Gene
lig1
- ID
- ZDB-GENE-110404-2
- Name
- ligase I, DNA, ATP-dependent
- Symbol
- lig1 Nomenclature History
- Previous Names
-
- si:dkeyp-35b8.5
- si:dkeyp-35b8.7
- wu:fc54a11
- Type
- protein_coding_gene
- Location
- Chr: 2 Mapping Details/Browsers
- Description
- Predicted to enable DNA ligase (ATP) activity. Predicted to be involved in Okazaki fragment processing involved in mitotic DNA replication. Predicted to act upstream of or within DNA metabolic process. Predicted to be active in nucleus. Human ortholog(s) of this gene implicated in immunodeficiency 96; inherited metabolic disorder; and primary immunodeficiency disease. Orthologous to human LIG1 (DNA ligase 1).
- Genome Resources
- Note
- None
- Comparative Information
-
- All Expression Data
- 1 figure from Leontovich et al., 2016
- 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 |
---|---|---|---|---|---|
la028825Tg | Transgenic insertion | Unknown | Unknown | DNA | |
sa12017 | Allele with one point mutation | Unknown | Premature Stop | ENU | |
sa12131 | Allele with one point mutation | Unknown | Premature Stop | ENU | |
sa33012 | 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 |
---|---|---|---|
immunodeficiency 96 | Alliance | Immunodeficiency 96 | 619774 |
Domain, Family, and Site Summary
Type | InterPro ID | Name |
---|---|---|
Conserved_site | IPR016059 | DNA ligase, ATP-dependent, conserved site |
Domain | IPR012308 | DNA ligase, ATP-dependent, N-terminal |
Domain | IPR012309 | DNA ligase, ATP-dependent, C-terminal |
Domain | IPR012310 | DNA ligase, ATP-dependent, central |
Family | IPR000977 | DNA ligase, ATP-dependent |
Family | IPR050191 | ATP-dependent DNA ligase |
Homologous_superfamily | IPR012340 | Nucleic acid-binding, OB-fold |
Homologous_superfamily | IPR036599 | DNA ligase, ATP-dependent, N-terminal domain superfamily |
Domain Details Per Protein
Protein | Additional Resources | Length | ATP-dependent DNA ligase | DNA ligase, ATP-dependent | DNA ligase, ATP-dependent, central | DNA ligase, ATP-dependent, conserved site | DNA ligase, ATP-dependent, C-terminal | DNA ligase, ATP-dependent, N-terminal | DNA ligase, ATP-dependent, N-terminal domain superfamily | Nucleic acid-binding, OB-fold |
---|---|---|---|---|---|---|---|---|---|---|
UniProtKB:B0S533 | InterPro | 1058 |
Interactions and Pathways
No data available
Plasmids
No data available
No data available
Relationship | Marker Type | Marker | Accession Numbers | Citations |
---|---|---|---|---|
Contained in | BAC | CH211-265G22 | ZFIN Curated Data | |
Contained in | BAC | DKEYP-35B8 | ZFIN Curated Data | |
Encodes | EST | fc54a11 |
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Type | Accession # | Sequence | Length (nt/aa) | Analysis |
---|---|---|---|---|
RNA | RefSeq:NM_001126388 (1) | 3177 nt | ||
Genomic | GenBank:BX005264 (1) | 212605 nt | ||
Polypeptide | UniProtKB:B0S533 (1) | 1058 aa |
- Lu, C., Luo, J., Liu, Y., Yang, X. (2020) The oxidative stress responses caused by phthalate acid esters increases mRNA abundance of base excision repair (BER) genes in vivo and in vitro. Ecotoxicology and environmental safety. 208:111525
- Leontovich, A.A., Intine, R.V., Sarras, M.P. (2016) Epigenetic Studies Point to DNA Replication/Repair Genes as a Basis for the Heritable Nature of Long Term Complications in Diabetes. Journal of Diabetes Research. 2016:2860780
- Thyme, S.B., Schier, A.F. (2016) Polq-Mediated End Joining Is Essential for Surviving DNA Double-Strand Breaks during Early Zebrafish Development. Cell Reports. 15(4):707-714
- Mans, D.A., Vermaat, J.S., Weijts, B.G., van Rooijen, E., van Reeuwijk, J., Boldt, K., Daenen, L.G., van der Groep, P., Rowland, B.D., Jans, J.J., Roepman, R., Voest, E.E., van Diest, P.J., Verhaar, M.C., de Bruin, A., and Giles, R.H. (2013) Regulation of E2F1 by the von Hippel-Lindau tumour suppressor protein predicts survival in renal cell cancer patients. The Journal of pathology. 231(1):117-29
- 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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