RPLP0 Gene

HGNC Family	L ribosomal proteins (RPL)
Name	ribosomal protein, large, P0
Description	Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal protein that is a component of the 60S subunit. The protein, which is the functional equivalent of the E. coli L10 ribosomal protein, belongs to the L10P family of ribosomal proteins. It is a neutral phosphoprotein with a C-terminal end that is nearly identical to the C-terminal ends of the acidic ribosomal phosphoproteins P1 and P2. The P0 protein can interact with P1 and P2 to form a pentameric complex consisting of P1 and P2 dimers, and a P0 monomer. The protein is located in the cytoplasm. Transcript variants derived from alternative splicing exist; they encode the same protein. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome. [provided by RefSeq, Jul 2008]
Summary	{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nRPLP0, also known as the ribosomal P0 protein or uL10, is an essential acidic component of the ribosomal “stalk” structure that anchors the P complex to the large ribosomal subunit. It plays a critical role in recruiting translational factors required for efficient protein synthesis and in the proper assembly of the P-stalk complex with P1/P2 partners. Studies using diverse expression systems have demonstrated that when expressed in eukaryotic cells its proper folding and phosphorylation are essential for its association with ribosomes and for supporting elongation factor–dependent GTPase activity."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": "\n\nIn addition to its canonical role in translation, RPLP0 is subject to regulatory phosphorylation and dynamic redistribution that modulate its interaction with the ribosome under stress. Under nucleolar stress conditions, for example, a free pool of RPLP0 accumulates in the cytoplasm and its N-terminal phosphorylation can impair ribosome binding, suggesting that posttranslational modifications fine-tune its function in the GTPase-associated center, thereby influencing overall translational activity and cell adaptation to environmental changes."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "3", "end_ref": "5"}]}, {"type": "t", "text": "\n\nRPLP0 also manifests extraribosomal functions that are directly linked to tumorigenesis. Its overexpression has been observed in various cancers including gynecologic, breast, hepatocellular, and colorectal tumors, where it can counteract tumor-suppressive mechanisms—for instance, by interacting with proteins such as GCIP to block inhibition of pRb phosphorylation—and thereby promote cell growth, colony formation, and metastasis. In gastric cancer, for example, RPLP0 interacts with cathepsin X to modulate key cell cycle regulators such as CDK2, while its antigenicity in tumor-associated contexts has also been noted."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "6", "end_ref": "9"}]}, {"type": "t", "text": "\n\nBeyond its roles in translation and cancer progression, RPLP0 is involved in DNA repair and immune responses. Its interaction with the paraspeckle protein NONO, for instance, promotes non-homologous end joining and enhances DNA-PK autophosphorylation following DNA double-strand breaks, underscoring a ribosome-independent function in the cellular response to genotoxic stress. Moreover, as a component of the immunogenic ribosomal P complex, RPLP0 serves as a target for autoantibodies in systemic lupus erythematosus, highlighting its potential as a marker of immune-mediated pathology."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "10", "end_ref": "12"}]}, {"type": "t", "text": "\n\nFurthermore, the stable expression and diagnostic relevance of RPLP0 have been demonstrated in contexts beyond cancer biology. It has been validated as one of the most stable reference genes for quantitative real‐time PCR in ovarian tissues, and its differential expression—along with that of TNF‑α—has been shown to serve as a robust biomarker for high-altitude pulmonary edema (HAPE) by modulating endothelial cell apoptosis and permeability."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "13"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Marek Tchórzewski, Dawid Krokowski, Wojciech Rzeski, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The subcellular distribution of the human ribosomal \"stalk\" components: P1, P2 and P0 proteins."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Int J Biochem Cell Biol (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/s1357-2725(02)00133-4"}], "href": "https://doi.org/10.1016/s1357-2725(02"}, {"type": "t", "text": "00133-4) PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12479870"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12479870"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Yohichi Abo, Akiko Hagiya, Takao Naganuma, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Baculovirus-mediated expression and isolation of human ribosomal phosphoprotein P0 carrying a GST-tag in a functional state."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem Biophys Res Commun (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbrc.2004.07.196"}], "href": "https://doi.org/10.1016/j.bbrc.2004.07.196"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15336536"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15336536"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Ana Artero-Castro, Mileidys Perez-Alea, Andrea Feliciano, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Disruption of the ribosomal P complex leads to stress-induced autophagy."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Autophagy (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1080/15548627.2015.1063764"}], "href": "https://doi.org/10.1080/15548627.2015.1063764"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26176264"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26176264"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Kamil Deryło, Barbara Michalec-Wawiórka, Dawid Krokowski, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The uL10 protein, a component of the ribosomal P-stalk, is released from the ribosome in nucleolar stress."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochim Biophys Acta Mol Cell Res (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbamcr.2017.10.002"}], "href": "https://doi.org/10.1016/j.bbamcr.2017.10.002"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28986221"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28986221"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Kamil Filipek, Barbara Michalec-Wawiórka, Aleksandra Boguszewska, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Phosphorylation of the N-terminal domain of ribosomal P-stalk protein uL10 governs its association with the ribosome."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "FEBS Lett (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/1873-3468.13885"}], "href": "https://doi.org/10.1002/1873-3468.13885"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "32668052"}], "href": "https://pubmed.ncbi.nlm.nih.gov/32668052"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "T-W Chang, C-C Chen, K-Y Chen, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Ribosomal phosphoprotein P0 interacts with GCIP and overexpression of P0 is associated with cellular proliferation in breast and liver carcinoma cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncogene (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/sj.onc.1210651"}], "href": "https://doi.org/10.1038/sj.onc.1210651"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17621266"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17621266"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Ana Artero-Castro, Josep Castellvi, Angel García, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Expression of the ribosomal proteins Rplp0, Rplp1, and Rplp2 in gynecologic tumors."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Hum Pathol (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.humpath.2010.04.020"}], "href": "https://doi.org/10.1016/j.humpath.2010.04.020"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21040949"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21040949"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Anne Teller, Doerthe Jechorek, Roland Hartig, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Dysregulation of apoptotic signaling pathways by interaction of RPLP0 and cathepsin X/Z in gastric cancer."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Pathol Res Pract (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.prp.2014.09.005"}], "href": "https://doi.org/10.1016/j.prp.2014.09.005"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25433997"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25433997"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Monica Benvenuto, Pierpaolo Sileri, Piero Rossi, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Natural humoral immune response to ribosomal P0 protein in colorectal cancer patients."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Transl Med (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1186/s12967-015-0455-7"}], "href": "https://doi.org/10.1186/s12967-015-0455-7"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25889931"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25889931"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Jing Li, Ying Shen, Jing He, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Significance of antibodies against the native ribosomal P protein complex and recombinant P0, P1, and P2 proteins in the diagnosis of Chinese patients with systemic lupus erythematosus."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Clin Lab Anal (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/jcla.21543"}], "href": "https://doi.org/10.1002/jcla.21543"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23400861"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23400861"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Zhen-Rui Shi, Guo-Zhen Tan, Zhen Meng, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Association of anti-acidic ribosomal protein P0 and anti-galectin 3 antibodies with the development of skin lesions in systemic lupus erythematosus."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Arthritis Rheumatol (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/art.38891"}], "href": "https://doi.org/10.1002/art.38891"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25307291"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25307291"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Yun-Long Wang, Wan-Wen Zhao, Shao-Mei Bai, et al. "}, {"type": "b", "children": [{"type": "t", "text": "DNA damage-induced paraspeckle formation enhances DNA repair and tumor radioresistance by recruiting ribosomal protein P0."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell Death Dis (2022)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41419-022-05092-1"}], "href": "https://doi.org/10.1038/s41419-022-05092-1"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "35974014"}], "href": "https://pubmed.ncbi.nlm.nih.gov/35974014"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Jie Fu, Lihong Bian, Li Zhao, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Identification of genes for normalization of quantitative real-time PCR data in ovarian tissues."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Acta Biochim Biophys Sin (Shanghai) (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/abbs/gmq062"}], "href": "https://doi.org/10.1093/abbs/gmq062"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20705598"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20705598"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Yi-Ling Ge, Pei-Jie Li, Ying-Rui Bu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "TNF-α and RPLP0 drive the apoptosis of endothelial cells and increase susceptibility to high-altitude pulmonary edema."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Apoptosis (2024)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s10495-024-02005-9"}], "href": "https://doi.org/10.1007/s10495-024-02005-9"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "39110356"}], "href": "https://pubmed.ncbi.nlm.nih.gov/39110356"}]}]}]}
Synonyms	RPP0, LP0, L10E, PRLP0
Proteins	RLA0_HUMAN
NCBI Gene ID	6175
API
Download Associations
Predicted Functions
Co-expressed Genes
Expression in Tissues and Cell Lines

Functional Associations

RPLP0 has 18,279 functional associations with biological entities spanning 8 categories (molecular profile, organism, chemical, functional term, phrase or reference, disease, phenotype or trait, structural feature, cell line, cell type or tissue, gene, protein or microRNA) extracted from 108 datasets.

Click the + buttons to view associations for RPLP0 from the datasets below.

If available, associations are ranked by standardized value

Harmonizome 3.0

RPLP0 Gene

Functional Associations

Please acknowledge the Harmonizome in your publications by citing the following reference(s):

	Dataset	Summary
	Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles	tissues with high or low expression of RPLP0 gene relative to other tissues from the Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles dataset.
	Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by Microarray	tissue samples with high or low expression of RPLP0 gene relative to other tissue samples from the Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by Microarray dataset.
	Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by RNA-seq	tissue samples with high or low expression of RPLP0 gene relative to other tissue samples from the Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by RNA-seq dataset.
	Allen Brain Atlas Prenatal Human Brain Tissue Gene Expression Profiles	tissues with high or low expression of RPLP0 gene relative to other tissues from the Allen Brain Atlas Prenatal Human Brain Tissue Gene Expression Profiles dataset.
	BioGPS Cell Line Gene Expression Profiles	cell lines with high or low expression of RPLP0 gene relative to other cell lines from the BioGPS Cell Line Gene Expression Profiles dataset.
	BioGPS Human Cell Type and Tissue Gene Expression Profiles	cell types and tissues with high or low expression of RPLP0 gene relative to other cell types and tissues from the BioGPS Human Cell Type and Tissue Gene Expression Profiles dataset.
	BioGPS Mouse Cell Type and Tissue Gene Expression Profiles	cell types and tissues with high or low expression of RPLP0 gene relative to other cell types and tissues from the BioGPS Mouse Cell Type and Tissue Gene Expression Profiles dataset.
	CCLE Cell Line Gene CNV Profiles	cell lines with high or low copy number of RPLP0 gene relative to other cell lines from the CCLE Cell Line Gene CNV Profiles dataset.
	CCLE Cell Line Proteomics	Cell lines associated with RPLP0 protein from the CCLE Cell Line Proteomics dataset.
	CellMarker Gene-Cell Type Associations	cell types associated with RPLP0 gene from the CellMarker Gene-Cell Type Associations dataset.
	ChEA Transcription Factor Binding Site Profiles	transcription factor binding site profiles with transcription factor binding evidence at the promoter of RPLP0 gene from the CHEA Transcription Factor Binding Site Profiles dataset.
	ChEA Transcription Factor Targets	transcription factors binding the promoter of RPLP0 gene in low- or high-throughput transcription factor functional studies from the CHEA Transcription Factor Targets dataset.
	ChEA Transcription Factor Targets 2022	transcription factors binding the promoter of RPLP0 gene in low- or high-throughput transcription factor functional studies from the CHEA Transcription Factor Targets 2022 dataset.
	CMAP Signatures of Differentially Expressed Genes for Small Molecules	small molecule perturbations changing expression of RPLP0 gene from the CMAP Signatures of Differentially Expressed Genes for Small Molecules dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores	cellular components containing RPLP0 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores 2025	cellular components containing RPLP0 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.
	COMPARTMENTS Experimental Protein Localization Evidence Scores	cellular components containing RPLP0 protein in low- or high-throughput protein localization assays from the COMPARTMENTS Experimental Protein Localization Evidence Scores dataset.
	COMPARTMENTS Experimental Protein Localization Evidence Scores 2025	cellular components containing RPLP0 protein in low- or high-throughput protein localization assays from the COMPARTMENTS Experimental Protein Localization Evidence Scores 2025 dataset.
	COMPARTMENTS Text-mining Protein Localization Evidence Scores	cellular components co-occuring with RPLP0 protein in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.
	COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025	cellular components co-occuring with RPLP0 protein in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.
	CORUM Protein Complexes	protein complexs containing RPLP0 protein from the CORUM Protein Complexes dataset.
	COSMIC Cell Line Gene CNV Profiles	cell lines with high or low copy number of RPLP0 gene relative to other cell lines from the COSMIC Cell Line Gene CNV Profiles dataset.
	COSMIC Cell Line Gene Mutation Profiles	cell lines with RPLP0 gene mutations from the COSMIC Cell Line Gene Mutation Profiles dataset.
	CTD Gene-Chemical Interactions	chemicals interacting with RPLP0 gene/protein from the curated CTD Gene-Chemical Interactions dataset.
	CTD Gene-Disease Associations	diseases associated with RPLP0 gene/protein from the curated CTD Gene-Disease Associations dataset.
	DeepCoverMOA Drug Mechanisms of Action	small molecule perturbations with high or low expression of RPLP0 protein relative to other small molecule perturbations from the DeepCoverMOA Drug Mechanisms of Action dataset.
	DISEASES Experimental Gene-Disease Association Evidence Scores 2025	diseases associated with RPLP0 gene in GWAS datasets from the DISEASES Experimental Gene-Disease Assocation Evidence Scores 2025 dataset.
	DISEASES Text-mining Gene-Disease Association Evidence Scores	diseases co-occuring with RPLP0 gene in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores dataset.
	DISEASES Text-mining Gene-Disease Association Evidence Scores 2025	diseases co-occuring with RPLP0 gene in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.
	DisGeNET Gene-Disease Associations	diseases associated with RPLP0 gene in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.
	ENCODE Histone Modification Site Profiles	histone modification site profiles with high histone modification abundance at RPLP0 gene from the ENCODE Histone Modification Site Profiles dataset.
	ENCODE Transcription Factor Binding Site Profiles	transcription factor binding site profiles with transcription factor binding evidence at the promoter of RPLP0 gene from the ENCODE Transcription Factor Binding Site Profiles dataset.
	ENCODE Transcription Factor Targets	transcription factors binding the promoter of RPLP0 gene in ChIP-seq datasets from the ENCODE Transcription Factor Targets dataset.
	ESCAPE Omics Signatures of Genes and Proteins for Stem Cells	PubMedIDs of publications reporting gene signatures containing RPLP0 from the ESCAPE Omics Signatures of Genes and Proteins for Stem Cells dataset.
	GDSC Cell Line Gene Expression Profiles	cell lines with high or low expression of RPLP0 gene relative to other cell lines from the GDSC Cell Line Gene Expression Profiles dataset.
	GeneRIF Biological Term Annotations	biological terms co-occuring with RPLP0 gene in literature-supported statements describing functions of genes from the GeneRIF Biological Term Annotations dataset.
	GeneSigDB Published Gene Signatures	PubMedIDs of publications reporting gene signatures containing RPLP0 from the GeneSigDB Published Gene Signatures dataset.
	GEO Signatures of Differentially Expressed Genes for Diseases	disease perturbations changing expression of RPLP0 gene from the GEO Signatures of Differentially Expressed Genes for Diseases dataset.
	GEO Signatures of Differentially Expressed Genes for Gene Perturbations	gene perturbations changing expression of RPLP0 gene from the GEO Signatures of Differentially Expressed Genes for Gene Perturbations dataset.
	GEO Signatures of Differentially Expressed Genes for Kinase Perturbations	kinase perturbations changing expression of RPLP0 gene from the GEO Signatures of Differentially Expressed Genes for Kinase Perturbations dataset.