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RCN2 protein, human

Known as: reticulocalbin 2, EF-hand calcium binding domain protein, human, Endoplasmic Reticulum Calcium-Binding Protein 55kD, Reticulocalbin 2 
Reticulocalbin-2 (317 aa, ~37 kDa) is encoded by the human RCN2 gene. This protein is involved in calcium binding.
National Institutes of Health

Related topics

Related topics

7 relations
Calcium BindingCalcium-Binding DomainCalcium-Binding ProteinsEndoplasmic Reticulum
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Papers overview

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2019
2019
Stearate-Induced Apoptosis in Human Pancreatic β-Cells is Associated with Changes in Membrane Protein Expression and These Changes are Inhibited by Oleate.
PURPOSE Lipotoxicity is implicated in type 2 diabetes pathogenesis. Its molecular mechanisms are not completely understood. The… Expand
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2018
2018
Fetal regional brain protein signature in FASD rat model.
Fetal alcohol spectrum disorders (FASD) describe neurodevelopmental deficits in children exposed to alcohol in utero. We… Expand
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2017
2017
Reticulocalbin-2 enhances hepatocellular carcinoma proliferation via modulating the EGFR-ERK pathway
This corrects the article DOI: 10.1038/onc.2017.230 
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2017
2017
Reticulocalbin-2 enhances hepatocellular carcinoma proliferation via modulating the EGFR-ERK pathway
Hepatocellular carcinoma (HCC) is a major health threat worldwide. Although the involvement of reticulocalbin-2 (RCN2) in cell… Expand
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Highly Cited
2011
Highly Cited
2011
Changes in the Chondrocyte and Extracellular Matrix Proteome during Post-natal Mouse Cartilage Development*
Skeletal growth by endochondral ossification involves tightly coordinated chondrocyte differentiation that creates reserve… Expand
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2007
2007
Proteomic analysis of human cerebral endothelial cells activated by multiple sclerosis serum and IFNbeta-1b.
Several groups have recently described the endothelial cell (EC) as an important target of pathological mediators in multiple… Expand
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2007
2007
Proteomic Analysis of Human Cerebral Endothelial Cells Activated by Multiple Sclerosis Serum and IFNβ-1b
Several groups have recently described the endothelial cell (EC) as an important target of pathological mediators in multiple… Expand
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2006
2006
HPV16 E6 natural variants exhibit different activities in functional assays relevant to the carcinogenic potential of E6.
Genetic studies have revealed natural amino acid variations within the human papillomavirus (HPV) type 16 E6 oncoprotein. To… Expand
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1999
1999
Potential drugs against cervical cancer: zinc-ejecting inhibitors of the human papillomavirus type 16 E6 oncoprotein.
BACKGROUND The principal agent in the etiology of cervical cancer, i.e., human papillomavirus (HPV) type 16, encodes three… Expand
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1998
1998
The identification of a conserved binding motif within human papillomavirus type 16 E6 binding peptides, E6AP and E6BP.
A 16-mer peptide library was screened using the yeast two-hybrid system to identify peptides which specifically interact with the… Expand
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