ELL (gene): Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''RNA polymerase II elongation factor ELL''' is an [[enzyme]] that in humans is encoded by the ''ELL'' [[gene]].<ref name="pmid7991593">{{cite journal | vauthors = Thirman MJ, Levitan DA, Kobayashi H, Simon MC, Rowley JD | title = Cloning of ELL, a gene that fuses to MLL in a t(11;19)(q23;p13.1) in acute myeloid leukemia | journal = Proc Natl Acad Sci U S A | volume = 91 | issue = 25 | pages = 12110–4 | date = Jan 1995 | pmid = 7991593 | pmc = 45386 | doi = 10.1073/pnas.91.25.12110 }}</ref><ref name="pmid8596958">{{cite journal | vauthors = Shilatifard A, Lane WS, Jackson KW, Conaway RC, Conaway JW | title = An RNA polymerase II elongation factor encoded by the human ELL gene | journal = Science | volume = 271 | issue = 5257 | pages = 1873–6 | date = Apr 1996 | pmid = 8596958 | pmc = | doi = 10.1126/science.271.5257.1873 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ELL elongation factor RNA polymerase II| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8178| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Interactions ==
{{GNF_Protein_box
| image = PBB_Protein_ELL_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2doa.
| PDB = {{PDB2|2doa}}
| Name = Elongation factor RNA polymerase II
| HGNCid = 23114
| Symbol = ELL
| AltSymbols =; C19orf17; DKFZp434I1916; ELL1; Men
| OMIM = 600284
| ECnumber = 
| Homologene = 4762
| MGIid = 109377
| GeneAtlas_image1 = PBB_GE_ELL_204096_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_ELL_204095_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_ELL_gnf1h09335_s_at_tn.png
| Function = {{GNF_GO|id=GO:0008159 |text = positive transcription elongation factor activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006368 |text = RNA elongation from RNA polymerase II promoter}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 8178
    | Hs_Ensembl = ENSG00000105656
    | Hs_RefseqProtein = NP_006523
    | Hs_RefseqmRNA = NM_006532
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 19
    | Hs_GenLoc_start = 18414475
    | Hs_GenLoc_end = 18493918
    | Hs_Uniprot = P55199
    | Mm_EntrezGene = 13716
    | Mm_Ensembl = ENSMUSG00000070002
    | Mm_RefseqmRNA = NM_007924
    | Mm_RefseqProtein = NP_031950
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 8
    | Mm_GenLoc_start = 73468694
    | Mm_GenLoc_end = 73521845
    | Mm_Uniprot = Q3TXY9
  }}
}}
'''Elongation factor RNA polymerase II''', also known as '''ELL''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ELL elongation factor RNA polymerase II| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8178| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
ELL (gene) has been shown to [[Protein-protein interaction|interact]] with [[P53]].<ref name=pmid10358050>{{cite journal | vauthors = Shinobu N, Maeda T, Aso T, Ito T, Kondo T, Koike K, Hatakeyama M | title = Physical interaction and functional antagonism between the RNA polymerase II elongation factor ELL and p53 | journal = J. Biol. Chem. | volume = 274 | issue = 24 | pages = 17003–10 | date = Jun 1999 | pmid = 10358050 | doi = 10.1074/jbc.274.24.17003 }}</ref>
{{PBB_Summary
| section_title =  
| summary_text =  
}}


==References==
== References ==
{{reflist|2}}
{{reflist}}
==Further reading==
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Iwabuchi K, Bartel PL, Li B, Marraccino R, Fields S | title = Two cellular proteins that bind to wild-type but not mutant p53. | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 91 | issue = 13 | pages = 6098–102 | year = 1994 | pmid = 8016121 | pmc = 44145 | doi = 10.1073/pnas.91.13.6098 }}
| citations =
* {{cite journal | vauthors = Maruyama K, Sugano S | title = Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. | journal = Gene | volume = 138 | issue = 1–2 | pages = 171–4 | year = 1994 | pmid = 8125298 | doi = 10.1016/0378-1119(94)90802-8 }}
*{{cite journal  | author=Thirman MJ, Levitan DA, Kobayashi H, ''et al.'' |title=Cloning of ELL, a gene that fuses to MLL in a t(11;19)(q23;p13.1) in acute myeloid leukemia. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 25 |pages= 12110-4 |year= 1995 |pmid= 7991593 |doi=  }}
* {{cite journal | vauthors = Shilatifard A, Haque D, Conaway RC, Conaway JW | title = Structure and function of RNA polymerase II elongation factor ELL. Identification of two overlapping ELL functional domains that govern its interaction with polymerase and the ternary elongation complex | journal = J. Biol. Chem. | volume = 272 | issue = 35 | pages = 22355–63 | year = 1997 | pmid = 9268387 | doi = 10.1074/jbc.272.35.22355 }}
*{{cite journal | author=Iwabuchi K, Bartel PL, Li B, ''et al.'' |title=Two cellular proteins that bind to wild-type but not mutant p53. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 13 |pages= 6098-102 |year= 1994 |pmid= 8016121 |doi= }}
* {{cite journal | vauthors = Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S | title = Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library | journal = Gene | volume = 200 | issue = 1–2 | pages = 149–56 | year = 1997 | pmid = 9373149 | doi = 10.1016/S0378-1119(97)00411-3 }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
* {{cite journal | vauthors = Shilatifard A | title = Identification and purification of the Holo-ELL complex. Evidence for the presence of ELL-associated proteins that suppress the transcriptional inhibitory activity of ELL | journal = J. Biol. Chem. | volume = 273 | issue = 18 | pages = 11212–7 | year = 1998 | pmid = 9556611 | doi = 10.1074/jbc.273.18.11212 }}
*{{cite journal  | author=Shilatifard A, Lane WS, Jackson KW, ''et al.'' |title=An RNA polymerase II elongation factor encoded by the human ELL gene. |journal=Science |volume=271 |issue= 5257 |pages= 1873-6 |year= 1996 |pmid= 8596958 |doi=  }}
* {{cite journal | vauthors = Li XY, Green MR | title = The HIV-1 Tat cellular coactivator Tat-SF1 is a general transcription elongation factor | journal = Genes Dev. | volume = 12 | issue = 19 | pages = 2992–6 | year = 1998 | pmid = 9765201 | pmc = 317190 | doi = 10.1101/gad.12.19.2992 }}
*{{cite journal | author=Shilatifard A, Haque D, Conaway RC, Conaway JW |title=Structure and function of RNA polymerase II elongation factor ELL. Identification of two overlapping ELL functional domains that govern its interaction with polymerase and the ternary elongation complex. |journal=J. Biol. Chem. |volume=272 |issue= 35 |pages= 22355-63 |year= 1997 |pmid= 9268387 |doi= }}
* {{cite journal | vauthors = Shinobu N, Maeda T, Aso T, Ito T, Kondo T, Koike K, Hatakeyama M | title = Physical interaction and functional antagonism between the RNA polymerase II elongation factor ELL and p53 | journal = J. Biol. Chem. | volume = 274 | issue = 24 | pages = 17003–10 | year = 1999 | pmid = 10358050 | doi = 10.1074/jbc.274.24.17003 }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
* {{cite journal | vauthors = Schmidt AE, Miller T, Schmidt SL, Shiekhattar R, Shilatifard A | title = Cloning and characterization of the EAP30 subunit of the ELL complex that confers derepression of transcription by RNA polymerase II | journal = J. Biol. Chem. | volume = 274 | issue = 31 | pages = 21981–5 | year = 1999 | pmid = 10419521 | doi = 10.1074/jbc.274.31.21981 }}
*{{cite journal | author=Shilatifard A |title=Identification and purification of the Holo-ELL complex. Evidence for the presence of ELL-associated proteins that suppress the transcriptional inhibitory activity of ELL. |journal=J. Biol. Chem. |volume=273 |issue= 18 |pages= 11212-7 |year= 1998 |pmid= 9556611 |doi= }}
* {{cite journal | vauthors = Kim MK, Nikodem VM | title = hnRNP U inhibits carboxy-terminal domain phosphorylation by TFIIH and represses RNA polymerase II elongation | journal = Mol. Cell. Biol. | volume = 19 | issue = 10 | pages = 6833–44 | year = 2000 | pmid = 10490622 | pmc = 84680 | doi =  }}
*{{cite journal | author=Li XY, Green MR |title=The HIV-1 Tat cellular coactivator Tat-SF1 is a general transcription elongation factor. |journal=Genes Dev. |volume=12 |issue= 19 |pages= 2992-6 |year= 1998 |pmid= 9765201 |doi= }}
* {{cite journal | vauthors = Lavau C, Luo RT, Du C, Thirman MJ | title = Retrovirus-mediated gene transfer of MLL-ELL transforms primary myeloid progenitors and causes acute myeloid leukemias in mice | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 97 | issue = 20 | pages = 10984–9 | year = 2000 | pmid = 10995463 | pmc = 27135 | doi = 10.1073/pnas.190167297 }}
*{{cite journal | author=Shinobu N, Maeda T, Aso T, ''et al.'' |title=Physical interaction and functional antagonism between the RNA polymerase II elongation factor ELL and p53. |journal=J. Biol. Chem. |volume=274 |issue= 24 |pages= 17003-10 |year= 1999 |pmid= 10358050 |doi= }}
* {{cite journal | vauthors = Simone F, Polak PE, Kaberlein JJ, Luo RT, Levitan DA, Thirman MJ | title = EAF1, a novel ELL-associated factor that is delocalized by expression of the MLL-ELL fusion protein | journal = Blood | volume = 98 | issue = 1 | pages = 201–9 | year = 2001 | pmid = 11418481 | doi = 10.1182/blood.V98.1.201 }}
*{{cite journal | author=Schmidt AE, Miller T, Schmidt SL, ''et al.'' |title=Cloning and characterization of the EAP30 subunit of the ELL complex that confers derepression of transcription by RNA polymerase II. |journal=J. Biol. Chem. |volume=274 |issue= 31 |pages= 21981-5 |year= 1999 |pmid= 10419521 |doi= }}
* {{cite journal | vauthors = Luo RT, Lavau C, Du C, Simone F, Polak PE, Kawamata S, Thirman MJ | title = The elongation domain of ELL is dispensable but its ELL-associated factor 1 interaction domain is essential for MLL-ELL-induced leukemogenesis | journal = Mol. Cell. Biol. | volume = 21 | issue = 16 | pages = 5678–87 | year = 2001 | pmid = 11463848 | pmc = 87288 | doi = 10.1128/MCB.21.16.5678-5687.2001 }}
*{{cite journal | author=Kim MK, Nikodem VM |title=hnRNP U inhibits carboxy-terminal domain phosphorylation by TFIIH and represses RNA polymerase II elongation. |journal=Mol. Cell. Biol. |volume=19 |issue= 10 |pages= 6833-44 |year= 2000 |pmid= 10490622 |doi=  }}
* {{cite journal | vauthors = Simone F, Luo RT, Polak PE, Kaberlein JJ, Thirman MJ | title = ELL-associated factor 2 (EAF2), a functional homolog of EAF1 with alternative ELL binding properties | journal = Blood | volume = 101 | issue = 6 | pages = 2355–62 | year = 2003 | pmid = 12446457 | doi = 10.1182/blood-2002-06-1664 }}
*{{cite journal | author=Lavau C, Luo RT, Du C, Thirman MJ |title=Retrovirus-mediated gene transfer of MLL-ELL transforms primary myeloid progenitors and causes acute myeloid leukemias in mice. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 20 |pages= 10984-9 |year= 2000 |pmid= 10995463 |doi= 10.1073/pnas.190167297 }}
* {{cite journal | vauthors = Polak PE, Simone F, Kaberlein JJ, Luo RT, Thirman MJ | title = ELL and EAF1 are Cajal body components that are disrupted in MLL-ELL leukemia | journal = Mol. Biol. Cell | volume = 14 | issue = 4 | pages = 1517–28 | year = 2003 | pmid = 12686606 | pmc = 153119 | doi = 10.1091/mbc.E02-07-0394 }}
*{{cite journal | author=Wiemann S, Weil B, Wellenreuther R, ''et al.'' |title=Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. |journal=Genome Res. |volume=11 |issue= 3 |pages= 422-35 |year= 2001 |pmid= 11230166 |doi= 10.1101/gr.154701 }}
* {{cite journal | vauthors = Wiederschain D, Kawai H, Gu J, Shilatifard A, Yuan ZM | title = Molecular basis of p53 functional inactivation by the leukemic protein MLL-ELL | journal = Mol. Cell. Biol. | volume = 23 | issue = 12 | pages = 4230–46 | year = 2003 | pmid = 12773566 | pmc = 156137 | doi = 10.1128/MCB.23.12.4230-4246.2003 }}
*{{cite journal  | author=Simone F, Polak PE, Kaberlein JJ, ''et al.'' |title=EAF1, a novel ELL-associated factor that is delocalized by expression of the MLL-ELL fusion protein. |journal=Blood |volume=98 |issue= 1 |pages= 201-9 |year= 2001 |pmid= 11418481 |doi= }}
*{{cite journal | author=Luo RT, Lavau C, Du C, ''et al.'' |title=The elongation domain of ELL is dispensable but its ELL-associated factor 1 interaction domain is essential for MLL-ELL-induced leukemogenesis. |journal=Mol. Cell. Biol. |volume=21 |issue= 16 |pages= 5678-87 |year= 2001 |pmid= 11463848 |doi= 10.1128/MCB.21.16.5678-5687.2001 }}
*{{cite journal | author=Simone F, Luo RT, Polak PE, ''et al.'' |title=ELL-associated factor 2 (EAF2), a functional homolog of EAF1 with alternative ELL binding properties. |journal=Blood |volume=101 |issue= 6 |pages= 2355-62 |year= 2003 |pmid= 12446457 |doi= 10.1182/blood-2002-06-1664 }}
*{{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  | author=Polak PE, Simone F, Kaberlein JJ, ''et al.'' |title=ELL and EAF1 are Cajal body components that are disrupted in MLL-ELL leukemia. |journal=Mol. Biol. Cell |volume=14 |issue= 4 |pages= 1517-28 |year= 2003 |pmid= 12686606 |doi= 10.1091/mbc.E02-07-0394 }}
*{{cite journal | author=Wiederschain D, Kawai H, Gu J, ''et al.'' |title=Molecular basis of p53 functional inactivation by the leukemic protein MLL-ELL. |journal=Mol. Cell. Biol. |volume=23 |issue= 12 |pages= 4230-46 |year= 2003 |pmid= 12773566 |doi= }}
*{{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 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{PDB Gallery|geneid=8178}}
{{WikiDoc Sources}}
 
 
{{gene-19-stub}}

Latest revision as of 02:03, 27 October 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

RNA polymerase II elongation factor ELL is an enzyme that in humans is encoded by the ELL gene.[1][2][3]

Interactions

ELL (gene) has been shown to interact with P53.[4]

References

  1. ↑ Thirman MJ, Levitan DA, Kobayashi H, Simon MC, Rowley JD (Jan 1995). "Cloning of ELL, a gene that fuses to MLL in a t(11;19)(q23;p13.1) in acute myeloid leukemia". Proc Natl Acad Sci U S A. 91 (25): 12110–4. doi:10.1073/pnas.91.25.12110. PMC 45386. PMID 7991593.
  2. ↑ Shilatifard A, Lane WS, Jackson KW, Conaway RC, Conaway JW (Apr 1996). "An RNA polymerase II elongation factor encoded by the human ELL gene". Science. 271 (5257): 1873–6. doi:10.1126/science.271.5257.1873. PMID 8596958.
  3. ↑ "Entrez Gene: ELL elongation factor RNA polymerase II".
  4. ↑ Shinobu N, Maeda T, Aso T, Ito T, Kondo T, Koike K, Hatakeyama M (Jun 1999). "Physical interaction and functional antagonism between the RNA polymerase II elongation factor ELL and p53". J. Biol. Chem. 274 (24): 17003–10. doi:10.1074/jbc.274.24.17003. PMID 10358050.

Further reading


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