RAE1: Difference between revisions

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Latest revision as of 07:15, 10 January 2019

mRNA export factor is a protein that in humans is encoded by the RAE1 gene.^[1]^[2]^[3]

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.^[3]

Interactions

RAE1 has been shown to interact with NUP98.^[4]

References

↑ 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.
↑ ^3.0 ^3.1 "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. UNITED STATES. 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. 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.
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 on a gene on human chromosome 20 is a stub. You can help Wikipedia by expanding it.

[pmid9370289-1] 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.

[pmid9256445-2] 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-3] 3.0 ^3.1 "Entrez Gene: RAE1 RAE1 RNA export 1 homolog (S. pombe)".

[pmid10209021-4] 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. UNITED STATES. 145 (2): 237–54. doi:10.1083/jcb.145.2.237. ISSN 0021-9525. PMC 2133102. PMID 10209021.

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@@ Line 1: / Line 1: @@
-<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
+{{Infobox_gene}}
-{{PBB_Controls
+'''mRNA export factor''' is a [[protein]] that in humans is encoded by the ''RAE1'' [[gene]].<ref name="pmid9370289">{{cite journal |vauthors=Bharathi A, Ghosh A, Whalen WA, Yoon JH, Pu R, Dasso M, Dhar R | title = The human RAE1 gene is a functional homologue of Schizosaccharomyces pombe rae1 gene involved in nuclear export of Poly(A)+ RNA | journal = Gene | volume = 198 | issue = 1–2 | pages = 251–8 |date=Dec 1997 | pmid = 9370289 | pmc =  | doi =10.1016/S0378-1119(97)00322-3  }}</ref><ref name="pmid9256445">{{cite journal |vauthors=Kraemer D, Blobel G | title = mRNA binding protein mrnp 41 localizes to both nucleus and cytoplasm | journal = Proc Natl Acad Sci U S A | volume = 94 | issue = 17 | pages = 9119–24 |date=Sep 1997 | pmid = 9256445 | pmc = 23064 | doi =10.1073/pnas.94.17.9119  | bibcode =1997PNAS...94.9119K }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: RAE1 RAE1 RNA export 1 homolog (S. pombe)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8480| accessdate = }}</ref>
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-}}
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-{{GNF_Protein_box
- | image =
- | image_source =
- | PDB =
- | Name = RAE1 RNA export 1 homolog (S. pombe)
- | HGNCid = 9828
- | Symbol = RAE1
- | AltSymbols =; FLJ30608; MGC117333; MGC126076; MGC126077; MIG14; MRNP41; Mnrp41; dJ481F12.3; dJ800J21.1
- | OMIM = 603343
- | ECnumber =
- | Homologene = 2676
- | MGIid = 1913929
-  | Function = {{GNF_GO|id=GO:0003723 |text = RNA binding}} {{GNF_GO|id=GO:0008017 |text = microtubule binding}}
-  | Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005640 |text = nuclear outer membrane}} {{GNF_GO|id=GO:0005643 |text = nuclear pore}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005856 |text = cytoskeleton}}
- | Process = {{GNF_GO|id=GO:0006406 |text = mRNA export from nucleus}} {{GNF_GO|id=GO:0051227 |text = spindle assembly}}
- | Orthologs = {{GNF_Ortholog_box
-    | Hs_EntrezGene = 8480
-    | Hs_Ensembl = ENSG00000101146
-    | Hs_RefseqProtein = NP_001015885
-    | Hs_RefseqmRNA = NM_001015885
-    | Hs_GenLoc_db =
-    | Hs_GenLoc_chr = 20
-    | Hs_GenLoc_start = 55359535
-    | Hs_GenLoc_end = 55387618
-    | Hs_Uniprot = P78406
-    | Mm_EntrezGene = 66679
-    | Mm_Ensembl = ENSMUSG00000027509
-    | Mm_RefseqmRNA = NM_175112
-    | Mm_RefseqProtein = NP_780321
-    | Mm_GenLoc_db =
-    | Mm_GenLoc_chr = 2
-    | Mm_GenLoc_start = 172643076
-    | Mm_GenLoc_end = 172658671
-    | Mm_Uniprot = Q6PAS9
-  }}
-}}
-'''RAE1 RNA export 1 homolog (S. pombe)''', also known as '''RAE1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RAE1 RAE1 RNA export 1 homolog (S. pombe)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8480| accessdate = }}</ref>
-<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
+<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
 {{PBB_Summary
 | section_title =
-| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: RAE1 RAE1 RNA export 1 homolog (S. pombe)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8480| accessdate = }}</ref>
+| summary_text = 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.<ref name="entrez" />
 }}
-==References==
+==Interactions==
-{{reflist|2}}
+RAE1 has been shown to [[Protein-protein interaction|interact]] with [[NUP98]].<ref name=pmid10209021>{{cite journal |doi=10.1083/jcb.145.2.237 |last=Pritchard |first=C E |authorlink= |author2=Fornerod M |author3=Kasper L H |author4=van Deursen J M  |date=Apr 1999 |title=RAE1 is a shuttling mRNA export factor that binds to a GLEBS-like NUP98 motif at the nuclear pore complex through multiple domains |journal=J. Cell Biol. |volume=145 |issue=2 |pages=237–54 |publisher= |location = UNITED STATES| issn = 0021-9525| pmid = 10209021 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |pmc=2133102 }}</ref>
-==Further reading==
+== References ==
+<references/>
+== Further reading ==
 {{refbegin | 2}}
 {{PBB_Further_reading
 | citations =
-*{{cite journal  | author=Nomura M, Zou Z, Joh T, ''et al.'' |title=Genomic structures and characterization of Rae1 family members encoding GPI-anchored cell surface proteins and expressed predominantly in embryonic mouse brain. |journal=J. Biochem. |volume=120 |issue= 5 |pages= 987-95 |year= 1997 |pmid= 8982867 |doi=  }}
+*{{cite journal   |vauthors=Nomura M, Zou Z, Joh T, etal |title=Genomic structures and characterization of Rae1 family members encoding GPI-anchored cell surface proteins and expressed predominantly in embryonic mouse brain. |journal=J. Biochem. |volume=120 |issue= 5 |pages= 987–95 |year= 1997 |pmid= 8982867 |doi=  10.1093/oxfordjournals.jbchem.a021517}}
-*{{cite journal  | author=Kraemer D, Blobel G |title=mRNA binding protein mrnp 41 localizes to both nucleus and cytoplasm. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 17 |pages= 9119-24 |year= 1997 |pmid= 9256445 |doi=  }}
+*{{cite journal   |vauthors=Yoon JH, Whalen WA, Bharathi A, etal |title=Npp106p, a Schizosaccharomyces pombe nucleoporin similar to Saccharomyces cerevisiae Nic96p, functionally interacts with Rae1p in mRNA export. |journal=Mol. Cell. Biol. |volume=17 |issue= 12 |pages= 7047–60 |year= 1997 |pmid= 9372936 |doi=  | pmc=232561  }}
-*{{cite journal  | author=Bharathi A, Ghosh A, Whalen WA, ''et al.'' |title=The human RAE1 gene is a functional homologue of Schizosaccharomyces pombe rae1 gene involved in nuclear export of Poly(A)+ RNA. |journal=Gene |volume=198 |issue= 1-2 |pages= 251-8 |year= 1997 |pmid= 9370289 |doi=  }}
+*{{cite journal   |vauthors=Matsuoka Y, Takagi M, Ban T, etal |title=Identification and characterization of nuclear pore subcomplexes in mitotic extract of human somatic cells. |journal=Biochem. Biophys. Res. Commun. |volume=254 |issue= 2 |pages= 417–23 |year= 1999 |pmid= 9918853 |doi= 10.1006/bbrc.1998.9953 }}
-*{{cite journal  | author=Yoon JH, Whalen WA, Bharathi A, ''et al.'' |title=Npp106p, a Schizosaccharomyces pombe nucleoporin similar to Saccharomyces cerevisiae Nic96p, functionally interacts with Rae1p in mRNA export. |journal=Mol. Cell. Biol. |volume=17 |issue= 12 |pages= 7047-60 |year= 1997 |pmid= 9372936 |doi=  }}
+*{{cite journal  |vauthors=Pritchard CE, Fornerod M, Kasper LH, van Deursen JM |title=RAE1 is a shuttling mRNA export factor that binds to a GLEBS-like NUP98 motif at the nuclear pore complex through multiple domains. |journal=J. Cell Biol. |volume=145 |issue= 2 |pages= 237–54 |year= 1999 |pmid= 10209021 |doi=10.1083/jcb.145.2.237  | pmc=2133102  }}
-*{{cite journal  | author=Matsuoka Y, Takagi M, Ban T, ''et al.'' |title=Identification and characterization of nuclear pore subcomplexes in mitotic extract of human somatic cells. |journal=Biochem. Biophys. Res. Commun. |volume=254 |issue= 2 |pages= 417-23 |year= 1999 |pmid= 9918853 |doi= 10.1006/bbrc.1998.9953 }}
+*{{cite journal   |vauthors=Bachi A, Braun IC, Rodrigues JP, etal |title=The C-terminal domain of TAP interacts with the nuclear pore complex and promotes export of specific CTE-bearing RNA substrates. |journal=RNA |volume=6 |issue= 1 |pages= 136–58 |year= 2000 |pmid= 10668806 |doi=10.1017/S1355838200991994  | pmc=1369901  }}
-*{{cite journal  | author=Pritchard CE, Fornerod M, Kasper LH, van Deursen JM |title=RAE1 is a shuttling mRNA export factor that binds to a GLEBS-like NUP98 motif at the nuclear pore complex through multiple domains. |journal=J. Cell Biol. |volume=145 |issue= 2 |pages= 237-54 |year= 1999 |pmid= 10209021 |doi=  }}
+*{{cite journal   |vauthors=Yoon JH, Love DC, Guhathakurta A, etal |title=Mex67p of Schizosaccharomyces pombe interacts with Rae1p in mediating mRNA export. |journal=Mol. Cell. Biol. |volume=20 |issue= 23 |pages= 8767–82 |year= 2000 |pmid= 11073978 |doi=10.1128/MCB.20.23.8767-8782.2000  | pmc=86506  }}
-*{{cite journal  | author=Bachi A, Braun IC, Rodrigues JP, ''et al.'' |title=The C-terminal domain of TAP interacts with the nuclear pore complex and promotes export of specific CTE-bearing RNA substrates. |journal=RNA |volume=6 |issue= 1 |pages= 136-58 |year= 2000 |pmid= 10668806 |doi=  }}
+*{{cite journal  |vauthors=Sabri N, Visa N |title=The Ct-RAE1 protein interacts with Balbiani ring RNP particles at the nuclear pore. |journal=RNA |volume=6 |issue= 11 |pages= 1597–609 |year= 2000 |pmid= 11105759 |doi=10.1017/S1355838200001138  | pmc=1370029  }}
-*{{cite journal  | author=Yoon JH, Love DC, Guhathakurta A, ''et al.'' |title=Mex67p of Schizosaccharomyces pombe interacts with Rae1p in mediating mRNA export. |journal=Mol. Cell. Biol. |volume=20 |issue= 23 |pages= 8767-82 |year= 2000 |pmid= 11073978 |doi=  }}
+*{{cite journal   |vauthors=Wang X, Babu JR, Harden JM, etal |title=The mitotic checkpoint protein hBUB3 and the mRNA export factor hRAE1 interact with GLE2p-binding sequence (GLEBS)-containing proteins. |journal=J. Biol. Chem. |volume=276 |issue= 28 |pages= 26559–67 |year= 2001 |pmid= 11352911 |doi= 10.1074/jbc.M101083200 }}
-*{{cite journal  | author=Sabri N, Visa N |title=The Ct-RAE1 protein interacts with Balbiani ring RNP particles at the nuclear pore. |journal=RNA |volume=6 |issue= 11 |pages= 1597-609 |year= 2000 |pmid= 11105759 |doi=  }}
+*{{cite journal   |vauthors=O'Callaghan CA, Cerwenka A, Willcox BE, etal |title=Molecular competition for NKG2D: H60 and RAE1 compete unequally for NKG2D with dominance of H60. |journal=Immunity |volume=15 |issue= 2 |pages= 201–11 |year= 2001 |pmid= 11520456 |doi=10.1016/S1074-7613(01)00187-X  }}
-*{{cite journal  | author=Wang X, Babu JR, Harden JM, ''et al.'' |title=The mitotic checkpoint protein hBUB3 and the mRNA export factor hRAE1 interact with GLE2p-binding sequence (GLEBS)-containing proteins. |journal=J. Biol. Chem. |volume=276 |issue= 28 |pages= 26559-67 |year= 2001 |pmid= 11352911 |doi= 10.1074/jbc.M101083200 }}
+*{{cite journal   |vauthors=Deloukas P, Matthews LH, Ashurst J, etal |title=The DNA sequence and comparative analysis of human chromosome 20. |journal=Nature |volume=414 |issue= 6866 |pages= 865–71 |year= 2002 |pmid= 11780052 |doi= 10.1038/414865a |bibcode=2001Natur.414..865D }}
-*{{cite journal  | author=O'Callaghan CA, Cerwenka A, Willcox BE, ''et al.'' |title=Molecular competition for NKG2D: H60 and RAE1 compete unequally for NKG2D with dominance of H60. |journal=Immunity |volume=15 |issue= 2 |pages= 201-11 |year= 2001 |pmid= 11520456 |doi=  }}
+*{{cite journal  |vauthors=Kraemer D, Dresbach T, Drenckhahn D |title=Mrnp41 (Rae 1p) associates with microtubules in HeLa cells and in neurons. |journal=Eur. J. Cell Biol. |volume=80 |issue= 12 |pages= 733–40 |year= 2002 |pmid= 11831386 |doi=10.1078/0171-9335-00216  }}
-*{{cite journal  | author=Deloukas P, Matthews LH, Ashurst J, ''et al.'' |title=The DNA sequence and comparative analysis of human chromosome 20. |journal=Nature |volume=414 |issue= 6866 |pages= 865-71 |year= 2002 |pmid= 11780052 |doi= 10.1038/414865a }}
+*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 |bibcode=2002PNAS...9916899M }}
-*{{cite journal  | author=Kraemer D, Dresbach T, Drenckhahn D |title=Mrnp41 (Rae 1p) associates with microtubules in HeLa cells and in neurons. |journal=Eur. J. Cell Biol. |volume=80 |issue= 12 |pages= 733-40 |year= 2002 |pmid= 11831386 |doi=  }}
+*{{cite journal   |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
-*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
+*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928 }}
-*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
+*{{cite journal   |vauthors=Faria PA, Chakraborty P, Levay A, etal |title=VSV disrupts the Rae1/mrnp41 mRNA nuclear export pathway. |journal=Mol. Cell |volume=17 |issue= 1 |pages= 93–102 |year= 2005 |pmid= 15629720 |doi= 10.1016/j.molcel.2004.11.023 }}
-*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
+*{{cite journal   |vauthors=Benzinger A, Muster N, Koch HB, etal |title=Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer. |journal=Mol. Cell. Proteomics |volume=4 |issue= 6 |pages= 785–95 |year= 2005 |pmid= 15778465 |doi= 10.1074/mcp.M500021-MCP200 }}
-*{{cite journal  | author=Faria PA, Chakraborty P, Levay A, ''et al.'' |title=VSV disrupts the Rae1/mrnp41 mRNA nuclear export pathway. |journal=Mol. Cell |volume=17 |issue= 1 |pages= 93-102 |year= 2005 |pmid= 15629720 |doi= 10.1016/j.molcel.2004.11.023 }}
+*{{cite journal  |vauthors=Blower MD, Nachury M, Heald R, Weis K |title=A Rae1-containing ribonucleoprotein complex is required for mitotic spindle assembly. |journal=Cell |volume=121 |issue= 2 |pages= 223–34 |year= 2005 |pmid= 15851029 |doi= 10.1016/j.cell.2005.02.016 }}
-*{{cite journal  | author=Benzinger A, Muster N, Koch HB, ''et al.'' |title=Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer. |journal=Mol. Cell Proteomics |volume=4 |issue= 6 |pages= 785-95 |year= 2005 |pmid= 15778465 |doi= 10.1074/mcp.M500021-MCP200 }}
+*{{cite journal  |vauthors=Wong RW, Blobel G, Coutavas E |title=Rae1 interaction with NuMA is required for bipolar spindle formation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=103 |issue= 52 |pages= 19783–7 |year= 2007 |pmid= 17172455 |doi= 10.1073/pnas.0609582104  | pmc=1750899 |bibcode=2006PNAS..10319783W }}
-*{{cite journal  | author=Blower MD, Nachury M, Heald R, Weis K |title=A Rae1-containing ribonucleoprotein complex is required for mitotic spindle assembly. |journal=Cell |volume=121 |issue= 2 |pages= 223-34 |year= 2005 |pmid= 15851029 |doi= 10.1016/j.cell.2005.02.016 }}
-*{{cite journal  | author=Wong RW, Blobel G, Coutavas E |title=Rae1 interaction with NuMA is required for bipolar spindle formation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=103 |issue= 52 |pages= 19783-7 |year= 2007 |pmid= 17172455 |doi= 10.1073/pnas.0609582104 }}
 }}
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RAE1: Difference between revisions

Latest revision as of 07:15, 10 January 2019

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