Gene
st8sia2
- ID
- ZDB-GENE-020919-4
- Name
- ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 2
- Symbol
- st8sia2 Nomenclature History
- Previous Names
- Type
- protein_coding_gene
- Location
- Chr: 18 Mapping Details/Browsers
- Description
- Enables sialyltransferase activity. Predicted to be involved in N-glycan processing; oligosaccharide metabolic process; and protein glycosylation. Predicted to be located in Golgi apparatus and membrane. Is expressed in several structures, including nervous system; neural keel; neural tube; pleuroperitoneal region; and unfertilized egg. Orthologous to human ST8SIA2 (ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 2).
- Genome Resources
- Note
- None
- Comparative Information
-
- All Expression Data
- 21 figures from 9 publications
- Cross-Species Comparison
- High Throughput Data
- Thisse Expression Data
-
- cb394 (14 images)
Wild Type Expression Summary
Phenotype Summary
Mutations
| Allele | Type | Localization | Consequence | Mutagen | Supplier |
|---|---|---|---|---|---|
| la011718Tg | Transgenic insertion | Unknown | Unknown | DNA | |
| sa12977 | Allele with one point mutation | Unknown | Premature Stop | ENU | |
| sa23308 | Allele with one point mutation | Unknown | Premature Stop | ENU |
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Human Disease
Domain, Family, and Site Summary
Domain Details Per Protein
| Protein | Length | Glycosyltransferase 29 (Sialyltransferase) | Glycosyl transferase family 29 | GT29-like superfamiliy | Sialyltransferase |
|---|---|---|---|---|---|
|
UniProtKB:Q8QH83
|
381 |
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| Type | Name | Annotation Method | Has Havana Data | Length (nt) | Analysis |
|---|---|---|---|---|---|
| mRNA |
st8sia2-201
(1)
|
Ensembl | 2,321 nt |
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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 | CH211-196L7 | ZFIN Curated Data | |
| Encodes | EST | cb394 | Thisse et al., 2001 | |
| Encodes | EST | ibd5161 | ||
| Encodes | cDNA | MGC:55237 | ZFIN Curated Data |
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| Type | Accession # | Sequence | Length (nt/aa) | Analysis |
|---|---|---|---|---|
| RNA | RefSeq:NM_153662 (1) | 2326 nt | ||
| Genomic | GenBank:BX649578 (1) | 211922 nt | ||
| Polypeptide | UniProtKB:Q8QH83 (1) | 381 aa |
- Pollock, N.M., Leighton, P., Neil, G., Allison, W.T. (2021) Transcriptomic analysis of zebrafish prion protein mutants supports conserved cross-species function of the cellular prion protein. Prion. 15:70-81
- Chang, L.Y., Teppa, E., Noel, M., Gilormini, P.A., Decloquement, M., Lion, C., Biot, C., Mir, A.M., Cogez, V., Delannoy, P., Khoo, K.H., Petit, D., Guérardel, Y., Harduin-Lepers, A. (2019) Novel Zebrafish Mono-α2,8-sialyltransferase (ST8Sia VIII): An Evolutionary Perspective of α2,8-Sialylation. International Journal of Molecular Sciences. 20(3)
- Yamakawa, N., Vanbeselaere, J., Chang, L.Y., Yu, S.Y., Ducrocq, L., Harduin-Lepers, A., Kurata, J., Aoki-Kinoshita, K.F., Sato, C., Khoo, K.H., Kitajima, K., Guerardel, Y. (2018) Systems glycomics of adult zebrafish identifies organ-specific sialylation and glycosylation patterns. Nature communications. 9:4647
- 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
- Langhauser, M., Ustinova, J., Rivera-Milla, E., Ivannikov, D., Seidl, C., Slomka, C., Finne, J., Yoshihara, Y., Bastmeyer, M., and Bentrop, J. (2012) Ncam1a and Ncam1b: Two carriers of polysialic acid with different functions in the developing zebrafish nervous system. Glycobiology. 22(2):196-209
- Vanbeselaere, J., Chang, L.Y., Harduin-Lepers, A., Fabre, E., Yamakawa, N., Slomianny, C., Biot, C., Khoo, K.H., and Guerardel, Y. (2012) Mapping the expressed glycome and glycosyltransferases of zebrafish liver cells as a relevant model system for glycosylation studies. Journal of Proteome Research. 11(4):2164-2177
- Harduin-Lepers, A. (2010) Comprehensive Analysis of sialyltransferases in vertebrate genomes.. Glycobiology. 2010:2:29-61
- Cañestro, C., Catchen, J.M., Rodriguez-Mari, A., Yokoi, H., and Postlethwait, J.H. (2009) Consequences of lineage-specific gene loss on functional evolution of surviving paralogs: ALDH1A and retinoic acid signaling in vertebrate genomes. PLoS Genetics. 5(5):e1000496
- Chang, L.Y., Harduin-Lepers, A., Kitajima, K., Sato, C., Huang, C.J., Khoo, K.H., and Guérardel, Y. (2009) Developmental regulation of oligosialylation in zebrafish. Glycoconjugate journal. 26(3):247-261
- Chang, L.Y., Mir, A.M., Thisse, C., Guérardel, Y., Delannoy, P., Thisse, B., and Harduin-Lepers, A. (2009) Molecular cloning and characterization of the expression pattern of the zebrafish alpha2, 8-sialyltransferases (ST8Sia) in the developing nervous system. Glycoconjugate journal. 26(3):263-275
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