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Synaptotagmin binding, cytoplasmic RNA interacting protein

This gene encodes a member of the cellular heterogeneous nuclear ribonucleoprotein (hnRNP) family. hnRNPs are RNA binding proteins that complex with heterogeneous nuclear RNA (hnRNA) and regulate alternative splicing, polyadenylation, and other aspects of mRNA metabolism and transport. The encoded protein plays a role in multiple aspects of mRNA maturation and is associated with several multiprotein complexes including the apoB RNA editing-complex and survival of motor neurons (SMN) complex. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene, and a pseudogene of this gene is located on the short arm of chromosome 20. [provided by RefSeq, Dec 2011] (from NCBI)
Top mentioned proteins: V1a, CAN, fibrillin-1, apolipoprotein B, APOBEC-1
Papers on NSAP1
(1)H, (13)C and (15)N resonance assignment of WHEP domains of human glutamyl-prolyl tRNA synthetase.
Kim et al., Taejŏn, South Korea. In Biomol Nmr Assign, Apr 2015
While, R23 repeats interacts with NSAP1, which inhibits mRNA binding.
SYNCRIP-dependent Nox2 mRNA destabilization impairs ROS formation in M2-polarized macrophages.
von Knethen et al., Frankfurt am Main, Germany. In Antioxid Redox Signal, 2015
An mRNA pulldown approach coupled to mass spectrometry analysis identified the RNA-binding protein SYNCRIP attached to the Nox2 mRNA 3' untranslated region (3'UTR).
The Activation-Induced Assembly of an RNA/Protein Interactome Centered on the Splicing Factor U2AF2 Regulates Gene Expression in Human CD4 T Cells.
Salomon et al., Los Angeles, United States. In Plos One, 2014
While knocking down the PIM, SYNCRIP, impacts a limited but immunologically important set of U2AF2-bound transcripts, knockdown of U2AF1 significantly impairs assembly of the majority of protein and mRNA components in the activation-induced interactome.
Flow-cytometric visualization of C>U mRNA editing reveals the dynamics of the process in live cells.
Conticello et al., Florence, Italy. In Rna Biol, 2014
Namely we show the interplay of APOBEC1 with known interactors (ACF, hnRNP-C1, GRY-RBP) in cells that are RNA editing-proficient (HuH-7) or -deficient (HEK-293T), and the effects of restricted cellular localization of APOBEC1 on the efficiency of the editing.
The RNA-editing enzyme APOBEC1 requires heterogeneous nuclear ribonucleoprotein Q isoform 6 for efficient interaction with interleukin-8 mRNA.
Shimotohno et al., Ichikawa, Japan. In J Biol Chem, 2014
Heterogeneous nuclear ribonucleoprotein Q (hnRNPQ) was essential to the APOBEC1/IL8 mRNA association in HuH7.5 cells.
Identification of miR-494 direct targets involved in senescence of human diploid fibroblasts.
Faraonio et al., Napoli, Italy. In Faseb J, 2014
Functional miR-494 binding sites were confirmed in 3'-untranslated regions (UTRs) of 4 of them [heterogeneous nuclear ribonucleoprotein A3 (hnRNPA3), protein disulfide isomerase A3 (PDIA3), UV excision repair protein RAD23 homolog B (RAD23B), and synaptotagmin-binding cytoplasmic RNA-interacting protein (SYNCRIP)/heterogeneous nuclear ribonucleoprotein Q (hnRNPQ)].
Proteomic analysis reveals that MAEL, a component of nuage, interacts with stress granule proteins in cancer cells.
Zhou et al., Changsha, China. In Oncol Rep, 2014
The interactions between MAEL and 8 of these SG components (PABPC1, YBX1, KHSRP, SYNCRIP, DDX39, ELAV1, EIF4A1 and EIF3F) were confirmed by anti-tag immunoprecipitation.
The hnRNP-Q protein LIF2 participates in the plant immune response.
Gaudin et al., Versailles, France. In Plos One, 2013
Similar to its human homolog, NSAP1/SYNCRIP, a trans-acting factor involved in both cellular processes and the viral life cycle, LIF2 may regulate the conflicting aspects of development and defense programs, suggesting that a conserved evolutionary trade-off between growth and defense pathways exists in eukaryotes.
Syncrip/hnRNP Q influences synaptic transmission and regulates BMP signaling at the Drosophila neuromuscular synapse.
Davis et al., Basel, Switzerland. In Biol Open, 2013
Here, we identify the conserved RNA binding protein Syncrip as a new factor that modulates the efficiency of vesicle release from the motoneuron and is required for correct synapse structure.
Heterogeneous nuclear ribonucleoprotein Q is a novel substrate of SH2 domain-containing phosphatase-2.
Kitagawa et al., Ōsaka, Japan. In J Biochem, 2013
By using the substrate-trapping method with the phosphatase-dead SHP2 mutant, in which C459 was substituted by serine, and the matrix-assisted laser desorption/ionization-time of flight (MALDI-TOF) mass spectrometric analysis, we found that heterogeneous nuclear ribonucleoprotein Q (hnRNP Q), a protein implicated in RNA metabolisms, was a novel substrate of SHP2.
Identification of proteins specifically interacting with YB-1 mRNA 3' UTR and the effect of hnRNP Q on YB-1 mRNA translation.
Ovchinnikov et al., Moscow, Russia. In Biochemistry (mosc), 2013
One of these, hnRNP Q, was shown to specifically interact with the regulatory element (RE) in YB-1 mRNA 3' UTR and to inhibit translation of this mRNA.
Control of translation and miRNA-dependent repression by a novel poly(A) binding protein, hnRNP-Q.
Sonenberg et al., Montréal, Canada. In Plos Biol, 2012
We demonstrate that isoform 2 of the mouse heterogeneous nuclear protein Q (hnRNP-Q2/SYNCRIP) binds poly(A) by default when PABP binding is inhibited.
Heterogenous nuclear ribonucleoprotein Q increases protein expression from HIV-1 Rev-dependent transcripts.
Hadian et al., München, Germany. In Virol J, 2012
Recent data show interaction of the HIV-1 Rev regulatory protein with a subset of hnRNP proteins, that includes hnRNP Q, suggesting that hnRNPs can contribute to regulation of HIV-1 gene expression by Rev. FINDINGS: In this work we address the effect of hnRNP Q on Rev-dependent gene expression.
Negative regulation of RhoA translation and signaling by hnRNP-Q1 affects cellular morphogenesis.
Bassell et al., Atlanta, United States. In Mol Biol Cell, 2012
results revealed essential role for hnRNP-Q1 in regulating dendritic development and focal adhesions, which are mediated by negatively regulating RhoA protein synthesis and signaling; findings provide insight into regulation of RhoA signaling and mechanisms underlying cellular morphogenesis
Rhythmic interaction between Period1 mRNA and hnRNP Q leads to circadian time-dependent translation.
Kim et al., South Korea. In Mol Cell Biol, 2012
The circadian-dependent translation of Per1 mRNA was controlled by an internal ribosomal entry site element in the 5= untranslated region of mPer1 mRNA along with the trans-acting factor mouse heterogeneous nuclear ribonucleoprotein Q.
Identification of a heterogeneous nuclear ribonucleoprotein-recognition region in the HIV Rev protein.
Brack-Werner et al., München, Germany. In J Biol Chem, 2009
Data demonstrate that expression levels of hnRNP A1, Q, K, R, and U influence HIV-1 production by persistently infected
The GAIT system: a gatekeeper of inflammatory gene expression.
Fox et al., Cleveland, United States. In Trends Biochem Sci, 2009
In myeloid cells, interferon (IFN)-gamma induces formation of the heterotetrameric, IFN-gamma-activated inhibitor of translation (GAIT) complex comprising glutamyl-prolyl tRNA synthetase (EPRS), NS1-associated protein 1 (NSAP1), ribosomal protein L13a and glyceraldehyde-3-phosphate dehydrogenase (GAPDH).
SYNCRIP (synaptotagmin-binding, cytoplasmic RNA-interacting protein) is a host factor involved in hepatitis C virus RNA replication.
Lai et al., Los Angeles, United States. In Virology, 2009
SYNCRIP participates in both RNA replication and translation in HCV life cycle.
Galectin-3 stabilizes heterogeneous nuclear ribonucleoprotein Q to maintain proliferation of human colon cancer cells.
Park et al., South Korea. In Cell Mol Life Sci, 2009
Results demonstrate that galectin-3 stabilizes hnRNP Q via complex formation, and reduction in the hnRNP Q level leads to slow proliferation and less susceptibility to 5-FU.
A mechanism for translationally coupled mRNA turnover: interaction between the poly(A) tail and a c-fos RNA coding determinant via a protein complex.
Shyu et al., Houston, United States. In Cell, 2000
Five mCRD-associated proteins were identified: Unr, a purine-rich RNA binding protein; PABP, a poly(A) binding protein; PAIP-1, a poly(A) binding protein interacting protein; hnRNP D, an AU-rich element binding protein; and NSAP1, an hnRNP R-like protein.
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