Gene
kyat3.2
- ID
- ZDB-GENE-040426-1299
- Name
- kynurenine aminotransferase 3, tandem duplicate 2
- Symbol
- kyat3.2 Nomenclature History
- Previous Names
-
- ccbl2 (1)
- kyat3
- zgc:63929
- Type
- protein_coding_gene
- Location
- Chr: 6 Mapping Details/Browsers
- Description
- Predicted to enable kynurenine-glyoxylate transaminase activity and kynurenine-oxoglutarate transaminase activity. Predicted to be involved in kynurenine metabolic process. Predicted to act upstream of or within biosynthetic process. Predicted to be active in mitochondrion. Is expressed in several structures, including lens; liver; midbrain neural keel; myotome; and solid lens vesicle. Orthologous to human KYAT3 (kynurenine aminotransferase 3).
- Genome Resources
- Note
- None
- Comparative Information
-
- All Expression Data
- 7 figures from 2 publications
- Cross-Species Comparison
- High Throughput Data
- Thisse Expression Data
-
- MGC:63929 (7 images)
Wild Type Expression Summary
- All Phenotype Data
- No data available
- Cross-Species Comparison
- Alliance
Phenotype Summary
Mutations
No data available
Human Disease
Domain, Family, and Site Summary
Type | InterPro ID | Name |
---|---|---|
Domain | IPR004839 | Aminotransferase, class I/classII, large domain |
Family | IPR051326 | Kynurenine--oxoglutarate transaminase |
Homologous_superfamily | IPR015421 | Pyridoxal phosphate-dependent transferase, major domain |
Homologous_superfamily | IPR015422 | Pyridoxal phosphate-dependent transferase, small domain |
Homologous_superfamily | IPR015424 | Pyridoxal phosphate-dependent transferase |
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Domain Details Per Protein
Protein | Additional Resources | Length | Aminotransferase, class I/classII, large domain | Kynurenine--oxoglutarate transaminase | Pyridoxal phosphate-dependent transferase | Pyridoxal phosphate-dependent transferase, major domain | Pyridoxal phosphate-dependent transferase, small domain |
---|---|---|---|---|---|---|---|
UniProtKB:A0A8M9QA74 | InterPro | 352 | |||||
UniProtKB:A0A8M2BG14 | InterPro | 422 | |||||
UniProtKB:A0A8M2BG21 | InterPro | 419 | |||||
UniProtKB:Q7T3E5 | InterPro | 450 | |||||
UniProtKB:A0A8M1PEC5 | InterPro | 450 |
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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 | CH73-97H19 | ZFIN Curated Data | |
Contained in | BAC | CH211-180M24 | ZFIN Curated Data | |
Encodes | cDNA | MGC:63929 | ZFIN Curated Data |
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Type | Accession # | Sequence | Length (nt/aa) | Analysis |
---|---|---|---|---|
RNA | RefSeq:NM_200344 (1) | 1638 nt | ||
Genomic | GenBank:CU019652 (1) | 250385 nt | ||
Polypeptide | UniProtKB:A0A8M1PEC5 (1) | 450 aa |
- He, T., Lykov, N., Luo, X., Wang, H., Du, Z., Chen, Z., Chen, S., Zhu, L., Zhao, Y., Tzeng, C. (2023) Protective Effects of Lactobacillus gasseri against High-Cholesterol Diet-Induced Fatty Liver and Regulation of Host Gene Expression Profiles. International Journal of Molecular Sciences. 24(3):
- Huang, C.X., Chen, N., Wu, X.J., He, Y., Huang, C.H., Liu, H., Wang, W.M., Wang, H.L. (2017) Zebrafish let-7b acts downstream of hypoxia-inducible factor-1α to assist in hypoxia-mediated cell proliferation and cell cycle regulation. Life sciences. 171:21-29
- Zhang, D., Wang, J., Zhou, C., Xiao, W. (2017) Zebrafish akt2 is essential for survival, growth, bone development, and glucose homeostasis. Mechanisms of Development. 143:42-52
- 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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