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POM121 membrane glycoprotein

p145, POM121
The nuclear envelope creates distinct nuclear and cytoplasmic compartments in eukaryotic cells. It consists of two concentric membranes perforated by nuclear pores, large protein complexes that form aqueous channels to regulate the flow of macromolecules between the nucleus and the cytoplasm. These complexes are composed of at least 100 different polypeptide subunits, many of which belong to the nucleoporin family. This gene encodes a member of the FG-repeat-containing nucleoporins. The protein encoded by this gene is an integral membrane protein that localizes to the central spoke ring complex and participates in anchoring the nuclear pore complex to the nuclear envelope. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene, and multiple pseudogenes have been identified. [provided by RefSeq, Mar 2012] (from NCBI)
Top mentioned proteins: CAN, Nucleoporin, ABL, BCR, ACID
Papers on p145
Gene structure variation in segmental duplication block C of human chromosome 7q 11.23 during primate evolution.
Kim et al., Ch'ŏnan, South Korea. In Gene, Jan 2016
We analyzed the structure of POM121, NSUN5, FKBP6, and TRIM50 genes in the LCRs of block C. Based on computational analysis, POM121B created by a segmental duplication acquired a new exonic region, whereas NSUN5B (NSUN5C) showed structural variation by integration of HERV-K LTR after duplication from the original NSUN5 gene.
Single-molecule localization microscopy using mCherry.
Ewers et al., London, United Kingdom. In Chemphyschem, 2014
We were able to image the C-terminus of the nuclear pore protein POM121, which is on the inside of the pore and not readily accessible for external labeling.
Functional heterogeneity of PAX5 chimeras reveals insight for leukemia development.
Strehl et al., Vienna, Austria. In Mol Cancer Res, 2014
To gain mechanistic insight into the role of PAX5 fusion proteins in leukemogenesis, the biochemical and functional properties of uncharacterized fusions: PAX5-DACH1, PAX5-DACH2, PAX5-ETV6, PAX5-HIPK1, and PAX5-POM121 were ascertained.
The imprinted NPAP1 gene in the Prader-Willi syndrome region belongs to a POM121-related family of retrogenes.
Horsthemke et al., Essen, Germany. In Genome Biol Evol, 2014
Phylogenetic analysis revealed that NPAP1, NPAP1L, and another group of genes (UPF0607), which is also restricted to primates, are closely related to the vertebrate transmembrane nucleoporin gene POM121, although they lack the transmembrane domain.
PAX5 fusion genes in t(7;9)(q11.2;p13) leukemia: a case report and review of the literature.
Strehl et al., Vienna, Austria. In Mol Cytogenet, 2013
or POM121 (7q11.23),
M-protein-derived conformational peptide epitope vaccine candidate against Group A Streptococcus.
Toth et al., Australia. In Curr Drug Deliv, 2013
Moreover, the antibodies produced against this epitope were able to recognize the native p145 sequence from M-protein.
A time-lapse imaging assay to study nuclear envelope breakdown.
Ullman et al., Salt Lake City, United States. In Methods Mol Biol, 2012
Here, we describe such a strategy in which the plasma membrane of cells expressing fluorescently tagged nucleoporin POM121 and Histone H2B is permeabilized with digitonin.
Membrane microdomain-associated uroplakin IIIa contributes to Src-dependent mechanisms of anti-apoptotic proliferation in human bladder carcinoma cells.
Sato et al., Kyoto, Japan. In Biol Open, 2012
Our previous study demonstrated that tyrosine phosphorylation of p145(met)/β-subunit of hepatocyte growth factor receptor by epidermal growth factor receptor and Src contributes to the anti-apoptotic growth of human bladder carcinoma cell 5637 under serum-starved conditions.
The imprinted NPAP1/C15orf2 gene in the Prader-Willi syndrome region encodes a nuclear pore complex associated protein.
Horsthemke et al., Essen, Germany. In Hum Mol Genet, 2012
By protein BLAST analysis and InterProScan signature recognition search, we found sequence similarity of C15orf2 to the nuclear pore complex (NPC) protein POM121.
A dominant-negative form of POM121 binds chromatin and disrupts the two separate modes of nuclear pore assembly.
Harel et al., Haifa, Israel. In J Cell Sci, 2011
Here, we show that a soluble internal fragment of the membrane nucleoporin POM121 has a dominant-negative effect on both modes of assembly in a cell-free reconstitution system.
POM121 and Sun1 play a role in early steps of interphase NPC assembly.
Hetzer et al., Los Angeles, United States. In J Cell Biol, 2011
The propose a model in which POM121 and Sun1 interact transiently to promote early steps of interphase nuclear pore complexes assembly.
Localization of Pom121 to the inner nuclear membrane is required for an early step of interphase nuclear pore complex assembly.
Imamoto et al., Saitama, Japan. In Mol Biol Cell, 2011
Data suggest that the nuclear migration of Pom121 and its subsequent interaction with inner nuclear membrane proteins are required to initiate interphase nuclear pore complex assembly.
Pom121 links two essential subcomplexes of the nuclear pore complex core to the membrane.
Wozniak et al., Edmonton, Canada. In J Cell Biol, 2010
The the N terminus of Pom121 directly binds the beta-propeller regions of Nup155 and Nup160.
NLS-mediated NPC functions of the nucleoporin Pom121.
Antonin et al., Heidelberg, Germany. In Febs Lett, 2010
The nuclear localization signal sites of Pom121 affect its function in nuclear pore complex assembly both by influencing nucleoporin interactions and pore membrane structure.
Cell cycle-dependent differences in nuclear pore complex assembly in metazoa.
Hetzer et al., Los Angeles, United States. In Cell, 2010
Conversely, the transmembrane nucleoporin POM121 is critical for the incorporation of the Nup107/160 complex into new assembly sites specifically during interphase.
Two distinct human POM121 genes: requirement for the formation of nuclear pore complexes.
Imamoto et al., Wako, Japan. In Febs Lett, 2007
RNAi experiments showed that efficient depletion of both Pom121 proteins significantly reduces assembled nuclear pore complexes on nuclear envelope.
Function and assembly of nuclear pore complex proteins.
Burke et al., Calgary, Canada. In Biochem Cell Biol, 1998
To date, it has been possible to define a time course of postmitotic assembly for a group of NPC components (CAN/Nup214, Nup153, POM121, p62 and Tpr) relative to the integral inner nuclear membrane protein LAP2 and the NPC membrane glycoprotein gp210.
A novel 145 kd brain cytosolic protein reconstitutes Ca(2+)-regulated secretion in permeable neuroendocrine cells.
Martin et al., Madison, United States. In Cell, 1992
We have identified a novel brain protein, p145, as a cytosolic factor that reconstitutes Ca(2+)-activated secretion in two neuroendocrine cell types.
A novel abl protein expressed in Philadelphia chromosome positive acute lymphoblastic leukaemia.
Wiedemann et al., In Nature, 1987
The c-abl protooncogene is translocated from chromosome 9 band q34 into bcr and the biochemical consequence of this molecular rearrangement is the production of an abnormal fusion protein bcr-abl p210 with enhanced protein-tyrosine kinase activity compared to the normal p145 c-abl protein.
Expression of a translocated c-abl gene in hybrids of mouse fibroblasts and chronic myelogenous leukaemia cells.
Croce et al., In Nature, 1986
CML cells carrying the t(9;22) chromosomal translocation are known to produce an 8-kilobase (kb) c-abl transcript in addition to the normal 6- and 7-kb transcripts and to express the normal p145 abl protein and a p210 c-abl protein possessing a tyrosine kinase activity not detected in the p145 species.
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