RBM14

RNA-binding protein 14 is a protein that in humans is encoded by the RBM14 gene.[5][6]

RBM14
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2DNP
Identifiers
Aliases	RBM14, COAA, PSP2, SIP, SYTIP1, TMEM137, RNA binding motif protein 14
External IDs	OMIM: 612409 MGI: 1929092 HomoloGene: 4614 GeneCards: RBM14
Gene location (Human) Chr. Chromosome 11 (human)[1] Band 11q13.2 Start 66,616,582 bp[1] End 66,627,347 bp[1]
Gene location (Mouse) Chr. Chromosome 19 (mouse)[2] Band 19|19 A Start 4,800,569 bp[2] End 4,811,634 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • GO:0001948 protein binding • protein binding, bridging • GO:0001104 transcription coregulator activity • ligand-dependent nuclear receptor transcription coactivator activity • nucleic acid binding • RNA binding Cellular component • nucleolus • mediator complex • transcription regulator complex • cytoplasm • cell nucleus • nuclear speck • nucleoplasm • ribonucleoprotein Biological process • glucocorticoid receptor signaling pathway • response to hormone • SMAD protein signal transduction • DNA recombination • DNA repair • regulation of transcription, DNA-templated • DNA replication • intracellular estrogen receptor signaling pathway • transcription, DNA-templated • negative regulation of centriole replication • histone deacetylation • positive regulation of transcription from RNA polymerase II promoter • centriole assembly • activation of innate immune response • immune system process • innate immune system Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	10432	56275
Ensembl	ENSG00000239306	ENSMUSG00000006456
UniProt	Q96PK6	Q8C2Q3
RefSeq (mRNA)	NM_032886 NM_001198836 NM_001198837 NM_006328	NM_019869
RefSeq (protein)	NP_001185765 NP_001185766 NP_006319	NP_063922
Location (UCSC)	Chr 11: 66.62 – 66.63 Mb	Chr 19: 4.8 – 4.81 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Interactions

RBM14 has been shown to interact with TARBP2.[7]

Model organisms

Model organisms have been used in the study of RBM14 function. A conditional knockout mouse line called Rbm14^{tm1a(KOMP)Wtsi} was generated at the Wellcome Trust Sanger Institute.[8] Male and female animals underwent a standardized phenotypic screen[9] to determine the effects of deletion.[10][11][12][13] Additional screens performed: - In-depth immunological phenotyping[14]

Rbm14 knockout mouse phenotype

Characteristic	Phenotype
All data available at.[9][14]
Peripheral blood leukocytes 6 Weeks	Normal
Insulin	Normal
Haematology 6 Weeks	Normal
Homozygous viability at P14	Normal
Homozygous Fertility	Normal
Body weight	Normal
Neurological assessment	Normal
Grip strength	Normal
Dysmorphology	Normal
Indirect calorimetry	Normal
Glucose tolerance test	Normal
Auditory brainstem response	Normal
DEXA	Normal
Radiography	Normal
Eye morphology	Normal
Clinical chemistry	Normal
Haematology 16 Weeks	Normal
Peripheral blood leukocytes 16 Weeks	Normal
Heart weight	Normal
Cytotoxic T Cell Function	Normal
Spleen Immunophenotyping	Normal
Mesenteric Lymph Node Immunophenotyping	Normal
Bone Marrow Immunophenotyping	Normal
Epidermal Immune Composition	Normal

References

1. GRCh38: Ensembl release 89: ENSG00000239306 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000006456 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. "Entrez Gene: RBM14 RNA binding motif protein 14".
7. 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.
8. 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. S2CID 85911512.
9. "International Mouse Phenotyping Consortium".
10. 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.
11. Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
12. 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. S2CID 18872015.
13. 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.
14. "Infection and Immunity Immunophenotyping (3i) Consortium".

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. S2CID 14132033.
• 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. S2CID 13709685.
• 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. S2CID 14294292.
• 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. S2CID 7827573.
• 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.