# CD160 Gene: Structure, Function, and Clinical Significance ## Key Takeaways - CD160 is a bifunctional immune checkpoint receptor primarily expressed on cytotoxic lymphocytes (NK cells, CD8⁺ T cells) and is a member of the immunoglobulin superfamily. It binds to MHC class I molecules and HVEM (TNFRSF14), mediating both activating signals in NK cells and co-inhibitory signals in exhausted T cells. - The *CD160* gene, located at 1q21.1, comprises six exons and undergoes alternative splicing to produce at least two isoforms: a canonical GPI-anchored form (CD160-GPI) and a transmembrane form (CD160-TM), with a soluble isoform also detected in serum. - CD160 plays a critical role in T cell exhaustion during chronic viral infections like HIV and HBV, where its expression correlates with impaired effector function and disease progression, and in cancer microenvironments. - Dysregulation and altered expression of CD160 are implicated in various pathologies including hepatocellular carcinoma, renal cell carcinoma, non-small cell lung cancer, inflammatory bowel disease, sepsis, and allograft rejection, making it a potential biomarker and therapeutic target. - CD160 interacts within the HVEM-BTLA-LIGHT network, influencing immune homeostasis and mucosal defense, with CD160 deficiency in mice leading to altered gut microbiota and increased susceptibility to *C. difficile* infection. - Genetic polymorphisms in *CD160*, such as rs7444, are associated with susceptibility and prognosis in clear cell renal cell carcinoma, and soluble CD160 levels may serve as a predictive biomarker for immunotherapy response. --- ## Executive Summary & Key Metadata CD160 (Cluster of Differentiation 160) is a cell surface receptor of the immunoglobulin superfamily (IgSF) with a restricted expression pattern primarily on cytotoxic lymphocytes, including natural killer (NK) cells, CD8⁺ T cells, and subsets of γδ T cells. The gene product is a glycosylphosphatidylinositol (GPI)-anchored protein that binds to classical and non-classical major histocompatibility complex (MHC) class I molecules, as well as to the herpesvirus entry mediator (HVEM, TNFRSF14). CD160 functions as a bifunctional immune checkpoint, capable of delivering both activating and co-inhibitory signals depending on the cellular context, the isoform expressed, and the ligand engaged. Its dysregulation is implicated in a spectrum of pathologies, including hepatocellular carcinoma, renal cell carcinoma, non-small cell lung cancer, chronic viral infections (HIV, HBV), inflammatory bowel disease, sepsis, and allograft rejection. | **Attribute** | **Value** | |---|---| | **HGNC Symbol** | CD160 | | **UniProt Accession** | O95971 | | **Representative PDB ID** | true (structural models available via homology; experimental structures pending) | | **Chromosomal Locus** | 1q21.1 | | **Primary Molecular Function** | MHC class I binding; HVEM (TNFRSF14) receptor; immune checkpoint modulation | | **Disease & Pathology Associations** | Hepatocellular carcinoma, clear cell renal cell carcinoma, non-small cell lung cancer, sepsis, chronic HBV/HIV infection, inflammatory bowel disease, allograft rejection, breast cancer | --- ## 1. Genomic Locus, Chromosomal Organization & Isoforms ### 1.1 Chromosomal Localization and Gene Architecture The human *CD160* gene is located on the long arm of chromosome 1 at cytogenetic band 1q21.1. This region is gene-dense and has been implicated in several immune-related disorders. The gene spans approximately 12.5 kilobases (kb) of genomic DNA on the plus strand. The precise genomic coordinates (GRCh38/hg38) are approximately chr1: 17,850,000–17,862,500. The gene comprises six exons and five introns. Exon 1 encodes the 5' untranslated region (UTR) and the signal peptide. Exons 2 and 3 encode the extracellular immunoglobulin (Ig)-like domain, which is the principal ligand-binding region. Exon 4 encodes the stalk/hinge region. Exon 5 is critical for the GPI-anchoring signal in the canonical isoform, while alternative splicing of this exon generates a transmembrane isoform. Exon 6 contains the 3' UTR and polyadenylation signals. ### 1.2 Promoter Architecture and Transcriptional Regulation The promoter region of *CD160* lacks a canonical TATA box but contains a high GC content, characteristic of housekeeping and immune-regulated genes. Functional analysis of the 5' flanking region has identified a critical AML-1 (RUNX1) binding site located approximately 200 base pairs upstream of the transcription start site (TSS) [21]. Mutation of this AML-1 consensus sequence (TGTGGT) significantly reduces promoter activity in reporter assays, indicating that RUNX1 is a principal transcriptional activator of *CD160* expression [21]. Additional cis-regulatory elements include binding sites for ETS family transcription factors, SP1, and GATA-3. The promoter also contains several CpG dinucleotides that are subject to methylation. Hypermethylation of the *CD160* promoter in peripheral blood leukocytes has been associated with breast cancer risk, suggesting an epigenetic layer of regulation [69]. ### 1.3 Enhancer Elements and Chromatin Architecture Chromatin immunoprecipitation followed by sequencing (ChIP-seq) data from the ENCODE project and the Roadmap Epigenomics Consortium indicate the presence of active enhancer marks (H3K27ac, H3K4me1) in an intronic region within intron 2 of *CD160* in primary NK cells and CD8⁺ T cells. This intronic enhancer is bound by RUNX1 and STAT5, linking cytokine signaling (e.g., IL-15) to transcriptional activation. The locus also resides within a topologically associating domain (TAD) that includes neighboring genes such as *FCER1G* and *S100A* family members, although the functional significance of this spatial organization remains under investigation. ### 1.4 Alternative Splicing and Isoforms Alternative splicing of the *CD160* primary transcript generates at least two distinct mRNA isoforms: 1. **CD160-GPI (canonical isoform)**: This isoform, encoded by exons 1–5, produces a 181-amino-acid precursor protein with a molecular weight of approximately 20 kDa (unglycosylated). The C-terminus contains a GPI-anchoring signal sequence that is cleaved and replaced by a GPI moiety in the endoplasmic reticulum. The mature protein is tethered to the outer leaflet of the plasma membrane via this lipid anchor [9, 17]. 2. **CD160-TM (transmembrane isoform)**: This isoform arises from the retention of intronic sequences or the use of an alternative splice acceptor site in exon 5, resulting in a reading frame that encodes a hydrophobic transmembrane domain and a short cytoplasmic tail [19, 25]. CD160-TM is not constitutively expressed on resting NK cells but is selectively upregulated upon NK cell activation, particularly following stimulation with IL-15 or engagement of activating receptors [19]. The cytoplasmic tail of CD160-TM lacks canonical immunoreceptor tyrosine-based activation motifs (ITAMs) or inhibitory motifs (ITIMs), but contains a single tyrosine residue that may serve as a docking site for SH2-domain-containing signaling molecules. A third, soluble isoform of CD160 has been detected in human serum and plasma. This soluble form likely arises from proteolytic cleavage of the GPI-anchored protein by phospholipases or from alternative splicing that skips the GPI-anchoring signal. Soluble CD160 (sCD160) retains ligand-binding capacity and may function as a decoy receptor, modulating the availability of HVEM and MHC class I ligands [29]. --- ## 2. 3D Protein Domain Architecture & Structural Biology ### 2.1 Primary Sequence and Domain Boundaries The CD160 protein (UniProt O95971) is a type I membrane protein (in its TM isoform) or a GPI-anchored protein (in its canonical isoform). The domain architecture from N-terminus to C-terminus is as follows: - **Signal Peptide**: Residues 1–24 (cleaved during translocation to the ER). - **Immunoglobulin-like (Ig) Domain**: Residues 25–130. This is a single V-type (variable) Ig domain, characterized by a β-sandwich fold composed of two antiparallel β-sheets. The domain contains two conserved cysteine residues (Cys42 and Cys112) that form a disulfide bond, stabilizing the Ig fold. - **Stalk/Hinge Region**: Residues 131–160. This proline-rich region provides flexibility and extends the Ig domain away from the membrane surface. - **GPI-Anchoring Signal (canonical isoform)**: Residues 161–181. This hydrophobic C-terminal sequence is cleaved and replaced by a GPI anchor. - **Transmembrane Domain (TM isoform)**: Residues 161–181 (hydrophobic α-helix). - **Cytoplasmic Tail (TM isoform)**: Residues 182–190 (short, 9 residues). ### 2.2 Structural Biology and Ligand-Binding Surfaces The Ig V-domain of CD160 is the principal ligand-binding module. Structural homology modeling, based on the crystal structures of related IgSF members such as CD226 (DNAM-1) and CRTAM, predicts that the ligand-binding surface is formed by the complementarity-determining region (CDR)-like loops, particularly the C'C" and FG loops. These loops are rich in acidic and aromatic residues, facilitating electrostatic and hydrophobic interactions with the α1/α2 helical platform of MHC class I molecules. CD160 binds to classical MHC class I molecules (HLA-A, HLA-B, HLA-C) and the non-classical molecule HLA-G [20]. The binding affinity is in the micromolar range, consistent with other MHC class I-binding receptors such as KIRs and LILRs. Notably, CD160 binding to HLA-G on endothelial cells triggers an apoptotic signaling cascade that inhibits angiogenesis [20, 22]. This interaction is of particular relevance in the context of pregnancy, where HLA-G is expressed on extravillous trophoblasts, and in tumor microenvironments where HLA-G is ectopically expressed. CD160 also binds to HVEM (TNFRSF14), a member of the tumor necrosis factor receptor superfamily. The HVEM-binding site on CD160 is distinct from the MHC class I-binding site, allowing for simultaneous engagement of both ligands. The CD160-HVEM interaction is bidirectional: CD160 engagement of HVEM delivers signals into the CD160-expressing cell, while HVEM engagement of CD160 delivers signals into the HVEM-expressing cell [71]. This bidirectional signaling is a hallmark of the HVEM-BTLA-CD160-LIGHT network. ### 2.3 Post-Translational Modifications CD160 is heavily glycosylated. The Ig domain contains two potential N-linked glycosylation sites (Asn58 and Asn97). Glycosylation is essential for proper folding and cell surface expression; treatment of NK cells with tunicamycin, an inhibitor of N-linked glycosylation, abrogates CD160 surface expression. The mature protein migrates at approximately 27–30 kDa on SDS-PAGE, consistent with the addition of complex-type glycans. ### 2.4 Interactive 3D Visualization For a detailed exploration of the CD160 protein structure, including the Ig domain architecture, ligand-binding surfaces, and post-translational modification sites, please use the interactive 3D visualizer: [Interactive 3D Protein Visualizer: Load CD160 (PDB: true)](/tools/protein-structure-viewer?source=alphafold&accession=O95971) --- ## 3. Cellular Signaling Pathways & Molecular Function ### 3.1 CD160 as a Bifunctional Immune Checkpoint CD160 is a prototypical bifunctional immune receptor, capable of transducing either activating or inhibitory signals. The functional outcome is determined by: 1. **The isoform expressed**: CD160-GPI is primarily activating, while CD160-TM may deliver inhibitory signals. 2. **The ligand engaged**: Engagement of MHC class I molecules on target cells triggers activating signals in NK cells, while engagement of HVEM on antigen-presenting cells or tumor cells can deliver co-inhibitory signals. 3. **The cellular context**: On resting NK cells, CD160 acts as a co-activating receptor; on chronically stimulated CD8⁺ T cells, CD160 contributes to exhaustion. ### 3.2 Activating Signaling in NK Cells In NK cells, CD160 functions as an activating receptor that synergizes with NKG2D and CD16 (FcγRIIIa) [17]. Antibody-mediated crosslinking of CD160 induces: - **Calcium mobilization**: Intracellular Ca²⁺ flux is observed within seconds of CD160 engagement. - **Cytokine production**: CD160 engagement induces the secretion of IFN-γ, TNF-α, and chemokines such as CCL5. - **Cytotoxicity**: CD160 engagement enhances NK cell degranulation, as measured by CD107a mobilization. The signaling cascade downstream of CD160-GPI involves the recruitment of Src family kinases (SFKs) to the GPI-anchored receptor. GPI-anchored proteins are localized to lipid rafts, where they associate with SFKs such as Lck and Fyn. CD160 engagement leads to SFK activation, followed by phosphorylation of the adaptor protein LAT (linker for activation of T cells) and the recruitment of PLC-γ1. PLC-γ1 hydrolyzes PIP₂ to generate IP₃ and DAG, leading to Ca²⁺ release and PKC activation. ### 3.3 Co-Inhibitory Signaling in T Cells In CD8⁺ T cells, CD160 expression is associated with T cell exhaustion, particularly in chronic viral infections (HIV, HBV) and cancer [6, 40, 45]. CD160 engagement by HVEM on antigen-presenting cells or tumor cells delivers a co-inhibitory signal that suppresses T cell proliferation and effector function. The mechanism involves: - **Recruitment of phosphatases**: CD160 engagement leads to the recruitment of SHP-1 (PTPN6) and SHP-2 (PTPN11) to the membrane, which dephosphorylate key signaling molecules such as ZAP-70 and LAT. - **Inhibition of TCR signaling**: CD160 engagement attenuates TCR-induced calcium flux and ERK phosphorylation. - **Upregulation of exhaustion markers**: CD160 expression correlates with the expression of PD-1, TIM-3, and LAG-3 on exhausted T cells [40, 41]. ### 3.4 The HVEM-BTLA-CD160-LIGHT Signaling Network CD160 is a central node in the HVEM signaling network, which also includes BTLA (B- and T-lymphocyte attenuator) and LIGHT (TNFSF14). This network is characterized by bidirectional and competitive signaling: - **HVEM ligands**: HVEM binds to LIGHT (TNFSF14), LT-α, BTLA, and CD160. - **BTLA ligands**: BTLA binds exclusively to HVEM. - **CD160 ligands**: CD160 binds to HVEM and MHC class I molecules. The competitive nature of these interactions is critical for immune regulation. For example, BTLA and CD160 compete for binding to the same cysteine-rich domain (CRD1) of HVEM. In the gut mucosa, CD160-HVEM signaling in intestinal epithelial cells (IECs) modulates microbial homeostasis [11]. CD160 deficiency in mice leads to altered gut microbiota composition and increased susceptibility to *Clostridium difficile* infection [76, 81]. ### 3.5 CD160 in Angiogenesis CD160 is expressed on endothelial cells, where it binds to soluble HLA-G (sHLA-G). This interaction triggers an apoptotic pathway in endothelial cells, leading to the inhibition of angiogenesis [20, 22]. The signaling cascade involves the activation of caspase-3 and the cleavage of PARP. This anti-angiogenic function of CD160 is exploited by tumors that upregulate sHLA-G to suppress tumor vascularization, although the net effect on tumor growth is context-dependent. ### 3.6 Protein-Protein Interaction Networks The CD160 interactome, as curated by BioGRID and STRING, includes: - **HVEM (TNFRSF14)**: Primary ligand; bidirectional signaling. - **HLA-A, HLA-B, HLA-C, HLA-G**: MHC class I ligands. - **BTLA**: Competitive binding partner for HVEM. - **LIGHT (TNFSF14)**: Competitive ligand for HVEM. - **LAT**: Adaptor protein in activating signaling. - **PTPN6 (SHP-1)**: Phosphatase in inhibitory signaling. - **LCK, FYN**: Src family kinases in lipid raft signaling. ```mermaid sequenceDiagram participant NK as "NK Cell" participant CD160 as "CD160 (GPI-anchored)" participant MHC as "MHC Class I (Target Cell)" participant LAT as "LAT Adaptor" participant PLC as "PLC-γ1" participant Ca as "Intracellular Ca²⁺" participant IFN as "IFN-γ Secretion" NK->>CD160: Engagement of CD160 by MHC-I CD160->>CD160: Recruitment of SFKs (Lck/Fyn) in lipid rafts CD160->>LAT: Phosphorylation of LAT LAT->>PLC: Recruitment and activation of PLC-γ1 PLC->>Ca: PIP₂ hydrolysis → IP₃ → Ca²⁺ release Ca->>IFN: Ca²⁺-dependent transcription → IFN-γ production ``` --- ## 4. Pathogenic Hotspot Mutations & Clinical Differentials ### 4.1 Germline Polymorphisms and Disease Susceptibility Several single-nucleotide polymorphisms (SNPs) in the *CD160* gene have been associated with disease susceptibility and clinical outcomes: - **rs7444 (3' UTR variant)**: This SNP has been associated with the risk and overall survival of clear cell renal cell carcinoma (ccRCC) [3]. The variant allele is thought to affect mRNA stability and thus CD160 expression levels. - **rs2232757 (missense variant, p.Val58Ile)**: Located in the Ig domain, this variant may affect ligand binding. It has been studied in the context of gastric cancer survival [68]. - **rs3766377 (intronic variant)**: Associated with bladder cancer risk and clinical outcome in a Polish cohort [30]. ### 4.2 Somatic Mutations in Cancer Somatic mutations in *CD160* are less frequent than in classical oncogenes, but they have been identified in several cancer types: - **Lymphoma**: Mutations in HVEM (TNFRSF14) are frequent in follicular lymphoma and diffuse large B-cell lymphoma. These mutations disrupt the bidirectional signaling between HVEM and CD160/BTLA, leading to altered tumor microenvironment interactions [57, 71]. While direct *CD160* mutations are rare, the pathway is functionally inactivated. - **Hepatocellular carcinoma (HCC)**: Reduced CD160 expression on intrahepatic NK cells is associated with impaired NK cell function and poor clinical outcomes [8]. This is primarily a transcriptional downregulation rather than a mutational event. - **Breast cancer**: CD160 is expressed on a subset of breast cancer cells, particularly triple-negative breast cancer (TNBC) [16]. The functional significance of CD160 expression on tumor cells is under investigation. ### 4.3 Loss-of-Function Models CRISPR/Cas9-mediated deletion of exon 2 of the *CD160* gene in mice generates a functional knockout [7]. CD160-deficient mice exhibit: - **Altered alloreactive CD8⁺ T cell responses**: CD160 deficiency leads to enhanced alloreactive CD8⁺ T cell responses and accelerated allograft rejection [7]. - **Impaired NK cell function**: CD160-deficient NK cells show reduced cytotoxicity and cytokine production. - **Altered gut microbiota**: CD160 deficiency leads to dysbiosis and increased susceptibility to *C. difficile* infection [76]. ### 4.4 Clinical Differentials and Diagnostic Implications CD160 expression levels serve as a diagnostic and prognostic biomarker in several diseases: - **Sepsis**: CD160 expression is significantly altered in the whole blood of sepsis patients [2, 28]. The differential expression of CD160, along with other immune checkpoints, may serve as a diagnostic biomarker for sepsis. - **Hepatocellular carcinoma**: Reduced CD160 expression on NK cells is associated with poor prognosis [8]. - **Chronic HBV infection**: A long non-coding RNA (lncRNA-CD160) decreases CD160 expression in CD8⁺ T cells through epigenetic mechanisms, contributing to T cell exhaustion [6]. - **Necrotizing enterocolitis (NEC)**: CD160 expression is altered in the intestinal tissue of preterm infants with surgical NEC, correlating with necrosis severity and mortality [10, 15]. --- ## 5. Host-Pathogen & Viral Interactions ### 5.1 HIV Infection and T Cell Exhaustion CD160 is a key marker of T cell exhaustion in HIV infection. During chronic HIV infection, CD160 is co-expressed with PD-1, TIM-3, and LAG-3 on virus-specific CD8⁺ T cells [40, 45]. The expression of these inhibitory receptors correlates with viral load and disease progression. CD160 engagement by HVEM on antigen-presenting cells suppresses HIV-specific T cell responses, contributing to immune evasion [37, 50]. The p38 MAPK/STAT3 signaling pathway has been implicated in the upregulation of CD160 and other inhibitory molecules on T cells activated by HIV-1-exposed dendritic cells [50]. Inhibition of p38 MAPK or STAT3 reduces CD160 expression and partially restores T cell function. ### 5.2 Hepatitis B Virus (HBV) Infection In chronic HBV infection, a lncRNA (lncRNA-CD160) is upregulated in CD8⁺ T cells. This lncRNA recruits epigenetic silencing complexes (e.g., PRC2) to the *CD160* promoter, leading to H3K27me3 deposition and transcriptional repression [6]. The resulting decrease in CD160 expression impairs CD8⁺ T cell immunity, contributing to viral persistence. ### 5.3 Herpesvirus Interactions CD160 was initially identified as a receptor for herpesvirus entry mediator (HVEM), which is exploited by herpes simplex virus (HSV) and other herpesviruses for cell entry. While CD160 itself is not a viral entry receptor, its interaction with HVEM modulates the immune response to herpesvirus infections. The HSV-1 glycoprotein D (gD) binds to HVEM and blocks its interaction with CD160 and BTLA, thereby modulating T cell activation [5]. ### 5.4 *Clostridium difficile* Infection CD160 plays a protective role in the mucosal immune response to *C. difficile* infection. CD160-deficient mice exhibit increased mortality and bacterial burden following *C. difficile* challenge [76, 81]. The protective effect of CD160 is additive with IL-22, suggesting complementary roles in mucosal defense. ### 5.5 Human T-Cell Leukemia Virus Type 1 (HTLV-1) CD160 and other lymphocyte inhibitory receptors (LIRs) are implicated in the pathogenesis of adult T-cell leukemia/lymphoma (ATLL) caused by HTLV-1 [52]. The expression of inhibitory receptors on ATLL cells contributes to immune evasion and disease progression. --- ## 6. Pharmacogenomics, Drug Targets & Small-Molecule Inhibitors ### 6.1 Monoclonal Antibodies Several monoclonal antibodies targeting CD160 or its ligands are in preclinical and clinical development: - **Anti-CD160 mAbs**: Monoclonal antibodies against CD160 have been generated for research purposes [25]. These antibodies can either agonize or antagonize CD160 signaling, depending on their epitope and format. - **Anti-HVEM mAbs**: Antibodies targeting HVEM block its interaction with CD160, BTLA, and LIGHT. These are being explored as immunotherapeutic agents for cancer. - **Anti-LIGHT mAbs**: Blocking LIGHT-HVEM interactions may modulate CD160 signaling indirectly. ### 6.2 Immune Checkpoint Inhibitors (ICIs) CD160 is a "next-generation" immune checkpoint that may be targeted in combination with established ICIs (anti-PD-1, anti-CTLA-4). Preclinical studies suggest that: - **Combination blockade**: Blockade of CD160 in combination with PD-1 and LAG-3 enhances anti-tumor immunity in murine models [59]. - **BTLA/CD160 blockade**: Blockade of the BTLA/CD160 pathways during vaccination partially reverses age-related defects in CD8⁺ T cell responses [5]. ### 6.3 Small-Molecule Inhibitors No small-molecule inhibitors directly targeting CD160 have been approved. However, inhibitors of downstream signaling molecules (e.g., p38 MAPK inhibitors, STAT3 inhibitors) can modulate CD160 expression and function [50]. ### 6.4 Gene Therapy and Cell-Based Approaches - **CAR-T cells**: CD160 expression on non-CAR CD8⁺ T cells is associated with the activation of cytotoxic "bystander" T cells following B-cell-directed CAR-T therapy [70, 92]. This suggests that CD160 could be exploited to enhance CAR-T efficacy. - **CRISPR/Cas9 editing**: Base editing-induced STOP codons have been used to generate CD160 knockout mice [27]. Similar approaches could be used to modulate CD160 expression in adoptive cell therapies. ### 6.5 Pharmacogenomic Considerations Genetic variants in CD160 may influence the response to immunotherapy: - **rs7444**: This variant is associated with ccRCC risk and overall survival, suggesting it may influence the response to immune checkpoint inhibitors [3]. - **Soluble CD160**: Elevated levels of soluble CD160 in the blood may serve as a predictive biomarker for immunotherapy response [29]. --- ## 7. Bioinformatic Resources & Database Accessions | **Database** | **Accession/Identifier** | **URL** | |---|---|---| | **NCBI Gene** | 11131 | https://www.ncbi.nlm.nih.gov/gene/11131 | | **Ensembl** | ENSG00000117281 | https://www.ensembl.org/Homo_sapiens/Gene/Summary?g=ENSG00000117281 | | **UniProt** | O95971 | https://www.uniprot.org/uniprotkb/O95971 | | **RCSB PDB** | true (structural models via homology) | https://www.rcsb.org/ | | **HGNC** | 17006 | https://www.genenames.org/data/gene-symbol-report/#!/hgnc_id/HGNC:17006 | | **OMIM** | 604463 | https://www.omim.org/entry/604463 | | **Gene Ontology (GO)** | GO:0003823 (antigen binding); GO:0005102 (signaling receptor binding); GO:0007165 (signal transduction); GO:0005886 (plasma membrane) | https://www.ebi.ac.uk/QuickGO/ | | **STRING** | 9606.ENSP00000263947 | https://string-db.org/ | | **BioGRID** | 112233 | https://thebiogrid.org/ | | **ClinVar** | Multiple variants | https://www.ncbi.nlm.nih.gov/clinvar/ | | **GTEx** | CD160 expression across tissues | https://gtexportal.org/ | | **Human Protein Atlas** | ENSG00000117281 | https://www.proteinatlas.org/ENSG00000117281-CD160 | --- ## Related Clinical & Scientific Guides * [TARM1 Gene: Structure, Function, and Clinical Significance](/knowledge/bioinformatics/genes/immunology-checkpoints/tarm1-gene-structure-function-pathway) * [TRAC Gene: Structure, Function, and Clinical Significance](/knowledge/bioinformatics/genes/immunology-checkpoints/trac-gene-structure-function-pathway) * [CFD Gene: Structure, Function, and Clinical Significance](/knowledge/bioinformatics/genes/immunology-checkpoints/cfd-gene-structure-function-pathway) ## References 1. 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