ST3GAL3

ST3 beta-galactoside alpha-2,3-sialyltransferase 3, also known as ST3GAL3, is a human sialyltransferase gene.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 = ]

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.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 = ]

References

Further reading

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

PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes