RPLP1 Gene

HGNC Family	L ribosomal proteins (RPL)
Name	ribosomal protein, large, P1
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 phosphoprotein that is a component of the 60S subunit. The protein, which is a functional equivalent of the E. coli L7/L12 ribosomal protein, belongs to the L12P family of ribosomal proteins. It plays an important role in the elongation step of protein synthesis. Unlike most ribosomal proteins, which are basic, the encoded protein is acidic. Its C-terminal end is nearly identical to the C-terminal ends of the ribosomal phosphoproteins P0 and P2. The P1 protein can interact with P0 and P2 to form a pentameric complex consisting of P1 and P2 dimers, and a P0 monomer. The protein is located in the cytoplasm. Two alternatively spliced transcript variants that encode different proteins have been observed. 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": "\nRPLP1 is a key component of the ribosomal P complex that plays multifaceted roles in protein synthesis and cell proliferation. Early studies demonstrated that overexpression of RPLP1 can immortalize primary cells and is associated with transformation and tumorigenesis in gynecologic tumors, where its enhanced expression correlates with aggressive disease features such as p53 positivity, myometrial invasion, and lymph node metastasis. In cervical cancer, RPLP1 functions downstream of calponin 3 to promote cell viability and motility. In addition, RPLP1—as part of the P protein duo that modulates ribosomal subunit joining and overall translation efficiency—exhibits a unique cytoplasmic localization that may reflect its late assembly onto maturing ribosomes."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "5"}]}, {"type": "t", "text": "\n\nStudies addressing viral interactions have revealed additional roles for RPLP1. Functionally, RPLP1 facilitates the recruitment of translational factors and supports elongation by relieving ribosome pausing; this is critical for the efficient translation of viral proteins, as evidenced by its role in dengue virus envelope protein synthesis and in modulating picornaviral IRES–dependent translation. Moreover, the ribosomal stalk—including RPLP1—enables efficient binding of toxins such as the ricin A-chain, while its depletion causes accumulation of reactive oxygen species that trigger endoplasmic reticulum stress, an unfolded protein response, and autophagy–all of which underscore its importance in maintaining translational homeostasis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "6", "end_ref": "8"}]}, {"type": "t", "text": "\n\nBeyond its central roles in translation and viral protein biogenesis, RPLP1 is implicated in a spectrum of disease processes. Autoantibodies against native and recombinant RPLP1 components have been detected in systemic lupus erythematosus, suggesting a potential role as diagnostic markers. In endometriosis, adenomyosis, and endometrial adenocarcinoma, elevated RPLP1 expression promotes cell survival and migration, indicating its contribution to the invasive phenotype of these conditions. Intriguingly, in the context of HIV-1 infection, higher levels and nuclear translocation of RPLP1 in long-term non-progressors interfere with viral transcription by occupying C/EBPβ binding sites in the viral long terminal repeat, thereby reinforcing viral latency. Finally, preliminary data hint at an as-yet-undefined role for RPLP1 in regulating protein translation during metabolic dysfunction-associated steatohepatitis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "9", "end_ref": "14"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "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": 2, "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": 3, "children": [{"type": "t", "text": "Francisco Martinez-Azorin, Miguel Remacha, Juan P G Ballesta "}, {"type": "b", "children": [{"type": "t", "text": "Functional characterization of ribosomal P1/P2 proteins in human cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem J (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1042/BJ20080049"}], "href": "https://doi.org/10.1042/BJ20080049"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18422483"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18422483"}]}, {"type": "r", "ref": 4, "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": 5, "children": [{"type": "t", "text": "Lili Xia, Yongfang Yue, Mingyue Li, et al. "}, {"type": "b", "children": [{"type": "t", "text": "CNN3 acts as a potential oncogene in cervical cancer by affecting RPLP1 mRNA expression."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Sci Rep (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41598-020-58947-y"}], "href": "https://doi.org/10.1038/s41598-020-58947-y"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "32051425"}], "href": "https://pubmed.ncbi.nlm.nih.gov/32051425"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Kerrie L May, Xiao-Ping Li, Francisco Martínez-Azorín, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The P1/P2 proteins of the human ribosomal stalk are required for ribosome binding and depurination by ricin in human cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "FEBS J (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1111/j.1742-4658.2012.08752.x"}], "href": "https://doi.org/10.1111/j.1742-4658.2012.08752.x"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22909382"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22909382"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Francisco Martínez-Azorín, Miguel Remacha, Encarnación Martínez-Salas, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Internal translation initiation on the foot-and-mouth disease virus IRES is affected by ribosomal stalk conformation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "FEBS Lett (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.febslet.2008.07.039"}], "href": "https://doi.org/10.1016/j.febslet.2008.07.039"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18675807"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18675807"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Rafael K Campos, H R Sagara Wijeratne, Premal Shah, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Ribosomal stalk proteins RPLP1 and RPLP2 promote biogenesis of flaviviral and cellular multi-pass transmembrane proteins."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nucleic Acids Res (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/nar/gkaa717"}], "href": "https://doi.org/10.1093/nar/gkaa717"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "32890404"}], "href": "https://pubmed.ncbi.nlm.nih.gov/32890404"}]}, {"type": "r", "ref": 9, "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": 10, "children": [{"type": "t", "text": "Zahraa Alali, Amanda Graham, Kimberly Swan, et al. "}, {"type": "b", "children": [{"type": "t", "text": "60S acidic ribosomal protein P1 (RPLP1) is elevated in human endometriotic tissue and in a murine model of endometriosis and is essential for endometriotic epithelial cell survival in vitro."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Hum Reprod (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/molehr/gaz065"}], "href": "https://doi.org/10.1093/molehr/gaz065"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "31899515"}], "href": "https://pubmed.ncbi.nlm.nih.gov/31899515"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Patrycja Horbowicz-Drożdżal, Karol Kamel, Sebastian Kmiecik, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Phosphorylation of the conserved C-terminal domain of ribosomal P-proteins impairs the mode of interaction with plant toxins."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "FEBS Lett (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/1873-3468.14170"}], "href": "https://doi.org/10.1002/1873-3468.14170"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "34328639"}], "href": "https://pubmed.ncbi.nlm.nih.gov/34328639"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Riley Peterson, Paige Minchella, Wei Cui, et al. "}, {"type": "b", "children": [{"type": "t", "text": "RPLP1 Is Up-Regulated in Human Adenomyosis and Endometrial Adenocarcinoma Epithelial Cells and Is Essential for Cell Survival and Migration In Vitro."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Int J Mol Sci (2023)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.3390/ijms24032690"}], "href": "https://doi.org/10.3390/ijms24032690"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "36769010"}], "href": "https://pubmed.ncbi.nlm.nih.gov/36769010"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Weijing Yang, Hong Wang, Zhaolong Li, et al. "}, {"type": "b", "children": [{"type": "t", "text": "RPLP1 restricts HIV-1 transcription by disrupting C/EBPβ binding to the LTR."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Commun (2024)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41467-024-49622-1"}], "href": "https://doi.org/10.1038/s41467-024-49622-1"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "38906865"}], "href": "https://pubmed.ncbi.nlm.nih.gov/38906865"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Madhulika Tripathi, Karine Gauthier, Reddemma Sandireddy, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Esrra regulates Rplp1-mediated translation of lysosome proteins suppressed in metabolic dysfunction-associated steatohepatitis and reversed by alternate day fasting."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Metab (2024)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.molmet.2024.101997"}], "href": "https://doi.org/10.1016/j.molmet.2024.101997"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "39032642"}], "href": "https://pubmed.ncbi.nlm.nih.gov/39032642"}]}]}]}
Synonyms	RPP1, LP1
Proteins	RLA1_HUMAN
NCBI Gene ID	6176
API
Download Associations
Predicted Functions
Co-expressed Genes
Expression in Tissues and Cell Lines

Functional Associations

RPLP1 has 24,140 functional associations with biological entities spanning 8 categories (molecular profile, organism, functional term, phrase or reference, chemical, disease, phenotype or trait, structural feature, cell line, cell type or tissue, gene, protein or microRNA) extracted from 114 datasets.

Click the + buttons to view associations for RPLP1 from the datasets below.

If available, associations are ranked by standardized value

Harmonizome 3.0

RPLP1 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 RPLP1 gene relative to other tissues from the Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles dataset.
	Allen Brain Atlas Aging Dementia and Traumatic Brain Injury Tissue Sample Gene Expression Profiles	tissue samples with high or low expression of RPLP1 gene relative to other tissue samples from the Allen Brain Atlas Aging Dementia and Traumatic Brain Injury Tissue Sample Gene Expression Profiles dataset.
	Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by RNA-seq	tissue samples with high or low expression of RPLP1 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 RPLP1 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 RPLP1 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 RPLP1 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 RPLP1 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 RPLP1 gene relative to other cell lines from the CCLE Cell Line Gene CNV Profiles dataset.
	CCLE Cell Line Proteomics	Cell lines associated with RPLP1 protein from the CCLE Cell Line Proteomics dataset.
	CellMarker Gene-Cell Type Associations	cell types associated with RPLP1 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 RPLP1 gene from the CHEA Transcription Factor Binding Site Profiles dataset.
	ChEA Transcription Factor Targets	transcription factors binding the promoter of RPLP1 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 RPLP1 gene in low- or high-throughput transcription factor functional studies from the CHEA Transcription Factor Targets 2022 dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores	cellular components containing RPLP1 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores 2025	cellular components containing RPLP1 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.
	COMPARTMENTS Experimental Protein Localization Evidence Scores	cellular components containing RPLP1 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 RPLP1 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 RPLP1 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 RPLP1 protein in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.
	CORUM Protein Complexes	protein complexs containing RPLP1 protein from the CORUM Protein Complexes dataset.
	COSMIC Cell Line Gene CNV Profiles	cell lines with high or low copy number of RPLP1 gene relative to other cell lines from the COSMIC Cell Line Gene CNV Profiles dataset.
	COSMIC Cell Line Gene Mutation Profiles	cell lines with RPLP1 gene mutations from the COSMIC Cell Line Gene Mutation Profiles dataset.
	CTD Gene-Chemical Interactions	chemicals interacting with RPLP1 gene/protein from the curated CTD Gene-Chemical Interactions dataset.
	CTD Gene-Disease Associations	diseases associated with RPLP1 gene/protein from the curated CTD Gene-Disease Associations dataset.
	DeepCoverMOA Drug Mechanisms of Action	small molecule perturbations with high or low expression of RPLP1 protein relative to other small molecule perturbations from the DeepCoverMOA Drug Mechanisms of Action dataset.
	DISEASES Experimental Gene-Disease Association Evidence Scores	diseases associated with RPLP1 gene in GWAS datasets from the DISEASES Experimental Gene-Disease Assocation Evidence Scores dataset.
	DISEASES Text-mining Gene-Disease Association Evidence Scores	diseases co-occuring with RPLP1 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 RPLP1 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 RPLP1 gene in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.
	DisGeNET Gene-Phenotype Associations	phenotypes associated with RPLP1 gene in GWAS and other genetic association datasets from the DisGeNET Gene-Phenoptype Associations dataset.
	ENCODE Histone Modification Site Profiles	histone modification site profiles with high histone modification abundance at RPLP1 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 RPLP1 gene from the ENCODE Transcription Factor Binding Site Profiles dataset.
	ENCODE Transcription Factor Targets	transcription factors binding the promoter of RPLP1 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 RPLP1 from the ESCAPE Omics Signatures of Genes and Proteins for Stem Cells dataset.
	GAD High Level Gene-Disease Associations	diseases associated with RPLP1 gene in GWAS and other genetic association datasets from the GAD High Level Gene-Disease Associations dataset.
	GDSC Cell Line Gene Expression Profiles	cell lines with high or low expression of RPLP1 gene relative to other cell lines from the GDSC Cell Line Gene Expression Profiles dataset.
	GeneRIF Biological Term Annotations	biological terms co-occuring with RPLP1 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 RPLP1 from the GeneSigDB Published Gene Signatures dataset.
	GEO Signatures of Differentially Expressed Genes for Diseases	disease perturbations changing expression of RPLP1 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 RPLP1 gene from the GEO Signatures of Differentially Expressed Genes for Gene Perturbations dataset.