Gene
hck
- ID
- ZDB-GENE-090313-72
- Name
- HCK proto-oncogene, Src family tyrosine kinase
- Symbol
- hck Nomenclature History
- Previous Names
-
- si:ch211-200e2.4
- Type
- protein_coding_gene
- Location
- Chr: 23 Mapping Details/Browsers
- Description
- Predicted to enable non-membrane spanning protein tyrosine kinase activity and signaling receptor binding activity. Predicted to be involved in cell differentiation and cell surface receptor protein tyrosine kinase signaling pathway. Predicted to act upstream of or within protein phosphorylation. Predicted to be located in membrane. Predicted to be active in plasma membrane. Orthologous to human HCK (HCK proto-oncogene, Src family tyrosine kinase).
- Genome Resources
- Note
- None
- Comparative Information
-
- All Expression Data
- 1 figure from Yoo et al., 2011
- 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 |
|---|---|---|---|---|---|
| sa24256 | Allele with one point mutation | Unknown | Premature Stop | ENU |
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No data available
Human Disease
| Disease Ontology Term | Multi-Species Data | OMIM Term | OMIM Phenotype ID |
|---|---|---|---|
| Autoinflammation with pulmonary and cutaneous vasculitis | 620296 |
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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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| UniProtKB:A0A0R4J755 | InterPro | 499 |
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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 | CH211-156D2 | ZFIN Curated Data | |
| Contained in | BAC | CH211-200E2 | ZFIN Curated Data |
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| Type | Accession # | Sequence | Length (nt/aa) | Analysis |
|---|---|---|---|---|
| RNA | RefSeq:XM_068216859 (1) | 6854 nt | ||
| Genomic | GenBank:CU633736 (1) | 70088 nt | ||
| Polypeptide | UniProtKB:A0A0R4J755 (1) | 499 aa |
- Natarajan, N., Abbas, Y., Bryant, D.M., Gonzalez-Rosa, J.M., Sharpe, M., Uygur, A., Cocco-Delgado, L.H., Ho, N.N., Gerard, N.P., Gerard, C.J., Macrae, C.A., Burns, C.E., Burns, C.G., Whited, J.L., Lee, R.T. (2018) Complement Receptor C5aR1 Plays an Evolutionarily Conserved Role in Successful Cardiac Regeneration. Circulation. 137(20):2152-2165
- Cardoso, J.C., Bergqvist, C.A., Felix, R.C., Larhammar, D. (2016) Corticotropin-releasing hormone family evolution: five ancestral genes remain in some lineages. Journal of molecular endocrinology. 57(1):73-86
- 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
- Nachtigall, P., Dias, M., Pinhal, D. (2014) Evolution and genomic organization of muscle microRNAs in fish genomes. BMC Evolutionary Biology. 14:196
- 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
- Yoo, S.K., Starnes, T.W., Deng, Q., and Huttenlocher, A. (2011) Lyn is a redox sensor that mediates leukocyte wound attraction in vivo. Nature. 480(7375):109-12
- Sundström, G., Dreborg, S., and Larhammar, D. (2010) Concomitant duplications of opioid peptide and receptor genes before the origin of jawed vertebrates. PLoS One. 5(5):e10512
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