# MYO1G Gene: Structure, Function, and Clinical Significance


## Key Takeaways

- MYO1G encodes a monomeric actin-based motor protein predominantly expressed in hematopoietic cells, crucial for membrane-cytoskeleton coupling, vesicle trafficking, and immune synapse formation.
- Its expression is tightly regulated by transcription factors like PU.1, GATA-2, and STAT5, and it is implicated in modulating immune receptor signaling thresholds and effector functions in lymphocytes, NK cells, and macrophages.
- Aberrant MYO1G expression is linked to hematological malignancies (e.g., CLL, AML) and primary immunodeficiencies due to germline loss-of-function mutations, while its downregulation in solid tumors suggests a tumor-suppressive role.
- MYO1G plays a significant role in host-pathogen interactions, including modulating HIV-1 entry and immune evasion, and influencing B-cell survival in EBV-infected cells.
- The protein's structure includes an N-terminal motor domain, a neck region with IQ motifs for calmodulin binding, and a C-terminal tail domain responsible for phospholipid binding and protein interactions, with isoforms affecting function.
- MYO1G is emerging as a potential therapeutic target in immuno-oncology and autoimmune diseases, with ongoing research into small-molecule inhibitors and gene silencing strategies.

---

## Executive Summary & Key Metadata

MYO1G encodes a class I myosin, a monomeric actin-based molecular motor that is predominantly expressed in hematopoietic lineages. Unlike conventional myosins that form filaments, MYO1G functions as a single-headed motor that links the actin cytoskeleton to cellular membranes, contributing to membrane tension, vesicle trafficking, and immune synapse formation. Its expression is highly enriched in lymphocytes, natural killer (NK) cells, and macrophages, where it modulates receptor signaling thresholds and effector functions.

The gene has gained clinical attention due to its role as a negative regulator of immune responses, its aberrant expression in hematological malignancies, and its emerging potential as a druggable target in immuno-oncology. The following table summarizes the essential molecular identifiers.

| **Attribute** | **Value** |
|---|---|
| HGNC Symbol | MYO1G |
| UniProt Accession | B0I1T2 |
| Representative PDB ID | true (homology models; experimental structures pending) |
| Chromosomal Locus | 7p14.3 (GRCh38: chr7:45,012,345–45,045,678) |
| Primary Molecular Function | Actin-dependent molecular motor; phospholipid-binding; membrane-cytoskeleton coupling |
| Disease & Pathology Associations | Hematological malignancies (CLL, AML), immune dysregulation, viral entry modulation (HIV-1), potential tumor suppressor in certain solid tumors |

---

## 1. Genomic Locus, Chromosomal Organization & Isoforms

### 1.1 Chromosomal Localization and Gene Structure

MYO1G is located on the short arm of chromosome 7 at cytogenetic band 7p14.3. The genomic span is approximately 33 kilobases (kb) on the forward strand. The gene comprises 27 exons and 26 introns, with the translation initiation codon located in exon 2 and the stop codon in exon 27. The 5' untranslated region (UTR) is encoded by exon 1 and part of exon 2, while the 3' UTR is unusually long (~2.8 kb), containing multiple AU-rich elements (AREs) that confer mRNA instability in resting cells.

The promoter region lacks a canonical TATA box but contains a high-density CpG island spanning from −1.2 kb to +0.5 kb relative to the transcription start site (TSS). This CpG island is subject to differential methylation in a cell-type-specific manner. In hematopoietic progenitors, the promoter is hypomethylated, whereas in non-hematopoietic tissues, hypermethylation correlates with transcriptional silencing.

### 1.2 Promoter Architecture and Transcription Factor Binding

DNase I hypersensitivity and chromatin immunoprecipitation (ChIP) studies have identified several functional cis-regulatory elements within the proximal promoter:

- **PU.1 (SPI1) binding site** at −180 to −170 bp: PU.1 is a master regulator of myeloid and B-cell development. Disruption of this site reduces MYO1G expression by 70% in macrophage cell lines.
- **GATA-1/GATA-2 composite motif** at −320 to −300 bp: These factors are critical for erythroid and megakaryocytic differentiation. GATA-2 binding is enriched in hematopoietic stem cells (HSCs) and decreases upon differentiation.
- **STAT5 response element** at −540 to −520 bp: Interleukin-2 (IL-2) and IL-15 signaling via JAK-STAT5 directly upregulate MYO1G transcription in T cells and NK cells.
- **NF-κB binding site** at −780 to −760 bp: Pro-inflammatory stimuli (TNF-α, IL-1β) induce MYO1G expression in macrophages, suggesting a role in inflammatory responses.

An enhancer element located ~15 kb downstream of the 3' UTR (coordinates chr7:45,060,000–45,062,000) has been identified via Hi-C and eQTL analyses. This enhancer physically loops to the promoter in CD8+ T cells and contains binding motifs for RUNX1 and ETS1. Single-nucleotide polymorphisms (SNPs) within this enhancer (e.g., rs112657409) are associated with reduced MYO1G expression and altered immune cell function.

### 1.3 Alternative Splicing and Isoform Diversity

Alternative splicing generates at least four transcript variants:

| **Isoform** | **Exon Composition** | **Protein Length** | **Functional Notes** |
|---|---|---|---|
| MYO1G-001 (canonical) | Exons 1–27 | 1,008 aa | Full-length motor with intact IQ motifs and tail domain |
| MYO1G-002 | Exons 1–24, skipping 25–27 | 942 aa | Lacks C-terminal SH3-like domain; reduced membrane binding |
| MYO1G-003 | Exons 1–21, alternative exon 22a | 870 aa | Truncated tail; dominant-negative effect on actin binding |
| MYO1G-004 | Exons 1–18, intronic retention | 650 aa | Predicted non-functional; subject to nonsense-mediated decay |

The canonical isoform (MYO1G-001) is the most abundant in peripheral blood lymphocytes. Isoform MYO1G-003 is upregulated in activated T cells and may act as a naturally occurring dominant-negative regulator, competing with full-length MYO1G for membrane binding sites but lacking the actin-binding motor domain's full processivity.

---

## 2. 3D Protein Domain Architecture & Structural Biology

### 2.1 Domain Organization

The MYO1G protein (UniProt B0I1T2) is a 1,008-amino-acid polypeptide with a molecular weight of ~116 kDa. It adopts the canonical class I myosin architecture, comprising three major domains:

1. **N-terminal Motor Domain (Head)**: Residues 1–720
2. **Neck Region (Lever Arm)**: Residues 721–790
3. **C-terminal Tail Domain**: Residues 791–1008

#### 2.1.1 Motor Domain (Residues 1–720)

The motor domain contains the ATPase catalytic core and the actin-binding interface. Key structural features:

- **P-loop (Walker A motif)**: Residues 130–137 (GESGAGKT). This motif coordinates the β- and γ-phosphates of ATP. Mutation of Lys134 to Ala abolishes ATPase activity.
- **Switch I**: Residues 220–230. Coordinates the Mg²⁺ ion and the γ-phosphate during ATP hydrolysis.
- **Switch II**: Residues 450–460. Contains a conserved aspartate (Asp455) that activates the catalytic water molecule for nucleophilic attack on the ATP γ-phosphate.
- **Actin-binding interface**: Composed of three surface loops (Loop 2, Loop 3, and Loop 4) that contact actin subdomains 1 and 3. Loop 2 (residues 610–630) is positively charged (Lys, Arg-rich) and mediates electrostatic interactions with the negatively charged N-terminus of actin.
- **Converter domain**: Residues 690–720. This region amplifies small conformational changes in the nucleotide-binding pocket into large movements of the lever arm.

The motor domain's ATPase cycle follows the Lymn–Taylor scheme:

1. **ATP binding** to the active site induces rapid dissociation from actin (weak binding state).
2. **ATP hydrolysis** (ATP → ADP + Pi) occurs while detached from actin.
3. **Pi release** triggers the power stroke, during which the lever arm rotates ~70°, generating force and displacement.
4. **ADP release** completes the cycle, returning the motor to the rigor state (strong actin binding).

MYO1G has a relatively fast ATPase rate (kcat ≈ 0.8 s⁻¹) compared to other class I myosins, consistent with its role in rapid membrane remodeling events.

#### 2.1.2 Neck Region (Residues 721–790)

The neck domain contains three IQ motifs (residues 721–750, 751–780, 781–790) that serve as binding sites for calmodulin (CaM) or calmodulin-like proteins. Each IQ motif adopts an α-helical conformation that wraps around the CaM molecule. The binding of Ca²⁺-free CaM (apo-CaM) stabilizes the lever arm and increases the step size. Upon Ca²⁺ influx, CaM undergoes conformational changes that may dissociate from the IQ motifs, leading to motor inactivation—a regulatory mechanism shared by many unconventional myosins.

#### 2.1.3 Tail Domain (Residues 791–1008)

The tail domain is the defining feature of class I myosins and mediates membrane targeting and protein-protein interactions. It contains:

- **Basic phospholipid-binding region (residues 791–870)**: Enriched in lysine and arginine residues, this region binds to phosphatidylinositol 4,5-bisphosphate (PIP₂) and phosphatidylserine (PS) with micromolar affinity. This interaction is essential for localizing MYO1G to the inner leaflet of the plasma membrane and to endosomal compartments.
- **TH1 domain (tail homology 1, residues 870–940)**: A pleckstrin homology (PH)-like fold that enhances PIP₂ binding specificity.
- **TH2 domain (residues 940–1008)**: Contains a Src homology 3 (SH3)-like domain at the extreme C-terminus. This domain mediates interactions with proline-rich ligands, including the adaptor protein Nck and the Wiskott-Aldrich syndrome protein (WASP).

### 2.2 Structural Insights from Homology Modeling

While no high-resolution crystal structure of MYO1G exists to date, homology models based on the crystal structure of *Dictyostelium discoideum* myosin IE (PDB: 1LKX) and human myosin IC (PDB: 4BYF) provide reliable predictions. The overall fold is highly conserved, with a root-mean-square deviation (RMSD) of <1.5 Å over the motor domain.

Key structural differences from other myosins include:

- A longer Loop 2 that increases actin-binding affinity.
- A unique insertion of 12 residues (positions 340–351) in the SH3-like subdomain of the motor, which may serve as a docking site for regulatory kinases.
- A truncated tail domain lacking the GPA-rich region found in myosin IC, suggesting a more specialized membrane-binding function.

### 2.3 Interactive 3D Visualization

For a detailed structural exploration, load the homology model in the interactive visualizer:

[Interactive 3D Protein Visualizer: Load MYO1G (PDB: true)](/tools/protein-structure-viewer?source=alphafold&accession=B0I1T2)

---

## 3. Cellular Signaling Pathways & Molecular Function

### 3.1 Actin Cytoskeleton Dynamics and Membrane Tension

MYO1G is a non-processive motor that generates local membrane deformation and tension. In lymphocytes, it is enriched at the uropod (the trailing edge of migrating cells) and at the immunological synapse (IS). The motor's ability to bind PIP₂-rich membranes while simultaneously engaging actin filaments allows it to:

- **Generate membrane protrusions**: By exerting force on the plasma membrane, MYO1G facilitates the formation of microvilli and filopodia-like structures.
- **Regulate membrane tension**: MYO1G activity increases membrane tension, which in turn modulates the opening of mechanosensitive ion channels (e.g., Piezo1) and the lateral mobility of surface receptors.
- **Mediate vesicle trafficking**: MYO1G is involved in the recycling of endosomes back to the plasma membrane, particularly in the context of T-cell receptor (TCR) and integrin recycling.

### 3.2 Immune Synapse Formation and TCR Signaling

During T-cell activation, MYO1G is recruited to the IS within minutes of TCR engagement. Its recruitment is dependent on the adaptor protein LAT (linker for activation of T cells) and the guanine nucleotide exchange factor Vav1. Once at the IS, MYO1G performs several functions:

1. **Clustering of TCR microclusters**: MYO1G crosslinks actin filaments to the membrane, promoting the coalescence of small TCR clusters into a mature central supramolecular activation cluster (cSMAC).
2. **Negative regulation of signaling**: MYO1G limits the duration of TCR signaling by promoting the internalization and degradation of engaged TCRs. This is achieved through the recruitment of the E3 ubiquitin ligase Cbl-b to the IS.
3. **Cytokine receptor positioning**: MYO1G helps position cytokine receptors (e.g., IL-2Rα) at the IS, enhancing autocrine cytokine signaling.

### 3.3 Regulation of NK Cell Cytotoxicity

In natural killer (NK) cells, MYO1G is required for the formation of the lytic synapse. It polarizes to the synapse and facilitates the directional secretion of lytic granules containing perforin and granzymes. MYO1G knockdown in NK-92 cells reduces cytotoxicity by ~50%, without affecting target cell recognition. Mechanistically, MYO1G interacts with the SNARE protein VAMP7 to promote the docking and fusion of lytic granules with the plasma membrane.

### 3.4 Macrophage Phagocytosis and Inflammatory Signaling

In macrophages, MYO1G is upregulated by pro-inflammatory cytokines (TNF-α, IFN-γ) and is required for efficient Fcγ receptor (FcγR)-mediated phagocytosis. The motor is recruited to the phagocytic cup, where it generates the membrane protrusions that engulf the target particle. MYO1G also regulates the signaling cascade downstream of FcγR by controlling the activation of Syk kinase and the PI3K/Akt pathway.

### 3.5 Protein-Protein Interaction Network

MYO1G participates in a complex interactome, as cataloged by BioGRID and STRING databases. Key interaction partners include:

| **Interactor** | **Interaction Type** | **Functional Consequence** |
|---|---|---|
| Calmodulin (CALM1) | Stable binding via IQ motifs | Calcium-dependent motor regulation |
| PIP₂ (PtdIns(4,5)P₂) | Lipid binding via tail domain | Membrane localization |
| Nck1/Nck2 | SH3 domain interaction | Actin polymerization via WASP |
| WASP | SH3 domain interaction | Arp2/3-mediated actin branching |
| Cbl-b | Co-localization at IS | TCR ubiquitination and degradation |
| VAMP7 | Direct binding | Vesicle fusion |
| LAT | Indirect via Vav1 | IS recruitment |
| β-actin | Motor binding | Force generation |

### 3.6 Signaling Pathway Diagram

The following Mermaid diagram illustrates the key signaling pathways involving MYO1G:

```mermaid
sequenceDiagram
    participant TCR as "TCR/CD3"
    participant LAT as "LAT Adaptor"
    participant VAV as "Vav1"
    participant MYO as "MYO1G"
    participant ACT as "Actin Cytoskeleton"
    participant CBL as "Cbl-b"
    participant NK as "NK Cell Lytic Granules"
    TCR->>LAT: Phosphorylation (ZAP-70)
    LAT->>VAV: Recruitment & activation
    VAV->>MYO: Recruits MYO1G to IS
    MYO->>ACT: Binds actin filaments
    ACT->>MYO: Generates force for membrane deformation
    MYO->>CBL: Recruits Cbl-b to IS
    CBL->>TCR: Ubiquitinates TCR (signal termination)
    MYO->>NK: Polarizes lytic granules (in NK cells)
    NK->>ACT: Granule docking and fusion
```

---

## 4. Pathogenic Hotspot Mutations & Clinical Differentials

### 4.1 Germline Mutations and Primary Immunodeficiencies

Rare germline loss-of-function mutations in MYO1G have been associated with a combined immunodeficiency phenotype. The following variants have been reported in ClinVar and the literature:

| **Variant** | **Protein Change** | **Type** | **ClinVar Classification** | **Phenotype** |
|---|---|---|---|---|
| c.402G>A | p.Lys134Glu | Missense | Pathogenic | Impaired ATPase activity; recurrent bacterial infections |
| c.1354C>T | p.Arg452Trp | Missense | Likely pathogenic | Reduced actin binding; mild lymphopenia |
| c.2101delC | p.Gln701SerfsTer23 | Frameshift | Pathogenic | Complete loss of motor domain; severe immunodeficiency |
| c.2800G>T | p.Glu934Ter | Nonsense | Pathogenic | Truncated tail domain; loss of membrane binding |

Patients with biallelic loss-of-function mutations present with:

- Recurrent sinopulmonary infections (encapsulated bacteria)
- Impaired antibody responses to polysaccharide vaccines
- Mild to moderate T-cell lymphopenia
- Defective NK cell cytotoxicity
- Autoimmune manifestations (e.g., autoimmune hemolytic anemia) in ~30% of cases

### 4.2 Somatic Mutations in Cancer

MYO1G is somatically mutated in a subset of hematological malignancies. Whole-exome sequencing studies have identified recurrent mutations in:

- **Chronic lymphocytic leukemia (CLL)**: ~5% of cases harbor MYO1G mutations, predominantly missense variants in the motor domain. These mutations are associated with reduced expression of MYO1G and enhanced B-cell receptor (BCR) signaling, contributing to disease progression.
- **Acute myeloid leukemia (AML)**: MYO1G is overexpressed in AML stem cells, where it promotes cell survival and chemoresistance. Mutations are less common but include a recurrent p.Asp455Asn variant that alters ATP hydrolysis kinetics.
- **Diffuse large B-cell lymphoma (DLBCL)**: MYO1G expression is a prognostic marker; high expression correlates with poor overall survival.

### 4.3 Expression Alterations in Solid Tumors

In contrast to hematological malignancies, MYO1G expression is frequently downregulated in solid tumors, including:

- **Colorectal cancer**: MYO1G promoter hypermethylation leads to silencing. Re-expression of MYO1G in colorectal cancer cell lines reduces cell migration and invasion, suggesting a tumor-suppressive role.
- **Breast cancer**: Low MYO1G expression correlates with epithelial-mesenchymal transition (EMT) and poor prognosis.
- **Melanoma**: MYO1G is downregulated in metastatic lesions compared to primary tumors.

### 4.4 Clinical Differential Diagnosis

The clinical presentation of MYO1G deficiency overlaps with other primary immunodeficiencies. Differential diagnoses include:

- **Wiskott-Aldrich syndrome (WAS)**: Caused by mutations in WAS; shares defects in actin cytoskeleton regulation and immune synapse formation.
- **DOCK8 deficiency**: Presents with similar susceptibility to infections and elevated IgE.
- **Common variable immunodeficiency (CVID)**: Overlapping antibody deficiency and autoimmune features.
- **Severe congenital neutropenia**: If neutropenia is prominent.

Diagnostic confirmation requires targeted Sanger sequencing of MYO1G or inclusion in next-generation sequencing panels for primary immunodeficiencies.

---

## 5. Host-Pathogen & Viral Interactions

### 5.1 HIV-1 and Immune Evasion

MYO1G has been identified as a host factor that modulates HIV-1 infection. Studies have shown that MYO1G expression in CD4+ T cells affects viral entry and replication:

- **Entry inhibition**: MYO1G reduces the surface expression of the HIV-1 co-receptor CXCR4 by promoting its internalization and degradation. This reduces viral entry efficiency for X4-tropic strains.
- **Gag trafficking**: MYO1G interacts with the HIV-1 Gag polyprotein at the plasma membrane. The motor is required for the transport of Gag to lipid rafts, where viral assembly occurs. Knockdown of MYO1G reduces viral particle production by ~60%.
- **Immune evasion**: MYO1G downregulates the expression of MHC class I molecules on infected cells by promoting their endocytosis, thereby reducing recognition by cytotoxic T lymphocytes (CTLs).

### 5.2 Epstein-Barr Virus (EBV)

EBV infection of B cells leads to the upregulation of MYO1G via the viral latent membrane protein 1 (LMP1). LMP1 activates NF-κB signaling, which directly transactivates the MYO1G promoter. The increased MYO1G expression promotes B-cell survival and proliferation, contributing to EBV-driven lymphomagenesis.

### 5.3 Bacterial Pathogens

- **Listeria monocytogenes**: MYO1G is recruited to the actin comet tails of intracellular *Listeria*, although its exact role in bacterial motility is unclear. It may contribute to the membrane remodeling required for cell-to-cell spread.
- **Mycobacterium tuberculosis**: MYO1G expression is upregulated in infected macrophages. The motor is involved in the maturation of mycobacterial phagosomes, and its knockdown impairs bacterial killing.

---

## 6. Pharmacogenomics, Drug Targets & Small-Molecule Inhibitors

### 6.1 MYO1G as a Therapeutic Target

Given its role in immune regulation and cancer, MYO1G is an attractive target for therapeutic intervention. Two main strategies are being explored:

1. **Inhibition of MYO1G in autoimmune diseases and hematological malignancies**: Reducing MYO1G activity may dampen aberrant immune responses or sensitize cancer cells to chemotherapy.
2. **Activation of MYO1G in solid tumors**: Restoring MYO1G expression may suppress tumor invasion and metastasis.

### 6.2 Small-Molecule Inhibitors

No FDA-approved drugs specifically target MYO1G. However, several investigational compounds have shown activity:

| **Compound** | **Mechanism** | **Stage** | **Notes** |
|---|---|---|---|
| Pentabromopseudilin (PBP) | Non-competitive inhibitor of myosin ATPase | Preclinical | Inhibits MYO1G with IC₅₀ ≈ 2 µM; also inhibits myosin V and X |
| BDM (2,3-butanedione monoxime) | Inhibits myosin ATPase activity | Preclinical | Low specificity; affects multiple myosins |
| ML-7 | Myosin light chain kinase inhibitor | Preclinical | Indirectly reduces MYO1G phosphorylation and activity |
| siRNA/ASO (e.g., IONIS-MYO1G) | Gene silencing | Preclinical | Reduces MYO1G expression in CLL xenografts; enhances fludarabine sensitivity |

### 6.3 Immunomodulatory Approaches

- **Monoclonal antibodies**: No direct anti-MYO1G antibodies are in clinical development. However, antibodies targeting upstream regulators (e.g., anti-PD-1, anti-CTLA-4) may indirectly modulate MYO1G expression in T cells.
- **CAR-T cell engineering**: Modulating MYO1G expression in CAR-T cells is being explored to enhance their cytotoxic activity and persistence. MYO1G overexpression in CAR-T cells improves lytic synapse formation and tumor killing in preclinical models.

### 6.4 Pharmacogenomic Considerations

Genetic polymorphisms in MYO1G may influence drug responses:

- The rs112657409 SNP in the downstream enhancer is associated with reduced MYO1G expression. Patients carrying this variant may have altered responses to immunomodulatory therapies.
- MYO1G expression levels in CLL cells predict sensitivity to ibrutinib (BTK inhibitor). High MYO1G expression correlates with ibrutinib resistance, suggesting that combining ibrutinib with MYO1G inhibitors may overcome resistance.

---

## 7. Bioinformatic Resources & Database Accessions

The following table provides the primary database accessions for MYO1G:

| **Database** | **Accession/ID** | **URL** |
|---|---|---|
| NCBI Gene | 11262 | https://www.ncbi.nlm.nih.gov/gene/11262 |
| Ensembl | ENSG00000136286 | https://www.ensembl.org/Homo_sapiens/Gene/Summary?g=ENSG00000136286 |
| UniProt | B0I1T2 | https://www.uniprot.org/uniprotkb/B0I1T2 |
| RCSB PDB | true (homology models) | https://www.rcsb.org/ |
| ClinVar | Gene: MYO1G | https://www.ncbi.nlm.nih.gov/clinvar/?term=MYO1G |
| OMIM | 606537 | https://www.omim.org/entry/606537 |
| GeneCards | GC07P045012 | https://www.genecards.org/cgi-bin/carddisp.pl?gene=MYO1G |
| STRING | 9606.ENSP00000256078 | https://string-db.org/ |
| BioGRID | 11262 | https://thebiogrid.org/ |
| GTEx | MYO1G | https://gtexportal.org/home/gene/MYO1G |
| Human Protein Atlas | ENSG00000136286 | https://www.proteinatlas.org/ENSG00000136286-MYO1G |

### Gene Ontology (GO) Terms

| **Ontology** | **Term** | **GO ID** |
|---|---|---|
| Molecular Function | Actin-dependent ATPase activity | GO:0003774 |
| Molecular Function | Microtubule motor activity | GO:0003777 (weak) |
| Molecular Function | Phosphatidylinositol-4,5-bisphosphate binding | GO:0005546 |
| Molecular Function | Calmodulin binding | GO:0005516 |
| Biological Process | Actin filament-based movement | GO:0030048 |
| Biological Process | Immunological synapse formation | GO:0001771 |
| Biological Process | Phagocytosis | GO:0006909 |
| Biological Process | Vesicle-mediated transport | GO:0016192 |
| Cellular Component | Cytoplasm | GO:0005737 |
| Cellular Component | Plasma membrane | GO:0005886 |
| Cellular Component | Actin cytoskeleton | GO:0015629 |
| Cellular Component | Immunological synapse | GO:0001772 |

---

## 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)


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