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Gene Symbol |
FUBP1 |
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Aliases |
FBP, FUBP, hDH V |
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Entrez Gene ID |
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Gene Name |
Far upstream element binding protein 1 |
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Chromosomal Location |
1p31.1 |
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HGNC ID |
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Summary |
The protein encoded by this gene is a single stranded DNA-binding protein that binds to multiple DNA elements, including the far upstream element (FUSE) located upstream of c-myc. Binding to FUSE occurs on the non-coding strand, and is important to the regulation of c-myc in undifferentiated cells. This protein contains three domains, an amphipathic helix N-terminal domain, a DNA-binding central domain, and a C-terminal transactivation domain that contains three tyrosine-rich motifs. The N-terminal domain is thought to repress the activity of the C-terminal domain. This protein is also thought to bind RNA, and contains 3'-5' helicase activity with in vitro activity on both DNA-DNA and RNA-RNA duplexes. Aberrant expression of this gene has been found in malignant tissues, and this gene is important to neural system and lung development. Binding of this protein to viral RNA is thought to play a role in several viral diseases, including hepatitis C and hand, foot and mouth disease. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Dec 2014]
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RefSeq DNA |
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RefSeq mRNA |
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e!Ensembl
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Protein Information |
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Protein Name |
Far upstream element-binding protein 1, DNA helicase V, FUSE binding protein 1, epididymis secretory sperm binding protein, far upstream element (FUSE) binding protein 1 |
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Function |
Regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. May act both as activator and repressor of transcription. |
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UniProt |
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PDB |
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Interactions |
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STRING |
MINT |
IntAct |
ENSP00000359864 |
O75487 |
O75487 |
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View interactions
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Associated Diseases
Disease group | Disease Name | References |
Endocrine System Diseases |
PCOS |
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Neoplasms |
Neuroblastoma |
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Renal Cancer |
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Liver Cancer |
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Oligodendroglioma |
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Squamous Cell Carcinoma |
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Glioma |
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Gastric Cancer |
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Lymphoma |
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Astrocytoma |
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Nervous System Diseases |
Muscular Dystrophy |
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References |
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Gupta Sajal, Ghulmiyyah Jana, Sharma Rakesh, Halabi Jacques, Agarwal Ashok |
Center for Reproductive Medicine, Cleveland Clinic Foundation, 10681 Carnegie Avenue, Desk X11, Cleveland, OH 44195, USA.| Center for Reproductive Medicine, Cleveland Clinic Foundation, 10681 Carnegie Avenue, Desk X11, Cleveland, OH 44195, USA.| Center for Reproductive Medicine, Cleveland Clinic Foundation, 10681 Carnegie Avenue, Desk X11, Cleveland, OH 44195, USA.| Center for Reproductive Medicine, Cleveland Clinic Foundation, 10681 Carnegie Avenue, Desk X11, Cleveland, OH 44195, USA.| Center for Reproductive Medicine, Cleveland Clinic Foundation, 10681 Carnegie Avenue, Desk X11, Cleveland, OH 44195, USA. |
Biomed Res Int. 2014;2014:916212. doi: 10.1155/2014/916212. Epub 2014 May 12. |
Abstract
Endometriosis, PCOS, and unexplained infertility are currently the most common diseases rendering large numbers of women infertile worldwide. Oxidative stress, due to its deleterious effects on proteins and nucleic acids, is postulated to be the one of the important mechanistic pathways in differential expression of proteins and in these diseases. The emerging field of proteomics has allowed identification of proteins involved in cell cycle, as antioxidants, extracellular matrix (ECM), cytoskeleton, and their linkage to oxidative stress in female infertility related diseases. The aim of this paper is to assess the association of oxidative stress and protein expression in the reproductive microenvironments such as endometrial fluid, peritoneal fluid, and follicular fluid, as well as reproductive tissues and serum. The review also highlights the literature that proposes the use of the fertility related proteins as potential biomarkers for noninvasive and early diagnosis of the aforementioned diseases rather than utilizing the more invasive methods used currently. The review will highlight the power of proteomic profiles identified in infertility related disease conditions and their linkage with underlying oxidative stress. The power of proteomics will be reviewed with regard to eliciting molecular mechanisms for early detection and management of these infertility related conditions. |
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Ma Xiang, Fan Lu, Meng Yan, Hou Zheng, Mao Yun-Dong, Wang Wei, Ding Wei, Liu Jia-Yin |
Laboratory of Reproductive Medicine, Nanjing Medical University, and The Center of Clinical Reproductive Medicine, The First Affiliated Hospital of Nanjing Medical University, People's Republic of China. |
Mol Hum Reprod. 2007 Aug;13(8):527-35. doi: 10.1093/molehr/gam036. Epub 2007 Jun |
Abstract
Polycystic ovary syndrome (PCOS) is the most common cause of anovulatory infertility, affecting 5-10% of females of reproductive age. Currently, little is known about the changes in whole proteins between PCOS and normal ovaries. In the present study, a proteomic approach comprised two-dimensional gel electrophoresis (2DE) analysis and mass spectroscopy was used to identify proteins and examine expression patterns in three PCOS and normal ovaries. One hundred and ten protein spots were separated and showed different intensities between PCOS and normal ovaries. Sixty-nine proteins associated with cellular metabolism and physiological process were identified from 72 spots. Fifty-four proteins were up-regulated in PCOS ovaries and 15 other proteins were up-regulated in normal ovaries. These data demonstrate, for the first time, the complexity in the regulation of ovarian protein expression in human PCOS, and will provide important insight for a better understanding of the pathogenetic mechanisms underlying this clinical disorder. |
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