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Heterogeneous nuclear ribonucleoprotein K

hnRNP K, heterogeneous nuclear ribonucleoprotein K
This gene belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA binding proteins and they complex with heterogeneous nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and transport. While all of the hnRNPs are present in the nucleus, some seem to shuttle between the nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic acid binding properties. The protein encoded by this gene is located in the nucleoplasm and has three repeats of KH domains that binds to RNAs. It is distinct among other hnRNP proteins in its binding preference; it binds tenaciously to poly(C). This protein is also thought to have a role during cell cycle progession. Several alternatively spliced transcript variants have been described for this gene, however, not all of them are fully characterized. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CAN, fibrillin-1, ACID, V1a, Src
Papers using hnRNP K antibodies
Riluzole protects against glutamate-induced slowing of neurofilament axonal transport
White Anthony R et al., In Molecular Neurodegeneration, 2008
... Monoclonal antisera to hnRNP A1 and hnRNP K were purchased from Abcam (Waterloo, Australia) ...
Papers on hnRNP K
Identification and interplay of sequence specific DNA binding proteins involved in regulation of human Pregnane and Xenobiotic Receptor gene.
Tyagi et al., New Delhi, India. In Exp Cell Res, Jan 2016
Here, we report the identification of 54kDa CE binding protein as a heterogeneous nuclear ribonucleoprotein K (hnRNPK) and demonstrate the effect of hnRNP K and Sp1 on PXR promoter transcriptional activity.
Nuclear AURKA acquires kinase-independent transactivating function to enhance breast cancer stem cell phenotype.
Liu et al., Dalian, China. In Nat Commun, Dec 2015
Instead, AURKA preferentially interacts with heterogeneous nuclear ribonucleoprotein K (hnRNP K) in the nucleus and acts as a transcription factor in a complex that induces a shift in MYC promoter usage and activates the MYC promoter.
hnRNP K Is a Haploinsufficient Tumor Suppressor that Regulates Proliferation and Differentiation Programs in Hematologic Malignancies.
Post et al., Houston, United States. In Cancer Cell, Nov 2015
hnRNP K regulates cellular programs, and changes in its expression and mutational status have been implicated in neoplastic malignancies.
Keratin-dependent regulation of Aire and gene expression in skin tumor keratinocytes.
Coulombe et al., Baltimore, United States. In Nat Genet, Aug 2015
The induction of Aire mRNA in keratinocytes depends on a functional interaction between K17 and the heterogeneous nuclear ribonucleoprotein hnRNP K. Further, K17 colocalizes with Aire protein in the nucleus of tumor-prone keratinocytes, and each factor is bound to a specific promoter region featuring an NF-κB consensus sequence in a relevant subset of K17- and Aire-dependent proinflammatory genes.
[Molecular Mechanism of Action of hnRNP K and RTN3 in the Replication of Enterovirus 71].
Zhang et al., In Bing Du Xue Bao, Mar 2015
Recent work has identified some of cell factors of the host that participate in the synthesis of the RNA and proteins of EV71 (e.g., hnRNP K, reticulon 3 (RTN 3)).
KH-RNA interactions: back in the groove.
Ramos et al., London, United Kingdom. In Curr Opin Struct Biol, Feb 2015
The hnRNP K-homology (KH) domain is a single stranded nucleic acid binding domain that mediates RNA target recognition by a large group of gene regulators.
Host MicroRNA miR-197 Plays a Negative Regulatory Role in the Enterovirus 71 Infectious Cycle by Targeting the RAN Protein.
Horng et al., Taiwan. In J Virol, 2014
EV71-induced downregulation of miR-197 expression increased the expression of RAN, which supported the nuclear transport of the essential viral proteins 3D/3CD and host protein hnRNP K for viral replication.
Cytoplasmic Accumulation of Heterogeneous Nuclear Ribonucleoprotein K Strongly Promotes Tumor Invasion in Renal Cell Carcinoma Cells.
Nakatani et al., Ōsaka, Japan. In Plos One, 2014
While overexpression of hnRNP K has been shown to be related to tumorigenesis in several cancers, both the expression patterns and biological mechanisms of hnRNP K in renal cell carcinoma (RCC) cells remain unclear.
Cytoplasmic hnRNPK interacts with GSK3β and is essential for the osteoclast differentiation.
Liu et al., Guangzhou, China. In Sci Rep, 2014
We have previously identified the heterogeneous nuclear ribonucleoprotein K (hnRNPK) as a putative GSK3β interactor.
Emerging roles of heterogeneous nuclear ribonucleoprotein K (hnRNP K) in cancer progression.
Balbi et al., Genova, Italy. In Cancer Lett, 2014
The heterogeneous nuclear ribonucleoprotein K (hnRNP K) is a nucleic acid-binding protein that serves as a docking platform integrating transduction pathways to nucleic acid -directed processes.
The role of mammalian MAPK signaling in regulation of cytokine mRNA stability and translation.
Gaestel et al., Hannover, Germany. In J Interferon Cytokine Res, 2014
This regulation involves mRNA elements, such as AU-rich motifs, and mRNA-binding proteins, such as tristetraprolin (TTP), HuR, and hnRNPK-homology (KH) type splicing regulatory protein (KSRP).
Role of Sam68 in post-transcriptional gene regulation.
Sánchez-Margalet et al., Sevilla, Spain. In Int J Mol Sci, 2012
Sam68 belongs to this class of heteronuclear ribonucleoprotein particle K (hnRNP K) homology (KH) single domain-containing family of RNA-binding proteins that also contains some domains predicted to bind critical components in signal transduction pathways.
DNA damage-induced heterogeneous nuclear ribonucleoprotein K sumoylation regulates p53 transcriptional activation.
Srebrow et al., Buenos Aires, Argentina. In J Biol Chem, 2012
DNA damage-induced Pc2 activation to the p53 transcriptional co-activation through hnRNP K sumoylation.
All human granzymes target hnRNP K that is essential for tumor cell viability.
Bovenschen et al., Utrecht, Netherlands. In J Biol Chem, 2012
hnRNP K is indispensable for tumor cell viability and targeting of hnRNP K by granzymes contributes to or reinforces the cell death mechanisms by which cytotoxic lymphocytes eliminate tumor cells.
Heterogeneous ribonucleoprotein K and thymidine phosphorylase are independent prognostic and therapeutic markers for oral squamous cell carcinoma.
Chang et al., Taiwan. In Oral Oncol, 2012
Elevated cytoplasmic hnRNP K and TP overexpression are associated with poorer survival in oral squamous cell carcinoma patients
Aurora-A phosphorylates hnRNPK and disrupts its interaction with p53.
Lin et al., Taipei, Taiwan. In Febs Lett, 2011
Via phosphorylating hnRNPK Aurora-A participates in regulating p53 activity during DNA damage.
Heterogeneous nuclear ribonucleoprotein K and nucleolin as transcriptional activators of the vascular endothelial growth factor promoter through interaction with secondary DNA structures.
Sun et al., Tucson, United States. In Biochemistry, 2011
Heterogeneous nuclear ribonucleoprotein K and nucleolin transcriptionally activate the vascular endothelial growth factor promoter through interaction with secondary DNA structures
MDM2-dependent downregulation of p21 and hnRNP K provides a switch between apoptosis and growth arrest induced by pharmacologically activated p53.
Selivanova et al., Stockholm, Sweden. In Cancer Cell, 2009
MDM2 released from p53 by RITA promotes degradation of p21 and the p53 cofactor hnRNP K, required for p21 transcription
p53 and MDM2: antagonists or partners in crime?
Lozano et al., Nashville, United States. In Cancer Cell, 2009
A study by Enge et al. in this issue of Cancer Cell shows that the ability of MDM2 to target hnRNP K for degradation contributes to the decision to induce apoptosis rather than cell-cycle arrest.
hnRNP K: an HDM2 target and transcriptional coactivator of p53 in response to DNA damage.
Jackson et al., Cambridge, United Kingdom. In Cell, 2006
hnRNP K is a HDM2 target and serves as a cofactor for p53. HnRNP K plays key roles in coordinating transcriptional responses to DNA damage.
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