RBM14

Available structures

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

MGI: 1929092 HomoloGene: 4614 GeneCards: RBM14

Gene ontology
Molecular function	• nucleotide binding • protein binding • poly(A) RNA binding • protein binding, bridging • RNA polymerase II transcription cofactor activity • ligand-dependent nuclear receptor transcription coactivator activity • nucleic acid binding • RNA binding
Cellular component	• nucleolus • intracellular ribonucleoprotein complex • mediator complex • nucleoplasm • transcription factor complex • cytoplasm • nucleus
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
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

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_001185765.1 NP_001185766.1 NP_001185774.1 NP_006319.1


NP_063922.2

Location (UCSC)

Chr 11: 66.62 – 66.63 Mb

Chr 19: 4.8 – 4.81 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

RNA-binding protein 14 is a protein that in humans is encoded by the RBM14 gene.^[3]^[4]

Interactions

RBM14 has been shown to interact with TARBP2.^[5]

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.^[6] Male and female animals underwent a standardized phenotypic screen^[7] to determine the effects of deletion.^[8]^[9]^[10]^[11] Additional screens performed: - In-depth immunological phenotyping^[12]

*Rbm14* knockout mouse phenotype
Characteristic	Phenotype
All data available at.^[7]^[12]
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

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ 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.
↑ "Entrez Gene: RBM14 RNA binding motif protein 14".
↑ 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.
↑ 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.
1 2 "International Mouse Phenotyping Consortium".
↑ 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.
↑ Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
↑ 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.
↑ 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.
1 2 "Infection and Immunity Immunophenotyping (3i) Consortium".

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.

PDB gallery

2dnp: Solution structure of RNA binding domain 2 in RNA-binding protein 14

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RBM14

Interactions

Model organisms

References

Further reading