co-activator activator (SIP/CoAA), a human nuclear receptor co-activator with similarity to EWS and TLS/FUS family of proteins”. The Journal of Biological Chemistry. 280 (52): 42863–76. doi:10.1074/jbc.M502963200. PMID 16227627.
  • Nousiainen M, Silljé HH, Sauer G, Nigg EA, Körner R (Apr 2006). “Phosphoproteome analysis of the human mitotic spindle”. Proceedings of the National Academy of Sciences of the United States of America. 103 (14): 5391–6. doi:10.1073/pnas.0507066103. PMC 1459365. PMID 16565220.
  • Lim J, Hao T, Shaw C, Patel AJ, Szabó G, Rual JF, Fisk CJ, Li N, Smolyar A, Hill DE, Barabási AL, Vidal M, Zoghbi HY (May 2006). “A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration”. Cell. 125 (4): 801–14. doi:10.1016/j.cell.2006.03.032. PMID 16713569.
  • Sui Y, Yang Z, Xiong S, Zhang L, Blanchard KL, Peiper SC, Dynan WS, Tuan D, Ko L (Feb 2007). “Gene amplification and associated loss of 5′ regulatory sequences of CoAA in human cancers”. Oncogene. 26 (6): 822–35. doi:10.1038/sj.onc.1209847. PMID 16878147.
  • Beausoleil SA, Villén J, Gerber SA, Rush J, Gygi SP (Oct 2006). “A probability-based approach for high-throughput protein phosphorylation analysis and site localization”. Nature Biotechnology. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID 16964243.
  • Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (Nov 2006). “Global, in vivo, and site-specific phosphorylation dynamics in signaling networks”. Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
  • Yang Z, Sui Y, Xiong S, Liour SS, Phillips AC, Ko L (2007). “Switched alternative splicing of oncogene CoAA during embryonal carcinoma stem cell differentiation”. Nucleic Acids Research. 35 (6): 1919–32. doi:10.1093/nar/gkl1092. PMC 1874587. PMID 17337438.