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mutLBSgeneDB |
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| Gene summary for EPHA4 |
 Gene summary |
| Basic gene Info. | Gene symbol | EPHA4 |
| Gene name | EPH receptor A4 | |
| Synonyms | HEK8|SEK|TYRO1 | |
| Cytomap | UCSC genome browser: 2q36.1 | |
| Type of gene | protein-coding | |
| RefGenes | NM_004438.3, | |
| Description | EK8EPH-like kinase 8TYRO1 protein tyrosine kinaseephrin type-A receptor 4receptor protein-tyrosine kinase HEK8tyrosine-protein kinase TYRO1tyrosine-protein kinase receptor SEK | |
| Modification date | 20141207 | |
| dbXrefs | MIM : 602188 | |
| HGNC : HGNC | ||
| Ensembl : ENSG00000116106 | ||
| HPRD : 03719 | ||
| Protein | UniProt: P54764 go to UniProt's Cross Reference DB Table | |
| Expression | CleanEX: HS_EPHA4 | |
| BioGPS: 2043 | ||
| Pathway | NCI Pathway Interaction Database: EPHA4 | |
| KEGG: EPHA4 | ||
| REACTOME: EPHA4 | ||
| Pathway Commons: EPHA4 | ||
| Context | iHOP: EPHA4 | |
| ligand binding site mutation search in PubMed: EPHA4 | ||
| UCL Cancer Institute: EPHA4 | ||
| Assigned class in mutLBSgeneDB | A: This gene has a literature evidence and it belongs to targetable_mutLBSgenes. | |
| References showing study about ligand binding site mutation for EPHA4. | 1. "Qin H, Noberini R, Huan X, Shi J, Pasquale EB, Song J. Structural characterization of the EphA4-Ephrin-B2 complex reveals new features enabling Eph-ephrin binding promiscuity. J Biol Chem. 2010 Jan 1;285(1):644-54. doi: 10.1074/jbc.M109.064824. Epub 2009 Oct 29. PubMed PMID: 19875447; PubMed Central PMCID: PMC2804212. " 19875447 | |
| Gene ontology having evidence of Inferred from Direct Assay (IDA) from Entrez |
| GO ID | GO Term | PubMed ID | GO:0018108 | peptidyl-tyrosine phosphorylation | 12775584 | GO:0046777 | protein autophosphorylation | 12775584 | GO:2001108 | positive regulation of Rho guanyl-nucleotide exchange factor activity | 12775584 |
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| Ligand binding site mutations for EPHA4 |
| Lollipop-style diagram of mutations at LBS in amino-acid sequence. We represented ligand binding site mutations only. (You can see big image via clicking.)  : non-synonymous mutation on LBS, Circle size denotes number of samples. |
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| Cancer type specific mutLBS sorted by frequency |
| LBS | AAchange of nsSNV | Cancer type | # samples | K889 | T891I | COAD | 1 | M115 | V114I | GBM | 1 | V57 | E56A | HNSC | 1 | W45 | I46R | LUAD | 1 | I59 | D61N | SKCM | 1 | R198 | R198H | UCEC | 1 | Q71 | Y70C | UCEC | 1 |
| cf) Cancer type abbreviation. BLCA: Bladder urothelial carcinoma, BRCA: Breast invasive carcinoma, CESC: Cervical squamous cell carcinoma and endocervical adenocarcinoma, COAD: Colon adenocarcinoma, GBM: Glioblastoma multiforme, LGG: Brain lower grade glioma, HNSC: Head and neck squamous cell carcinoma, KICH: Kidney chromophobe, KIRC: Kidney renal clear cell carcinoma, KIRP: Kidney renal papillary cell carcinoma, LAML: Acute myeloid leukemia, LUAD: Lung adenocarcinoma, LUSC: Lung squamous cell carcinoma, OV: Ovarian serous cystadenocarcinoma, PAAD: Pancreatic adenocarcinoma, PRAD: Prostate adenocarcinoma, SKCM: Skin cutaneous melanoma, STAD: Stomach adenocarcinoma, THCA: Thyroid carcinoma, UCEC: Uterine corpus endometrial carcinoma. |
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| Protein structure related information for EPHA4 |
| Relative protein structure stability change (ΔΔE) using Mupro 1.1 Mupro score denotes assessment of the effect of mutations on thermodynamic stability. (ΔΔE<0: mutation decreases stability, ΔΔE>0: mutation increases stability) |
 : nsSNV at non-LBS : nsSNV at LBS |
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| nsSNVs sorted by the relative stability change of protein structure by each mutation Blue: mutations of positive stability change. and red : the most recurrent mutation for this gene. |
| LBS | AAchange of nsSNV | Relative stability change | M115 | V114I | -1.6322247 | R198 | R198H | -1.4746955 | V57 | E56A | -1.3415911 | I59 | D61N | -0.83498955 | W45 | I46R | -0.63847927 | K889 | T891I | -0.46983852 | Q71 | Y70C | -0.45926896 |
| (MuPro1.1: Jianlin Cheng et al., Prediction of Protein Stability Changes for Single-Site Mutations Using Support Vector Machines, PROTEINS: Structure, Function, and Bioinformatics. 2006, 62:1125-1132) |
| Structure image for EPHA4 from PDB |
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| Differential gene expression and gene-gene network for EPHA4 |
| Differential gene expression between mutated and non-mutated LBS samples in all 16 major cancer types |
| Differential co-expressed gene network based on protein-protein interaction data (CePIN) |
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| Phenotype information for EPHA4 |
| Gene level disease information (DisGeNet) |
| Disease ID | Disease name | # PubMed | Association type |
| Mutation level pathogenic information (ClinVar annotation) |
| Allele ID | AA change | Clinical significance | Origin | Phenotype IDs |
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| Pharmacological information for EPHA4 |
| Gene expression profile of anticancer drug treated cell-lines (CCLE) Heatmap showing the correlation between gene expression and drug response across all the cell-lines. We chose the top 20 among 138 drugs.We used Pearson's correlation coefficient. |
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| Gene-centered drug-gene interaction network |
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| Drug information targeting mutLBSgene (Approved drugs only) |
| Drug status | DrugBank ID | Name | Type | Drug structure |
| Gene-centered ligand-gene interaction network |
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| Ligands binding to mutated ligand binding site of EPHA4 go to BioLip |
| Ligand ID | Ligand short name | Ligand long name | PDB ID | PDB name | mutLBS | III | Peptide ligand (ALA,PRO,TYR,CYS,VAL,TYR,ARG,BAL,SER,TRP,SER,CYS,NH2) | 4w4z | A | I59 Q71 | III | Peptide ligand (ALA,PRO,TYR,CYS,VAL,TYR,ARG,BAL,SER,TRP,SER,CYS,NH2) | 4w4z | B | I59 Q71 | III | Peptide ligand (ALA,PRO,TYR,CYS,VAL,TYR,ARG,BAL,SER,TRP,SER,CYS,NH2) | 4w4z | C | I59 Q71 | III | Peptide ligand (ALA,PRO,TYR,CYS,VAL,TYR,ARG,BAL,SER,TRP,SER,CYS,NH2) | 4w4z | D | I59 Q71 | III | Peptide ligand (ALA,PRO,TYR,CYS,VAL,TYR,ARG,GLY,SER,TRP,SER,CYS) | 4w50 | C | I59 Q71 | III | Peptide ligand (ALA,PRO,TYR,CYS,VAL,TYR,ARG,GLY,SER,TRP,SER,CYS) | 4w50 | D | I59 Q71 | POL | PROPAN-1-OL | 2wo1 | A | R198 | BU2 | BUTANE-1,3-DIOL | 4w50 | D | R198 | III | Peptide ligand (ALA,PRO,TYR,CYS,VAL,TYR,ARG,GLY,SER,TRP,SER,CYS) | 4w50 | B | V57 I59 Q71 | III | Peptide ligand (ALA,PRO,TYR,CYS,VAL,TYR,ARG,GLY,SER,TRP,SER,CYS) | 4w50 | A | V57 I59 Q71 M115 | POL | PROPAN-1-OL | 2wo1 | A | W45 |
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| Conservation information for LBS of EPHA4 |
| Multiple alignments for P54764 in multiple species |
| LBS | AA sequence | # species | Species | A193 | VGACIALVSVR | 3 | Homo sapiens, Gallus gallus, Mus musculus | A193 | QGICLSLLNVK | 1 | Caenorhabditis elegans | C191 | QDVGACIALVS | 3 | Homo sapiens, Gallus gallus, Mus musculus | C191 | EEQGICLSLLN | 1 | Caenorhabditis elegans | C73 | RTYQVCNVMEP | 2 | Homo sapiens, Gallus gallus | C73 | RAYVTCNYDMI | 1 | Caenorhabditis elegans | C73 | RTYQVCNVMEA | 1 | Mus musculus | D151 | TIA-ADESFTQ | 3 | Homo sapiens, Gallus gallus, Mus musculus | D151 | RLARSNSNMTT | 1 | Caenorhabditis elegans | D172 | NTEIRDVGPLS | 2 | Homo sapiens, Mus musculus | D172 | DSDTKTIR--- | 1 | Caenorhabditis elegans | D172 | NTEVRDVGPLS | 1 | Gallus gallus | D35 | EVTLLDSRSVQ | 3 | Homo sapiens, Gallus gallus, Mus musculus | D35 | QEVLFDLSKVG | 1 | Caenorhabditis elegans | E100 | QRVYIEIKFTL | 3 | Homo sapiens, Gallus gallus, Mus musculus | E100 | RRIYIELLFNT | 1 | Caenorhabditis elegans | E169 | MKLNTEIRDVG | 2 | Homo sapiens, Mus musculus | E169 | MEIDSDTKTIR | 1 | Caenorhabditis elegans | E169 | MKLNTEVRDVG | 1 | Gallus gallus | E30 | VYPANEVTLLD | 3 | Homo sapiens, Gallus gallus, Mus musculus | E30 | --TSHQEVLFD | 1 | Caenorhabditis elegans | E77 | VCNVMEPSQNN | 2 | Homo sapiens, Gallus gallus | E77 | TCNYDMINPSN | 1 | Caenorhabditis elegans | E77 | VCNVMEASQNN | 1 | Mus musculus | I159 | FTQVDIGDRIM | 3 | Homo sapiens, Gallus gallus, Mus musculus | I159 | MTTETLG---M | 1 | Caenorhabditis elegans | I170 | KLNTEIRDVGP | 2 | Homo sapiens, Mus musculus | I170 | EIDSDTKTIR- | 1 | Caenorhabditis elegans | I170 | KLNTEVRDVGP | 1 | Gallus gallus | I192 | DVGACIALVSV | 3 | Homo sapiens, Gallus gallus, Mus musculus | I192 | EQGICLSLLNV | 1 | Caenorhabditis elegans | I59 | WEEVSIMDEKN | 3 | Homo sapiens, Gallus gallus, Mus musculus | I59 | WRNPAATDEKH | 1 | Caenorhabditis elegans | K102 | VYIEIKFTLRD | 3 | Homo sapiens, Gallus gallus, Mus musculus | K102 | IYIELLFNTRD | 1 | Caenorhabditis elegans | K179 | GPLSKKGFYLA | 3 | Homo sapiens, Gallus gallus, Mus musculus | K179 | R--------IA | 1 | Caenorhabditis elegans | K889 | NPNSLKRTGSE | 2 | Gallus gallus, Mus musculus | K889 | NPNSLKRTGTE | 1 | Homo sapiens | K889 | QPTLIEHDPGE | 1 | Caenorhabditis elegans | L105 | EIKFTLRDCNS | 3 | Homo sapiens, Gallus gallus, Mus musculus | L105 | ELLFNTRDCDA | 1 | Caenorhabditis elegans | L111 | RDCNSLPGVMG | 3 | Homo sapiens, Gallus gallus, Mus musculus | L111 | RDCDAYLNPKS | 1 | Caenorhabditis elegans | L166 | DRIMKLNTEIR | 2 | Homo sapiens, Mus musculus | L166 | ---MEIDSDTK | 1 | Caenorhabditis elegans | L166 | DRIMKLNTEVR | 1 | Gallus gallus | L194 | GACIALVSVRV | 3 | Homo sapiens, Gallus gallus, Mus musculus | L194 | GICLSLLNVKI | 1 | Caenorhabditis elegans | M115 | SLPGVMGTCKE | 3 | Homo sapiens, Gallus gallus, Mus musculus | M115 | AYLNPKS-CKE | 1 | Caenorhabditis elegans | M164 | IGDRIMKLNTE | 3 | Homo sapiens, Gallus gallus, Mus musculus | M164 | LG---MEIDSD | 1 | Caenorhabditis elegans | M76 | QVCNVMEPSQN | 2 | Homo sapiens, Gallus gallus | M76 | VTCNYDMINPS | 1 | Caenorhabditis elegans | M76 | QVCNVMEASQN | 1 | Mus musculus | N74 | TYQVCNVMEPS | 2 | Homo sapiens, Gallus gallus | N74 | AYVTCNYDMIN | 1 | Caenorhabditis elegans | N74 | TYQVCNVMEAS | 1 | Mus musculus | P112 | DCNSLPGVMGT | 3 | Homo sapiens, Gallus gallus, Mus musculus | P112 | DCDAYLNPKS- | 1 | Caenorhabditis elegans | Q71 | PIRTYQVCNVM | 3 | Homo sapiens, Gallus gallus, Mus musculus | Q71 | NQRAYVTCNYD | 1 | Caenorhabditis elegans | R106 | IKFTLRDCNSL | 3 | Homo sapiens, Gallus gallus, Mus musculus | R106 | LLFNTRDCDAY | 1 | Caenorhabditis elegans | R162 | VDIGDRIMKLN | 3 | Homo sapiens, Gallus gallus, Mus musculus | R162 | ETLG---MEID | 1 | Caenorhabditis elegans | R198 | ALVSVRVFYKK | 3 | Homo sapiens, Gallus gallus, Mus musculus | R198 | SLLNVKIYYRI | 1 | Caenorhabditis elegans | R37 | TLLDSRSVQGE | 3 | Homo sapiens, Gallus gallus, Mus musculus | R37 | VLFDLSKVGSD | 1 | Caenorhabditis elegans | R68 | KNTPIRTYQVC | 3 | Homo sapiens, Gallus gallus, Mus musculus | R68 | KHANQRAYVTC | 1 | Caenorhabditis elegans | R96 | REGAQRVYIEI | 3 | Homo sapiens, Gallus gallus, Mus musculus | R96 | VKTARRIYIEL | 1 | Caenorhabditis elegans | S153 | A-ADESFTQVD | 3 | Homo sapiens, Gallus gallus, Mus musculus | S153 | ARSNSNMTTET | 1 | Caenorhabditis elegans | S196 | CIALVSVRVFY | 3 | Homo sapiens, Gallus gallus, Mus musculus | S196 | CLSLLNVKIYY | 1 | Caenorhabditis elegans | S36 | VTLLDSRSVQG | 3 | Homo sapiens, Gallus gallus, Mus musculus | S36 | EVLFDLSKVGS | 1 | Caenorhabditis elegans | T104 | IEIKFTLRDCN | 3 | Homo sapiens, Gallus gallus, Mus musculus | T104 | IELLFNTRDCD | 1 | Caenorhabditis elegans | T90 | RTDWITREGAQ | 2 | Homo sapiens, Mus musculus | T90 | FSHFIEVKTAR | 1 | Caenorhabditis elegans | T90 | RTDWIPREGAQ | 1 | Gallus gallus | V195 | ACIALVSVRVF | 3 | Homo sapiens, Gallus gallus, Mus musculus | V195 | ICLSLLNVKIY | 1 | Caenorhabditis elegans | V57 | GGWEEVSIMDE | 3 | Homo sapiens, Gallus gallus, Mus musculus | V57 | ETWRNPAATDE | 1 | Caenorhabditis elegans | V75 | YQVCNVMEPSQ | 2 | Homo sapiens, Gallus gallus | V75 | YVTCNYDMINP | 1 | Caenorhabditis elegans | V75 | YQVCNVMEASQ | 1 | Mus musculus | W45 | QGELGWIASPL | 3 | Homo sapiens, Gallus gallus, Mus musculus | W45 | GSDLKWDQVSL | 1 | Caenorhabditis elegans | W88 | WLRTDWITREG | 2 | Homo sapiens, Mus musculus | W88 | WLFSHFIEVKT | 1 | Caenorhabditis elegans | W88 | WLRTDWIPREG | 1 | Gallus gallus | Y98 | GAQRVYIEIKF | 3 | Homo sapiens, Gallus gallus, Mus musculus | Y98 | TARRIYIELLF | 1 | Caenorhabditis elegans |
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