Gene
rmi1
- ID
- ZDB-GENE-040426-829
- Name
- RMI1, RecQ mediated genome instability 1, homolog (S. cerevisiae)
- Symbol
- rmi1 Nomenclature History
- Previous Names
-
- zgc:55882 (1)
- Type
- protein_coding_gene
- Location
- Chr: 8 Mapping Details/Browsers
- Description
- Predicted to enable nucleotide binding activity. Predicted to be involved in double-strand break repair via homologous recombination and resolution of meiotic recombination intermediates. Predicted to act upstream of or within DNA replication. Predicted to be located in nucleus. Predicted to be part of RecQ family helicase-topoisomerase III complex. Predicted to be active in nuclear body. Orthologous to human RMI1 (RecQ mediated genome instability 1).
- Genome Resources
- Note
- None
- Comparative Information
-
- All Expression Data
- 1 figure from Thisse et al., 2004
- Cross-Species Comparison
- High Throughput Data
- Thisse Expression Data
-
- MGC:55882 (1 image)
Wild Type Expression Summary
- All Phenotype Data
- No data available
- Cross-Species Comparison
- Alliance
Phenotype Summary
Mutations
Allele | Type | Localization | Consequence | Mutagen | Supplier |
---|---|---|---|---|---|
la010560Tg | Transgenic insertion | Unknown | Unknown | DNA |
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No data available
Human Disease
Domain, Family, and Site Summary
Type | InterPro ID | Name |
---|---|---|
Domain | IPR013894 | RecQ mediated genome instability protein 1, OB-fold domain |
Domain | IPR032199 | RecQ-mediated genome instability protein 1, C-terminal OB-fold domain |
Domain | IPR049363 | RMI1, N-terminal domain |
Homologous_superfamily | IPR042470 | RecQ mediated genome instability protein, N-terminal OB-fold domain superfamily |
Homologous_superfamily | IPR044881 | RecQ-mediated genome instability protein 1, N-terminal helical domain superfamily |
Domain Details Per Protein
Protein | Additional Resources | Length | RecQ-mediated genome instability protein 1, C-terminal OB-fold domain | RecQ-mediated genome instability protein 1, N-terminal helical domain superfamily | RecQ mediated genome instability protein 1, OB-fold domain | RecQ mediated genome instability protein, N-terminal OB-fold domain superfamily | RMI1, N-terminal domain |
---|---|---|---|---|---|---|---|
UniProtKB:B2GPA1 | InterPro | 519 | |||||
UniProtKB:A0A8M9QDM9 | InterPro | 519 | |||||
UniProtKB:Q7ZVM9 | InterPro | 519 |
Interactions and Pathways
No data available
Plasmids
No data available
No data available
Relationship | Marker Type | Marker | Accession Numbers | Citations |
---|---|---|---|---|
Contained in | BAC | CH211-148P15 | ZFIN Curated Data | |
Encodes | cDNA | MGC:55882 | ZFIN Curated Data | |
Encodes | cDNA | MGC:191442 | ZFIN Curated Data |
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Type | Accession # | Sequence | Length (nt/aa) | Analysis |
---|---|---|---|---|
RNA | RefSeq:NM_200180 (1) | 2059 nt | ||
Genomic | GenBank:CU682767 (2) | 49117 nt | ||
Polypeptide | UniProtKB:A0A8M9QDM9 (1) | 519 aa |
- Li, L., Chen, M., Liu, W., Tai, P., Liu, X., Liu, J.X. (2022) Zebrafish cox17 modulates primitive erythropoiesis via regulation of mitochondrial metabolism to facilitate hypoxia tolerance. FASEB journal : official publication of the Federation of American Societies for Experimental Biology. 36:e22596
- Desvignes, T., Sydes, J., Montfort, J., Bobe, J., Postlethwait, J.H. (2021) Evolution after whole genome duplication: teleost microRNAs. Molecular Biology and Evolution. 38(8):3308-3331
- Hugo, S.E., Schlegel, A. (2017) A genetic model to study increased hexosamine biosynthetic flux. Endocrinology. 158(8):2420-2426
- 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
- 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
- Tiefenbach, J., Moll, P.R., Nelson, M.R., Hu, C., Baev, L., Kislinger, T., and Krause, H.M. (2010) A live zebrafish-based screening system for human nuclear receptor ligand and cofactor discovery. PLoS One. 5(3):e9797
- 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
- Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G., Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D., Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K., Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F., Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L., Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L., Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S., Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J., Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J., McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S., Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W., Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A., Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y., Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M., Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E., Schnerch,A., Schein,J.E., Jones,S.J., and Marra,M.A. (2002) Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proceedings of the National Academy of Sciences of the United States of America. 99(26):16899-903
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