RAE1

RAE1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	3MMY, 4OWR
Identifiers
Aliases	RAE1, MIG14, MRNP41, Mnrp41, dJ481F12.3, dJ800J21.1, ribonucleic acid export 1, Gle2
External IDs	OMIM: 603343 MGI: 1913929 HomoloGene: 2676 GeneCards: RAE1
Gene location (Human)
Chr.	Chromosome 20 (human)
End	57,379,211 bp
Gene location (Mouse)
Chr.	Chromosome 2 (mouse)
End	172,857,532 bp
RNA expression pattern
	Top expressed in
	secondary oocyte; ; sperm; ; internal globus pallidus; ; embryo; ; spongy bone; ; ganglionic eminence; ; bone marrow; ; amniotic fluid; ; cavity of mouth; ; endothelial cell;
	Top expressed in
	otic placode; ; spermatocyte; ; saccule; ; spermatid; ; neural tube; ; somite; ; ganglionic eminence; ; yolk sac; ; maxillary prominence; ; abdominal wall;
	More reference expression data
	n/a
Gene ontology
Molecular function	microtubule binding; RNA binding; protein binding; ubiquitin binding;
Cellular component	cytoplasm; nuclear pore; nucleus; nuclear envelope; fibrillar center; mitotic spindle pole; spindle pole; cytoskeleton; host cell;
Biological process	cellular response to organic cyclic compound; viral process; regulation of mitotic spindle organization; transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery; RNA export from nucleus; protein import into nucleus; cell cycle; cell division; mRNA export from nucleus; regulation of glycolytic process; tRNA export from nucleus; protein sumoylation; viral transcription; regulation of gene silencing by miRNA; intracellular transport of virus; regulation of cellular response to heat;
	Sources:Amigo / QuickGO
Orthologs
	8480
	66679
	ENSG00000101146
	ENSMUSG00000027509
	P78406
	Q8C570
	NM_001015885; NM_003610
	NM_175112
	NP_001015885; NP_003601
	NP_780321
	Wikidata
View/Edit Human	View/Edit Mouse

mRNA export factor is a protein that in humans is encoded by the RAE1 gene.^[5]^[6]^[7]

Mutations in the Schizosaccharomyces pombe Rae1 and Saccharomyces cerevisiae Gle2 genes have been shown to result in accumulation of poly(A)-containing mRNA in the nucleus, suggesting that the encoded proteins are involved in RNA export. The protein encoded by this gene is a homolog of yeast Rae1. It contains four WD40 motifs, and has been shown to localize to distinct foci in the nucleoplasm, to the nuclear rim, and to meshwork-like structures throughout the cytoplasm. This gene is thought to be involved in nucleocytoplasmic transport, and in directly or indirectly attaching cytoplasmic mRNPs to the cytoskeleton. Alternatively spliced transcript variants encoding the same protein have been found for this gene.^[7]

Interactions

RAE1 has been shown to interact with NUP98.^[8]

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000101146 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000027509 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Bharathi A, Ghosh A, Whalen WA, Yoon JH, Pu R, Dasso M, Dhar R (Dec 1997). "The human RAE1 gene is a functional homologue of Schizosaccharomyces pombe rae1 gene involved in nuclear export of Poly(A)+ RNA". Gene. 198 (1–2): 251–8. doi:10.1016/S0378-1119(97)00322-3. PMID 9370289.
↑ Kraemer D, Blobel G (Sep 1997). "mRNA binding protein mrnp 41 localizes to both nucleus and cytoplasm". Proc Natl Acad Sci U S A. 94 (17): 9119–24. Bibcode:1997PNAS...94.9119K. doi:10.1073/pnas.94.17.9119. PMC 23064. PMID 9256445.
1 2 "Entrez Gene: RAE1 RAE1 RNA export 1 homolog (S. pombe)".
↑ Pritchard, C E; Fornerod M; Kasper L H; van Deursen J M (Apr 1999). "RAE1 is a shuttling mRNA export factor that binds to a GLEBS-like NUP98 motif at the nuclear pore complex through multiple domains". J. Cell Biol. 145 (2): 237–54. doi:10.1083/jcb.145.2.237. ISSN 0021-9525. PMC 2133102. PMID 10209021.

Nomura M, Zou Z, Joh T, et al. (1997). "Genomic structures and characterization of Rae1 family members encoding GPI-anchored cell surface proteins and expressed predominantly in embryonic mouse brain". J. Biochem. 120 (5): 987–95. doi:10.1093/oxfordjournals.jbchem.a021517. PMID 8982867.
Yoon JH, Whalen WA, Bharathi A, et al. (1997). "Npp106p, a Schizosaccharomyces pombe nucleoporin similar to Saccharomyces cerevisiae Nic96p, functionally interacts with Rae1p in mRNA export". Mol. Cell. Biol. 17 (12): 7047–60. doi:10.1128/MCB.17.12.7047. PMC 232561. PMID 9372936.
Matsuoka Y, Takagi M, Ban T, et al. (1999). "Identification and characterization of nuclear pore subcomplexes in mitotic extract of human somatic cells". Biochem. Biophys. Res. Commun. 254 (2): 417–23. doi:10.1006/bbrc.1998.9953. PMID 9918853.
Pritchard CE, Fornerod M, Kasper LH, van Deursen JM (1999). "RAE1 is a shuttling mRNA export factor that binds to a GLEBS-like NUP98 motif at the nuclear pore complex through multiple domains". J. Cell Biol. 145 (2): 237–54. doi:10.1083/jcb.145.2.237. PMC 2133102. PMID 10209021.
Bachi A, Braun IC, Rodrigues JP, et al. (2000). "The C-terminal domain of TAP interacts with the nuclear pore complex and promotes export of specific CTE-bearing RNA substrates". RNA. 6 (1): 136–58. doi:10.1017/S1355838200991994. PMC 1369901. PMID 10668806.
Yoon JH, Love DC, Guhathakurta A, et al. (2000). "Mex67p of Schizosaccharomyces pombe interacts with Rae1p in mediating mRNA export". Mol. Cell. Biol. 20 (23): 8767–82. doi:10.1128/MCB.20.23.8767-8782.2000. PMC 86506. PMID 11073978.
Sabri N, Visa N (2000). "The Ct-RAE1 protein interacts with Balbiani ring RNP particles at the nuclear pore". RNA. 6 (11): 1597–609. doi:10.1017/S1355838200001138. PMC 1370029. PMID 11105759.
Wang X, Babu JR, Harden JM, et al. (2001). "The mitotic checkpoint protein hBUB3 and the mRNA export factor hRAE1 interact with GLE2p-binding sequence (GLEBS)-containing proteins". J. Biol. Chem. 276 (28): 26559–67. doi:10.1074/jbc.M101083200. PMID 11352911.
O'Callaghan CA, Cerwenka A, Willcox BE, et al. (2001). "Molecular competition for NKG2D: H60 and RAE1 compete unequally for NKG2D with dominance of H60". Immunity. 15 (2): 201–11. doi:10.1016/S1074-7613(01)00187-X. PMID 11520456.
Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20". Nature. 414 (6866): 865–71. Bibcode:2001Natur.414..865D. doi:10.1038/414865a. PMID 11780052.
Kraemer D, Dresbach T, Drenckhahn D (2002). "Mrnp41 (Rae 1p) associates with microtubules in HeLa cells and in neurons". Eur. J. Cell Biol. 80 (12): 733–40. doi:10.1078/0171-9335-00216. PMID 11831386.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Faria PA, Chakraborty P, Levay A, et al. (2005). "VSV disrupts the Rae1/mrnp41 mRNA nuclear export pathway". Mol. Cell. 17 (1): 93–102. doi:10.1016/j.molcel.2004.11.023. PMID 15629720.
Benzinger A, Muster N, Koch HB, et al. (2005). "Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer". Mol. Cell. Proteomics. 4 (6): 785–95. doi:10.1074/mcp.M500021-MCP200. PMID 15778465.
Blower MD, Nachury M, Heald R, Weis K (2005). "A Rae1-containing ribonucleoprotein complex is required for mitotic spindle assembly". Cell. 121 (2): 223–34. doi:10.1016/j.cell.2005.02.016. PMID 15851029. S2CID 242561.
Wong RW, Blobel G, Coutavas E (2007). "Rae1 interaction with NuMA is required for bipolar spindle formation". Proc. Natl. Acad. Sci. U.S.A. 103 (52): 19783–7. Bibcode:2006PNAS..10319783W. doi:10.1073/pnas.0609582104. PMC 1750899. PMID 17172455.

This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.

[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000101146 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000027509 - 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.

[pmid9370289-5] Bharathi A, Ghosh A, Whalen WA, Yoon JH, Pu R, Dasso M, Dhar R (Dec 1997). "The human RAE1 gene is a functional homologue of Schizosaccharomyces pombe rae1 gene involved in nuclear export of Poly(A)+ RNA". Gene. 198 (1–2): 251–8. doi:10.1016/S0378-1119(97)00322-3. PMID 9370289.

[pmid9256445-6] Kraemer D, Blobel G (Sep 1997). "mRNA binding protein mrnp 41 localizes to both nucleus and cytoplasm". Proc Natl Acad Sci U S A. 94 (17): 9119–24. Bibcode:1997PNAS...94.9119K. doi:10.1073/pnas.94.17.9119. PMC 23064. PMID 9256445.

[entrez-7] 1 2 "Entrez Gene: RAE1 RAE1 RNA export 1 homolog (S. pombe)".

[pmid10209021-8] Pritchard, C E; Fornerod M; Kasper L H; van Deursen J M (Apr 1999). "RAE1 is a shuttling mRNA export factor that binds to a GLEBS-like NUP98 motif at the nuclear pore complex through multiple domains". J. Cell Biol. 145 (2): 237–54. doi:10.1083/jcb.145.2.237. ISSN 0021-9525. PMC 2133102. PMID 10209021.

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

Interactions

References

Further reading