C1QBP Gene

Name	complement component 1, q subcomponent binding protein
Description	The human complement subcomponent C1q associates with C1r and C1s in order to yield the first component of the serum complement system. The protein encoded by this gene is known to bind to the globular heads of C1q molecules and inhibit C1 activation. This protein has also been identified as the p32 subunit of pre-mRNA splicing factor SF2, as well as a hyaluronic acid-binding protein. [provided by RefSeq, Jul 2008]
Summary	{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\n C1q‐binding protein (C1QBP), also known as p32, gC1qR, or HABP1, is a multifunctional molecule whose diverse roles span from the regulation of mitochondrial homeostasis to modulation of immune signaling and cell migration. Within mitochondria, C1QBP binds RNA and associates with the mitoribosome to support the synthesis of mitochondrial‐encoded proteins, thereby ensuring proper respiratory chain function; loss or mutation of C1QBP impairs mitochondrial translation and bioenergetics, contributing to cardiomyopathy, myopathy, and multisystem disorders."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "4"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n At the cell surface, C1QBP (as gC1qR) acts as a receptor for a variety of ligands – including viral proteins such as the hepatitis C virus core and herpes simplex virus ICP34.5, as well as microbial and endogenous factors – thereby modulating key immune responses. Engagement of cell‐surface C1QBP attenuates antiviral signaling cascades (for example, by interfering with RIG-I– and MDA5–dependent pathways) and alters T‐cell activation by impairing early receptor‐proximal events and inducing cell cycle arrest, often via stabilization of inhibitors such as p27; these effects contribute to viral persistence and immune evasion."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "5", "end_ref": "8"}]}, {"type": "t", "text": "\n "}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n In addition, C1QBP plays important roles in regulating cell adhesion and migration. It is expressed in membrane microdomains that contribute to lamellipodia formation and tumor cell motility, thereby promoting cancer cell metastasis and affecting tumor metabolism by shifting the balance between oxidative phosphorylation and glycolysis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "9", "end_ref": "12"}]}, {"type": "t", "text": "\n "}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n Furthermore, through interactions with key regulatory proteins such as ARF and CDC2L5, C1QBP influences apoptotic pathways and RNA splicing events that impact cell survival and proliferation."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "13"}]}, {"type": "t", "text": " Finally, by modulating mitochondrial permeability transition through binding to cyclophilin D, C1QBP can protect cells from oxidative stress–induced cell death."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "15"}, {"type": "fg_f", "ref": "4"}]}, {"type": "t", "text": "\n "}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n In summary, C1QBP integrates mitochondrial metabolism, immune regulation, and signal transduction pathways. Its dual localization – functioning in mitochondrial protein synthesis and as a cell surface receptor mediating interactions with viral, microbial, and host factors – underlies its critical roles in maintaining cellular homeostasis while its dysregulation contributes to infectious pathogenesis, tumor progression, and metabolic disorders."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "9"}, {"type": "fg_f", "ref": "1"}, {"type": "fg_f", "ref": "13"}, {"type": "fg_fs", "start_ref": "5", "end_ref": "7"}, {"type": "fg_f", "ref": "11"}, {"type": "fg_f", "ref": "16"}, {"type": "fg_f", "ref": "14"}, {"type": "fg_f", "ref": "2"}, {"type": "fg_f", "ref": "15"}]}, {"type": "t", "text": "\n "}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Mikako Yagi, Takeshi Uchiumi, Shinya Takazaki, et al. "}, {"type": "b", "children": [{"type": "t", "text": "p32/gC1qR is indispensable for fetal development and mitochondrial translation: importance of its RNA-binding ability."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nucleic Acids Res (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/nar/gks774"}], "href": "https://doi.org/10.1093/nar/gks774"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22904065"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22904065"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "René G Feichtinger, Monika Oláhová, Yoshihito Kishita, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Biallelic C1QBP Mutations Cause Severe Neonatal-, Childhood-, or Later-Onset Cardiomyopathy Associated with Combined Respiratory-Chain Deficiencies."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Am J Hum Genet (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.ajhg.2017.08.015"}], "href": "https://doi.org/10.1016/j.ajhg.2017.08.015"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28942965"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28942965"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Toshiro Saito, Takeshi Uchiumi, Mikako Yagi, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Cardiomyocyte-specific loss of mitochondrial p32/C1qbp causes cardiomyopathy and activates stress responses."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cardiovasc Res (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/cvr/cvx095"}], "href": "https://doi.org/10.1093/cvr/cvx095"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28498888"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28498888"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Allison M McGee, Christopher P Baines "}, {"type": "b", "children": [{"type": "t", "text": "Complement 1q-binding protein inhibits the mitochondrial permeability transition pore and protects against oxidative stress-induced death."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem J (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1042/BJ20101431"}], "href": "https://doi.org/10.1042/BJ20101431"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20950273"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20950273"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Lijuan Xu, Nengming Xiao, Feng Liu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Inhibition of RIG-I and MDA5-dependent antiviral response by gC1qR at mitochondria."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.0811029106"}], "href": "https://doi.org/10.1073/pnas.0811029106"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19164550"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19164550"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Zhi Qiang Yao, Audrey Eisen-Vandervelde, Stephen N Waggoner, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Direct binding of hepatitis C virus core to gC1qR on CD4+ and CD8+ T cells leads to impaired activation of Lck and Akt."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Virol (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1128/JVI.78.12.6409-6419.2004"}], "href": "https://doi.org/10.1128/JVI.78.12.6409-6419.2004"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15163734"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15163734"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Ying Zhang, Cheng J Ma, Lei Ni, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Cross-talk between programmed death-1 and suppressor of cytokine signaling-1 in inhibition of IL-12 production by monocytes/macrophages in hepatitis C virus infection."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Immunol (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.4049/jimmunol.1002006"}], "href": "https://doi.org/10.4049/jimmunol.1002006"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21263070"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21263070"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Zhi Q Yao, Ellis King, Deborah Prayther, et al. "}, {"type": "b", "children": [{"type": "t", "text": "T cell dysfunction by hepatitis C virus core protein involves PD-1/PDL-1 signaling."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Viral Immunol (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1089/vim.2006.0096"}], "href": "https://doi.org/10.1089/vim.2006.0096"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17603844"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17603844"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Valentina Fogal, Adam D Richardson, Priya P Karmali, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Mitochondrial p32 protein is a critical regulator of tumor metabolism via maintenance of oxidative phosphorylation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Biol (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1128/MCB.01101-09"}], "href": "https://doi.org/10.1128/MCB.01101-09"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20100866"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20100866"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Valentina Fogal, Lianglin Zhang, Stan Krajewski, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Mitochondrial/cell-surface protein p32/gC1qR as a molecular target in tumor cells and tumor stroma."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cancer Res (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1158/0008-5472.CAN-07-6752"}], "href": "https://doi.org/10.1158/0008-5472.CAN-07-6752"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18757437"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18757437"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Ki-Bum Kim, Jae-Sung Yi, Nga Nguyen, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Cell-surface receptor for complement component C1q (gC1qR) is a key regulator for lamellipodia formation and cancer metastasis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M111.233304"}], "href": "https://doi.org/10.1074/jbc.M111.233304"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21536672"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21536672"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Xiaofang Zhang, Fei Zhang, Lin Guo, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Interactome analysis reveals that C1QBP (complement component 1, q subcomponent binding protein) is associated with cancer cell chemotaxis and metastasis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Proteomics (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/mcp.M113.029413"}], "href": "https://doi.org/10.1074/mcp.M113.029413"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23924515"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23924515"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Koji Itahana, Yanping Zhang "}, {"type": "b", "children": [{"type": "t", "text": "Mitochondrial p32 is a critical mediator of ARF-induced apoptosis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cancer Cell (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.ccr.2008.04.002"}], "href": "https://doi.org/10.1016/j.ccr.2008.04.002"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18538737"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18538737"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Yasmine Even, Sandrine Durieux, Marie-Line Escande, et al. "}, {"type": "b", "children": [{"type": "t", "text": "CDC2L5, a Cdk-like kinase with RS domain, interacts with the ASF/SF2-associated protein p32 and affects splicing in vivo."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Biochem (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/jcb.20986"}], "href": "https://doi.org/10.1002/jcb.20986"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16721827"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16721827"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Mansi Prakash, Smita Kale, Ilora Ghosh, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Hyaluronan-binding protein 1 (HABP1/p32/gC1qR) induces melanoma cell migration and tumor growth by NF-kappa B dependent MMP-2 activation through integrin α(v)β(3) interaction."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell Signal (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.cellsig.2011.04.009"}], "href": "https://doi.org/10.1016/j.cellsig.2011.04.009"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21627988"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21627988"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Stephen N Waggoner, Michael W Cruise, Rachel Kassel, et al. "}, {"type": "b", "children": [{"type": "t", "text": "gC1q receptor ligation selectively down-regulates human IL-12 production through activation of the phosphoinositide 3-kinase pathway."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Immunol (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.4049/jimmunol.175.7.4706"}], "href": "https://doi.org/10.4049/jimmunol.175.7.4706"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16177118"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16177118"}]}]}]}
Synonyms	GC1QBP, p32, SF2P32, GC1QR, GC1Q-R, COXPD33, HABP1, SF2AP32
Proteins	C1QBP_HUMAN
NCBI Gene ID	708
API
Download Associations
Predicted Functions
Co-expressed Genes
Expression in Tissues and Cell Lines

Functional Associations

C1QBP has 12,214 functional associations with biological entities spanning 8 categories (molecular profile, organism, chemical, disease, phenotype or trait, functional term, phrase or reference, structural feature, cell line, cell type or tissue, gene, protein or microRNA) extracted from 130 datasets.

Click the + buttons to view associations for C1QBP from the datasets below.

If available, associations are ranked by standardized value

Harmonizome 3.0

C1QBP Gene

Functional Associations

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

	Dataset	Summary
	Achilles Cell Line Gene Essentiality Profiles	cell lines with fitness changed by C1QBP gene knockdown relative to other cell lines from the Achilles Cell Line Gene Essentiality Profiles dataset.
	Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles	tissues with high or low expression of C1QBP gene relative to other tissues from the Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles dataset.
	Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles	tissues with high or low expression of C1QBP gene relative to other tissues from the Allen Brain Atlas Adult Mouse 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 C1QBP 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 Microarray	tissue samples with high or low expression of C1QBP 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 C1QBP 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 C1QBP 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 C1QBP 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 C1QBP 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 C1QBP gene relative to other cell types and tissues from the BioGPS Mouse Cell Type and Tissue Gene Expression Profiles dataset.
	Carcinogenome Chemical Perturbation Carcinogenicity Signatures	small molecule perturbations changing expression of C1QBP gene from the Carcinogenome Chemical Perturbation Carcinogenicity Signatures dataset.
	CCLE Cell Line Gene CNV Profiles	cell lines with high or low copy number of C1QBP gene relative to other cell lines from the CCLE Cell Line Gene CNV Profiles dataset.
	CCLE Cell Line Gene Expression Profiles	cell lines with high or low expression of C1QBP gene relative to other cell lines from the CCLE Cell Line Gene Expression Profiles dataset.
	CCLE Cell Line Proteomics	Cell lines associated with C1QBP protein from the CCLE Cell Line Proteomics dataset.
	CellMarker Gene-Cell Type Associations	cell types associated with C1QBP 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 C1QBP gene from the CHEA Transcription Factor Binding Site Profiles dataset.
	ChEA Transcription Factor Targets	transcription factors binding the promoter of C1QBP 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 C1QBP gene in low- or high-throughput transcription factor functional studies from the CHEA Transcription Factor Targets 2022 dataset.
	ClinVar Gene-Phenotype Associations 2025	phenotypes associated with C1QBP gene from the curated ClinVar Gene-Phenotype Associations 2025 dataset.
	CM4AI U2OS Cell Map Protein Localization Assemblies	assemblies containing C1QBP protein from integrated AP-MS and IF data from the CM4AI U2OS Cell Map Protein Localization Assemblies dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores	cellular components containing C1QBP protein from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores 2025	cellular components containing C1QBP protein from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.
	COMPARTMENTS Experimental Protein Localization Evidence Scores	cellular components containing C1QBP 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 C1QBP 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 C1QBP 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 C1QBP protein in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.
	CORUM Protein Complexes	protein complexs containing C1QBP protein from the CORUM Protein Complexes dataset.
	COSMIC Cell Line Gene Mutation Profiles	cell lines with C1QBP gene mutations from the COSMIC Cell Line Gene Mutation Profiles dataset.
	CTD Gene-Chemical Interactions	chemicals interacting with C1QBP gene/protein from the curated CTD Gene-Chemical Interactions dataset.
	CTD Gene-Disease Associations	diseases associated with C1QBP gene/protein from the curated CTD Gene-Disease Associations dataset.
	DeepCoverMOA Drug Mechanisms of Action	small molecule perturbations with high or low expression of C1QBP 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 C1QBP 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 C1QBP 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 C1QBP 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 C1QBP gene in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.
	DisGeNET Gene-Phenotype Associations	phenotypes associated with C1QBP gene in GWAS and other genetic association datasets from the DisGeNET Gene-Phenoptype Associations dataset.
	DrugBank Drug Targets	interacting drugs for C1QBP protein from the curated DrugBank Drug Targets dataset.
	ENCODE Histone Modification Site Profiles	histone modification site profiles with high histone modification abundance at C1QBP 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 C1QBP gene from the ENCODE Transcription Factor Binding Site Profiles dataset.
	ENCODE Transcription Factor Targets	transcription factors binding the promoter of C1QBP gene in ChIP-seq datasets from the ENCODE Transcription Factor Targets dataset.