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词条 ST3GAL3
释义

  1. Function

  2. See also

  3. References

  4. Further reading

{{Infobox_gene}}ST3 beta-galactoside alpha-2,3-sialyltransferase 3, also known as ST3GAL3, is a protein which in humans is encoded by the ST3GAL3 gene.[1][2]

Function

The protein encoded by this gene is a type II membrane protein that catalyzes the transfer of sialic acid from CMP-sialic acid to galactose-containing substrates. The encoded protein is normally found in the Golgi apparatus but can be proteolytically processed to a soluble form. This protein is a member of glycosyltransferase family 29. Multiple transcript variants encoding several different isoforms have been found for this gene.[2]

Mutations in the ST3GAL3 gene was recently shown to be the cause of autosomal recessive mental retardation 12. Since the mutations disrupt a glycosylation pathway, this disorder may be considererd a congenital disorder of glycosylation.

See also

  • Sialyltransferase

References

1. ^{{cite journal | vauthors = Kitagawa H, Paulson JC | title = Cloning and expression of human Gal beta 1,3(4)GlcNAc alpha 2,3-sialyltransferase | journal = Biochemical and Biophysical Research Communications | volume = 194 | issue = 1 | pages = 375–82 | date = Jul 1993 | pmid = 8333853 | doi = 10.1006/bbrc.1993.1830 }}
2. ^{{cite web | title = Entrez Gene: ST3GAL3 ST3 beta-galactoside alpha-2,3-sialyltransferase 3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6487| accessdate = }}

Further reading

{{refbegin|colwidth=30em}}
  • {{cite journal | vauthors = Kalyanaraman VS, Rodriguez V, Veronese F, Rahman R, Lusso P, DeVico AL, Copeland T, Oroszlan S, Gallo RC, Sarngadharan MG | title = Characterization of the secreted, native gp120 and gp160 of the human immunodeficiency virus type 1 | journal = AIDS Research and Human Retroviruses | volume = 6 | issue = 3 | pages = 371–80 | date = Mar 1990 | pmid = 2187500 | doi = 10.1089/aid.1990.6.371 }}
  • {{cite journal | vauthors = Pal R, Hoke GM, Sarngadharan MG | title = Role of oligosaccharides in the processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1 | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 86 | issue = 9 | pages = 3384–8 | date = May 1989 | pmid = 2541446 | pmc = 287137 | doi = 10.1073/pnas.86.9.3384 }}
  • {{cite journal | vauthors = Dewar RL, Vasudevachari MB, Natarajan V, Salzman NP | title = Biosynthesis and processing of human immunodeficiency virus type 1 envelope glycoproteins: effects of monensin on glycosylation and transport | journal = Journal of Virology | volume = 63 | issue = 6 | pages = 2452–6 | date = Jun 1989 | pmid = 2542563 | pmc = 250699 | doi = }}
  • {{cite journal | vauthors = Kozarsky K, Penman M, Basiripour L, Haseltine W, Sodroski J, Krieger M | title = Glycosylation and processing of the human immunodeficiency virus type 1 envelope protein | journal = Journal of Acquired Immune Deficiency Syndromes | volume = 2 | issue = 2 | pages = 163–9 | year = 1989 | pmid = 2649653 | doi = }}
  • {{cite journal | vauthors = Robinson WE, Montefiori DC, Mitchell WM | title = Evidence that mannosyl residues are involved in human immunodeficiency virus type 1 (HIV-1) pathogenesis | journal = AIDS Research and Human Retroviruses | volume = 3 | issue = 3 | pages = 265–82 | year = 1988 | pmid = 2829950 | doi = 10.1089/aid.1987.3.265 }}
  • {{cite journal | vauthors = Kitagawa H, Paulson JC | title = Differential expression of five sialyltransferase genes in human tissues | journal = The Journal of Biological Chemistry | volume = 269 | issue = 27 | pages = 17872–8 | date = Jul 1994 | pmid = 8027041 | doi = }}
  • {{cite journal | vauthors = Kitagawa H, Paulson JC | title = Cloning and expression of human Gal beta 1,3(4)GlcNAc alpha 2,3-sialyltransferase | journal = Biochemical and Biophysical Research Communications | volume = 194 | issue = 1 | pages = 375–82 | date = Jul 1993 | pmid = 8333853 | doi = 10.1006/bbrc.1993.1830 }}
  • {{cite journal | vauthors = Burger PC, Lötscher M, Streiff M, Kleene R, Kaissling B, Berger EG | title = Immunocytochemical localization of alpha2,3(N)-sialyltransferase (ST3Gal III) in cell lines and rat kidney tissue sections: evidence for golgi and post-golgi localization | journal = Glycobiology | volume = 8 | issue = 3 | pages = 245–57 | date = Mar 1998 | pmid = 9451034 | doi = 10.1093/glycob/8.3.245 }}
  • {{cite journal | vauthors = Taniguchi A, Morishima T, Tsujita Y, Matsumoto Y, Matsumoto K | title = Genomic structure, expression, and transcriptional regulation of human Gal beta 1,3 GalNAc alpha 2,3-sialyltransferase gene | journal = Biochemical and Biophysical Research Communications | volume = 300 | issue = 2 | pages = 570–6 | date = Jan 2003 | pmid = 12504121 | doi = 10.1016/S0006-291X(02)02899-1 }}
  • {{cite journal | vauthors = Taniguchi A, Saito K, Kubota T, Matsumoto K | title = Characterization of the promoter region of the human Galbeta1,3(4)GlcNAc alpha2,3-sialyltransferase III (hST3Gal III) gene | journal = Biochimica et Biophysica Acta | volume = 1626 | issue = 1–3 | pages = 92–6 | date = Apr 2003 | pmid = 12697334 | doi = 10.1016/s0167-4781(03)00021-6 }}
  • {{cite journal | vauthors = Saito S, Aoki H, Ito A, Ueno S, Wada T, Mitsuzuka K, Satoh M, Arai Y, Miyagi T | title = Human alpha2,3-sialyltransferase (ST3Gal II) is a stage-specific embryonic antigen-4 synthase | journal = The Journal of Biological Chemistry | volume = 278 | issue = 29 | pages = 26474–9 | date = Jul 2003 | pmid = 12716912 | doi = 10.1074/jbc.M213223200 }}
  • {{cite journal | vauthors = Grahn A, Barkhordar GS, Larson G | title = Cloning and sequencing of nineteen transcript isoforms of the human alpha2,3-sialyltransferase gene, ST3Gal III; its genomic organisation and expression in human tissues | journal = Glycoconjugate Journal | volume = 19 | issue = 3 | pages = 197–210 | date = Mar 2002 | pmid = 12815231 | doi = 10.1023/A:1024253808424 }}
  • {{cite journal | vauthors = Gretschel S, Haensch W, Schlag PM, Kemmner W | title = Clinical relevance of sialyltransferases ST6GAL-I and ST3GAL-III in gastric cancer | journal = Oncology | volume = 65 | issue = 2 | pages = 139–45 | year = 2003 | pmid = 12931020 | doi = 10.1159/000072339 }}
  • {{cite journal | vauthors = Jeanneau C, Chazalet V, Augé C, Soumpasis DM, Harduin-Lepers A, Delannoy P, Imberty A, Breton C | title = Structure-function analysis of the human sialyltransferase ST3Gal I: role of n-glycosylation and a novel conserved sialylmotif | journal = The Journal of Biological Chemistry | volume = 279 | issue = 14 | pages = 13461–8 | date = Apr 2004 | pmid = 14722111 | doi = 10.1074/jbc.M311764200 }}
  • {{cite journal | vauthors = Grahn A, Barkhordar GS, Larson G | title = Identification of seven new alpha2,3-sialyltransferase III, ST3Gal III, transcripts from human foetal brain | journal = Glycoconjugate Journal | volume = 20 | issue = 7–8 | pages = 493–500 | year = 2005 | pmid = 15316282 | doi = 10.1023/B:GLYC.0000038295.87747.0b }}
  • {{cite journal | vauthors = Van Dyken SJ, Green RS, Marth JD | title = Structural and mechanistic features of protein O glycosylation linked to CD8+ T-cell apoptosis | journal = Molecular and Cellular Biology | volume = 27 | issue = 3 | pages = 1096–111 | date = Feb 2007 | pmid = 17101770 | pmc = 1800694 | doi = 10.1128/MCB.01750-06 }}
  • {{cite journal | vauthors = Hu H, Eggers K, Chen W, Garshasbi M, Motazacker MM, Wrogemann K, Kahrizi K, Tzschach A, Hosseini M, Bahman I, Hucho T, Mühlenhoff M, Gerardy-Schahn R, Najmabadi H, Ropers HH, Kuss AW | title = ST3GAL3 mutations impair the development of higher cognitive functions | journal = American Journal of Human Genetics | volume = 89 | issue = 3 | pages = 407–14 | date = Sep 2011 | doi = 10.1016/j.ajhg.2011.08.008 | pmid = 21907012 | series = 3 | pmc=3169827}}
  • {{cite journal |vauthors=Szabo R, Skropeta D, etal |title=Advancement of Sialyltransferase Inhibitors: Therapeutic Challenges and Opportunities. |journal=Med. Res. Rev. |volume=37 |pages= 210–270 |year= 2017 |doi= 10.1002/med.21407 }}
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