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Proteasome maturation protein

UMP1, POMP, Ump1p
The protein encoded by this gene is a molecular chaperone that binds 20S preproteasome components and is essential for 20S proteasome formation. The 20S proteasome is the proteolytically active component of the 26S proteasome complex. The encoded protein is degraded before the maturation of the 20S proteasome is complete. A variant in the 5' UTR of this gene has been associated with KLICK syndrome, a rare skin disorder.[provided by RefSeq, Aug 2010] (from NCBI)
Top mentioned proteins: Ubiquitin, CAN, V1a, PCNA, p53
Papers on UMP1
The Nuclear Factor (Erythroid-derived 2)-like 2 and Proteasome Maturation Protein Axis Mediate Bortezomib Resistance in Multiple Myeloma.
Orlowski et al., Suzhou, China. In J Biol Chem, Jan 2016
We considered the possibility that this could be associated with enhanced proteasome activity in part through the action of the proteasome maturation protein (POMP).
MCM3AP and POMP Mutations Cause a DNA-Repair and DNA-Damage-Signaling Defect in an Immunodeficient Child.
Wiesmüller et al., Ulm, Germany. In Hum Mutat, Dec 2015
Two de novo mutated candidate genes, MCM3AP encoding germinal center (GC)-associated nuclear protein (GANP) and POMP encoding proteasome maturation protein (POMP), were identified by whole exome sequencing (WES) and confirmed by Sanger sequencing in a child with complex phenotype displaying immunodeficiency, genomic instability, skin changes and myelodysplasia.
Additive loss-of-function proteasome subunit mutations in CANDLE/PRAAS patients promote type I IFN production.
Goldbach-Mansky et al., In J Clin Invest, Dec 2015
Here, we identified 8 mutations in 4 proteasome genes, PSMA3 (encodes α7), PSMB4 (encodes β7), PSMB9 (encodes β1i), and proteasome maturation protein (POMP), that have not been previously associated with disease and 1 mutation in PSMB8 that has not been previously reported.
A component of the mitochondrial outer membrane proteome of T. brucei probably contains covalent bound fatty acids.
Niemann et al., Bern, Switzerland. In Exp Parasitol, Aug 2015
Here we examine POMP39, a protein previously described to be present in the outer mitochondrial membrane proteome (POMP) of the protozoan parasite Trypanosoma brucei.
MicroRNA-101 Suppresses Tumor Cell Proliferation by Acting as an Endogenous Proteasome Inhibitor via Targeting the Proteasome Assembly Factor POMP.
Dobbelstein et al., Göttingen, Germany. In Mol Cell, Aug 2015
Here we show that the microRNA-101 (miR-101) targets the proteasome maturation protein POMP, leading to impaired proteasome assembly and activity, and resulting in accumulation of p53 and cyclin-dependent kinase inhibitors, cell cycle arrest, and apoptosis.
Blocking Cancer Growth with Less POMP or Proteasomes.
Collins et al., Boston, United States. In Mol Cell, Aug 2015
In this issue, Zhang et al. (2015) report that miR-101 suppresses the expression of chaperone POMP and 20S assembly, and certain cancers raise proteasome content by losing miR-101.
Identification of Saccharomyces cerevisiae Genes Whose Deletion Causes Synthetic Effects in Cells with Reduced Levels of the Nuclear Pif1 DNA Helicase.
Zakian et al., Princeton, United States. In G3 (bethesda), 2014
This study identified eleven genes that were synthetic lethal (APM1, ARG80, CDH1, GCR1, GTO3, PRK1, RAD10, SKT5, SOP4, UMP1, and YCK1) and three genes that were synthetic sick (DEF1, YIP4, and HOM3) with pif1-m2.
Proteasome activation as a novel anti-aging strategy.
Gonos, Greece. In Free Radic Biol Med, 2014
Stable over-expression of catalytic subunits or POMP resulted in enhanced proteasome assembly and activities and increased cell survival following treatments with various oxidants.
Nrf2, a regulator of the proteasome, controls self-renewal and pluripotency in human embryonic stem cells.
Kosik et al., Santa Barbara, United States. In Stem Cells, 2014
As an underlying mechanism, our data show that Nrf2 regulates proteasome activity in hESCs partially through proteasome maturation protein (POMP), a proteasome chaperone, which in turn controls the proliferation of self-renewing hESCs, three germ layer differentiation and cellular reprogramming.
Genetic modifiers of menopausal hormone replacement therapy and breast cancer risk: a genome-wide interaction study.
Breast Cancer Association Consortium et al., Melbourne, Australia. In Endocr Relat Cancer, 2013
We observed effect modification of current MHT use on overall BC risk by two SNPs on chr13 near POMP (combined Pint≤8.9 × 10(-6)), two SNPs in SLC25A21 (combined Pint≤4.8 × 10(-5)), and three SNPs in PLCG2 (combined Pint≤4.5 × 10(-5)).
Genetic amplification of the NOTCH modulator LNX2 upregulates the WNT/β-catenin pathway in colorectal cancer.
Ried et al., Bethesda, United States. In Cancer Res, 2013
The functional space of the genes NUPL1, LNX2, POLR1D, POMP, SLC7A1, DIS3, KLF5, and GPR180 was established by global expression profiling after RNAi exposure.
Biochemical and biophysical characterization of recombinant yeast proteasome maturation factor ump1.
Macedo-Ribeiro et al., Porto, Portugal. In Comput Struct Biotechnol J, 2012
Protein degradation is essential for maintaining cellular homeostasis.
siRNA silencing of proteasome maturation protein (POMP) activates the unfolded protein response and constitutes a model for KLICK genodermatosis.
Dahl et al., Uppsala, Sweden. In Plos One, 2011
KLICK is caused by reduced levels of POMP, leading to proteasome insufficiency in differentiating keratinocytes
A single-nucleotide deletion in the POMP 5' UTR causes a transcriptional switch and altered epidermal proteasome distribution in KLICK genodermatosis.
Dahl et al., Uppsala, Sweden. In Am J Hum Genet, 2010
A single-nucleotide deletion in the POMP 5' UTR causes a transcriptional switch and altered epidermal proteasome distribution in KLICK genodermatosis.
PACemakers of proteasome core particle assembly.
Dohmen et al., Faro, Portugal. In Structure, 2008
These complexes lack the beta7 subunit but contain UMP1, another assembly chaperone, and in yeast, at least to some degree, the activator protein Blm10.
The proteasome maturation protein POMP facilitates major steps of 20S proteasome formation at the endoplasmic reticulum.
Krüger et al., Berlin, Germany. In Embo Rep, 2007
Data show that POMP facilitates the main steps in 20S core complex formation at the ER to coordinate the assembly process and to provide cells with freshly formed proteasomes at their site of function.
The spectrum of spontaneous mutations caused by deficiency in proteasome maturase Ump1 in Saccharomyces cerevisiae.
Sledziewska-Gojska et al., Warsaw, Poland. In Curr Genet, 2007
The specificity of the mutator effect caused by ump1 is discussed in light of the proposed role of 26S proteasome activity in the regulation of postreplication DNA repair.
Possible tetramerisation of the proteasome maturation factor POMP/proteassemblin/hUmp1 and its subcellular localisation.
Illges et al., Switzerland. In Int J Biol Macromol, 2006
POMP/proteassemblin/hUmp1 may be tetramerised and is localized to the cytoplasm and the nucleus
20S proteasome biogenesis.
Enenkel et al., Berlin, Germany. In Biochimie, 2001
The complex biogenesis is tightly regulated which requires additional components such as the maturation factor Ump1/POMP, an ubiquitous protein in eukaryotic cells.
Ump1p is required for proper maturation of the 20S proteasome and becomes its substrate upon completion of the assembly.
Dohmen et al., Düsseldorf, Germany. In Cell, 1998
The S. cerevisiae Ump1p protein is a component of proteasome precursor complexes containing unprocessed beta subunits but is not detected in the mature 20S proteasome.
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