FANCG
Fanconi anemia, complementation group G | |||||||||||||
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Identifiers | |||||||||||||
Symbols | FANCG ; FAG; XRCC9 | ||||||||||||
External IDs | OMIM: 602956 MGI: 1926471 HomoloGene: 3402 GeneCards: FANCG Gene | ||||||||||||
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RNA expression pattern | |||||||||||||
More reference expression data | |||||||||||||
Orthologs | |||||||||||||
Species | Human | Mouse | |||||||||||
Entrez | 2189 | 60534 | |||||||||||
Ensembl | ENSG00000221829 | ENSMUSG00000028453 | |||||||||||
UniProt | O15287 | Q9EQR6 | |||||||||||
RefSeq (mRNA) | NM_004629 | NM_001163233 | |||||||||||
RefSeq (protein) | NP_004620 | NP_001156705 | |||||||||||
Location (UCSC) |
Chr 9: 35.07 – 35.08 Mb |
Chr 4: 43 – 43.01 Mb | |||||||||||
PubMed search | |||||||||||||
Fanconi anemia group G protein is a protein that in humans is encoded by the FANCG gene.[1][2][3]
Function
FANCG, involved in Fanconi anemia, confers resistance to both hygromycin B and mitomycin C. FANCG contains a 5-prime GC-rich untranslated region characteristic of housekeeping genes. The putative 622-amino acid protein has a leucine-zipper motif at its N-terminus. Fanconi anemia is an autosomal recessive disorder with diverse clinical symptoms, including developmental anomalies, bone marrow failure, and early occurrence of malignancies. A minimum of 8 FA genes have been identified. The FANCG gene is responsible for complementation group G.[3]
Interactions
FANCG has been shown to interact with FANCF,[4][5][6][7]
FANCA,[6][7][8][9][10][11][12][13][14][15][16][17][18][19][20][21][22][23] FANCE[7][21][24] and BRCA2.[25]
References
- ↑ Liu N, Lamerdin JE, Tucker JD, Zhou ZQ, Walter CA, Albala JS, Busch DB, Thompson LH (Sep 1997). "The human XRCC9 gene corrects chromosomal instability and mutagen sensitivities in CHO UV40 cells". Proc Natl Acad Sci U S A 94 (17): 9232–7. doi:10.1073/pnas.94.17.9232. PMC 23130. PMID 9256465.
- ↑ 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 (Nov 1997). "Evidence for at least eight Fanconi anemia genes". Am J Hum Genet 61 (4): 940–4. doi:10.1086/514881. PMC 1715980. PMID 9382107.
- 1 2 "Entrez Gene: FANCG Fanconi anemia, complementation group G".
- ↑ 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 (September 2004). "The Fanconi anemia gene product FANCF is a flexible adaptor protein". J. Biol. Chem. 279 (38): 39421–30. doi:10.1074/jbc.M407034200. PMID 15262960.
- ↑ de Winter JP, van der Weel L, de Groot J, Stone S, Waisfisz Q, Arwert F, Scheper RJ, Kruyt FA, Hoatlin ME, Joenje H (November 2000). "The Fanconi anemia protein FANCF forms a nuclear complex with FANCA, FANCC and FANCG". Hum. Mol. Genet. 9 (18): 2665–74. doi:10.1093/hmg/9.18.2665. PMID 11063725.
- 1 2 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.
- 1 2 3 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". Hum. Mol. Genet. 10 (4): 423–9. doi:10.1093/hmg/10.4.423. PMID 11157805.
- ↑ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
- ↑ Garcia-Higuera I, Kuang Y, Näf D, Wasik J, D'Andrea AD (July 1999). "Fanconi anemia proteins FANCA, FANCC, and FANCG/XRCC9 interact in a functional nuclear complex". Mol. Cell. Biol. 19 (7): 4866–73. PMC 84285. PMID 10373536.
- ↑ Park SJ, Ciccone SL, Beck BD, Hwang B, Freie B, Clapp DW, Lee SH (July 2004). "Oxidative stress/damage induces multimerization and interaction of Fanconi anemia proteins". J. Biol. Chem. 279 (29): 30053–9. doi:10.1074/jbc.M403527200. PMID 15138265.
- ↑ van de Vrugt HJ, Koomen M, Berns MA, de Vries Y, Rooimans MA, van der Weel L, Blom E, de Groot J, Schepers RJ, Stone S, Hoatlin ME, Cheng NC, Joenje H, Arwert F (March 2002). "Characterization, expression and complex formation of the murine Fanconi anaemia gene product Fancg". Genes Cells 7 (3): 333–42. doi:10.1046/j.1365-2443.2002.00518.x. PMID 11918676.
- ↑ Yagasaki H, Adachi D, Oda T, Garcia-Higuera I, Tetteh N, D'Andrea AD, Futaki M, Asano S, Yamashita T (December 2001). "A cytoplasmic serine protein kinase binds and may regulate the Fanconi anemia protein FANCA". Blood 98 (13): 3650–7. doi:10.1182/blood.V98.13.3650. PMID 11739169.
- ↑ Huber PA, Medhurst AL, Youssoufian H, Mathew CG (February 2000). "Investigation of Fanconi anemia protein interactions by yeast two-hybrid analysis". Biochem. Biophys. Res. Commun. 268 (1): 73–7. doi:10.1006/bbrc.1999.2055. PMID 10652215.
- ↑ Kruyt FA, Abou-Zahr F, Mok H, Youssoufian H (November 1999). "Resistance to mitomycin C requires direct interaction between the Fanconi anemia proteins FANCA and FANCG in the nucleus through an arginine-rich domain". J. Biol. Chem. 274 (48): 34212–8. doi:10.1074/jbc.274.48.34212. PMID 10567393.
- ↑ Reuter T, Herterich S, Bernhard O, Hoehn H, Gross HJ (January 2000). "Strong FANCA/FANCG but weak FANCA/FANCC interaction in the yeast 2-hybrid system". Blood 95 (2): 719–20. PMID 10627486.
- ↑ Blom E, van de Vrugt HJ, de Vries Y, de Winter JP, Arwert F, Joenje H (January 2004). "Multiple TPR motifs characterize the Fanconi anemia FANCG protein". DNA Repair (Amst.) 3 (1): 77–84. doi:10.1016/j.dnarep.2003.09.007. PMID 14697762.
- ↑ Kuang Y, Garcia-Higuera I, Moran A, Mondoux M, Digweed M, D'Andrea AD (September 2000). "Carboxy terminal region of the Fanconi anemia protein, FANCG/XRCC9, is required for functional activity". Blood 96 (5): 1625–32. PMID 10961856.
- ↑ Thomashevski A, High AA, Drozd M, Shabanowitz J, Hunt DF, Grant PA, Kupfer GM (June 2004). "The Fanconi anemia core complex forms four complexes of different sizes in different subcellular compartments". J. Biol. Chem. 279 (25): 26201–9. doi:10.1074/jbc.M400091200. PMID 15082718.
- ↑ Waisfisz Q, de Winter JP, Kruyt FA, de Groot J, van der Weel L, Dijkmans LM, Zhi Y, Arwert F, Scheper RJ, Youssoufian H, Hoatlin ME, Joenje H (August 1999). "A physical complex of the Fanconi anemia proteins FANCG/XRCC9 and FANCA". Proc. Natl. Acad. Sci. U.S.A. 96 (18): 10320–5. doi:10.1073/pnas.96.18.10320. PMC 17886. PMID 10468606.
- ↑ 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". Nat. Genet. 35 (2): 165–70. doi:10.1038/ng1241. PMID 12973351.
- 1 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.
- ↑ Otsuki T, Young DB, Sasaki DT, Pando MP, Li J, Manning A, Hoekstra M, Hoatlin ME, Mercurio F, Liu JM (2002). "Fanconi anemia protein complex is a novel target of the IKK signalsome". J. Cell. Biochem. 86 (4): 613–23. doi:10.1002/jcb.10270. PMID 12210728.
- ↑ Garcia-Higuera I, Kuang Y, Denham J, D'Andrea AD (November 2000). "The fanconi anemia proteins FANCA and FANCG stabilize each other and promote the nuclear accumulation of the Fanconi anemia complex". Blood 96 (9): 3224–30. PMID 11050007.
- ↑ 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". EMBO J. 21 (13): 3414–23. doi:10.1093/emboj/cdf355. PMC 125396. PMID 12093742.
- ↑ Hussain S, Witt E, Huber PA, Medhurst AL, Ashworth A, Mathew CG (October 2003). "Direct interaction of the Fanconi anaemia protein FANCG with BRCA2/FANCD1". Hum. Mol. Genet. 12 (19): 2503–10. doi:10.1093/hmg/ddg266. PMID 12915460.
Further reading
- de Winter JP, Waisfisz Q, Rooimans MA, et al. (1998). "The Fanconi anaemia group G gene FANCG is identical with XRCC9". Nat. Genet. 20 (3): 281–3. doi:10.1038/3093. PMID 9806548.
- Garcia-Higuera I, Kuang Y, Näf D, et al. (1999). "Fanconi Anemia Proteins FANCA, FANCC, and FANCG/XRCC9 Interact in a Functional Nuclear Complex". Mol. Cell. Biol. 19 (7): 4866–73. PMC 84285. PMID 10373536.
- Jelesko JG, Harper R, Furuya M, Gruissem W (1999). "Rare germinal unequal crossing-over leading to recombinant gene formation and gene duplication in Arabidopsis thaliana". Proc. Natl. Acad. Sci. U.S.A. 96 (18): 10302–7. doi:10.1073/pnas.96.18.10302. PMC 17883. PMID 10468603.
- Waisfisz Q, de Winter JP, Kruyt FA, et al. (1999). "A physical complex of the Fanconi anemia proteins FANCG/XRCC9 and FANCA". Proc. Natl. Acad. Sci. U.S.A. 96 (18): 10320–5. doi:10.1073/pnas.96.18.10320. PMC 17886. PMID 10468606.
- Kruyt FA, Abou-Zahr F, Mok H, Youssoufian H (1999). "Resistance to mitomycin C requires direct interaction between the Fanconi anemia proteins FANCA and FANCG in the nucleus through an arginine-rich domain". J. Biol. Chem. 274 (48): 34212–8. doi:10.1074/jbc.274.48.34212. PMID 10567393.
- Reuter T, Herterich S, Bernhard O, et al. (2000). "Strong FANCA/FANCG but weak FANCA/FANCC interaction in the yeast 2-hybrid system". Blood 95 (2): 719–20. PMID 10627486.
- Huber PA, Medhurst AL, Youssoufian H, Mathew CG (2000). "Investigation of Fanconi anemia protein interactions by yeast two-hybrid analysis". Biochem. Biophys. Res. Commun. 268 (1): 73–7. doi:10.1006/bbrc.1999.2055. PMID 10652215.
- Yamada T, Tachibana A, Shimizu T, et al. (2000). "Novel mutations of the FANCG gene causing alternative splicing in Japanese Fanconi anemia". J. Hum. Genet. 45 (3): 159–66. doi:10.1007/s100380050203. PMID 10807541.
- Kuang Y, Garcia-Higuera I, Moran A, et al. (2000). "Carboxy terminal region of the Fanconi anemia protein, FANCG/XRCC9, is required for functional activity". Blood 96 (5): 1625–32. PMID 10961856.
- Garcia-Higuera I, Kuang Y, Denham J, D'Andrea AD (2000). "The fanconi anemia proteins FANCA and FANCG stabilize each other and promote the nuclear accumulation of the Fanconi anemia complex". Blood 96 (9): 3224–30. PMID 11050007.
- de Winter JP, van der Weel L, de Groot J, et al. (2000). "The Fanconi anemia protein FANCF forms a nuclear complex with FANCA, FANCC and FANCG". Hum. Mol. Genet. 9 (18): 2665–74. doi:10.1093/hmg/9.18.2665. PMID 11063725.
- Demuth I, Wlodarski M, Tipping AJ, et al. (2000). "Spectrum of mutations in the Fanconi anaemia group G gene, FANCG/XRCC9". Eur. J. Hum. Genet. 8 (11): 861–8. doi:10.1038/sj.ejhg.5200552. PMID 11093276.
- Medhurst AL, Huber PA, Waisfisz Q, et al. (2001). "Direct interactions of the five known Fanconi anaemia proteins suggest a common functional pathway". Hum. Mol. Genet. 10 (4): 423–9. doi:10.1093/hmg/10.4.423. PMID 11157805.
- McMahon LW, Sangerman J, Goodman SR, et al. (2001). "Human alpha spectrin II and the FANCA, FANCC, and FANCG proteins bind to DNA containing psoralen interstrand cross-links". Biochemistry 40 (24): 7025–34. doi:10.1021/bi002917g. PMID 11401546.
- Yagasaki H, Adachi D, Oda T, et al. (2002). "A cytoplasmic serine protein kinase binds and may regulate the Fanconi anemia protein FANCA". Blood 98 (13): 3650–7. doi:10.1182/blood.V98.13.3650. PMID 11739169.
- Futaki M, Igarashi T, Watanabe S, et al. (2002). "The FANCG Fanconi anemia protein interacts with CYP2E1: possible role in protection against oxidative DNA damage". Carcinogenesis 23 (1): 67–72. doi:10.1093/carcin/23.1.67. PMID 11756225.
- van de Vrugt HJ (2002). "Characterization, expression and complex formation of the murine Fanconi anaemia gene product Fancg". Genes Cells 7 (3): 333–42. doi:10.1046/j.1365-2443.2002.00518.x. PMID 11918676.
- Pace P, Johnson M, Tan WM, et al. (2002). "FANCE: the link between Fanconi anaemia complex assembly and activity". EMBO J. 21 (13): 3414–23. doi:10.1093/emboj/cdf355. PMC 125396. PMID 12093742.