SUBCELLULAR LOCALIZATION
| plasma membrane
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| intracellular
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| intracellular,cytoplasm,organelle,Golgi
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| intracellular,cytoplasm,cytosolic
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| intracellular,nucleus,nucleoplasm
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text
| nuclear and cytoplasmic form have distinct and opposing functions in the regulation of prostate cancer cell proliferation (cytoplasmic enhancing cell proliferation and nuclear inhibiting this proliferation) |
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localizes in the cytoplasm of prostate epithelial cells at the early stage of prostate development when cells are proliferating, and its nuclear translocation is associated with cellular and functional differentiation in adult prostate tissue |
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expressed in the cytoplasm of germ cells of the fetal testis |
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expressed predominantly as nuclear proteins in fetal Leydig cells and human adult nonneoplastic testes, including germ cells and Leydig cells |
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PRMT5 and WDR77 were evenly distributed between cytoplasm and nucleus |
basic FUNCTION
| functioning to mediate the interaction of multiple substrates with the methylosome |
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involved in Sm protein rearrangements or pre-assembly required for snRNP biogenesis |
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required for proper expression of AR-target genes to maintain the differentiation of prostate epithelial cells, and its translocation from the nucleus into the cytoplasm in prostate cancer cells results in excessive prostate EC proliferation |
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distinct functions of the nuclear and the WDR77/PRMT5 complexes in the developing fetal testis and in the oncogenesis of testicular tumors |
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plays a critical role in the proliferation and differentiation of prostate epithelial cells |
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novel role for WDR77 in the control of astrocyte activation through CDKN1A and NFKB1 signaling |
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nuclear WDR77 is required for cell differentiation and prostate- specific protein secretion, but cytoplasmic protein is essential for proliferation of prostate epithelial cells |
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drives quiescent epithelial cells to re-enter the cell cycle and plays an essential role for growth of lung and prostate cancer cells |
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its expression causes the non-sensitivity of proliferating cells to TGFB1 signaling, thereby contributing to cellular proliferation during lung tumorigenesis |
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WDR77 can transform cells independent of AR and ESR, and PRMT5 has partial contribution to that process |
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likely WDR77 and PRMT5 simultaneously engage the protein substrate, orienting its targeted arginine to the catalytic site |