FANCE
FANCE | |||
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Gene ontology | |||
Molecular function | |||
Cellular component | |||
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Sources:Amigo / QuickGO |
Ensembl | |||||||||
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UniProt |
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RefSeq (mRNA) | |||||||||
RefSeq (protein) |
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Location (UCSC) | Chr 6: 35.45 – 35.47 Mb | Chr 17: 28.53 – 28.55 Mb | |||||||
PubMed search | [3] | [4] |
View/Edit Human | View/Edit Mouse |
Fanconi anemia, complementation group E protein is a protein that in humans is encoded by the FANCE gene.[5][6][7] 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.[7]
A
Gene Expression
FANCE is stated to have been expressed in 151 organs with the highest level in female gonads.[10]
Chromosomal Location
The location of the gene is in 6p21.31, where p is the short arm of chromosome 6 at position 21.31[11]
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) [11]
Protein Characteristics
The main complex of FA contains a nuclear multi-subunit complex of notably 8 FA proteins.[12] This adds a single ubiquiting chain to the FANCD2 following DNA damage or duplicative pressure.[13]
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.[14]
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.[14]
Function
It restores DNA cross-links and is needed for nuclear accumulation of FANCC, delivering a critical bridge between FA complex and FANCD2.[15]
FANCE-deficient mice exhibit a reduced number of oocytes and disruption of prophase I of meiosis[16] indicating that FANCE has an essential role in meiosis.
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.[15]
- 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,[17] for linking. From this, a chromosomal region on chromosome 6p is located for FANCE.[17]
- 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,[18] it limits primarily to the nucleus.[19]
Interactions
FANCE has been shown to
- FANCA,[19][12][20][21]
- FANCD2,[20][22][23]
- FANCF[20][24]
- FANCG,[19][12][20] and
- FANCC.[19][12][20][22][24]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000112039 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000007570 – 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.
- PMID 7662964.
- PMID 11001585.
- ^ a b "Entrez Gene: FANCE Fanconi anemia, complementation group E".
- ^ PMID 11239454.
- PMID 27986371.
- ^ "FANCE - Fanconi anemia group E protein - Homo sapiens (Human) - FANCE gene & protein". www.uniprot.org. Retrieved 2018-11-09.
- ^ a b "FANCE FA complementation group E [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2018-11-09.
- ^ PMID 11157805.
- PMID 11239454.
- ^ PMID 17308347.
- ^ a b "Anti-FANCE antibody (ab126177) | Abcam". www.abcam.com. Retrieved 2018-11-09.
- S2CID 249432754.
- ^ PMID 10205272.
- PMID 11001585.
- ^ PMID 12239156.
- ^ PMID 12093742.
- S2CID 10149290.
- ^ PMID 12649160.
- PMID 15115758.
- ^ PMID 15262960.
Further reading
- Wegner RD, Henrichs I, Joenje H, Schroeder-Kurth T (December 1996). "Fanconi anemia complementation group E: clinical and cytogenetic data of the first patient". Clinical Genetics. 50 (6): 479–82. S2CID 23242981.
- 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 (October 1997). "Evidence for at least eight Fanconi anemia genes". American Journal of Human Genetics. 61 (4): 940–4. PMID 9382107.
- 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. PMID 10205272.
- 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.
- 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. PMID 12093742.
- Taniguchi T, D'Andrea AD (October 2002). "The Fanconi anemia protein, FANCE, promotes the nuclear accumulation of FANCC". Blood. 100 (7): 2457–62. PMID 12239156.
- 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. PMID 12649160.
- Meetei AR, Sechi S, Wallisch M, Yang D, Young MK, Joenje H, Hoatlin ME, Wang W (May 2003). "A multiprotein nuclear complex connects Fanconi anemia and Bloom syndrome". Molecular and Cellular Biology. 23 (10): 3417–26. PMID 12724401.
- 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. S2CID 10149290.
- 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. PMID 15115758.
- Wang X, Andreassen PR, D'Andrea AD (July 2004). "Functional interaction of monoubiquitinated FANCD2 and BRCA2/FANCD1 in chromatin". Molecular and Cellular Biology. 24 (13): 5850–62. PMID 15199141.
- 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 (November 2004). "X-linked inheritance of Fanconi anemia complementation group B". Nature Genetics. 36 (11): 1219–24. PMID 15502827.
- 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 (September 2005). "A human ortholog of archaeal DNA repair protein Hef is defective in Fanconi anemia complementation group M". Nature Genetics. 37 (9): 958–63. PMID 16116422.
- Gordon SM, Alon N, Buchwald M (October 2005). "FANCC, FANCE, and FANCD2 form a ternary complex essential to the integrity of the Fanconi anemia DNA damage response pathway". The Journal of Biological Chemistry. 280 (43): 36118–25. PMID 16127171.