HNRNPDL Gene

HGNC Family	RNA binding motif containing (RBM)
Name	heterogeneous nuclear ribonucleoprotein D-like
Description	This gene belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA binding proteins and they complex with heterogeneous nuclear RNA (hnRNA). 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 seem to shuttle between the nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic acid binding properties. The protein encoded by this gene has two RRM domains that bind to RNAs. Three alternatively spliced transcript variants have been described for this gene. One of the variants is probably not translated because the transcript is a candidate for nonsense-mediated mRNA decay. The protein isoforms encoded by this gene are similar to its family member HNRPD. [provided by RefSeq, May 2011]
Summary	{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\n Although none of the studies above directly examine HNRNPDL, a synthesis of these findings on related heterogeneous nuclear ribonucleoproteins (hnRNPs) helps define a likely functional profile for this protein. In general, hnRNP family members—including those examined in these reports—act as multifunctional regulators of RNA metabolism. They coordinate alternative pre‐mRNA splicing, modulate mRNA stability and transport, and participate in the dynamic assembly of ribonucleoprotein granules that mediate cellular responses to diverse stimuli such as stress, developmental cues, and metabolic changes."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "4"}]}, {"type": "t", "text": " \n In several studies, related hnRNP proteins either directly repressed or promoted inclusion of alternative exons – a regulation that is critical for cell‐specific gene expression, metabolic reprogramming in cancer, and even neural function."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "5", "end_ref": "8"}]}, {"type": "t", "text": " \n Furthermore, several hnRNP proteins powerfully influence the assembly, composition, and dynamics of cytoplasmic stress granules or liquid–liquid phase‐separated compartments – processes now increasingly linked to neurodegeneration and other pathological states."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "9", "end_ref": "12"}]}, {"type": "t", "text": " \n Given its domain architecture and evolutionary relationship with other hnRNPs discussed in these reports, HNRNPDL is expected to act in a similar multifaceted capacity. In particular, HNRNPDL likely binds to specific RNA sequence or structural motifs to influence the processing and decay of target transcripts, contributes to the proper spatial distribution of mRNAs (for example, by facilitating their transport to specialized cytoplasmic compartments), and helps maintain transcriptome integrity during environmental or cell cycle–linked transitions. Misregulation of such processes, as observed for related family members, is tightly linked to neurodegenerative disorders and tumorigenesis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "13", "end_ref": "16"}]}, {"type": "t", "text": "\n "}]}, {"type": "t", "text": "\n "}, {"type": "p", "children": [{"type": "t", "text": "\n In summary, while direct studies on HNRNPDL remain limited, the collective evidence gained from analyses of related hnRNPs supports a model in which HNRNPDL functions as a key regulator of RNA processing. It is likely to fine‐tune alternative splicing choices, govern mRNA stability and transport, and perhaps participate in stress responses and liquid–liquid phase separation—all processes that, when disrupted, contribute to disease.\n "}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Weibo Luo, Hongxia Hu, Ryan Chang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Pyruvate kinase M2 is a PHD3-stimulated coactivator for hypoxia-inducible factor 1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.cell.2011.03.054"}], "href": "https://doi.org/10.1016/j.cell.2011.03.054"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21620138"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21620138"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Charles J David, Mo Chen, Marcela Assanah, et al. "}, {"type": "b", "children": [{"type": "t", "text": "HnRNP proteins controlled by c-Myc deregulate pyruvate kinase mRNA splicing in cancer."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nature (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/nature08697"}], "href": "https://doi.org/10.1038/nature08697"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20010808"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20010808"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Wilfried Rossoll, Sibylle Jablonka, Catia Andreassi, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Smn, the spinal muscular atrophy-determining gene product, modulates axon growth and localization of beta-actin mRNA in growth cones of motoneurons."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Biol (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1083/jcb.200304128"}], "href": "https://doi.org/10.1083/jcb.200304128"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "14623865"}], "href": "https://pubmed.ncbi.nlm.nih.gov/14623865"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Tsuyoshi Kashima, James L Manley "}, {"type": "b", "children": [{"type": "t", "text": "A negative element in SMN2 exon 7 inhibits splicing in spinal muscular atrophy."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Genet (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/ng1207"}], "href": "https://doi.org/10.1038/ng1207"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12833158"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12833158"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Daekyu Sun, Kexiao Guo, Jadrian J Rusche, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Facilitation of a structural transition in the polypurine/polypyrimidine tract within the proximal promoter region of the human VEGF gene by the presence of potassium and G-quadruplex-interactive agents."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nucleic Acids Res (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/nar/gki917"}], "href": "https://doi.org/10.1093/nar/gki917"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16239639"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16239639"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Mo Chen, Jian Zhang, James L Manley "}, {"type": "b", "children": [{"type": "t", "text": "Turning on a fuel switch of cancer: hnRNP proteins regulate alternative splicing of pyruvate kinase mRNA."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cancer Res (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1158/0008-5472.CAN-10-2513"}], "href": "https://doi.org/10.1158/0008-5472.CAN-10-2513"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20978194"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20978194"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "María S Domínguez-Sánchez, Sonia Barroso, Belén Gómez-González, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Genome instability and transcription elongation impairment in human cells depleted of THO/TREX."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "PLoS Genet (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1371/journal.pgen.1002386"}], "href": "https://doi.org/10.1371/journal.pgen.1002386"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22144908"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22144908"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Daniel Garneau, Timothée Revil, Jean-François Fisette, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Heterogeneous nuclear ribonucleoprotein F/H proteins modulate the alternative splicing of the apoptotic mediator Bcl-x."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M501070200"}], "href": "https://doi.org/10.1074/jbc.M501070200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15837790"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15837790"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Masato Hasegawa, Tetsuaki Arai, Takashi Nonaka, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Ann Neurol (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/ana.21425"}], "href": "https://doi.org/10.1002/ana.21425"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18546284"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18546284"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Nael H Alami, Rebecca B Smith, Monica A Carrasco, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Axonal transport of TDP-43 mRNA granules is impaired by ALS-causing mutations."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Neuron (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.neuron.2013.12.018"}], "href": "https://doi.org/10.1016/j.neuron.2013.12.018"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24507191"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24507191"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Karli K McDonald, Anaïs Aulas, Laurie Destroismaisons, et al. "}, {"type": "b", "children": [{"type": "t", "text": "TAR DNA-binding protein 43 (TDP-43) regulates stress granule dynamics via differential regulation of G3BP and TIA-1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Hum Mol Genet (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/hmg/ddr021"}], "href": "https://doi.org/10.1093/hmg/ddr021"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21257637"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21257637"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Alexander E Conicella, Gregory L Dignon, Gül H Zerze, et al. "}, {"type": "b", "children": [{"type": "t", "text": "TDP-43 α-helical structure tunes liquid-liquid phase separation and function."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.1912055117"}], "href": "https://doi.org/10.1073/pnas.1912055117"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "32132204"}], "href": "https://pubmed.ncbi.nlm.nih.gov/32132204"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Maria Paola Paronetto, Tilman Achsel, Autumn Massiello, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The RNA-binding protein Sam68 modulates the alternative splicing of Bcl-x."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Biol (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1083/jcb.200701005"}], "href": "https://doi.org/10.1083/jcb.200701005"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17371836"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17371836"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Dan Jin, Jiwei Guo, Yan Wu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "m"}, {"type": "a", "children": [{"type": "t", "text": "sup"}], "href": "sup"}, {"type": "t", "text": "6"}, {"type": "a", "children": [{"type": "t", "text": "/sup"}], "href": "/sup"}, {"type": "t", "text": "A demethylase ALKBH5 inhibits tumor growth and metastasis by reducing YTHDFs-mediated YAP expression and inhibiting miR-107/LATS2-mediated YAP activity in NSCLC."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cancer (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1186/s12943-020-01161-1"}], "href": "https://doi.org/10.1186/s12943-020-01161-1"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "32106857"}], "href": "https://pubmed.ncbi.nlm.nih.gov/32106857"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Melissa L Wilbert, Stephanie C Huelga, Katannya Kapeli, et al. "}, {"type": "b", "children": [{"type": "t", "text": "LIN28 binds messenger RNAs at GGAGA motifs and regulates splicing factor abundance."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.molcel.2012.08.004"}], "href": "https://doi.org/10.1016/j.molcel.2012.08.004"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22959275"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22959275"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Gracjan Michlewski, Javier F Cáceres "}, {"type": "b", "children": [{"type": "t", "text": "Antagonistic role of hnRNP A1 and KSRP in the regulation of let-7a biogenesis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Struct Mol Biol (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/nsmb.1874"}], "href": "https://doi.org/10.1038/nsmb.1874"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20639884"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20639884"}]}]}]}
Synonyms	HNRPDL, LGMDD3, JKTBP, JKTBP2, LAAUF1, LGMD1G
Proteins	HNRDL_HUMAN
NCBI Gene ID	9987
API
Download Associations
Predicted Functions
Co-expressed Genes
Expression in Tissues and Cell Lines

Functional Associations

HNRNPDL has 12,581 functional associations with biological entities spanning 7 categories (molecular profile, chemical, disease, phenotype or trait, functional term, phrase or reference, structural feature, cell line, cell type or tissue, gene, protein or microRNA) extracted from 114 datasets.

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

If available, associations are ranked by standardized value

Harmonizome 3.0

HNRNPDL 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 HNRNPDL 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 HNRNPDL 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 HNRNPDL 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 HNRNPDL 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 HNRNPDL 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 HNRNPDL 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 HNRNPDL 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 HNRNPDL 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 HNRNPDL 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 HNRNPDL gene from the Carcinogenome Chemical Perturbation Carcinogenicity Signatures dataset.
	CCLE Cell Line Gene CNV Profiles	cell lines with high or low copy number of HNRNPDL 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 HNRNPDL gene relative to other cell lines from the CCLE Cell Line Gene Expression Profiles dataset.
	CCLE Cell Line Proteomics	Cell lines associated with HNRNPDL protein from the CCLE Cell Line Proteomics dataset.
	ChEA Transcription Factor Binding Site Profiles	transcription factor binding site profiles with transcription factor binding evidence at the promoter of HNRNPDL gene from the CHEA Transcription Factor Binding Site Profiles dataset.
	ChEA Transcription Factor Targets	transcription factors binding the promoter of HNRNPDL 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 HNRNPDL 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 HNRNPDL gene from the curated ClinVar Gene-Phenotype Associations 2025 dataset.
	CM4AI U2OS Cell Map Protein Localization Assemblies	assemblies containing HNRNPDL protein from integrated AP-MS and IF data from the CM4AI U2OS Cell Map Protein Localization Assemblies dataset.
	CMAP Signatures of Differentially Expressed Genes for Small Molecules	small molecule perturbations changing expression of HNRNPDL gene from the CMAP Signatures of Differentially Expressed Genes for Small Molecules dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores	cellular components containing HNRNPDL protein from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores 2025	cellular components containing HNRNPDL protein from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.
	COMPARTMENTS Experimental Protein Localization Evidence Scores 2025	cellular components containing HNRNPDL 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 HNRNPDL 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 HNRNPDL protein in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.
	CORUM Protein Complexes	protein complexs containing HNRNPDL protein from the CORUM Protein Complexes dataset.
	COSMIC Cell Line Gene Mutation Profiles	cell lines with HNRNPDL gene mutations from the COSMIC Cell Line Gene Mutation Profiles dataset.
	CTD Gene-Chemical Interactions	chemicals interacting with HNRNPDL gene/protein from the curated CTD Gene-Chemical Interactions dataset.
	CTD Gene-Disease Associations	diseases associated with HNRNPDL gene/protein from the curated CTD Gene-Disease Associations dataset.
	DepMap CRISPR Gene Dependency	cell lines with fitness changed by HNRNPDL gene knockdown relative to other cell lines from the DepMap CRISPR Gene Dependency dataset.
	DISEASES Curated Gene-Disease Association Evidence Scores 2025	diseases involving HNRNPDL gene from the DISEASES Curated Gene-Disease Association Evidence Scores 2025 dataset.
	DISEASES Text-mining Gene-Disease Association Evidence Scores	diseases co-occuring with HNRNPDL 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 HNRNPDL 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 HNRNPDL gene in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.
	DisGeNET Gene-Phenotype Associations	phenotypes associated with HNRNPDL 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 HNRNPDL 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 HNRNPDL gene from the ENCODE Transcription Factor Binding Site Profiles dataset.
	ENCODE Transcription Factor Targets	transcription factors binding the promoter of HNRNPDL 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 HNRNPDL from the ESCAPE Omics Signatures of Genes and Proteins for Stem Cells dataset.
	GAD Gene-Disease Associations	diseases associated with HNRNPDL gene in GWAS and other genetic association datasets from the GAD Gene-Disease Associations dataset.
	GAD High Level Gene-Disease Associations	diseases associated with HNRNPDL gene in GWAS and other genetic association datasets from the GAD High Level Gene-Disease Associations dataset.