Protein-coding gene in the species Homo sapiens
| GAL3ST1 |
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| Identifiers |
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| Aliases | GAL3ST1, CST, galactose-3-O-sulfotransferase 1 |
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| External IDs | OMIM: 602300; MGI: 1858277; HomoloGene: 3574; GeneCards: GAL3ST1; OMA:GAL3ST1 - orthologs |
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| Gene location (Human) |
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 | | Chr. | Chromosome 22 (human)[1] |
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| | Band | 22q12.2 | Start | 30,554,635 bp[1] |
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| End | 30,574,665 bp[1] |
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| Gene location (Mouse) |
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 | | Chr. | Chromosome 11 (mouse)[2] |
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| | Band | 11|11 A1 | Start | 3,933,636 bp[2] |
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| End | 3,949,326 bp[2] |
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| RNA expression pattern |
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| Bgee | | Human | Mouse (ortholog) |
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| Top expressed in | - C1 segment
- tibial nerve
- gonad
- putamen
- duodenum
- nucleus accumbens
- amygdala
- caudate nucleus
- substantia nigra
- sural nerve
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| | Top expressed in | - pyloric antrum
- epithelium of stomach
- mucous cell of stomach
- right kidney
- duodenum
- lumbar subsegment of spinal cord
- anterior horn of spinal cord
- deep cerebellar nuclei
- sciatic nerve
- optic nerve
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| | More reference expression data |
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| BioGPS |  | | More reference expression data |
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| Gene ontology |
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| Molecular function | - transferase activity
- sulfotransferase activity
- galactosylceramide sulfotransferase activity
| | Cellular component | - integral component of membrane
- Golgi membrane
- Golgi apparatus
- integral component of plasma membrane
- membrane
| | Biological process | - glycolipid biosynthetic process
- myelination
- galactosylceramide biosynthetic process
- protein N-linked glycosylation
- spermatogenesis
- sphingolipid metabolic process
- lipid metabolism
| | Sources:Amigo / QuickGO |
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| Orthologs |
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| Species | Human | Mouse |
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| Entrez | | |
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| Ensembl | | |
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| UniProt | | |
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| RefSeq (mRNA) | NM_004861
NM_001318103
NM_001318104
NM_001318105
NM_001318106
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NM_001318107
NM_001318108
NM_001318109
NM_001318110
NM_001318111
NM_001318112
NM_001318113
NM_001318114
NM_001318115
NM_001318116 |
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NM_001177691
NM_001177703
NM_016922
NM_001382290
NM_001382291 |
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| RefSeq (protein) | NP_001305032
NP_001305033
NP_001305034
NP_001305035
NP_001305036
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NP_001305037
NP_001305038
NP_001305039
NP_001305040
NP_001305041
NP_001305042
NP_001305043
NP_001305044
NP_001305045
NP_004852 |
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NP_001171162
NP_001171174
NP_058618
NP_001369219
NP_001369220 |
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| Location (UCSC) | Chr 22: 30.55 – 30.57 Mb | Chr 11: 3.93 – 3.95 Mb |
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| PubMed search | [3] | [4] |
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| Wikidata |
| View/Edit Human | View/Edit Mouse |
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Galactosylceramide sulfotransferase is an enzyme that in humans is encoded by the GAL3ST1 gene.[5][6][7]
Sulfonation, an important step in the metabolism of many drugs, xenobiotics, hormones, and neurotransmitters, is catalyzed by sulfotransferases. The product of this gene is galactosylceramide sulfotransferase which catalyzes the conversion between 3'-phosphoadenylylsulfate + a galactosylceramide to adenosine 3',5'-bisphosphate + galactosylceramide sulfate. Activity of this sulfotransferase is enhanced in renal cell carcinoma.[7]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000128242 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000049721 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ Sanger Centre, The; Washington University Genome Sequencing Cente, The (Jan 1999). "Toward a complete human genome sequence". Genome Res. 8 (11): 1097–108. doi:10.1101/gr.8.11.1097. PMID 9847074.
- ^ Honke K, Tsuda M, Hirahara Y, Ishii A, Makita A, Wada Y (Apr 1997). "Molecular cloning and expression of cDNA encoding human 3'-phosphoadenylylsulfate:galactosylceramide 3'-sulfotransferase". J Biol Chem. 272 (8): 4864–8. doi:10.1074/jbc.272.8.4864. PMID 9030544.
- ^ a b "Entrez Gene: GAL3ST1 galactose-3-O-sulfotransferase 1".
Further reading
- Siegrist HP, Jutzi H, Steck AJ, et al. (1977). "Age-dependent modulation of 3'-phosphoadenosine-5'-phosphosulfate-galactosylceramide sulfotransferase by lipids extracted from the microsomal membranes and artificial lipid mixtures". Biochim. Biophys. Acta. 489 (1): 58–63. doi:10.1016/0005-2760(77)90231-4. PMID 911873.
- Stein C, Gieselmann V, Kreysing J, et al. (1989). "Cloning and expression of human arylsulfatase A". J. Biol. Chem. 264 (2): 1252–9. doi:10.1016/S0021-9258(19)85079-2. PMID 2562955.
- Fleischer B, Zambrano F (1973). "Localization of cerebroside-sulfotransferase activity in the Golgi apparatus of rat kidney". Biochem. Biophys. Res. Commun. 52 (3): 951–8. doi:10.1016/0006-291X(73)91029-2. PMID 4710574.
- Farrell DF, McKhann GM (1971). "Characterization of cerebroside sulfotransferase from rat brain". J. Biol. Chem. 246 (15): 4694–702. doi:10.1016/S0021-9258(18)61991-X. PMID 5562350.
- Costantino-Ceccarini E, Waehneldt TV, Ginalski H, et al. (1982). "Distribution of lipid synthesizing enzymes, 2',3'-cyclic nucleotide 3'-phosphodiesterase, and myelin proteins in rat forebrain subfractions during development". Neurochem. Res. 7 (1): 1–12. doi:10.1007/BF00965064. PMID 6280086. S2CID 32069166.
- Benjamins JA, Hadden T, Skoff RP (1982). "Cerebroside sulfotransferase in Golgi-enriched fractions from rat brain". J. Neurochem. 38 (1): 233–41. doi:10.1111/j.1471-4159.1982.tb10875.x. PMID 6955451. S2CID 23693243.
- Honke K, Yamane M, Ishii A, et al. (1996). "Purification and characterization of 3'-phosphoadenosine-5'-phosphosulfate:GalCer sulfotransferase from human renal cancer cells". J. Biochem. 119 (3): 421–7. doi:10.1093/oxfordjournals.jbchem.a021258. PMID 8830034.
- Tsuda M, Egashira M, Niikawa N, et al. (2000). "Cancer-associated alternative usage of multiple promoters of human GalCer sulfotransferase gene". Eur. J. Biochem. 267 (9): 2672–9. doi:10.1046/j.1432-1327.2000.01281.x. PMID 10785389.
- Eckhardt M, Fewou SN, Ackermann I, Gieselmann V (2002). "N-glycosylation is required for full enzymic activity of the murine galactosylceramide sulphotransferase". Biochem. J. 368 (Pt 1): 317–24. doi:10.1042/BJ20020946. PMC 1222978. PMID 12175333.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Collins JE, Wright CL, Edwards CA, et al. (2005). "A genome annotation-driven approach to cloning the human ORFeome". Genome Biol. 5 (10): R84. doi:10.1186/gb-2004-5-10-r84. PMC 545604. PMID 15461802.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
