ST3GAL3: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''ST3 beta-galactoside alpha-2,3-sialyltransferase 3''', also known as '''ST3GAL3''', is a [[protein]] which in humans is encoded by the ''ST3GAL3'' [[gene]].<ref name="pmid8333853">{{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 }}</ref><ref name="entrez">{{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 = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = ST3 beta-galactoside alpha-2,3-sialyltransferase 3
| HGNCid = 10866
| Symbol = ST3GAL3
| AltSymbols =; ST3GALII; SIAT6; ST3Gal III; ST3GalIII; ST3N
| OMIM = 606494
| ECnumber = 
| Homologene = 7539
| MGIid = 1316659
| Function = {{GNF_GO|id=GO:0008118 |text = N-acetyllactosaminide alpha-2,3-sialyltransferase activity}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0030173 |text = integral to Golgi membrane}}
| Process = {{GNF_GO|id=GO:0006486 |text = protein amino acid glycosylation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 6487
    | Hs_Ensembl = ENSG00000126091
    | Hs_RefseqProtein = NP_006270
    | Hs_RefseqmRNA = NM_006279
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 43945805
    | Hs_GenLoc_end = 44169418
    | Hs_Uniprot = Q11203
    | Mm_EntrezGene = 20441
    | Mm_Ensembl = ENSMUSG00000028538
    | Mm_RefseqmRNA = NM_009176
    | Mm_RefseqProtein = NP_033202
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 4
    | Mm_GenLoc_start = 117430086
    | Mm_GenLoc_end = 117632822
    | Mm_Uniprot = Q3UWD5
  }}
}}
'''ST3 beta-galactoside alpha-2,3-sialyltransferase 3''', also known as '''ST3GAL3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ST3GAL3 ST3 beta-galactoside alpha-2,3-sialyltransferase 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6487| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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 [[enzyme substrate|substrate]]s. The encoded protein is normally found in the [[Golgi apparatus]] but can be [[proteolysis|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.<ref name="entrez"/>
{{PBB_Summary
| section_title =
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: ST3GAL3 ST3 beta-galactoside alpha-2,3-sialyltransferase 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6487| accessdate = }}</ref>
}}


==References==
Interestingly, 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]].
{{reflist|2}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal  | author=Kalyanaraman VS, Rodriguez V, Veronese F, ''et al.'' |title=Characterization of the secreted, native gp120 and gp160 of the human immunodeficiency virus type 1. |journal=AIDS Res. Hum. Retroviruses |volume=6 |issue= 3 |pages= 371-80 |year= 1990 |pmid= 2187500 |doi=  }}
*{{cite journal  | author=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=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 9 |pages= 3384-8 |year= 1989 |pmid= 2541446 |doi=  }}
*{{cite journal  | author=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=J. Virol. |volume=63 |issue= 6 |pages= 2452-6 |year= 1989 |pmid= 2542563 |doi=  }}
*{{cite journal  | author=Kozarsky K, Penman M, Basiripour L, ''et al.'' |title=Glycosylation and processing of the human immunodeficiency virus type 1 envelope protein. |journal=J. Acquir. Immune Defic. Syndr. |volume=2 |issue= 2 |pages= 163-9 |year= 1989 |pmid= 2649653 |doi=  }}
*{{cite journal  | author=Robinson WE, Montefiori DC, Mitchell WM |title=Evidence that mannosyl residues are involved in human immunodeficiency virus type 1 (HIV-1) pathogenesis. |journal=AIDS Res. Hum. Retroviruses |volume=3 |issue= 3 |pages= 265-82 |year= 1988 |pmid= 2829950 |doi=  }}
*{{cite journal  | author=Kitagawa H, Paulson JC |title=Differential expression of five sialyltransferase genes in human tissues. |journal=J. Biol. Chem. |volume=269 |issue= 27 |pages= 17872-8 |year= 1994 |pmid= 8027041 |doi=  }}
*{{cite journal  | author=Kitagawa H, Paulson JC |title=Cloning and expression of human Gal beta 1,3(4)GlcNAc alpha 2,3-sialyltransferase. |journal=Biochem. Biophys. Res. Commun. |volume=194 |issue= 1 |pages= 375-82 |year= 1993 |pmid= 8333853 |doi= 10.1006/bbrc.1993.1830 }}
*{{cite journal  | author=Burger PC, Lötscher M, Streiff M, ''et al.'' |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 |year= 1998 |pmid= 9451034 |doi=  }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Taniguchi A, Morishima T, Tsujita Y, ''et al.'' |title=Genomic structure, expression, and transcriptional regulation of human Gal beta 1,3 GalNAc alpha 2,3-sialyltransferase gene. |journal=Biochem. Biophys. Res. Commun. |volume=300 |issue= 2 |pages= 570-6 |year= 2003 |pmid= 12504121 |doi=  }}
*{{cite journal  | author=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=Biochim. Biophys. Acta |volume=1626 |issue= 1-3 |pages= 92-6 |year= 2003 |pmid= 12697334 |doi=  }}
*{{cite journal  | author=Saito S, Aoki H, Ito A, ''et al.'' |title=Human alpha2,3-sialyltransferase (ST3Gal II) is a stage-specific embryonic antigen-4 synthase. |journal=J. Biol. Chem. |volume=278 |issue= 29 |pages= 26474-9 |year= 2003 |pmid= 12716912 |doi= 10.1074/jbc.M213223200 }}
*{{cite journal  | author=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=Glycoconj. J. |volume=19 |issue= 3 |pages= 197-210 |year= 2004 |pmid= 12815231 |doi= 10.1023/A:1024253808424 }}
*{{cite journal  | author=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  | author=Jeanneau C, Chazalet V, Augé C, ''et al.'' |title=Structure-function analysis of the human sialyltransferase ST3Gal I: role of n-glycosylation and a novel conserved sialylmotif. |journal=J. Biol. Chem. |volume=279 |issue= 14 |pages= 13461-8 |year= 2004 |pmid= 14722111 |doi= 10.1074/jbc.M311764200 }}
*{{cite journal  | author=Grahn A, Barkhordar GS, Larson G |title=Identification of seven new alpha2,3-sialyltransferase III, ST3Gal III, transcripts from human foetal brain. |journal=Glycoconj. J. |volume=20 |issue= 7-8 |pages= 493-500 |year= 2005 |pmid= 15316282 |doi= 10.1023/B:GLYC.0000038295.87747.0b }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | author=Van Dyken SJ, Green RS, Marth JD |title=Structural and mechanistic features of protein O glycosylation linked to CD8+ T-cell apoptosis. |journal=Mol. Cell. Biol. |volume=27 |issue= 3 |pages= 1096-111 |year= 2007 |pmid= 17101770 |doi= 10.1128/MCB.01750-06 }}
}}
{{refend}}


{{protein-stub}}
== See also ==
{{WikiDoc Sources}}
* [[Sialyltransferase]]
 
== References ==
{{reflist}}
 
== 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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Revision as of 02:41, 27 October 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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]

Interestingly, 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

References

  1. ↑ Kitagawa H, Paulson JC (Jul 1993). "Cloning and expression of human Gal beta 1,3(4)GlcNAc alpha 2,3-sialyltransferase". Biochemical and Biophysical Research Communications. 194 (1): 375–82. doi:10.1006/bbrc.1993.1830. PMID 8333853.
  2. ↑ 2.0 2.1 "Entrez Gene: ST3GAL3 ST3 beta-galactoside alpha-2,3-sialyltransferase 3".

Further reading


Retrieved from "https://www.wikidoc.org/index.php?title=ST3GAL3&oldid=1411349"