Gene
aatkb
- ID
- ZDB-GENE-100812-6
- Name
- apoptosis-associated tyrosine kinase b
- Symbol
- aatkb Nomenclature History
- Previous Names
- None
- Type
- protein_coding_gene
- Location
- Chr: 12 Mapping Details/Browsers
- Description
- Predicted to enable protein tyrosine kinase activity. Predicted to be involved in brain development and neuron apoptotic process. Predicted to act upstream of or within protein phosphorylation. Predicted to be located in membrane. Orthologous to human AATK (apoptosis associated tyrosine kinase).
- Genome Resources
- Note
- None
- Comparative Information
-
- All Expression Data
- 1 figure from Challa et al., 2013
- 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 |
---|---|---|---|---|---|
la027354Tg | Transgenic insertion | Unknown | Unknown | DNA | |
sa11207 | Allele with one point mutation | Unknown | Premature Stop | ENU | |
sa19043 | Allele with one point mutation | Unknown | Premature Stop | ENU | |
sa22160 | Allele with one point mutation | Unknown | Premature Stop | ENU | |
sa35358 | Allele with one point mutation | Unknown | Splice Site | ENU | |
sa42084 | Allele with one point mutation | Unknown | Premature Stop | ENU | |
sa45475 | Allele with one point mutation | Unknown | Premature Stop | ENU |
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No data available
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 | IPR001245 | Serine-threonine/tyrosine-protein kinase, catalytic domain |
Domain | IPR020635 | Tyrosine-protein kinase, catalytic domain |
Homologous_superfamily | IPR011009 | Protein kinase-like domain superfamily |
Domain Details Per Protein
Protein | Additional Resources | Length | Protein kinase, ATP binding site | Protein kinase domain | Protein kinase-like domain superfamily | Serine-threonine/tyrosine-protein kinase, catalytic domain | Tyrosine-protein kinase, active site | Tyrosine-protein kinase, catalytic domain |
---|---|---|---|---|---|---|---|---|
UniProtKB:A0A8M9QET8 | InterPro | 1572 | ||||||
UniProtKB:A0A8N7TCQ8 | InterPro | 1657 | ||||||
UniProtKB:A0A8M9Q963 | InterPro | 1657 | ||||||
UniProtKB:A0A8M2B2G2 | InterPro | 1572 | ||||||
UniProtKB:A0A8M3BEB4 | InterPro | 1482 |
Interactions and Pathways
No data available
Plasmids
No data available
No data available
Type | Accession # | Sequence | Length (nt/aa) | Analysis |
---|---|---|---|---|
RNA | RefSeq:XM_021472589 (1) | 7206 nt | ||
Genomic | GenBank:CT573318 | 182424 nt | ||
Polypeptide | UniProtKB:A0A8M9Q963 (1) | 1657 aa |
- 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
- 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
- Lo, J., Lee, S., Xu, M., Liu, F., Ruan, H., Eun, A., He, Y., Ma, W., Wang, W., Wen, Z., and Peng, J. (2003) 15,000 unique zebrafish EST clusters and their future use in microarray for profiling gene expression patterns during embryogenesis. Genome research. 13(3):455-466
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