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{{distinguish|France}}
{{distinguish|France}}
{{Infobox_gene}}
{{Infobox_gene|List of PDB id codes=2ILR, 2W18|Molecular Mass=58711 Da}}
'''Fanconi anemia group E protein''' is a [[protein]] that in humans is encoded by the ''FANCE'' [[gene]].<ref name="pmid7662964">{{cite journal |vauthors=Joenje H, Lo ten Foe JR, Oostra AB, van Berkel CG, Rooimans MA, Schroeder-Kurth T, Wegner RD, Gille JJ, Buchwald M, Arwert F | title = Classification of Fanconi anemia patients by complementation analysis: evidence for a fifth genetic subtype | journal = Blood | volume = 86 | issue = 6 | pages = 2156–60 | date = Oct 1995 | pmid = 7662964 | pmc =  | doi =  }}</ref><ref name="pmid11001585">{{cite journal |vauthors=de Winter JP, Léveillé F, van Berkel CG, Rooimans MA, van Der Weel L, Steltenpool J, Demuth I, Morgan NV, Alon N, Bosnoyan-Collins L, Lightfoot J, Leegwater PA, Waisfisz Q, Komatsu K, Arwert F, Pronk JC, Mathew CG, Digweed M, Buchwald M, Joenje H | title = Isolation of a cDNA representing the Fanconi anemia complementation group E gene | journal = Am J Hum Genet | volume = 67 | issue = 5 | pages = 1306–8 | date = Nov 2000 | pmid = 11001585 | pmc = 1288571 | doi = 10.1016/S0002-9297(07)62959-0 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: FANCE Fanconi anemia, complementation group E| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2178| accessdate = }}</ref>
'''Fanconi anemia, complementation group E protein''' is a [[protein]] that in humans is encoded by the ''FANCE'' [[gene]].<ref name="pmid7662964">{{cite journal | vauthors = Joenje H, Lo ten Foe JR, Oostra AB, van Berkel CG, Rooimans MA, Schroeder-Kurth T, Wegner RD, Gille JJ, Buchwald M, Arwert F | title = Classification of Fanconi anemia patients by complementation analysis: evidence for a fifth genetic subtype | journal = Blood | volume = 86 | issue = 6 | pages = 2156–60 | date = September 1995 | pmid = 7662964 | pmc =  | doi =  }}</ref><ref name="pmid11001585">{{cite journal | vauthors = de Winter JP, Léveillé F, van Berkel CG, Rooimans MA, van Der Weel L, Steltenpool J, Demuth I, Morgan NV, Alon N, Bosnoyan-Collins L, Lightfoot J, Leegwater PA, Waisfisz Q, Komatsu K, Arwert F, Pronk JC, Mathew CG, Digweed M, Buchwald M, Joenje H | title = Isolation of a cDNA representing the Fanconi anemia complementation group E gene | journal = American Journal of Human Genetics | volume = 67 | issue = 5 | pages = 1306–8 | date = November 2000 | pmid = 11001585 | pmc = 1288571 | doi = 10.1016/S0002-9297(07)62959-0 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: FANCE Fanconi anemia, complementation group E| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2178| access-date = }}</ref> The Fanconi anemia complementation group (FANC) currently includes [[FANCA]], [[FANCB]], [[Fanconi anemia, complementation group C|FANCC]], [[BRCA2|FANCD1]] (also called BRCA2), [[FANCD2]], [[FANCE]], [[FANCF]], [[FANCG]], and [[FANCL]]. Fanconi anemia is a genetically heterogeneous recessive disorder characterized by cytogenetic instability, hypersensitivity to DNA cross-linking agents, increased chromosomal breakage, and defective DNA repair. The members of the Fanconi anemia complementation group do not share sequence similarity; they are related by their assembly into a common nuclear protein complex. This gene encodes the protein for complementation groufcrp E.<ref name="entrez" />
 
A [[Cell nucleus|nuclear]] complex containing FANCE protein (as well as [[FANCC]], [[FANCF]] and [[FANCG]]) is essential for the activation of the [[FANCD2]] protein to the [[Ubiquitin|mono-ubiquitinated]] isoform.<ref name="Garcia-Higuera">{{cite journal | vauthors = Garcia-Higuera I, Taniguchi T, Ganesan S, Meyn MS, Timmers C, Hejna J, Grompe M, D'Andrea AD | title = Interaction of the Fanconi anemia proteins and BRCA1 in a common pathway | journal = Molecular Cell | volume = 7 | issue = 2 | pages = 249–62 | date = February 2001 | pmid = 11239454 | doi = 10.1016/s1097-2765(01)00173-3 }}</ref>  In normal, non-mutant cells, FANCD2 is mono-ubiquinated in response to DNA damage. FANCE together with [[FANCC]] acts as the substrate adapter for this reaction <ref>{{cite journal | vauthors = van Twest S, Murphy VJ, Hodson C, Tan W, Swuec P, O'Rourke JJ, Heierhorst J, Crismani W, Deans AJ | title = Mechanism of Ubiquitination and Deubiquitination in the Fanconi Anemia Pathway | journal = Molecular Cell | volume = 65 | issue = 2 | pages = 247–259 | date = January 2017 | pmid = 27986371 | doi = 10.1016/j.molcel.2016.11.005 }}</ref> Activated FANCD2 protein co-localizes with [[BRCA1]] (breast cancer susceptibility protein) at [[ionizing radiation]]-induced foci and in [[synaptonemal complex]]es of [[meiosis|meiotic]] chromosomes. Activated FANCD2 protein may function prior to the initiation of [[Genetic recombination|meiotic recombination]], perhaps to prepare chromosomes for synapses, or to regulate subsequent recombination events.<ref name="Garcia-Higuera" />
 
== Gene Expression ==
FANCE is stated to have been expressed in 151 organs with the highest level in female gonads.<ref>{{Cite web|url=https://www.uniprot.org/uniprot/Q9HB96|title=FANCE - Fanconi anemia group E protein - Homo sapiens (Human) - FANCE gene & protein|website=www.uniprot.org|language=en|access-date=2018-11-09}}</ref>
 
== Chromosomal Location ==
The location of the gene is in 6p21.31, where p is the short arm of chromosome 6 at position 21.31<ref name=":2">{{Cite web|url=https://www.ncbi.nlm.nih.gov/gene/2178|title=FANCE FA complementation group E [Homo sapiens (human)] - Gene - NCBI|website=www.ncbi.nlm.nih.gov|language=en|access-date=2018-11-09}}</ref>
 
The location at molecular level is in base pairs 35,452,339 to 35,467,106 on chromosome 6 (Homo sapiens Annotation Release 109, GRCh38.p12) <ref name=":2" />
 
== Protein Characteristics ==
The main complex of FA contains a nuclear multi-subunit complex of notably 8 FA proteins<ref>{{cite journal | vauthors = Medhurst AL, Huber PA, Waisfisz Q, de Winter  JP, Mathew CG | title = Direct interactions of the five known Fanconi anaemia proteins suggest a common functional pathway | journal = Human Molecular Genetics | volume = 10 | issue = 4 | pages = 423–9 | date = February 2001 | pmid = 11157805 }}</ref>. This adds a single ubiquiting chain to the FANCD2 following DNA damage or duplicative pressure<ref>{{cite journal | vauthors = Garcia-Higuera I, Taniguchi T, Ganesan S, Meyn MS, Timmers C, Hejna J, Grompe M, D'Andrea AD | title = Interaction of the Fanconi anemia proteins and BRCA1 in a common pathway | journal = Molecular Cell | volume = 7 | issue = 2 | pages = 249–62 | date = February 2001 | pmid = 11239454 }}</ref>.
 
For the collection of FANCC, FANCE is important in the nucleus and gathering of the core complex. Some characteristics of FANCE is that it can set itself with [[Ubiquitin|ubiquitinated]] FANCD2, BRCA2 and constructed nuclear foci. Also, as it is the only member showing direct union with FANCD2 and gives the needed links between FA core complex and FANCD2.<ref name=":0">{{cite journal | vauthors = Nookala RK, Hussain S, Pellegrini L | title = Insights into Fanconi Anaemia from the structure of human FANCE | journal = Nucleic Acids Research | volume = 35 | issue = 5 | pages = 1638–48 | date = 2007 | pmid = 17308347 | pmc = 1865054 | doi = 10.1093/nar/gkm033 }}</ref>
 
The structure of FANCE has an [[Epitope mapping|epitope]] on its surface that is found to be important for its binding with FANCD2. The existence of recurrent helical motif was not clear when analysis of amino acids were done.
 
=== Protein Structure ===
It consists of 13 α-helices, 1 3<sub>10</sub>-helix and no β-strand. Long shaped, non-globular shape and 70 Å n size. Width of 30 Å and thickness 20 Å. The protein folds continuously in right-handed manner from N- to C- terminal. Identifying it is easy because of its helices at the end of C-end<ref name=":0" />.


== Function ==
== Function ==
It restores DNA cross-links and is needed for nuclear accumulation of FANCC, delivering a critical bridge between FA complex and FANCD2.<ref name=":1">{{Cite web|url=https://www.abcam.com/fance-antibody-ab126177.html|title=Anti-FANCE antibody (ab126177) {{!}} Abcam|website=www.abcam.com|language=en|access-date=2018-11-09}}</ref>


The Fanconi anemia complementation group (FANC) currently includes FANCA, FANCB, FANCC, FANCD1 (also called BRCA2), FANCD2, FANCE, FANCF, FANCG, and FANCL. Fanconi anemia is a genetically heterogeneous recessive disorder characterized by cytogenetic instability, hypersensitivity to DNA crosslinking agents, increased chromosomal breakage, and defective DNA repair. The members of the Fanconi anemia complementation group do not share sequence similarity; they are related by their assembly into a common nuclear protein complex. This gene encodes the protein for complementation group E.<ref name="entrez" />
== Applications ==
 
* FANCE has its application in [[Western blot|Western Blot]] and [[Immunohistochemistry|IHC-P]] (Immunohistochemistry) where the predicted molecular weight was 58 kDa in Western blot and antigen recovery with citrate buffer pH6 was done before the onset of IHC-P <ref name=":1" />.
 
* FANCE is also used in [[Gene mapping|Gene Mapping]], here [[Zygosity|homozygosity mapping]], where it is fused with 3 DNA cells that will help in calculating the sensitivity to composites of Mitomycin C, a DNA cross-linking agent (Sigma). It also then examines the use of micro satellite markers D6S422 and D6S1610<ref>{{cite journal | vauthors = Waisfisz Q, Saar K, Morgan NV, Altay C, Leegwater PA, de Winter JP, Komatsu K, Evans GR, Wegner RD, Reis A, Joenje H, Arwert F, Mathew CG, Pronk JC, Digweed M | title = The Fanconi anemia group E gene, FANCE, maps to chromosome 6p | journal = American Journal of Human Genetics | volume = 64 | issue = 5 | pages = 1400–5 | date = May 1999 | pmid = 10205272 | pmc = 1377877 | doi = 10.1086/302385 }}</ref>, for linking. From this, a chromosomal region on chromosome 6p is located for FANCE<ref>{{cite journal | vauthors = Waisfisz Q, Saar K, Morgan NV, Altay C, Leegwater PA, de Winter JP, Komatsu K, Evans GR, Wegner RD, Reis A, Joenje H, Arwert F, Mathew CG, Pronk JC, Digweed M | title = The Fanconi anemia group E gene, FANCE, maps to chromosome 6p | journal = American Journal of Human Genetics | volume = 64 | issue = 5 | pages = 1400–5 | date = May 1999 | pmid = 10205272 | pmc = 1377877 | doi = 10.1086/302385 | url = https://doi.org/10.1086/302385 }}</ref>.
*[[Western blot|Immunoblotting]] showed that FANCE-L348M and FANCE-E263K mutants showed a division in the nuclear membrane of FA-E EUFA409 LCL indicating that irrespective of FANCE having putative nuclear localization signals,<ref>{{cite journal | vauthors = de Winter JP, Léveillé F, van Berkel CG, Rooimans MA, van Der Weel L, Steltenpool J, Demuth I, Morgan NV, Alon N, Bosnoyan-Collins L, Lightfoot J, Leegwater PA, Waisfisz Q, Komatsu K, Arwert F, Pronk JC, Mathew CG, Digweed M, Buchwald M, Joenje H | title = Isolation of a cDNA representing the Fanconi anemia complementation group E gene | journal = American Journal of Human Genetics | volume = 67 | issue = 5 | pages = 1306–8 | date = November 2000 | pmid = 11001585 | pmc = 1288571 | doi = 10.1016/s0002-9297(07)62959-0 | url = https://doi.org/10.1016/S0002-9297(07)62959-0 }}</ref> it limits primarily to the nucleus<ref>{{cite journal | vauthors = Taniguchi T, D'Andrea AD | title = The Fanconi anemia protein, FANCE, promotes the nuclear accumulation of FANCC | journal = Blood | volume = 100 | issue = 7 | pages = 2457–62 | date = October 2002 | pmid = 12239156 | doi = 10.1182/blood-2002-03-0860 | url = http://www.bloodjournal.org/content/100/7/2457 }}</ref>. 


== Interactions ==
== Interactions ==


FANCE has been shown to [[Protein-protein interaction|interact]] with:
FANCE has been shown to [[Protein-protein interaction|interact]] with:  
* [[FANCA]],<ref name = pmid12239156/><ref name = pmid11157805/><ref name = pmid12093742/><ref name = pmid12973351>{{cite journal | vauthors = Meetei AR, de Winter JP, Medhurst AL, Wallisch M, Waisfisz Q, van de Vrugt HJ, Oostra AB, Yan Z, Ling C, Bishop CE, Hoatlin ME, Joenje H, Wang W | title = A novel ubiquitin ligase is deficient in Fanconi anemia | journal = Nat. Genet. | volume = 35 | issue = 2 | pages = 165–70 | date = Oct 2003 | pmid = 12973351 | doi = 10.1038/ng1241 }}</ref>
* [[FANCA]],<ref name = pmid12239156/><ref name = pmid11157805/><ref name = pmid12093742/><ref name = pmid12973351>{{cite journal | vauthors = Meetei AR, de Winter JP, Medhurst AL, Wallisch M, Waisfisz Q, van de Vrugt HJ, Oostra AB, Yan Z, Ling C, Bishop CE, Hoatlin ME, Joenje H, Wang W | title = A novel ubiquitin ligase is deficient in Fanconi anemia | journal = Nature Genetics | volume = 35 | issue = 2 | pages = 165–70 | date = October 2003 | pmid = 12973351 | doi = 10.1038/ng1241 }}</ref>
* [[FANCD2]],<ref name = pmid12093742/><ref name = pmid12649160/><ref name = pmid15115758>{{cite journal |vauthors=Hussain S, Wilson JB, Medhurst AL, Hejna J, Witt E, Ananth S, Davies A, Masson JY, Moses R, West SC, de Winter JP, Ashworth A, Jones NJ, Mathew CG | title = Direct interaction of FANCD2 with BRCA2 in DNA damage response pathways | journal = Hum. Mol. Genet. | volume = 13 | issue = 12 | pages = 1241–8 | date = Jun 2004 | pmid = 15115758 | doi = 10.1093/hmg/ddh135 }}</ref>  
* [[FANCD2]],<ref name = pmid12093742/><ref name = pmid12649160/><ref name = pmid15115758>{{cite journal | vauthors = Hussain S, Wilson JB, Medhurst AL, Hejna J, Witt E, Ananth S, Davies A, Masson JY, Moses R, West SC, de Winter JP, Ashworth A, Jones NJ, Mathew CG | title = Direct interaction of FANCD2 with BRCA2 in DNA damage response pathways | journal = Human Molecular Genetics | volume = 13 | issue = 12 | pages = 1241–8 | date = June 2004 | pmid = 15115758 | doi = 10.1093/hmg/ddh135 }}</ref>  
* [[FANCF]]<ref name = pmid12093742/><ref name = pmid15262960/>  
* [[FANCF]]<ref name = pmid12093742/><ref name = pmid15262960>{{cite journal | vauthors = Léveillé F, Blom E, Medhurst AL, Bier P, Laghmani M, Johnson M, Rooimans MA, Sobeck A, Waisfisz Q, Arwert F, Patel KJ, Hoatlin ME, Joenje H, de Winter JP | title = The Fanconi anemia gene product FANCF is a flexible adaptor protein | journal = The Journal of Biological Chemistry | volume = 279 | issue = 38 | pages = 39421–30 | date = September 2004 | pmid = 15262960 | doi = 10.1074/jbc.M407034200 }}</ref>  
* [[FANCG]],<ref name = pmid12239156/><ref name = pmid11157805/><ref name = pmid12093742/> and
* [[FANCG]],<ref name = pmid12239156/><ref name = pmid11157805/><ref name = pmid12093742/> and
* [[Fanconi anemia, complementation group C|FANCC]].<ref name = pmid12239156>{{cite journal |vauthors=Taniguchi T, D'Andrea AD | title = The Fanconi anemia protein, FANCE, promotes the nuclear accumulation of FANCC | journal = Blood | volume = 100 | issue = 7 | pages = 2457–62 | date = Oct 2002 | pmid = 12239156 | doi = 10.1182/blood-2002-03-0860 }}</ref><ref name = pmid11157805>{{cite journal |vauthors=Medhurst AL, Huber PA, Waisfisz Q, de Winter JP, Mathew CG | title = Direct interactions of the five known Fanconi anaemia proteins suggest a common functional pathway | journal = Hum. Mol. Genet. | volume = 10 | issue = 4 | pages = 423–9 | date = Feb 2001 | pmid = 11157805 | doi = 10.1093/hmg/10.4.423}}</ref><ref name = pmid12093742>{{cite journal |vauthors=Pace P, Johnson M, Tan WM, Mosedale G, Sng C, Hoatlin M, de Winter J, Joenje H, Gergely F, Patel KJ | title = FANCE: the link between Fanconi anaemia complex assembly and activity | journal = EMBO J. | volume = 21 | issue = 13 | pages = 3414–23 | date = Jul 2002 | pmid = 12093742 | pmc = 125396 | doi = 10.1093/emboj/cdf355 }}</ref><ref name = pmid12649160>{{cite journal |vauthors=Gordon SM, Buchwald M | title = Fanconi anemia protein complex: mapping protein interactions in the yeast 2- and 3-hybrid systems | journal = Blood | volume = 102 | issue = 1 | pages = 136–41 | date = Jul 2003 | pmid = 12649160 | doi = 10.1182/blood-2002-11-3517 }}</ref><ref name = pmid15262960>{{cite journal |vauthors=Léveillé F, Blom E, Medhurst AL, Bier P, Laghmani el H, Johnson M, Rooimans MA, Sobeck A, Waisfisz Q, Arwert F, Patel KJ, Hoatlin ME, Joenje H, de Winter JP | title = The Fanconi anemia gene product FANCF is a flexible adaptor protein | journal = J. Biol. Chem. | volume = 279 | issue = 38 | pages = 39421–30 | date = Sep 2004 | pmid = 15262960 | doi = 10.1074/jbc.M407034200 }}</ref>
* [[Fanconi anemia, complementation group C|FANCC]].<ref name = pmid12239156>{{cite journal | vauthors = Taniguchi T, D'Andrea AD | title = The Fanconi anemia protein, FANCE, promotes the nuclear accumulation of FANCC | journal = Blood | volume = 100 | issue = 7 | pages = 2457–62 | date = October 2002 | pmid = 12239156 | doi = 10.1182/blood-2002-03-0860 }}</ref><ref name = pmid11157805>{{cite journal | vauthors = Medhurst AL, Huber PA, Waisfisz Q, de Winter JP, Mathew CG | title = Direct interactions of the five known Fanconi anaemia proteins suggest a common functional pathway | journal = Human Molecular Genetics | volume = 10 | issue = 4 | pages = 423–9 | date = February 2001 | pmid = 11157805 | doi = 10.1093/hmg/10.4.423 }}</ref><ref name = pmid12093742>{{cite journal | vauthors = Pace P, Johnson M, Tan WM, Mosedale G, Sng C, Hoatlin M, de Winter J, Joenje H, Gergely F, Patel KJ | title = FANCE: the link between Fanconi anaemia complex assembly and activity | journal = The EMBO Journal | volume = 21 | issue = 13 | pages = 3414–23 | date = July 2002 | pmid = 12093742 | pmc = 125396 | doi = 10.1093/emboj/cdf355 }}</ref><ref name = pmid12649160>{{cite journal | vauthors = Gordon SM, Buchwald M | title = Fanconi anemia protein complex: mapping protein interactions in the yeast 2- and 3-hybrid systems | journal = Blood | volume = 102 | issue = 1 | pages = 136–41 | date = July 2003 | pmid = 12649160 | doi = 10.1182/blood-2002-11-3517 }}</ref><ref name = pmid15262960 />


==References==
== References ==
{{Reflist}}
{{Reflist}}


==Further reading==
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
*{{cite journal |vauthors=Wegner RD, Henrichs I, Joenje H, Schroeder-Kurth T | title = Fanconi anemia complementation group E: clinical and cytogenetic data of the first patient | journal = Clin. Genet. | volume = 50 | issue = 6 | pages = 479–82 | year = 1997 | pmid = 9147877 | doi = 10.1111/j.1399-0004.1996.tb02716.x }}
* {{cite journal | vauthors = Wegner RD, Henrichs I, Joenje H, Schroeder-Kurth T | title = Fanconi anemia complementation group E: clinical and cytogenetic data of the first patient | journal = Clinical Genetics | volume = 50 | issue = 6 | pages = 479–82 | date = December 1996 | pmid = 9147877 | doi = 10.1111/j.1399-0004.1996.tb02716.x }}
*{{cite journal |vauthors=Joenje H, Oostra AB, Wijker M, di Summa FM, van Berkel CG, Rooimans MA, Ebell W, van Weel M, Pronk JC, Buchwald M, Arwert F | title = Evidence for at least eight Fanconi anemia genes | journal = Am. J. Hum. Genet. | volume = 61 | issue = 4 | pages = 940–4 | year = 1997 | pmid = 9382107 | pmc = 1715980 | doi = 10.1086/514881 }}
* {{cite journal | vauthors = Joenje H, Oostra AB, Wijker M, di Summa FM, van Berkel CG, Rooimans MA, Ebell W, van Weel M, Pronk JC, Buchwald M, Arwert F | title = Evidence for at least eight Fanconi anemia genes | journal = American Journal of Human Genetics | volume = 61 | issue = 4 | pages = 940–4 | date = October 1997 | pmid = 9382107 | pmc = 1715980 | doi = 10.1086/514881 }}
*{{cite journal |vauthors=Waisfisz Q, Saar K, Morgan NV, Altay C, Leegwater PA, de Winter JP, Komatsu K, Evans GR, Wegner RD, Reis A, Joenje H, Arwert F, Mathew CG, Pronk JC, Digweed M | title = The Fanconi anemia group E gene, FANCE, maps to chromosome 6p | journal = Am. J. Hum. Genet. | volume = 64 | issue = 5 | pages = 1400–5 | year = 1999 | pmid = 10205272 | pmc = 1377877 | doi = 10.1086/302385 }}
* {{cite journal | vauthors = Waisfisz Q, Saar K, Morgan NV, Altay C, Leegwater PA, de Winter JP, Komatsu K, Evans GR, Wegner RD, Reis A, Joenje H, Arwert F, Mathew CG, Pronk JC, Digweed M | title = The Fanconi anemia group E gene, FANCE, maps to chromosome 6p | journal = American Journal of Human Genetics | volume = 64 | issue = 5 | pages = 1400–5 | date = May 1999 | pmid = 10205272 | pmc = 1377877 | doi = 10.1086/302385 }}
*{{cite journal |vauthors=Medhurst AL, Huber PA, Waisfisz Q, de Winter JP, Mathew CG | title = Direct interactions of the five known Fanconi anaemia proteins suggest a common functional pathway | journal = Hum. Mol. Genet. | volume = 10 | issue = 4 | pages = 423–9 | year = 2001 | pmid = 11157805 | doi = 10.1093/hmg/10.4.423 }}
* {{cite journal | vauthors = Medhurst AL, Huber PA, Waisfisz Q, de Winter JP, Mathew CG | title = Direct interactions of the five known Fanconi anaemia proteins suggest a common functional pathway | journal = Human Molecular Genetics | volume = 10 | issue = 4 | pages = 423–9 | date = February 2001 | pmid = 11157805 | doi = 10.1093/hmg/10.4.423 }}
*{{cite journal |vauthors=Pace P, Johnson M, Tan WM, Mosedale G, Sng C, Hoatlin M, de Winter J, Joenje H, Gergely F, Patel KJ | title = FANCE: the link between Fanconi anaemia complex assembly and activity | journal = EMBO J. | volume = 21 | issue = 13 | pages = 3414–23 | year = 2002 | pmid = 12093742 | pmc = 125396 | doi = 10.1093/emboj/cdf355 }}
* {{cite journal | vauthors = Pace P, Johnson M, Tan WM, Mosedale G, Sng C, Hoatlin M, de Winter J, Joenje H, Gergely F, Patel KJ | title = FANCE: the link between Fanconi anaemia complex assembly and activity | journal = The EMBO Journal | volume = 21 | issue = 13 | pages = 3414–23 | date = July 2002 | pmid = 12093742 | pmc = 125396 | doi = 10.1093/emboj/cdf355 }}
*{{cite journal |vauthors=Taniguchi T, D'Andrea AD | title = The Fanconi anemia protein, FANCE, promotes the nuclear accumulation of FANCC | journal = Blood | volume = 100 | issue = 7 | pages = 2457–62 | year = 2002 | pmid = 12239156 | doi = 10.1182/blood-2002-03-0860 }}
* {{cite journal | vauthors = Taniguchi T, D'Andrea AD | title = The Fanconi anemia protein, FANCE, promotes the nuclear accumulation of FANCC | journal = Blood | volume = 100 | issue = 7 | pages = 2457–62 | date = October 2002 | pmid = 12239156 | doi = 10.1182/blood-2002-03-0860 }}
*{{cite journal |vauthors=Gordon SM, Buchwald M | title = Fanconi anemia protein complex: mapping protein interactions in the yeast 2- and 3-hybrid systems | journal = Blood | volume = 102 | issue = 1 | pages = 136–41 | year = 2003 | pmid = 12649160 | doi = 10.1182/blood-2002-11-3517 }}
* {{cite journal | vauthors = Gordon SM, Buchwald M | title = Fanconi anemia protein complex: mapping protein interactions in the yeast 2- and 3-hybrid systems | journal = Blood | volume = 102 | issue = 1 | pages = 136–41 | date = July 2003 | pmid = 12649160 | doi = 10.1182/blood-2002-11-3517 }}
*{{cite journal |vauthors=Meetei AR, Sechi S, Wallisch M, Yang D, Young MK, Joenje H, Hoatlin ME, Wang W | title = A multiprotein nuclear complex connects Fanconi anemia and Bloom syndrome | journal = Mol. Cell. Biol. | volume = 23 | issue = 10 | pages = 3417–26 | year = 2003 | pmid = 12724401 | pmc = 164758 | doi = 10.1128/MCB.23.10.3417-3426.2003 }}
* {{cite journal | vauthors = Meetei AR, Sechi S, Wallisch M, Yang D, Young MK, Joenje H, Hoatlin ME, Wang W | title = A multiprotein nuclear complex connects Fanconi anemia and Bloom syndrome | journal = Molecular and Cellular Biology | volume = 23 | issue = 10 | pages = 3417–26 | date = May 2003 | pmid = 12724401 | pmc = 164758 | doi = 10.1128/MCB.23.10.3417-3426.2003 }}
*{{cite journal | vauthors = Meetei AR, de Winter JP, Medhurst AL, Wallisch M, Waisfisz Q, van de Vrugt HJ, Oostra AB, Yan Z, Ling C, Bishop CE, Hoatlin ME, Joenje H, Wang W | title = A novel ubiquitin ligase is deficient in Fanconi anemia | journal = Nat. Genet. | volume = 35 | issue = 2 | pages = 165–70 | year = 2003 | pmid = 12973351 | doi = 10.1038/ng1241 }}
* {{cite journal | vauthors = Meetei AR, de Winter JP, Medhurst AL, Wallisch M, Waisfisz Q, van de Vrugt HJ, Oostra AB, Yan Z, Ling C, Bishop CE, Hoatlin ME, Joenje H, Wang W | title = A novel ubiquitin ligase is deficient in Fanconi anemia | journal = Nature Genetics | volume = 35 | issue = 2 | pages = 165–70 | date = October 2003 | pmid = 12973351 | doi = 10.1038/ng1241 }}
*{{cite journal |vauthors=Hussain S, Wilson JB, Medhurst AL, Hejna J, Witt E, Ananth S, Davies A, Masson JY, Moses R, West SC, de Winter JP, Ashworth A, Jones NJ, Mathew CG | title = Direct interaction of FANCD2 with BRCA2 in DNA damage response pathways | journal = Hum. Mol. Genet. | volume = 13 | issue = 12 | pages = 1241–8 | year = 2004 | pmid = 15115758 | doi = 10.1093/hmg/ddh135 }}
* {{cite journal | vauthors = Hussain S, Wilson JB, Medhurst AL, Hejna J, Witt E, Ananth S, Davies A, Masson JY, Moses R, West SC, de Winter JP, Ashworth A, Jones NJ, Mathew CG | title = Direct interaction of FANCD2 with BRCA2 in DNA damage response pathways | journal = Human Molecular Genetics | volume = 13 | issue = 12 | pages = 1241–8 | date = June 2004 | pmid = 15115758 | doi = 10.1093/hmg/ddh135 }}
*{{cite journal |vauthors=Wang X, Andreassen PR, D'Andrea AD | title = Functional interaction of monoubiquitinated FANCD2 and BRCA2/FANCD1 in chromatin | journal = Mol. Cell. Biol. | volume = 24 | issue = 13 | pages = 5850–62 | year = 2004 | pmid = 15199141 | pmc = 480901 | doi = 10.1128/MCB.24.13.5850-5862.2004 }}
* {{cite journal | vauthors = Wang X, Andreassen PR, D'Andrea AD | title = Functional interaction of monoubiquitinated FANCD2 and BRCA2/FANCD1 in chromatin | journal = Molecular and Cellular Biology | volume = 24 | issue = 13 | pages = 5850–62 | date = July 2004 | pmid = 15199141 | pmc = 480901 | doi = 10.1128/MCB.24.13.5850-5862.2004 }}
*{{cite journal |vauthors=Léveillé F, Blom E, Medhurst AL, Bier P, Laghmani el H, Johnson M, Rooimans MA, Sobeck A, Waisfisz Q, Arwert F, Patel KJ, Hoatlin ME, Joenje H, de Winter JP | title = The Fanconi anemia gene product FANCF is a flexible adaptor protein | journal = J. Biol. Chem. | volume = 279 | issue = 38 | pages = 39421–30 | year = 2004 | pmid = 15262960 | doi = 10.1074/jbc.M407034200 }}
* {{cite journal | vauthors = Meetei AR, Levitus M, Xue Y, Medhurst AL, Zwaan M, Ling C, Rooimans MA, Bier P, Hoatlin M, Pals G, de Winter JP, Wang W, Joenje H | title = X-linked inheritance of Fanconi anemia complementation group B | journal = Nature Genetics | volume = 36 | issue = 11 | pages = 1219–24 | date = November 2004 | pmid = 15502827 | doi = 10.1038/ng1458 }}
*{{cite journal |vauthors=Meetei AR, Levitus M, Xue Y, Medhurst AL, Zwaan M, Ling C, Rooimans MA, Bier P, Hoatlin M, Pals G, de Winter JP, Wang W, Joenje H | title = X-linked inheritance of Fanconi anemia complementation group B | journal = Nat. Genet. | volume = 36 | issue = 11 | pages = 1219–24 | year = 2004 | pmid = 15502827 | doi = 10.1038/ng1458 }}
* {{cite journal | vauthors = Meetei AR, Medhurst AL, Ling C, Xue Y, Singh TR, Bier P, Steltenpool J, Stone S, Dokal I, Mathew CG, Hoatlin M, Joenje H, de Winter JP, Wang W | title = A human ortholog of archaeal DNA repair protein Hef is defective in Fanconi anemia complementation group M | journal = Nature Genetics | volume = 37 | issue = 9 | pages = 958–63 | date = September 2005 | pmid = 16116422 | pmc = 2704909 | doi = 10.1038/ng1626 }}
*{{cite journal |vauthors=Meetei AR, Medhurst AL, Ling C, Xue Y, Singh TR, Bier P, Steltenpool J, Stone S, Dokal I, Mathew CG, Hoatlin M, Joenje H, de Winter JP, Wang W | title = A human ortholog of archaeal DNA repair protein Hef is defective in Fanconi anemia complementation group M | journal = Nat. Genet. | volume = 37 | issue = 9 | pages = 958–63 | year = 2005 | pmid = 16116422 | pmc = 2704909 | doi = 10.1038/ng1626 }}
* {{cite journal | vauthors = Gordon SM, Alon N, Buchwald M | title = FANCC, FANCE, and FANCD2 form a ternary complex essential to the integrity of the Fanconi anemia DNA damage response pathway | journal = The Journal of Biological Chemistry | volume = 280 | issue = 43 | pages = 36118–25 | date = October 2005 | pmid = 16127171 | doi = 10.1074/jbc.M507758200 }}
*{{cite journal |vauthors=Gordon SM, Alon N, Buchwald M | title = FANCC, FANCE, and FANCD2 form a ternary complex essential to the integrity of the Fanconi anemia DNA damage response pathway | journal = J. Biol. Chem. | volume = 280 | issue = 43 | pages = 36118–25 | year = 2006 | pmid = 16127171 | doi = 10.1074/jbc.M507758200 }}
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{{PDB Gallery|geneid=2178}}
{{PDB Gallery|geneid=2178}}


{{Gene-6-stub}}
{{Gene-6-stub}}

Latest revision as of 08:37, 9 November 2018

Not to be confused with France.
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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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View/Edit Human

Fanconi anemia, complementation group E protein is a protein that in humans is encoded by the FANCE gene.[1][2][3] The Fanconi anemia complementation group (FANC) currently includes FANCA, FANCB, FANCC, FANCD1 (also called BRCA2), FANCD2, FANCE, FANCF, FANCG, and FANCL. Fanconi anemia is a genetically heterogeneous recessive disorder characterized by cytogenetic instability, hypersensitivity to DNA cross-linking agents, increased chromosomal breakage, and defective DNA repair. The members of the Fanconi anemia complementation group do not share sequence similarity; they are related by their assembly into a common nuclear protein complex. This gene encodes the protein for complementation groufcrp E.[3]

A nuclear complex containing FANCE protein (as well as FANCC, FANCF and FANCG) is essential for the activation of the FANCD2 protein to the mono-ubiquitinated isoform.[4] In normal, non-mutant cells, FANCD2 is mono-ubiquinated in response to DNA damage. FANCE together with FANCC acts as the substrate adapter for this reaction [5] Activated FANCD2 protein co-localizes with BRCA1 (breast cancer susceptibility protein) at ionizing radiation-induced foci and in synaptonemal complexes of meiotic chromosomes. Activated FANCD2 protein may function prior to the initiation of meiotic recombination, perhaps to prepare chromosomes for synapses, or to regulate subsequent recombination events.[4]

Gene Expression

FANCE is stated to have been expressed in 151 organs with the highest level in female gonads.[6]

Chromosomal Location

The location of the gene is in 6p21.31, where p is the short arm of chromosome 6 at position 21.31[7]

The location at molecular level is in base pairs 35,452,339 to 35,467,106 on chromosome 6 (Homo sapiens Annotation Release 109, GRCh38.p12) [7]

Protein Characteristics

The main complex of FA contains a nuclear multi-subunit complex of notably 8 FA proteins[8]. This adds a single ubiquiting chain to the FANCD2 following DNA damage or duplicative pressure[9].

For the collection of FANCC, FANCE is important in the nucleus and gathering of the core complex. Some characteristics of FANCE is that it can set itself with ubiquitinated FANCD2, BRCA2 and constructed nuclear foci. Also, as it is the only member showing direct union with FANCD2 and gives the needed links between FA core complex and FANCD2.[10]

The structure of FANCE has an epitope on its surface that is found to be important for its binding with FANCD2. The existence of recurrent helical motif was not clear when analysis of amino acids were done.

Protein Structure

It consists of 13 α-helices, 1 310-helix and no β-strand. Long shaped, non-globular shape and 70 Å n size. Width of 30 Å and thickness 20 Å. The protein folds continuously in right-handed manner from N- to C- terminal. Identifying it is easy because of its helices at the end of C-end[10].

Function

It restores DNA cross-links and is needed for nuclear accumulation of FANCC, delivering a critical bridge between FA complex and FANCD2.[11]

Applications

  • FANCE has its application in Western Blot and IHC-P (Immunohistochemistry) where the predicted molecular weight was 58 kDa in Western blot and antigen recovery with citrate buffer pH6 was done before the onset of IHC-P [11].
  • FANCE is also used in Gene Mapping, here homozygosity mapping, where it is fused with 3 DNA cells that will help in calculating the sensitivity to composites of Mitomycin C, a DNA cross-linking agent (Sigma). It also then examines the use of micro satellite markers D6S422 and D6S1610[12], for linking. From this, a chromosomal region on chromosome 6p is located for FANCE[13].
  • Immunoblotting showed that FANCE-L348M and FANCE-E263K mutants showed a division in the nuclear membrane of FA-E EUFA409 LCL indicating that irrespective of FANCE having putative nuclear localization signals,[14] it limits primarily to the nucleus[15].

Interactions

FANCE has been shown to interact with:

References

  1. ↑ Joenje H, Lo ten Foe JR, Oostra AB, van Berkel CG, Rooimans MA, Schroeder-Kurth T, Wegner RD, Gille JJ, Buchwald M, Arwert F (September 1995). "Classification of Fanconi anemia patients by complementation analysis: evidence for a fifth genetic subtype". Blood. 86 (6): 2156–60. PMID 7662964.
  2. ↑ de Winter JP, Léveillé F, van Berkel CG, Rooimans MA, van Der Weel L, Steltenpool J, Demuth I, Morgan NV, Alon N, Bosnoyan-Collins L, Lightfoot J, Leegwater PA, Waisfisz Q, Komatsu K, Arwert F, Pronk JC, Mathew CG, Digweed M, Buchwald M, Joenje H (November 2000). "Isolation of a cDNA representing the Fanconi anemia complementation group E gene". American Journal of Human Genetics. 67 (5): 1306–8. doi:10.1016/S0002-9297(07)62959-0. PMC 1288571. PMID 11001585.
  3. ↑ 3.0 3.1 "Entrez Gene: FANCE Fanconi anemia, complementation group E".
  4. ↑ 4.0 4.1 Garcia-Higuera I, Taniguchi T, Ganesan S, Meyn MS, Timmers C, Hejna J, Grompe M, D'Andrea AD (February 2001). "Interaction of the Fanconi anemia proteins and BRCA1 in a common pathway". Molecular Cell. 7 (2): 249–62. doi:10.1016/s1097-2765(01)00173-3. PMID 11239454.
  5. ↑ van Twest S, Murphy VJ, Hodson C, Tan W, Swuec P, O'Rourke JJ, Heierhorst J, Crismani W, Deans AJ (January 2017). "Mechanism of Ubiquitination and Deubiquitination in the Fanconi Anemia Pathway". Molecular Cell. 65 (2): 247–259. doi:10.1016/j.molcel.2016.11.005. PMID 27986371.
  6. ↑ "FANCE - Fanconi anemia group E protein - Homo sapiens (Human) - FANCE gene & protein". www.uniprot.org. Retrieved 2018-11-09.
  7. ↑ 7.0 7.1 "FANCE FA complementation group E [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2018-11-09.
  8. ↑ Medhurst AL, Huber PA, Waisfisz Q, de Winter JP, Mathew CG (February 2001). "Direct interactions of the five known Fanconi anaemia proteins suggest a common functional pathway". Human Molecular Genetics. 10 (4): 423–9. PMID 11157805.
  9. ↑ Garcia-Higuera I, Taniguchi T, Ganesan S, Meyn MS, Timmers C, Hejna J, Grompe M, D'Andrea AD (February 2001). "Interaction of the Fanconi anemia proteins and BRCA1 in a common pathway". Molecular Cell. 7 (2): 249–62. PMID 11239454.
  10. ↑ 10.0 10.1 Nookala RK, Hussain S, Pellegrini L (2007). "Insights into Fanconi Anaemia from the structure of human FANCE". Nucleic Acids Research. 35 (5): 1638–48. doi:10.1093/nar/gkm033. PMC 1865054. PMID 17308347.
  11. ↑ 11.0 11.1 "Anti-FANCE antibody (ab126177) | Abcam". www.abcam.com. Retrieved 2018-11-09.
  12. ↑ Waisfisz Q, Saar K, Morgan NV, Altay C, Leegwater PA, de Winter JP, Komatsu K, Evans GR, Wegner RD, Reis A, Joenje H, Arwert F, Mathew CG, Pronk JC, Digweed M (May 1999). "The Fanconi anemia group E gene, FANCE, maps to chromosome 6p". American Journal of Human Genetics. 64 (5): 1400–5. doi:10.1086/302385. PMC 1377877. PMID 10205272.
  13. ↑ Waisfisz Q, Saar K, Morgan NV, Altay C, Leegwater PA, de Winter JP, Komatsu K, Evans GR, Wegner RD, Reis A, Joenje H, Arwert F, Mathew CG, Pronk JC, Digweed M (May 1999). "The Fanconi anemia group E gene, FANCE, maps to chromosome 6p". American Journal of Human Genetics. 64 (5): 1400–5. doi:10.1086/302385. PMC 1377877. PMID 10205272.
  14. ↑ de Winter JP, Léveillé F, van Berkel CG, Rooimans MA, van Der Weel L, Steltenpool J, Demuth I, Morgan NV, Alon N, Bosnoyan-Collins L, Lightfoot J, Leegwater PA, Waisfisz Q, Komatsu K, Arwert F, Pronk JC, Mathew CG, Digweed M, Buchwald M, Joenje H (November 2000). "Isolation of a cDNA representing the Fanconi anemia complementation group E gene". American Journal of Human Genetics. 67 (5): 1306–8. doi:10.1016/s0002-9297(07)62959-0. PMC 1288571. PMID 11001585.
  15. ↑ Taniguchi T, D'Andrea AD (October 2002). "The Fanconi anemia protein, FANCE, promotes the nuclear accumulation of FANCC". Blood. 100 (7): 2457–62. doi:10.1182/blood-2002-03-0860. PMID 12239156.
  16. ↑ 16.0 16.1 16.2 Taniguchi T, D'Andrea AD (October 2002). "The Fanconi anemia protein, FANCE, promotes the nuclear accumulation of FANCC". Blood. 100 (7): 2457–62. doi:10.1182/blood-2002-03-0860. PMID 12239156.
  17. ↑ 17.0 17.1 17.2 Medhurst AL, Huber PA, Waisfisz Q, de Winter JP, Mathew CG (February 2001). "Direct interactions of the five known Fanconi anaemia proteins suggest a common functional pathway". Human Molecular Genetics. 10 (4): 423–9. doi:10.1093/hmg/10.4.423. PMID 11157805.
  18. ↑ 18.0 18.1 18.2 18.3 18.4 Pace P, Johnson M, Tan WM, Mosedale G, Sng C, Hoatlin M, de Winter J, Joenje H, Gergely F, Patel KJ (July 2002). "FANCE: the link between Fanconi anaemia complex assembly and activity". The EMBO Journal. 21 (13): 3414–23. doi:10.1093/emboj/cdf355. PMC 125396. PMID 12093742.
  19. ↑ Meetei AR, de Winter JP, Medhurst AL, Wallisch M, Waisfisz Q, van de Vrugt HJ, Oostra AB, Yan Z, Ling C, Bishop CE, Hoatlin ME, Joenje H, Wang W (October 2003). "A novel ubiquitin ligase is deficient in Fanconi anemia". Nature Genetics. 35 (2): 165–70. doi:10.1038/ng1241. PMID 12973351.
  20. ↑ 20.0 20.1 Gordon SM, Buchwald M (July 2003). "Fanconi anemia protein complex: mapping protein interactions in the yeast 2- and 3-hybrid systems". Blood. 102 (1): 136–41. doi:10.1182/blood-2002-11-3517. PMID 12649160.
  21. ↑ Hussain S, Wilson JB, Medhurst AL, Hejna J, Witt E, Ananth S, Davies A, Masson JY, Moses R, West SC, de Winter JP, Ashworth A, Jones NJ, Mathew CG (June 2004). "Direct interaction of FANCD2 with BRCA2 in DNA damage response pathways". Human Molecular Genetics. 13 (12): 1241–8. doi:10.1093/hmg/ddh135. PMID 15115758.
  22. ↑ 22.0 22.1 Léveillé F, Blom E, Medhurst AL, Bier P, Laghmani M, Johnson M, Rooimans MA, Sobeck A, Waisfisz Q, Arwert F, Patel KJ, Hoatlin ME, Joenje H, de Winter JP (September 2004). "The Fanconi anemia gene product FANCF is a flexible adaptor protein". The Journal of Biological Chemistry. 279 (38): 39421–30. doi:10.1074/jbc.M407034200. PMID 15262960.

Further reading

Retrieved from "https://www.wikidoc.org/index.php?title=FANCE&oldid=1533231"