RBM14

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; OMA:RBM14 - orthologs
Gene location (Human) Chr. Chromosome 11 (human) [1] Band 11q13.2 Start 66,616,626 bp [1] End 66,629,934 bp [1]
Gene location (Mouse) Chr. Chromosome 19 (mouse) [2] Band 19|19 A Start 4,850,597 bp [2] End 4,861,662 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right uterine tube right hemisphere of cerebellum left ovary right ovary right testis ventricular zone left testis ganglionic eminence mucosa of transverse colon canal of the cervix Top expressed in internal carotid artery external carotid artery condyle primitive streak cumulus cell Paneth cell fossa Ileal epithelium ureter renal corpuscle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding protein-macromolecule adaptor activity transcription coregulator activity nuclear receptor coactivator activity nucleic acid binding RNA binding Cellular component nucleolus mediator complex transcription regulator complex cytoplasm nucleus nuclear speck nucleoplasm ribonucleoprotein complex 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 by RNA polymerase II centriole assembly activation of innate immune response immune system process innate immune response 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: 4.85 – 4.86 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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

Interactions

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

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.

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. Bibcode:2002CBio...12....1A. 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. Bibcode:2004PNAS..10112130B. 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. Bibcode:2006PNAS..103.5391N. 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 . PMC   9245580 . 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.