Gene
yes1
- ID
- ZDB-GENE-050126-1
- Name
- YES proto-oncogene 1, Src family tyrosine kinase
- Symbol
- yes1 Nomenclature History
- Previous Names
- None
- Type
- protein_coding_gene
- Location
- Chr: 2 Mapping Details/Browsers
- Description
- Enables protein tyrosine kinase activity. Acts upstream of or within several processes, including adherens junction maintenance; convergent extension involved in gastrulation; and protein autophosphorylation. Predicted to be located in several cellular components, including anchoring junction; centrosome; and cytosol. Predicted to be active in plasma membrane. Orthologous to human YES1 (YES proto-oncogene 1, Src family tyrosine kinase).
- Genome Resources
- Note
- None
- Comparative Information
-
- All Expression Data
- 6 figures from 4 publications
- Cross-Species Comparison
- High Throughput Data
- Thisse Expression Data
- No data available
Wild Type Expression Summary
- All Phenotype Data
- 1 Figure from Sempou et al., 2016
- Cross-Species Comparison
- Alliance
Phenotype Summary
Mutations
| Allele | Type | Localization | Consequence | Mutagen | Supplier |
|---|---|---|---|---|---|
| la010373Tg | Transgenic insertion | Unknown | Unknown | DNA |
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| Targeting Reagent | Created Alleles | Citations |
|---|---|---|
| MO1-yes1 | N/A | (8) |
| MO2-yes1 | N/A | Yoo et al., 2012 |
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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 |
| Domain | IPR000719 | Protein kinase domain |
| Domain | IPR000980 | SH2 domain |
| Domain | IPR001245 | Serine-threonine/tyrosine-protein kinase, catalytic domain |
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Domain Details Per Protein
| Protein | Additional Resources | Length | Non-receptor tyrosine kinases involved in cell signaling | Protein kinase, ATP binding site | Protein kinase domain | Protein kinase-like domain superfamily | Serine-threonine/tyrosine-protein kinase, catalytic domain | SH2 domain | SH2 domain superfamily | SH3 domain | SH3-like domain superfamily | Tyrosine-protein kinase, active site | Tyrosine-protein kinase, catalytic domain | Tyrosine-protein kinase Yes, SH3 domain |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| UniProtKB:A1A5H8 | InterPro | 546 |
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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 | CH211-212M21 | ZFIN Curated Data | |
| Encodes | cDNA | MGC:152910 | ZFIN Curated Data |
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| Type | Accession # | Sequence | Length (nt/aa) | Analysis |
|---|---|---|---|---|
| RNA | RefSeq:NM_001013270 (1) | 4545 nt | ||
| Genomic | GenBank:BX927088 (1) | 201361 nt | ||
| Polypeptide | UniProtKB:A1A5H8 (1) | 546 aa |
| Species | Symbol | Chromosome | Accession # | Evidence |
|---|---|---|---|---|
| Human | YES1 | 18 | Amino acid sequence comparison (2) |
- Giffen, K.P., Liu, H., Kramer, K.L., He, D.Z. (2019) Expression of Protein-Coding Gene Orthologs in Zebrafish and Mouse Inner Ear Non-sensory Supporting Cells. Frontiers in neuroscience. 13:1117
- 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
- Sempou, E., Biasini, E., Pinzón-Olejua, A., Harris, D.A., Málaga-Trillo, E. (2016) Activation of zebrafish Src family kinases by the prion protein is an amyloid-β-sensitive signal that prevents the endocytosis and degradation of E-cadherin/β-catenin complexes in vivo. Molecular neurodegeneration. 11:18
- 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
- Lin, C., Lin, C.N., Wang, Y.C., Liu, F.Y., Chien, Y.W., Chuang, Y.J., Lan, C.Y., Hsieh, W.P., Chen, B.S. (2014) Robustness analysis on interspecies interaction network for iron and glucose competition between Candida albicans and zebrafish during infection. BMC systems biology. 8 Suppl 5:S6
- 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
- Yoo, S.K., Freisinger, C.M., Lebert, D.C., and Huttenlocher, A. (2012) Early redox, Src family kinase, and calcium signaling integrate wound responses and tissue regeneration in zebrafish. The Journal of cell biology. 199(2):225-234
- Wong, K.S., Proulx, K., Rost, M.S., and Sumanas, S. (2009) Identification of vasculature-specific genes by microarray analysis of etsrp/etv2 overexpressing zebrafish embryos. Developmental Dynamics : an official publication of the American Association of Anatomists. 238(7):1836-1850
- Lemeer, S., Jopling, C., Gouw, J.W., Mohammed, S., Heck, A.J., Slijper, M., and den Hertog, J. (2008) Comparative phosphoproteomics of zebrafish Fyn/Yes morpholino knockdown embryos. Molecular & cellular proteomics : MCP. 7(11):2176-2187
- Huang, H., Lu, F.I., Jia, S., Meng, S., Cao, Y., Wang, Y., Ma, W., Yin, K., Wen, Z., Peng, J., Thisse, C., Thisse, B., and Meng, A. (2007) Amotl2 is essential for cell movements in zebrafish embryo and regulates c-Src translocation. Development (Cambridge, England). 134(5):979-988
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