Protein:ENAH |
Protein Summary |
 Gene summary |
| Gene name: ENAH | ASpdb.0 ID: 55740 | Gene | Gene symbol | ENAH | Gene ID | 55740 |
| Gene name | ENAH actin regulator |
| Synonyms | ENA|MENA|NDPP1 |
| Cytomap | 1q42.12 |
| Type of gene | protein-coding |
| Description | protein enabled homologMena delta 11aenabled homolog |
| Modification date | 20240407 |
| UniProtAcc | Q8N8S7 |
| Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | ENAH | GO:0005829 | cytosol | - |
| Gene | ENAH | GO:0005886 | plasma membrane | - |
| Gene | ENAH | GO:0005925 | focal adhesion | - |
| Gene | ENAH | GO:0030054 | cell junction | - |
AS Summary |
| Information of the canonical protein with experimentally identified structure from PDB (2023). |
| UniProt Acc | File name | PDB ID | Method | Resolution | Chain | Start | End |
| Q8N8S7-1 | Q8N8S7-1_2iyb_A.pdb | 2IYB | X-ray | 2.35 | A | 1 | 113 |
| ASpdb's canonical and alternatively spliced isoform information. |
| accession_id | gene_name | canonical_id | alternative_id | canonical_length | alternative_length | canonical_start | canonical_end | type | originalSEQ | variationSEQ | alternative_start | alternative_end |
| Q8N8S7 | ENAH | Q8N8S7-1 | Q8N8S7-2 | 591 | 570 | 514 | 534 | Deletion | none | none | 513 | 513 |
| Q8N8S7 | ENAH | Q8N8S7-1 | Q8N8S7-3 | 591 | 533 | 268 | 304 | Deletion | none | none | 267 | 267 |
| Q8N8S7 | ENAH | Q8N8S7-1 | Q8N8S7-3 | 591 | 533 | 513 | 533 | Deletion | none | none | 475 | 475 |
| Multiple sequence alignment of our canonical and alternatively spliced ENAH |
| Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of ENAH |
| UniProt-id | ENSG | ENST | ENSP |
| Q8N8S7-1 | ENSG00000154380.19 | ENST00000366844.7 | ENSP00000355809.2 |
| Q8N8S7-2 | ENSG00000154380.19 | ENST00000366843.7 | ENSP00000355808.2 |
| UniProt-id | NM ID | NP ID |
| Q8N8S7-1 | NM_001008493.2 | NP_001008493.1 |
| Q8N8S7-2 | NM_018212.5 | NP_060682.2 |
| Amino acid sequences of our canonical and alternatively spliced ENAH |
| accession_id | Protein sequence |
| Q8N8S7-1 | MSEQSICQARAAVMVYDDANKKWVPAGGSTGFSRVHIYHHTGNNTFRVVGRKIQDHQVVINCAIPKGLKYNQATQTFHQWRDARQVYGLN FGSKEDANVFASAMMHALEVLNSQETGPTLPRQNSQLPAQVQNGPSQEELEIQRRQLQEQQRQKELERERLERERMERERLERERLERER LERERLEQEQLERERQERERQERLERQERLERQERLERQERLDRERQERQERERLERLERERQERERQEQLEREQLEWERERRISSAAAP ASVETPLNSVLGDSSASEPGLQAASQPAETPSQQGIVLGPLAPPPPPPLPPGPAQASVALPPPPGPPPPPPLPSTGPPPPPPPPPLPNQV PPPPPPPPAPPLPASGFFLASMSEDNRPLTGLAAAIAGAKLRKVSRMEDTSFPSGGNAIGVNSASSKTDTGRGNGPLPLGGSGLMEEMSA LLARRRRIAEKGSTIETEQKEDKGEDSEPVTSKASSTSTPEPTRKPWERTNTMNGSKSPVISRRDSPRKNQIVFDNRSYDSLHRPKSTPL |
| Q8N8S7-2 | MSEQSICQARAAVMVYDDANKKWVPAGGSTGFSRVHIYHHTGNNTFRVVGRKIQDHQVVINCAIPKGLKYNQATQTFHQWRDARQVYGLN FGSKEDANVFASAMMHALEVLNSQETGPTLPRQNSQLPAQVQNGPSQEELEIQRRQLQEQQRQKELERERLERERMERERLERERLERER LERERLEQEQLERERQERERQERLERQERLERQERLERQERLDRERQERQERERLERLERERQERERQEQLEREQLEWERERRISSAAAP ASVETPLNSVLGDSSASEPGLQAASQPAETPSQQGIVLGPLAPPPPPPLPPGPAQASVALPPPPGPPPPPPLPSTGPPPPPPPPPLPNQV PPPPPPPPAPPLPASGFFLASMSEDNRPLTGLAAAIAGAKLRKVSRMEDTSFPSGGNAIGVNSASSKTDTGRGNGPLPLGGSGLMEEMSA LLARRRRIAEKGSTIETEQKEDKGEDSEPVTSKASSTSTPEPTRKPWERTNTMNGSKSPVISRPKSTPLSQPSANGVQTEGLDYDRLKQD |
| Q8N8S7-3 | MSEQSICQARAAVMVYDDANKKWVPAGGSTGFSRVHIYHHTGNNTFRVVGRKIQDHQVVINCAIPKGLKYNQATQTFHQWRDARQVYGLN FGSKEDANVFASAMMHALEVLNSQETGPTLPRQNSQLPAQVQNGPSQEELEIQRRQLQEQQRQKELERERLERERMERERLERERLERER LERERLEQEQLERERQERERQERLERQERLERQERLERQERLDRERQERQERERLERLERERQERERQEQLEREQLEWERERRISSAGIV LGPLAPPPPPPLPPGPAQASVALPPPPGPPPPPPLPSTGPPPPPPPPPLPNQVPPPPPPPPAPPLPASGFFLASMSEDNRPLTGLAAAIA GAKLRKVSRMEDTSFPSGGNAIGVNSASSKTDTGRGNGPLPLGGSGLMEEMSALLARRRRIAEKGSTIETEQKEDKGEDSEPVTSKASST |
Protein Functional Features |
| Main function of this protein. (from UniProt) |
| ENAH (go to UniProt):Q8N8S7 |
| Retention analysis result of protein across 39 protein features of UniProt such as six molecule processing features, 13 region features, four site features, six amino acid modification features, two natural variation features, five experimental info features, and 3 secondary structure features. Here, because of limited space for viewing, we only show the protein feature retention information belong to the 13 regional features. All retention annotation result can be downloaded at * Minus value of BPloci means that the break pointn is located before the CDS. |
| - Retained protein feature among the 13 regional features. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| Q8N8S7 | Region | 221 | 379 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=268;End=304 |
| Q8N8S7 | Region | 391 | 588 | Note=EVH2 | Type=Deletion;Start=514;End=534 |
| Q8N8S7 | Region | 391 | 588 | Note=EVH2 | Type=Deletion;Start=513;End=533 |
| Q8N8S7 | Region | 405 | 549 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=514;End=534 |
| Q8N8S7 | Region | 405 | 549 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=513;End=533 |
| Q8N8S7 | Compositional bias | 271 | 303 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=268;End=304 |
| Q8N8S7 | Compositional bias | 522 | 549 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=514;End=534 |
| Q8N8S7 | Compositional bias | 522 | 549 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=513;End=533 |
Gene Isoform Structures and Expression Levels for ENAH |
| Gene structures of our canonical and alternative spliced genes of ENAH * Click on the image to open the UCSC genome browser with custom track showing this image in a new window. |
| Expression levels of gene isoforms across GTEx. |
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| Expression levels of gene isoforms across TCGA. |
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Protein Structures |
| PDB and CIF files of the predicted protein structures * Here we show the 3D structure of the proteins using Mol*. AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Model confidence is shown from the pLDDT values per residue. pLDDT corresponds to the model’s prediction of its score on the local Distance Difference Test. It is a measure of local accuracy (from AlphfaFold website). To color code individual residues, we transformed individual PDB files into CIF format. |
| 3D view using mol* of Q8N8S7-1 |
| 3D view using mol* of Q8N8S7-2 |
| 3D view using mol* of Q8N8S7-3 |
pLDDT Score Distribution |
| pLDDT score distribution of the predicted protein structures from AlphaFold2 * AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. |
| pLDDT distribution across the protein length of Q8N8S7-1 |
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| pLDDT distribution across the protein length of Q8N8S7-2 |
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| pLDDT distribution across the protein length of Q8N8S7-3 |
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Ramachandran Plot of Protein Structures |
| Ramachandran plot of the torsional angles - phi (φ)and psi (ψ) - of the residues (amino acids) contained in this protein peptide. |
| Ramachandran plot of Q8N8S7-1 |
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| Ramachandran plot of Q8N8S7-2 |
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| Ramachandran plot of Q8N8S7-3 |
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Potential Active Site Information |
| The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite. |
| UniProt-id | Site score | Size | D score | Volume | Exposure | Enclosure | Contact | Phobic | Philic | Balance | Don/Acc | Residues |
| Q8N8S7-1 | 0.52 | 13 | 0.461 | 59.339 | 0.838 | 0.582 | 0.767 | 0.528 | 0.695 | 0.759 | 0.994 | 34,36,38,49,51,53,56
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| Q8N8S7-2 | 0.982 | 115 | 0.981 | 260.337 | 0.534 | 0.671 | 0.947 | 0.428 | 1.11 | 0.385 | 0.738 | 198,201,202,205,206,208,209,212,400,401,402,403,40 4,405,406 |
| Q8N8S7-3 | 0.488 | 19 | 0.443 | 35.672 | 0.824 | 0.471 | 0.596 | 0.343 | 0.764 | 0.449 | 1.046 | 198,201,202,205,206,209,210,213
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Protein Structure and Feature Comparision |
| Protein Structure Comparision Using Template Modeling Scores (TM-score). |
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| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Canonical validated structure (PDB)(green) |
| 3D view using mol* of Q8N8S7-1_Q8N8S7-1_2iyb_A.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical validated structure (PDB)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of Q8N8S7-1_2iyb_A_Q8N8S7-2.pdb |
| 3D view using mol* of Q8N8S7-1_2iyb_A_Q8N8S7-3.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of Q8N8S7-1_Q8N8S7-2.pdb |
| 3D view using mol* of Q8N8S7-1_Q8N8S7-3.pdb |
| Protein Feature Comparison of the protein sequendary structures among the protiens. |
| ./stats/secondary_structure/figure/Q8N8S7-1_vs_Q8N8S7-2.png |
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| ./stats/secondary_structure/figure/Q8N8S7-1_vs_Q8N8S7-3.png |
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| Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens. |
| ./stats/relative_asa/Q8N8S7-1_vs_Q8N8S7-2.png |
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| ./stats/relative_asa/Q8N8S7-1_vs_Q8N8S7-3.png |
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Protein-Protein Interaction |
| Interactors from UniProt. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| Interactors from STRING. |
| Gene name | Interactors |
Related Drugs to ENAH |
| Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
Related Diseases to ENAH |
| Previous studies relating to the alternative splicing of ENAH and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
| ENAH | 23129656 | Splicing program of human MENA produces a previously undescribed isoform associated with invasive, mesenchymal-like breast tumors. | "Human mena (hMENA), a member of the actin cytoskeleton regulators Ena/VASP, is overexpressed in high-risk preneoplastic lesions and in primary breast tumors and has been identified as playing a role in invasiveness and poor prognosis in breast cancers that express HER2. Here we identify a unique isoform, hMENAΔv6, derived from the hMENA alternative splicing program. In an isogenic model of human breast cancer progression, we show that hMENA(11a) is expressed in premalignant cells, whereas hMENAΔv6 expression is restricted to invasive cancer cells. ""Reversion"" of the malignant phenotype leads to concurrent down-regulation of all hMENA isoforms. In breast cancer cell lines, isoform-specific hMENA overexpression or knockdown revealed that in the absence of hMENA(11a), overexpression of hMENAΔv6 increased cell invasion, whereas overexpression of hMENA(11a) reduced the migratory and invasive ability of these cells. hMENA(11a) splicing was shown to be dependent on the epithelial regulator of splicing 1 (ESRP1), and forced expression of ESRP1 in invasive mesenchymal breast cancer cells caused a phenotypic switch reminiscent of a mesenchymal-to-epithelial transition (MET) characterized by changes in the cytoskeletal architecture, reexpression of hMENA(11a), and a reduction in cell invasion. hMENA-positive primary breast tumors, which are hMENA(11a)-negative, are more frequently E-cadherin low in comparison with tumors expressing hMENA(11a). These data suggest that polarized and growth-arrested cellular architecture correlates with absence of alternative hMENA isoform expression, and that the hMENA splicing program is relevant to malignant progression in invasive disease." | D001943 | Breast Neoplasms |
| ENAH | 23129656 | Splicing program of human MENA produces a previously undescribed isoform associated with invasive, mesenchymal-like breast tumors. | "Human mena (hMENA), a member of the actin cytoskeleton regulators Ena/VASP, is overexpressed in high-risk preneoplastic lesions and in primary breast tumors and has been identified as playing a role in invasiveness and poor prognosis in breast cancers that express HER2. Here we identify a unique isoform, hMENAΔv6, derived from the hMENA alternative splicing program. In an isogenic model of human breast cancer progression, we show that hMENA(11a) is expressed in premalignant cells, whereas hMENAΔv6 expression is restricted to invasive cancer cells. ""Reversion"" of the malignant phenotype leads to concurrent down-regulation of all hMENA isoforms. In breast cancer cell lines, isoform-specific hMENA overexpression or knockdown revealed that in the absence of hMENA(11a), overexpression of hMENAΔv6 increased cell invasion, whereas overexpression of hMENA(11a) reduced the migratory and invasive ability of these cells. hMENA(11a) splicing was shown to be dependent on the epithelial regulator of splicing 1 (ESRP1), and forced expression of ESRP1 in invasive mesenchymal breast cancer cells caused a phenotypic switch reminiscent of a mesenchymal-to-epithelial transition (MET) characterized by changes in the cytoskeletal architecture, reexpression of hMENA(11a), and a reduction in cell invasion. hMENA-positive primary breast tumors, which are hMENA(11a)-negative, are more frequently E-cadherin low in comparison with tumors expressing hMENA(11a). These data suggest that polarized and growth-arrested cellular architecture correlates with absence of alternative hMENA isoform expression, and that the hMENA splicing program is relevant to malignant progression in invasive disease." | D018450 | Disease Progression |
| ENAH | 23129656 | Splicing program of human MENA produces a previously undescribed isoform associated with invasive, mesenchymal-like breast tumors. | "Human mena (hMENA), a member of the actin cytoskeleton regulators Ena/VASP, is overexpressed in high-risk preneoplastic lesions and in primary breast tumors and has been identified as playing a role in invasiveness and poor prognosis in breast cancers that express HER2. Here we identify a unique isoform, hMENAΔv6, derived from the hMENA alternative splicing program. In an isogenic model of human breast cancer progression, we show that hMENA(11a) is expressed in premalignant cells, whereas hMENAΔv6 expression is restricted to invasive cancer cells. ""Reversion"" of the malignant phenotype leads to concurrent down-regulation of all hMENA isoforms. In breast cancer cell lines, isoform-specific hMENA overexpression or knockdown revealed that in the absence of hMENA(11a), overexpression of hMENAΔv6 increased cell invasion, whereas overexpression of hMENA(11a) reduced the migratory and invasive ability of these cells. hMENA(11a) splicing was shown to be dependent on the epithelial regulator of splicing 1 (ESRP1), and forced expression of ESRP1 in invasive mesenchymal breast cancer cells caused a phenotypic switch reminiscent of a mesenchymal-to-epithelial transition (MET) characterized by changes in the cytoskeletal architecture, reexpression of hMENA(11a), and a reduction in cell invasion. hMENA-positive primary breast tumors, which are hMENA(11a)-negative, are more frequently E-cadherin low in comparison with tumors expressing hMENA(11a). These data suggest that polarized and growth-arrested cellular architecture correlates with absence of alternative hMENA isoform expression, and that the hMENA splicing program is relevant to malignant progression in invasive disease." | D009361 | Neoplasm Invasiveness |
Clinically important variants in ENAH |
| (ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
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