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Heterogeneous nuclear ribonucleoprotein H1

hnRNP H, heterogeneous nuclear ribonucleoprotein H1, HNRPH1
This gene encodes a member of a subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA binding proteins that complex with heterogeneous nuclear RNA. 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 may shuttle between the nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic acid binding properties. The protein encoded by this gene has three repeats of quasi-RRM domains that bind to RNA and is very similar to the family member HNRPF. This gene may be associated with hereditary lymphedema type I. Alternatively spliced transcript variants have been described [provided by RefSeq, Mar 2012] (from NCBI)
Top mentioned proteins: CAN, H1, fibrillin-1, CIs, V1a
Papers on hnRNP H
Proteomic analysis of β-asarone induced cytotoxicity in human glioblastoma U251 cells.
New
Li et al., Chongqing, China. In J Pharm Biomed Anal, Dec 2015
Importantly, four proteins (heterogeneous nuclear ribonucleoprotein H1 (H), isoform CRA_b, heterogeneous nuclear ribonucleoprotein A2/B1, isoform CRA_a, ubiquitin carboxyl-terminal hydrolase isozyme L1 and cathepsin D) acting as either oncoproteins or tumor suppressors draw our special attention.
Dysregulation of microRNA-212 Promotes Castration Resistance via hnRNPH1-Mediated Regulation of AR and AR-V7: Implications for Racial Disparity of Prostate Cancer.
New
Abdel-Mageed et al., Somalia. In Clin Cancer Res, Dec 2015
The purpose of this study was to investigate the mechanistic role and assess clinical utility of the splicing factor heterogeneous nuclear ribonucleoprotein H1 (hnRNP H1) in PC progression among AA men.
Bortezomib inhibits Burkitt's lymphoma cell proliferation by downregulating sumoylated hnRNP K and c-Myc expression.
New
Liang et al., Taipei, Taiwan. In Oncotarget, Oct 2015
Among the proteins with altered expression, hnRNP K, hnRNP H, Hsp90α, Grp78, and Hsp7C were common to both Daudi and CA46 cells.
iTRAQ-based quantitative subcellular proteomic analysis of Avibirnavirus-infected cells.
New
Zhou et al., Hangzhou, China. In Electrophoresis, Jul 2015
Confocal microscopy showed colocalization of the viral protein VP3 with host proteins heterogeneous nuclear ribonucleoprotein H1, nuclear factor 45, apoptosis inhibitor 5, nuclear protein localization protein 4 and DEAD-box RNA helicase 42 during the virus infection.
Antisense RNA foci in the motor neurons of C9ORF72-ALS patients are associated with TDP-43 proteinopathy.
New
Shaw et al., Sheffield, United Kingdom. In Acta Neuropathol, Jul 2015
Immunohistochemistry and UV-crosslinking studies showed that sense and antisense RNA molecules share similar interactions with SRSF2, hnRNP K, hnRNP A1, ALYREF, and hnRNP H/F.
Age-related expression analysis of mouse liver nuclear protein binding to 3'-untranslated region of Period2 gene.
New
Kurachi et al., Sapporo, Japan. In J Physiol Sci, Jul 2015
Here, we describe other members of this protein family, hnRNP C and hnRNP H, which bind to the 3'-UTR of the mouse circadian clock gene Period 2 (mPer2).
SRSF1 and hnRNP H antagonistically regulate splicing of COLQ exon 16 in a congenital myasthenic syndrome.
Ohno et al., Nagoya, Japan. In Sci Rep, 2014
RNA affinity purification, mass spectrometry, and siRNA-mediated gene knocking down disclosed that the mutation disrupts binding of a splicing-enhancing RNA-binding protein, SRSF1, and de novo gains binding of a splicing-suppressing RNA-binding protein, hnRNP H. MS2-mediated artificial tethering of each factor demonstrated that SRSF1 and hnRNP H antagonistically modulate splicing by binding exclusively to the target in exon 16.
A targeted oligonucleotide enhancer of SMN2 exon 7 splicing forms competing quadruplex and protein complexes in functional conditions.
Eperon et al., Leicester, United Kingdom. In Cell Rep, 2014
Neither hnRNP H nor quadruplex formation contributes to ESE activity.
AMPKα2 translocates into the nucleus and interacts with hnRNP H: implications in metformin-mediated glucose uptake.
Kim et al., Seoul, South Korea. In Cell Signal, 2014
In addition, AMPKα2 was shown to directly interact with the heterogeneous nuclear ribonucleoprotein H (hnRNP H).
The ETFDH c.158A>G variation disrupts the balanced interplay of ESE- and ESS-binding proteins thereby causing missplicing and multiple Acyl-CoA dehydrogenation deficiency.
Andresen et al., Århus, Denmark. In Hum Mutat, 2014
This ESS motif binds splice inhibitory hnRNP A1, hnRNP A2/B1, and hnRNP H proteins.
Evolutionarily emerged G tracts between the polypyrimidine tract and 3' AG are splicing silencers enriched in genes involved in cancer.
Xie et al., Winnipeg, Canada. In Bmc Genomics, 2013
We show by mutagenesis analysis and RNA interference that the G tracts are splicing silencers and a group of the associated exons are controlled by the G tract binding proteins hnRNP H/F.
Aberrant O-GlcNAc-modified proteins expressed in primary colorectal cancer.
Champattanachai et al., Bangkok, Thailand. In Oncol Rep, 2013
Using 2-dimensional O-GlcNAc immunoblotting and LC-MS/MS analysis, 16 proteins were successfully identified and 8 proteins showed an increase in O-GlcNAcylation, including cytokeratin 18, heterogeneous nuclear ribonucleoproteins A2/B1 (hnRNP A2/B1), hnRNP H, annexin A2, annexin A7, laminin-binding protein, α-tubulin and protein DJ-1.
Dual role of G-runs and hnRNP F in the regulation of a mutation-activated pseudoexon in the fibrinogen gamma-chain transcript.
Duga et al., Milano, Italy. In Plos One, 2012
While hnRNP H did not significantly affect pseudoexon splicing, hnRNP F promoted pseudoexon inclusion, indicating that these two proteins have only partially redundant functions.
Dengue virus infection induces upregulation of hn RNP-H and PDIA3 for its multiplication in the host cell.
GeneRIF
Ganju et al., Delhi, India. In Virus Res, 2012
These results suggest that increased level of hnRNP-H and PDIA3 expression in Dengue virus infected THP1 cells assist in the viral replication by suppressing the TNF-alpha production.
Identification of hnRNPH1, NF45, and C14orf166 as novel host interacting partners of the mature hepatitis C virus core protein.
GeneRIF
Wang et al., Zhengzhou, China. In J Proteome Res, 2011
spatial interactions of hnRNPH1, NF45, and C14orf166 with HCVc174 likely modulate HCV or cellular functions during acute and chronic HCV infection
Splicing factor hnRNPH drives an oncogenic splicing switch in gliomas.
GeneRIF
Cartegni et al., New York City, United States. In Embo J, 2011
hnRNPH activity appears to be involved in the pathogenesis and progression of malignant gliomas as the centre of a splicing oncogenic switch
Autoregulatory circuit of human rpL3 expression requires hnRNP H1, NPM and KHSRP.
GeneRIF
Russo et al., Napoli, Italy. In Nucleic Acids Res, 2011
Insight on the crucial role of hnRNP H1 in the regulation of the alternative splicing of the rpL3 gene.
The expression profile of RNA-binding proteins in primary and metastatic colorectal cancer: relationship of heterogeneous nuclear ribonucleoproteins with prognosis.
GeneRIF
Murray et al., Aberdeen, United Kingdom. In Hum Pathol, 2011
Nuclear heterogeneous nuclear ribonucleo-protein H expression was related to survival in colorectal cancer.
HPV-16 RNA processing.
Review
Schwartz, Uppsala, Sweden. In Front Biosci, 2007
The early polyA signal is also under control of the early UTR sequence and multiple RNA elements in the L2 coding region that interact with hnRNP H.
Role of viral splicing elements and cellular RNA binding proteins in regulation of HIV-1 alternative RNA splicing.
Review
Madsen et al., Iowa City, United States. In Curr Hiv Res, 2006
These include exonic splicing silencers (ESS) and an intronic splicing silencer (ISS) that are selectively bound either by members of the hnRNP A/B family (hnRNPs A1, A1(B), A2, and B1) or by hnRNP H. Exonic splicing enhancers (ESE) are also present within the HIV-1 genome and are selectively bound by members of the SR protein family.
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