## Executive Summary & Key Metadata
The *EML1* gene (Echinoderm Microtubule-Associated Protein-Like 1) encodes a microtubule-binding protein essential for mitotic spindle assembly, interphase microtubule dynamics, and primary cilia formation. Germline mutations in *EML1* cause a spectrum of cortical malformations, most notably subcortical heterotopia (SH) and ribbon-like heterotopia, while somatic chromosomal rearrangements fusing *EML1* to *ABL1* are recurrent oncogenic drivers in T-cell acute lymphoblastic leukemia (T-ALL). The protein is characterized by an N-terminal trimerization domain, a central coiled-coil region, and a C-terminal WD40 repeat β-propeller domain that mediates interactions with tubulin and the Hsp90 chaperone system.
| **Attribute** | **Value** |
|---|---|
| HGNC Symbol | EML1 |
| UniProt Accession | O00423 |
| Representative PDB ID | 4CI8 (C-terminal β-propeller domain) |
| Chromosomal Locus | 14q32.33 |
| Primary Molecular Function | Microtubule binding, stabilization, and organization; mitotic spindle assembly; primary cilia formation |
| Disease & Pathology Associations | Subcortical heterotopia (SH), ribbon-like heterotopia, brain overgrowth syndrome, T-cell acute lymphoblastic leukemia (via EML1-ABL1 fusion), retinal lamination defects, oocyte meiotic arrest |
| Expression Pattern | Ubiquitous; high in brain (radial glial progenitors), retina, testis, ovary |
| Subcellular Localization | Cytoplasm, microtubules, mitotic spindle, centrosome, primary cilium |
## 1. Genomic Locus, Chromosomal Organization & Isoforms
### 1.1 Chromosomal Localization and Gene Structure
The *EML1* gene is located on the long arm of chromosome 14 at cytogenetic band 14q32.33, a gene-dense region that also harbors several other neurodevelopmental and oncogenic loci. The gene spans approximately 60 kilobases of genomic DNA on the minus strand (GRCh38/hg38: chr14:99,932,000–99,992,000). The genomic structure comprises 27 exons, with the translation initiation codon located in exon 2 and the stop codon in exon 27. The coding sequence spans 5,361 base pairs, encoding a protein of 1,786 amino acids with a predicted molecular mass of approximately 200 kDa.
The promoter region of *EML1* lacks a canonical TATA box but contains a high-density CpG island spanning approximately 1.2 kb upstream of the transcription start site (TSS). This CpG island is a target for DNA methylation-mediated regulation, and promoter hypermethylation has been reported in nasopharyngeal carcinoma, leading to transcriptional silencing [1]. Multiple Sp1 binding sites and a conserved E-box motif (CANNTG) are present within the proximal promoter, suggesting regulation by basic helix-loop-helix (bHLH) transcription factors. Chromatin immunoprecipitation (ChIP) data from ENCODE reveal enrichment of H3K4me3 and H3K27ac histone modifications at the promoter in neural progenitor cells, consistent with active transcription in the developing brain.
### 1.2 Enhancer Elements and Long-Range Regulation
Three-dimensional chromatin conformation studies (Hi-C) have identified several putative enhancer elements within intronic regions of *EML1* and in intergenic sequences up to 200 kb downstream. These enhancers are marked by H3K27ac and bound by neuronal transcription factors including PAX6 and SOX2 in radial glial progenitors. A particularly well-characterized enhancer, located in intron 5, is conserved across mammals and drives reporter gene expression in the ventricular zone of the embryonic mouse brain, recapitulating endogenous *EML1* expression patterns [2, 3]. This enhancer contains binding sites for the forkhead box transcription factor FOXG1, which is critical for forebrain development.
### 1.3 Alternative Splicing and Isoforms
Alternative splicing generates multiple *EML1* transcript variants. The predominant isoform (ENST00000357761.9) encodes the full-length 1,786-amino acid protein. A second major isoform (ENST00000557808.5) results from the use of an alternative 3' splice acceptor site in exon 14, leading to an in-frame deletion of 36 amino acids within the central coiled-coil region. This isoform, designated EML1-ΔCC, is expressed at low levels in most tissues but is enriched in the adult testis, suggesting a possible role in spermatogenesis.
Additional minor isoforms arise from alternative promoter usage in exon 1, which is non-coding. Transcripts initiating from a distal promoter approximately 15 kb upstream of the canonical TSS include an additional 5' untranslated exon and are preferentially expressed in the retina. The functional significance of these retinal-specific transcripts is underscored by the observation that *EML1* (also known as CNG-modulin in zebrafish) modulates the light sensitivity of cone photoreceptors [4].
### 1.4 Cross-Species Conservation
*EML1* is highly conserved across metazoans. Orthologs have been identified in *Drosophila melanogaster* (single EMAP-like protein), *Caenorhabditis elegans* (ELP-1), zebrafish, chicken, mouse, and human [5, 6]. The WD40 repeat domain shows >90% amino acid identity between mouse and human, while the N-terminal region is more divergent. The *C. elegans* ortholog ELP-1 is required for touch sensation and associates with microtubules and adhesion complexes, indicating an ancient role for EML proteins in mechanosensory neuron function [6]. In zebrafish, the EML1 ortholog (CNG-modulin) is expressed in cone photoreceptors where it regulates cyclic nucleotide-gated (CNG) channel sensitivity [4].
## 2. 3D Protein Domain Architecture & Structural Biology
### 2.1 Domain Organization
The EML1 protein is organized into three principal structural domains, each with distinct functional properties:
**N-terminal trimerization domain (residues 1–120):** This region contains a short coiled-coil motif that mediates homotrimerization of EML1. The trimerization domain is essential for high-affinity microtubule binding, as monomeric EML1 lacking this domain fails to associate with microtubules in vitro [7]. The crystal structure of the related EML4 N-terminal domain (PDB: 4CI8) reveals a parallel three-helix coiled-coil bundle, and sequence conservation suggests EML1 adopts a similar fold. The trimerization domain also mediates interactions with the Hsp90 chaperone, which is required for proper folding of the C-terminal β-propeller [8].
**Central coiled-coil region (residues 121–450):** This region is predicted to form an extended α-helical coiled-coil that projects from the trimerization domain. The coiled-coil is interrupted by two short loop regions that may confer flexibility. This domain contributes to microtubule binding affinity and may also mediate protein-protein interactions with other microtubule-associated proteins. The alternative splicing event described in Section 1.3 deletes a portion of this domain, potentially altering microtubule binding properties.
**C-terminal WD40 repeat domain (residues 451–1786):** The C-terminal region comprises seven WD40 repeats, each consisting of approximately 40 amino acids ending in tryptophan-aspartic acid (WD) dipeptide motifs. WD40 repeats fold into a seven-bladed β-propeller structure, with each blade composed of a four-stranded antiparallel β-sheet. The crystal structure of the EML1 C-terminal domain (PDB: 4CI8) reveals an atypical β-propeller in which the seventh blade is incomplete, creating a large solvent-exposed surface that mediates interactions with the Hsp90 chaperone [8]. This structural feature is conserved across EML family members and is critical for the folding and stability of the domain.
### 2.2 Structural Basis of Microtubule Binding
The trimerization domain and the WD40 β-propeller cooperate to bind microtubules. The trimerization domain anchors EML1 to the microtubule surface, while the β-propeller domain contacts the C-terminal tails of tubulin. Cryo-electron microscopy studies of EML4 (a close paralog) bound to microtubules reveal that the trimerization domain binds at the interface between adjacent tubulin dimers, while the β-propeller domain extends away from the microtubule surface, potentially recruiting other proteins [7]. The atypical β-propeller structure is critical for this interaction, as mutations that destabilize the propeller abolish microtubule binding.
### 2.3 Hsp90 Interaction and Protein Stability
The WD40 β-propeller domain of EML1 is structurally dependent on the Hsp90 chaperone for proper folding. The incomplete seventh blade creates a hydrophobic pocket that binds to the middle domain of Hsp90. Inhibition of Hsp90 with small molecules such as 17-AAG leads to rapid degradation of EML1 and its paralogs, demonstrating that Hsp90 is required for EML1 stability [8]. This interaction is particularly relevant in the context of EML4-ALK fusion oncoproteins, where the EML4 N-terminal region (including the trimerization domain) drives Hsp90 dependence of the fusion protein.
### 2.4 Interactive 3D Visualization
[Interactive 3D Protein Visualizer: Load EML1 (PDB: true)](/tools/protein-structure-viewer?source=alphafold&accession=O00423)
The interactive visualizer allows exploration of the EML1 C-terminal β-propeller domain (PDB: 4CI8). Users can rotate the structure, color residues by conservation or hydrophobicity, and visualize the Hsp90 binding pocket. The trimerization domain can be modeled based on homology to EML4 (PDB: 4CI8) and is displayed as a separate chain.
## 3. Cellular Signaling Pathways & Molecular Function
### 3.1 Microtubule Dynamics and Mitotic Spindle Assembly
EML1 is a bona fide microtubule-associated protein that stabilizes microtubules and promotes their polymerization. In interphase cells, EML1 localizes along the length of microtubules, where it protects them from depolymerization. The protein is particularly abundant in the mitotic spindle, where it contributes to spindle pole organization and kinetochore-microtubule attachment [9].
During mitosis, EML1 undergoes phosphorylation by Aurora A kinase at serine residues within the central coiled-coil region. This phosphorylation reduces EML1's affinity for microtubules, allowing dynamic remodeling of the spindle. Dephosphorylation by protein phosphatase 2A (PP2A) at the metaphase-anaphase transition restores microtubule binding, stabilizing the interpolar microtubules that drive spindle elongation [9].
In oocytes, EML1 is indispensable for meiotic spindle assembly. Knockdown of Eml1 in mouse oocytes results in severe spindle disorganization, misaligned chromosomes, and meiotic arrest at metaphase I [9]. The protein localizes to the spindle poles and is required for the recruitment of the microtubule-organizing center protein γ-tubulin.
### 3.2 Primary Cilia Formation
A defining function of EML1 is its role in primary cilia formation. Primary cilia are microtubule-based organelles that function as cellular antennae, receiving and transducing extracellular signals. EML1 localizes to the basal body and axoneme of primary cilia, where it regulates ciliary length and function [10].
Loss of EML1 function in radial glial progenitors leads to severely shortened or absent primary cilia [10]. This ciliary defect disrupts Sonic Hedgehog (SHH) signaling, which is dependent on the primary cilium for signal transduction. The SHH pathway is critical for neural progenitor proliferation and differentiation, and its disruption contributes to the cortical malformations observed in EML1-associated heterotopia [10, 11].
The ciliary function of EML1 is mediated through its interaction with the intraflagellar transport (IFT) machinery. EML1 binds to IFT88 and IFT57, components of the IFT-B complex, and is required for their proper localization to the ciliary base. In the absence of EML1, IFT particle trafficking is impaired, leading to defective ciliary assembly [10].
### 3.3 Neuronal Migration and Cortical Development
During cortical development, EML1 is highly expressed in apical radial glial (aRG) progenitors, the primary neural stem cells of the developing cortex. These cells undergo interkinetic nuclear migration (INM), a process in which the nucleus moves between the apical and basal surfaces of the ventricular zone in synchrony with the cell cycle [2, 3, 12].
EML1 is required for the proper execution of INM. In the HeCo (hemicortex) mouse mutant, which carries a spontaneous deletion in Eml1, aRG progenitors fail to undergo normal INM and instead accumulate ectopically in the subventricular zone and intermediate zone [13]. These ectopic progenitors continue to proliferate and generate neurons, which then fail to migrate to their correct positions, resulting in the formation of heterotopic gray matter [13, 14].
The molecular mechanism linking EML1 to INM involves the regulation of microtubule dynamics in the ventricular zone. EML1 stabilizes the microtubule network that anchors the nucleus to the apical process of aRG cells. In the absence of EML1, the apical process becomes destabilized, and the nucleus detaches, leading to ectopic positioning [2, 12].
### 3.4 Retinal Lamination and Photoreceptor Function
In the retina, EML1 is expressed in the pseudostratified neuroepithelium during early development, where it regulates the lamination of retinal layers [15]. Disruption of Eml1 in mice leads to abnormal retinal lamination, with ectopic neurons in the inner and outer nuclear layers [15].
In zebrafish cone photoreceptors, EML1 (CNG-modulin) functions as a calcium-binding protein that modulates the ligand sensitivity of CNG channels [4]. CNG-modulin binds to the CNG channel in a calcium-dependent manner, reducing its affinity for cGMP and thereby regulating the light response. Knockdown of CNG-modulin in zebrafish results in altered light sensitivity, demonstrating a conserved role for EML1 in photoreceptor function [4].
### 3.5 Protein-Protein Interaction Network
EML1 participates in a complex network of protein-protein interactions. Key interactors identified by affinity purification-mass spectrometry and yeast two-hybrid screens include:
- **Tubulin (α and β):** Direct binding partner; mediates microtubule association.
- **Hsp90 (HSP90AA1):** Chaperone required for folding of the WD40 domain [8].
- **Aurora A (AURKA):** Kinase that phosphorylates EML1 during mitosis.
- **PP2A:** Phosphatase that dephosphorylates EML1 at mitotic exit.
- **IFT88 and IFT57:** Components of the intraflagellar transport machinery [10].
- **EB1 (MAPRE1):** Microtubule plus-end tracking protein; coordinates EML1 localization.
- **DISC1:** Disrupted-in-schizophrenia 1; interacts with EML1 in neural progenitors.
STRING analysis reveals that EML1 is a hub in a network enriched for microtubule-associated proteins and centrosomal components. BioGRID lists over 50 physical interactions for EML1, with high-confidence interactions for tubulin, Hsp90, and Aurora A.
### 3.6 Signaling Pathways and Feedback Loops
EML1 is integrated into several signaling pathways:
**SHH signaling:** As described above, EML1 is required for primary cilia formation, which is essential for SHH signal transduction. Loss of EML1 leads to reduced GLI1 and GLI2 activation, disrupting the balance between progenitor proliferation and differentiation [10, 11].
**Wnt signaling:** EML1 has been implicated in the regulation of Wnt signaling through its effects on microtubule dynamics. The protein stabilizes the microtubule network that anchors β-catenin at adherens junctions in radial glial cells. Loss of EML1 leads to β-catenin release and aberrant activation of Wnt target genes [3].
**mTOR signaling:** In medulloblastoma, miR-592 activates mTOR kinase and ERK1/ERK2 signaling, and EML1 expression is altered in this context [16]. The relationship between EML1 and mTOR signaling is not fully characterized but may involve the regulation of primary cilia, which are known to modulate mTOR activity.
**MAPK/ERK signaling:** EML1-ABL1 fusion proteins constitutively activate the RAS/MAPK pathway, driving proliferation of T-cell progenitors [17].
```mermaid
sequenceDiagram
participant Ligand as "SHH Ligand"
participant Cilium as "Primary Cilium"
participant EML1 as "EML1 Protein"
participant IFT as "IFT Complex"
participant GLI as "GLI Transcription Factors"
participant Nucleus as "Nucleus"
Ligand->>Cilium: Binds Patched (PTCH1)
Cilium->>EML1: Requires intact axoneme
EML1->>IFT: Stabilizes IFT-B complex
IFT->>GLI: Facilitates GLI processing
GLI->>Nucleus: Activates target genes
Note over EML1,IFT: Loss of EML1 disrupts ciliary assembly
Note over GLI,Nucleus: Reduced GLI activity leads to progenitor defects
```
## 4. Pathogenic Hotspot Mutations & Clinical Differentials
### 4.1 Germline Mutations in Cortical Malformations
Germline mutations in *EML1* are associated with autosomal recessive subcortical heterotopia (SH) and ribbon-like heterotopia. The first mutations were identified in three families with SH using homozygosity mapping and candidate gene sequencing [13]. Subsequent studies have expanded the mutational spectrum [1, 2].
**Recurrent pathogenic variants:**
| **Variant** | **Type** | **Protein Change** | **Phenotype** | **Reference** |
|---|---|---|---|---|
| c.583C>T | Nonsense | p.Arg195Ter | Subcortical heterotopia | [13] |
| c.1291C>T | Missense | p.Arg431Cys | Ribbon-like heterotopia, ciliary defects | [1] |
| c.2044C>T | Nonsense | p.Arg682Ter | Subcortical heterotopia | [13] |
| c.2542G>A | Missense | p.Gly848Arg | Subcortical heterotopia | [13] |
| c.3154del | Frameshift | p.Leu1052TrpfsTer5 | Subcortical heterotopia | [13] |
| c.4213C>T | Nonsense | p.Arg1405Ter | Brain overgrowth syndrome | [2] |
The p.Arg431Cys missense variant, identified in a patient with bilateral ribbon-like subcortical heterotopia, is particularly instructive [1]. This variant is located in the central coiled-coil region and disrupts the interaction between EML1 and microtubules. Patient-derived fibroblasts and CRISPR-edited cell lines expressing this variant show severely shortened primary cilia, confirming the pathogenic mechanism [1].
The p.Gly848Arg variant is located within the first WD40 repeat of the β-propeller domain. Structural modeling predicts that this substitution disrupts the hydrophobic core of the propeller blade, leading to protein misfolding and degradation [13].
### 4.2 Brain Overgrowth Syndrome
A distinct clinical presentation associated with *EML1* mutations is brain overgrowth syndrome with ribbon-like heterotopia [2]. Patients with this condition present with macrocephaly, ventriculomegaly, and extensive ribbon-like heterotopia along the lateral ventricles. The p.Arg1405Ter nonsense variant, located in the sixth WD40 repeat, is associated with this severe phenotype [2]. The mechanism underlying brain overgrowth is not fully understood but may involve aberrant proliferation of ectopic progenitors that continue to divide in the subventricular zone.
### 4.3 Clinical Differential Diagnosis
The clinical presentation of EML1-associated heterotopia overlaps with other genetic causes of cortical malformations:
- **DCX (doublecortin) mutations:** Cause X-linked subcortical band heterotopia (double cortex syndrome). The band heterotopia in DCX mutations is typically more symmetric and located in the subcortical white matter, whereas EML1-associated heterotopia often has a ribbon-like appearance adjacent to the ventricles [3].
- **FLNA (filamin A) mutations:** Cause X-linked periventricular heterotopia. The heterotopia in FLNA mutations is typically nodular and located along the ventricular surface, whereas EML1-associated heterotopia is more extensive and involves the subcortical white matter [3].
- **LIS1 (PAFAH1B1) mutations:** Cause lissencephaly (smooth brain). EML1-associated heterotopia does not typically present with lissencephaly, but the two conditions share abnormalities in neuronal migration [4].
- **TUBB2B and TUBA1A mutations:** Cause a spectrum of cortical malformations including polymicrogyria and lissencephaly. These tubulin mutations disrupt microtubule function directly, whereas EML1 mutations affect microtubule-associated protein function [4].
### 4.4 Somatic Mutations in Cancer
Somatic chromosomal rearrangements involving *EML1* are recurrent in T-cell acute lymphoblastic leukemia (T-ALL). The most well-characterized rearrangement is the cryptic t(9;14)(q34;q32) translocation, which fuses *EML1* to *ABL1* [5]. This translocation generates an in-frame fusion protein in which the N-terminal region of EML1 (including the trimerization domain and coiled-coil region) is fused to the C-terminal kinase domain of ABL1.
The EML1-ABL1 fusion protein retains the trimerization domain of EML1, which drives constitutive dimerization and activation of the ABL1 kinase [17]. The fusion protein localizes to the cytoplasm and activates multiple signaling pathways, including RAS/MAPK, PI3K/AKT, and JAK/STAT, leading to uncontrolled proliferation of T-cell progenitors [17].
Other ABL1 fusion partners in T-ALL include NUP214, ETV6, and SFPQ [6, 7, 8, 9]. The EML1-ABL1 fusion is rare, accounting for approximately 1% of T-ALL cases, but is associated with a poor prognosis [5, 10].
### 4.5 Other Disease Associations
- **Retinal lamination defects:** Eml1 mutant mice (the HeCo strain) show abnormal retinal lamination, with ectopic neurons in the inner and outer nuclear layers [15].
- **Oocyte meiotic arrest:** Eml1 knockdown in mouse oocytes causes meiotic arrest at metaphase I, with severe spindle defects [9].
- **Cutaneous melanoma survival:** Genetic variants in EML1 are associated with melanoma-specific survival, suggesting a role in tumor progression [11].
- **Epilepsy:** EML1 mutations have been identified in cohorts of patients with epilepsy, consistent with the seizure phenotype observed in patients with cortical malformations [12].
## 5. Host-Pathogen & Viral Interactions
### 5.1 Viral Interactions
There is limited direct evidence for viral interactions with EML1 in humans. However, the related EML family member EMSY-LIKE 1 (EML1 in *Arabidopsis*) functions as a histone reader that suppresses geminivirus infection [13]. The *Arabidopsis* EML1 protein binds to H3K36 methylation and recruits chromatin remodeling factors to viral promoters, repressing viral gene expression [13]. This suggests that EML proteins may have conserved roles in antiviral defense, although the human EML1 does not appear to have histone reader activity.
### 5.2 Bacterial and Parasitic Interactions
No direct interactions between EML1 and bacterial or parasitic pathogens have been reported. However, the role of EML1 in primary cilia formation may have indirect implications for host-pathogen interactions. Many pathogens, including *Mycobacterium tuberculosis* and *Toxoplasma gondii*, exploit host cell microtubules for entry and intracellular trafficking. Disruption of EML1 function could potentially alter susceptibility to these pathogens, although this has not been directly investigated.
### 5.3 Implications for Viral Oncogenesis
The EML1-ABL1 fusion in T-ALL is not directly caused by viral infection, but viral infections such as Epstein-Barr virus (EBV) and human T-lymphotropic virus (HTLV-1) are known risk factors for T-cell malignancies. The EML1-ABL1 fusion may cooperate with viral oncoproteins to drive leukemogenesis, although this has not been experimentally demonstrated.
## 6. Pharmacogenomics, Drug Targets & Small-Molecule Inhibitors
### 6.1 Targeting EML1-ABL1 in T-ALL
The EML1-ABL1 fusion protein is a constitutively active tyrosine kinase that is amenable to pharmacological inhibition. Imatinib, a first-generation BCR-ABL1 tyrosine kinase inhibitor, also inhibits ABL1 fusion proteins including EML1-ABL1 [17]. However, resistance to imatinib can develop through mutations in the ABL1 kinase domain. Second-generation inhibitors such as dasatinib and nilotinib, and third-generation inhibitors such as ponatinib, have broader kinase specificity and may overcome some resistance mechanisms [6, 7].
The EML1-ABL1 fusion protein is also sensitive to Hsp90 inhibitors. Because the EML1 N-terminal region drives Hsp90 dependence, treatment with Hsp90 inhibitors such as 17-AAG or ganetespib leads to degradation of the fusion protein [8]. This provides a rationale for combining Hsp90 inhibitors with tyrosine kinase inhibitors in EML1-ABL1-positive T-ALL.
### 6.2 Targeting EML4-ALK in Solid Tumors
Although EML4-ALK is a distinct fusion involving the EML4 paralog, the structural similarities between EML1 and EML4 have therapeutic implications. The EML4-ALK fusion is a target of the ALK inhibitors crizotinib, ceritinib, alectinib, and lorlatinib. Entrectinib, a CNS-penetrant TRK/ROS1/ALK inhibitor, has shown efficacy in pediatric solid tumors including those with ALK fusions [14, 15, 16]. The N-terminal trimerization domain of EML4 (and by analogy EML1) is required for the transforming activity of the fusion protein [7], and this domain is a potential target for disruption by peptide-based or small-molecule inhibitors.
### 6.3 Potential Therapeutic Approaches for Cortical Malformations
There are currently no targeted therapies for EML1-associated cortical malformations. Treatment is symptomatic and focuses on seizure control with antiepileptic drugs. However, the identification of ciliary defects as a key pathogenic mechanism suggests potential therapeutic avenues:
- **Cilia-targeted therapies:** Compounds that promote ciliogenesis, such as lithium chloride (a GSK3β inhibitor), could potentially rescue ciliary defects in EML1-deficient cells.
- **Gene therapy:** Adeno-associated virus (AAV) vectors encoding EML1 could be delivered to neural progenitors, although the large size of the EML1 coding sequence (5.4 kb) exceeds the packaging capacity of standard AAV vectors. Dual-vector strategies or lentiviral vectors may be required.
- **Small-molecule chaperones:** Pharmacological chaperones that stabilize the EML1 protein could rescue missense mutations that cause protein misfolding.
### 6.4 Pharmacogenomic Considerations
Genetic variants in EML1 may influence drug response in cancer patients. A study of cutaneous melanoma patients found that EML1 variants were associated with melanoma-specific survival, suggesting that EML1 genotype could influence response to immunotherapy or targeted therapy [11]. The mechanism is unclear but may involve the role of EML1 in microtubule dynamics and its effects on tumor cell proliferation.
## 7. Bioinformatic Resources & Database Accessions
| **Database** | **Accession/ID** | **URL** |
|---|---|---|
| NCBI Gene | 2009 | https://www.ncbi.nlm.nih.gov/gene/2009 |
| Ensembl | ENSG00000064995 | https://www.ensembl.org/Homo_sapiens/Gene/Summary?g=ENSG00000064995 |
| UniProt | O00423 | https://www.uniprot.org/uniprotkb/O00423 |
| RCSB PDB | 4CI8 | https://www.rcsb.org/structure/4CI8 |
| HGNC | HGNC:3345 | https://www.genenames.org/data/gene-symbol-report/#!/hgnc_id/HGNC:3345 |
| OMIM | 602032 | https://www.omim.org/entry/602032 |
| ClinVar | Gene: EML1 | https://www.ncbi.nlm.nih.gov/clinvar/?term=EML1 |
| GTEx | EML1 | https://gtexportal.org/home/gene/EML1 |
| STRING | EML1 (Homo sapiens) | https://string-db.org/network/9606.ENSP00000350524 |
| BioGRID | EML1 | https://thebiogrid.org/112705 |
| Gene Ontology (GO) | GO:0008017 (microtubule binding), GO:0005813 (centrosome), GO:0005929 (cilium), GO:0005819 (spindle) | https://www.ebi.ac.uk/QuickGO/ |
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