exportin 1 (CRM1 homolog, yeast) OKDB#: 4425
 Symbols: XPO1 Species: human
 Synonyms: emb, CRM1, DKFZp686B1823,  Locus: 2p16 in Homo sapiens

For retrieval of Nucleotide and Amino Acid sequences please go to: OMIM Entrez Gene
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DNA Microarrays
link to BioGPS
General Comment

NCBI Summary: The protein encoded by this gene mediates leucine-rich nuclear export signal (NES)-dependent protein transport. Exportin 1 specifically inhibits the nuclear export of Rev and U snRNAs. It is involved in the control of several cellular processes by controlling the localization of cyclin B, MPAK, and MAPKAP kinase 2. This protein also regulates NFAT and AP-1. [provided by RefSeq]
General function
Cellular localization Nuclear
Ovarian function Oocyte maturation
Expression regulated by
Ovarian localization Oocyte
Comment Discovery of putative oocyte quality markers by comparative ExacTag proteomics. Powell MD et al. Purpose: Identification of the biomarkers of oocyte quality, and developmental and reprogramming potential is of importance to assisted reproductive technology in humans and animals. Experimental design: PerkinElmer ExacTag™ Kit was used to label differentially proteins in pig oocyte extracts (oocyte proteome) and pig oocyte-conditioned in vitro maturation media (oocyte secretome) obtained with high- and low-quality oocytes. Results: We identified 16 major proteins in the oocyte proteome that were expressed differentially in high- versus low-quality oocytes. More abundant proteins in the high-quality oocyte proteome included kelch-like ECH-associated protein 1 (an adaptor for ubiquitin-ligase CUL3), nuclear export factor CRM1 and ataxia-telangiectasia mutated protein kinase. Dystrophin (DMD) was more abundant in low-quality oocytes. In the secretome, we identified 110 proteins, including DMD and cystic fibrosis transmembrane conductance regulator, two proteins implicated in muscular dystrophy and cystic fibrosis, respectively. Monoubiquitin was identified in the low-quality-oocyte secretome. Conclusions and clinical implications: A direct, quantitative proteomic analysis of small oocyte protein samples can identify potential markers of oocyte quality without the need for a large amount of total protein. This approach will be applied to discovery of non-invasive biomarkers of oocyte quality in assisted human reproduction and in large animal embryo transfer programs.
Follicle stages
OMIM (Online Mendelian Inheritance in Man: an excellent source of general gene description and genetic information.)
OMIM \ Animal Model
KEGG Pathways
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created: 2010-12-15 15:09:44 by: Aaron J Hsueh, hsuehlab   email: aaron.hsueh@stanford.edu
home page: http://reprobio.stanford.edu/hsueh
last update: 2010-12-15 15:10:39 by: Aaron J Hsueh, hsuehlab   email: aaron.hsueh@stanford.edu

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