Gene
epha4l
- ID
- ZDB-GENE-990415-61
- Name
- eph receptor A4, like
- Symbol
- epha4l Nomenclature History
- Previous Names
-
- epha4c (1)
- rtk4
- Type
- protein_coding_gene
- Location
- Chr: 15 Mapping Details/Browsers
- Description
- Predicted to enable transmembrane-ephrin receptor activity. Predicted to be involved in axon guidance and ephrin receptor signaling pathway. Predicted to act upstream of or within cell adhesion; nervous system development; and protein phosphorylation. Predicted to be located in early endosome. Predicted to be active in dendrite and plasma membrane. Is expressed in liver.
- Genome Resources
- Note
- None
- Comparative Information
-
- All Expression Data
- 2 figures from 2 publications
- Cross-Species Comparison
- High Throughput Data
- Thisse Expression Data
- No data available
Wild Type Expression Summary
- All Phenotype Data
- No data available
- Cross-Species Comparison
- Alliance
Phenotype Summary
Mutations
Allele | Type | Localization | Consequence | Mutagen | Supplier |
---|---|---|---|---|---|
la019409Tg | Transgenic insertion | Unknown | Unknown | DNA | |
la019410Tg | Transgenic insertion | Unknown | Unknown | DNA | |
sa15788 | Allele with one point mutation | Unknown | Premature Stop | ENU | |
sa22719 | Allele with one point mutation | Unknown | Splice Site | ENU | |
sa22720 | Allele with one point mutation | Unknown | Premature Stop | ENU | |
sa28531 | Allele with one point mutation | Unknown | Splice Site | ENU |
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Human Disease
Domain, Family, and Site Summary
Type | InterPro ID | Name |
---|---|---|
Active_site | IPR008266 | Tyrosine-protein kinase, active site |
Binding_site | IPR017441 | Protein kinase, ATP binding site |
Conserved_site | IPR001426 | Tyrosine-protein kinase, receptor class V, conserved site |
Domain | IPR000719 | Protein kinase domain |
Domain | IPR001090 | Ephrin receptor ligand binding domain |
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Domain Details Per Protein
Protein | Additional Resources | Length | Ephrin receptor ligand binding domain | Ephrin receptor, transmembrane domain | Ephrin receptor type-A /type-B | Ephrin receptor tyrosine kinases | Ephrin type-A receptor 4, SAM domain | Fibronectin type III | Fibronectin type III superfamily | Galactose-binding-like domain superfamily | Growth factor receptor cysteine-rich domain superfamily | Immunoglobulin-like fold | Protein kinase, ATP binding site | Protein kinase domain | Protein kinase-like domain superfamily | Serine-threonine/tyrosine-protein kinase, catalytic domain | Sterile alpha motif domain | Sterile alpha motif/pointed domain superfamily | Tyrosine-protein kinase, active site | Tyrosine-protein kinase, catalytic domain | Tyrosine-protein kinase ephrin type A/B receptor-like | Tyrosine-protein kinase, receptor class V, conserved site |
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
UniProtKB:F1QJD4 | InterPro | 988 |
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Type | Name | Annotation Method | Has Havana Data | Length (nt) | Analysis |
---|---|---|---|---|---|
mRNA |
epha4l-201
(1)
|
Ensembl | 8,510 nt |
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Interactions and Pathways
No data available
Plasmids
No data available
No data available
Relationship | Marker Type | Marker | Accession Numbers | Citations |
---|---|---|---|---|
Contained in | BAC | CH211-191A16 | ZFIN Curated Data | |
Contained in | BAC | DKEY-96G2 | ZFIN Curated Data |
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Type | Accession # | Sequence | Length (nt/aa) | Analysis |
---|---|---|---|---|
RNA | RefSeq:XM_682606 (1) | 5724 nt | ||
Genomic | GenBank:CR925728 (2) | 151799 nt | ||
Polypeptide | UniProtKB:F1QJD4 (1) | 988 aa |
No data available
- Hu, T., Liu, L., Wang, H., Yang, M., Xu, B., Xie, H., Lin, Z., Jin, X., Wang, P., Liu, Y., Sun, H., Liu, S. (2024) RCAN family member 3 deficiency contributes to noncompaction of the ventricular myocardium. Journal of genetics and genomics = Yi chuan xue bao. 51(5):543-553
- Cao, S., Dong, Z., Dong, X., Jia, W., Zhou, F., Zhao, Q. (2023) Zebrafish sox2 Is Required for the Swim Bladder Inflation by Controlling the Swim-Up Behavior. Zebrafish. 20:101810-18
- Keatinge, M., Tsarouchas, T.M., Munir, T., Porter, N.J., Larraz, J., Gianni, D., Tsai, H.H., Becker, C.G., Lyons, D.A., Becker, T. (2021) CRISPR gRNA phenotypic screening in zebrafish reveals pro-regenerative genes in spinal cord injury. PLoS Genetics. 17:e1009515
- Bayés, À., Collins, M.O., Reig-Viader, R., Gou, G., Goulding, D., Izquierdo, A., Choudhary, J.S., Emes, R.D., Grant, S.G. (2017) Evolution of complexity in the zebrafish synapse proteome. Nature communications. 8:14613
- Wang, J., Leng, X., Wang, G., Wan, X., Cao, H. (2017) The construction of intrahepatic cholangiocarcinoma model in zebrafish. Scientific Reports. 7:13419
- Elkon, R., Milon, B., Morrison, L., Shah, M., Vijayakumar, S., Racherla, M., Leitch, C.C., Silipino, L., Hadi, S., Weiss-Gayet, M., Barras, E., Schmid, C.D., Ait-Lounis, A., Barnes, A., Song, Y., Eisenman, D.J., Eliyahu, E., Frolenkov, G.I., Strome, S.E., Durand, B., Zaghloul, N.A., Jones, S.M., Reith, W., Hertzano, R. (2015) RFX transcription factors are essential for hearing in mice. Nature communications. 6:8549
- Challa, A.K., and Chatti, K. (2013) Conservation and Early Expression of Zebrafish Tyrosine Kinases Support the Utility of Zebrafish as a Model for Tyrosine Kinase Biology. Zebrafish. 10(3):264-74
- Crespo, B., Lan-Chow-Wing, O., Rocha, A., Zanuy, S., Gómez, A. (2013) foxl2 and foxl3 are two ancient paralogs that remain fully functional in teleosts. General and comparative endocrinology. 194:81-93
- Varshney, G.K., Lu, J., Gildea, D., Huang, H., Pei, W., Yang, Z., Huang, S.C., Schoenfeld, D.S., Pho, N., Casero, D., Hirase, T., Mosbrook-Davis, D.M., Zhang, S., Jao, L.E., Zhang, B., Woods, I.G., Zimmerman, S., Schier, A.F., Wolfsberg, T., Pellegrini, M., Burgess, S.M., and Lin, S. (2013) A large-scale zebrafish gene knockout resource for the genome-wide study of gene function. Genome research. 23(4):727-735
- Wang, D., Jao, L.E., Zheng, N., Dolan, K., Ivey, J., Zonies, S., Wu, X., Wu, K., Yang, H., Meng, Q., Zhu, Z., Zhang, B., Lin, S., and Burgess, S.M. (2007) Efficient genome-wide mutagenesis of zebrafish genes by retroviral insertions. Proceedings of the National Academy of Sciences of the United States of America. 104(30):12428-12433
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