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.[6]
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 considered a congenital disorder of glycosylation.
^ abcGRCh38: Ensembl release 89: ENSG00000126091 - Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000028538 - 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.
^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.
Kalyanaraman VS, Rodriguez V, Veronese F, Rahman R, Lusso P, DeVico AL, Copeland T, Oroszlan S, Gallo RC, Sarngadharan MG (Mar 1990). "Characterization of the secreted, native gp120 and gp160 of the human immunodeficiency virus type 1". AIDS Research and Human Retroviruses. 6 (3): 371–80. doi:10.1089/aid.1990.6.371. PMID 2187500.
Pal R, Hoke GM, Sarngadharan MG (May 1989). "Role of oligosaccharides in the processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1". Proceedings of the National Academy of Sciences of the United States of America. 86 (9): 3384–8. Bibcode:1989PNAS...86.3384P. doi:10.1073/pnas.86.9.3384. PMC287137. PMID 2541446.
Dewar RL, Vasudevachari MB, Natarajan V, Salzman NP (Jun 1989). "Biosynthesis and processing of human immunodeficiency virus type 1 envelope glycoproteins: effects of monensin on glycosylation and transport". Journal of Virology. 63 (6): 2452–6. doi:10.1128/JVI.63.6.2452-2456.1989. PMC250699. PMID 2542563.
Kozarsky K, Penman M, Basiripour L, Haseltine W, Sodroski J, Krieger M (1989). "Glycosylation and processing of the human immunodeficiency virus type 1 envelope protein". Journal of Acquired Immune Deficiency Syndromes. 2 (2): 163–9. PMID 2649653.
Robinson WE, Montefiori DC, Mitchell WM (1988). "Evidence that mannosyl residues are involved in human immunodeficiency virus type 1 (HIV-1) pathogenesis". AIDS Research and Human Retroviruses. 3 (3): 265–82. doi:10.1089/aid.1987.3.265. PMID 2829950.
Kitagawa H, Paulson JC (Jul 1994). "Differential expression of five sialyltransferase genes in human tissues". The Journal of Biological Chemistry. 269 (27): 17872–8. doi:10.1016/S0021-9258(17)32390-6. PMID 8027041.
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.
Burger PC, Lötscher M, Streiff M, Kleene R, Kaissling B, Berger EG (Mar 1998). "Immunocytochemical localization of alpha2,3(N)-sialyltransferase (ST3Gal III) in cell lines and rat kidney tissue sections: evidence for golgi and post-golgi localization". Glycobiology. 8 (3): 245–57. doi:10.1093/glycob/8.3.245. PMID 9451034.
Taniguchi A, Morishima T, Tsujita Y, Matsumoto Y, Matsumoto K (Jan 2003). "Genomic structure, expression, and transcriptional regulation of human Gal beta 1,3 GalNAc alpha 2,3-sialyltransferase gene". Biochemical and Biophysical Research Communications. 300 (2): 570–6. doi:10.1016/S0006-291X(02)02899-1. PMID 12504121.
Taniguchi A, Saito K, Kubota T, Matsumoto K (Apr 2003). "Characterization of the promoter region of the human Galbeta1,3(4)GlcNAc alpha2,3-sialyltransferase III (hST3Gal III) gene". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1626 (1–3): 92–6. doi:10.1016/s0167-4781(03)00021-6. PMID 12697334.
Saito S, Aoki H, Ito A, Ueno S, Wada T, Mitsuzuka K, Satoh M, Arai Y, Miyagi T (Jul 2003). "Human alpha2,3-sialyltransferase (ST3Gal II) is a stage-specific embryonic antigen-4 synthase". The Journal of Biological Chemistry. 278 (29): 26474–9. doi:10.1074/jbc.M213223200. PMID 12716912.
Grahn A, Barkhordar GS, Larson G (Mar 2002). "Cloning and sequencing of nineteen transcript isoforms of the human alpha2,3-sialyltransferase gene, ST3Gal III; its genomic organisation and expression in human tissues". Glycoconjugate Journal. 19 (3): 197–210. doi:10.1023/A:1024253808424. PMID 12815231. S2CID 23897339.
Gretschel S, Haensch W, Schlag PM, Kemmner W (2003). "Clinical relevance of sialyltransferases ST6GAL-I and ST3GAL-III in gastric cancer". Oncology. 65 (2): 139–45. doi:10.1159/000072339. PMID 12931020. S2CID 6438454.
Jeanneau C, Chazalet V, Augé C, Soumpasis DM, Harduin-Lepers A, Delannoy P, Imberty A, Breton C (Apr 2004). "Structure-function analysis of the human sialyltransferase ST3Gal I: role of n-glycosylation and a novel conserved sialylmotif". The Journal of Biological Chemistry. 279 (14): 13461–8. doi:10.1074/jbc.M311764200. PMID 14722111.
Grahn A, Barkhordar GS, Larson G (2005). "Identification of seven new alpha2,3-sialyltransferase III, ST3Gal III, transcripts from human foetal brain". Glycoconjugate Journal. 20 (7–8): 493–500. doi:10.1023/B:GLYC.0000038295.87747.0b. PMID 15316282. S2CID 1544031.
Van Dyken SJ, Green RS, Marth JD (Feb 2007). "Structural and mechanistic features of protein O glycosylation linked to CD8+ T-cell apoptosis". Molecular and Cellular Biology. 27 (3): 1096–111. doi:10.1128/MCB.01750-06. PMC1800694. PMID 17101770.
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 (Sep 2011). "ST3GAL3 mutations impair the development of higher cognitive functions". American Journal of Human Genetics. 89 (3): 407–14. doi:10.1016/j.ajhg.2011.08.008. PMC3169827. PMID 21907012.
Szabo R, Skropeta D, et al. (2017). "Advancement of Sialyltransferase Inhibitors: Therapeutic Challenges and Opportunities". Med. Res. Rev. 37 (2): 210–270. doi:10.1002/med.21407. PMID 27678392. S2CID 26280291.
This article on a gene on human chromosome 1 is a stub. You can help Wikipedia by expanding it.
st3gal3, beta, galactoside, alpha, sialyltransferase, also, known, protein, which, humans, encoded, gene, identifiersaliases, eiee15, mrt12, siat6, st3galii, st3galiii, st3n, beta, galactoside, alpha, sialyltransferase, st3gal, dee15external, idsomim, 606494, . ST3 beta galactoside alpha 2 3 sialyltransferase 3 also known as ST3GAL3 is a protein which in humans is encoded by the ST3GAL3 gene 5 6 ST3GAL3IdentifiersAliasesST3GAL3 EIEE15 MRT12 SIAT6 ST3GALII ST3GalIII ST3N ST3 beta galactoside alpha 2 3 sialyltransferase 3 ST3Gal III DEE15External IDsOMIM 606494 MGI 1316659 HomoloGene 7539 GeneCards ST3GAL3Gene location Human Chr Chromosome 1 human 1 Band1p34 1Start43 705 824 bp 1 End43 931 165 bp 1 Gene location Mouse Chr Chromosome 4 mouse 2 Band4 4 D1 D2 1Start117 789 351 bp 2 End117 992 111 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed ingastrocnemius muscleganglionic eminencespermprefrontal cortexBrodmann area 9nucleus accumbenshypothalamuspopliteal arteryright coronary arteryputamenTop expressed inmotor neuronright ventriclemasseter muscleankleinternal carotid arteryintercostal muscleleft lobe of liverdigastric muscletemporal muscletriceps brachii muscleMore reference expression dataBioGPSn aGene ontologyMolecular functiontransferase activity glycosyltransferase activity sialyltransferase activity beta galactoside CMP alpha 2 3 sialyltransferase activity N acetyllactosaminide alpha 2 3 sialyltransferase activityCellular componentintegral component of membrane Golgi apparatus membrane extracellular region Golgi cisterna membrane Golgi membraneBiological processsialylation protein glycosylation O glycan processing keratan sulfate biosynthetic process oligosaccharide metabolic process protein N linked glycosylation via asparagineSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez648720441EnsemblENSG00000126091ENSMUSG00000028538UniProtQ11203P97325RefSeq mRNA NM 001270459NM 001270460NM 001270461NM 001270462NM 001270463NM 001270464NM 001270465NM 001270466NM 006279NM 174963NM 174964NM 174965NM 174966NM 174967NM 174968NM 174969NM 174970NM 174971NM 174972NM 001350619NM 001350620NM 001350621NM 001363573NM 001161774NM 001285520NM 001285521NM 009176RefSeq protein NP 001257388NP 001257389NP 001257390NP 001257391NP 001257392NP 001257393NP 001257394NP 001257395NP 006270NP 777623NP 777624NP 777625NP 777626NP 777627NP 777628NP 777629NP 777630NP 777631NP 001337548NP 001337549NP 001337550NP 001350502NP 001155246NP 001272449NP 001272450NP 033202Location UCSC Chr 1 43 71 43 93 MbChr 4 117 79 117 99 MbPubMed search 3 4 WikidataView Edit HumanView Edit Mouse Contents 1 Function 2 See also 3 References 4 Further readingFunction editThe 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 6 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 considered a congenital disorder of glycosylation See also editSialyltransferaseReferences edit a b c GRCh38 Ensembl release 89 ENSG00000126091 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000028538 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 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 a b Entrez Gene ST3GAL3 ST3 beta galactoside alpha 2 3 sialyltransferase 3 Further reading editKalyanaraman VS Rodriguez V Veronese F Rahman R Lusso P DeVico AL Copeland T Oroszlan S Gallo RC Sarngadharan MG Mar 1990 Characterization of the secreted native gp120 and gp160 of the human immunodeficiency virus type 1 AIDS Research and Human Retroviruses 6 3 371 80 doi 10 1089 aid 1990 6 371 PMID 2187500 Pal R Hoke GM Sarngadharan MG May 1989 Role of oligosaccharides in the processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1 Proceedings of the National Academy of Sciences of the United States of America 86 9 3384 8 Bibcode 1989PNAS 86 3384P doi 10 1073 pnas 86 9 3384 PMC 287137 PMID 2541446 Dewar RL Vasudevachari MB Natarajan V Salzman NP Jun 1989 Biosynthesis and processing of human immunodeficiency virus type 1 envelope glycoproteins effects of monensin on glycosylation and transport Journal of Virology 63 6 2452 6 doi 10 1128 JVI 63 6 2452 2456 1989 PMC 250699 PMID 2542563 Kozarsky K Penman M Basiripour L Haseltine W Sodroski J Krieger M 1989 Glycosylation and processing of the human immunodeficiency virus type 1 envelope protein Journal of Acquired Immune Deficiency Syndromes 2 2 163 9 PMID 2649653 Robinson WE Montefiori DC Mitchell WM 1988 Evidence that mannosyl residues are involved in human immunodeficiency virus type 1 HIV 1 pathogenesis AIDS Research and Human Retroviruses 3 3 265 82 doi 10 1089 aid 1987 3 265 PMID 2829950 Kitagawa H Paulson JC Jul 1994 Differential expression of five sialyltransferase genes in human tissues The Journal of Biological Chemistry 269 27 17872 8 doi 10 1016 S0021 9258 17 32390 6 PMID 8027041 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 Burger PC Lotscher M Streiff M Kleene R Kaissling B Berger EG Mar 1998 Immunocytochemical localization of alpha2 3 N sialyltransferase ST3Gal III in cell lines and rat kidney tissue sections evidence for golgi and post golgi localization Glycobiology 8 3 245 57 doi 10 1093 glycob 8 3 245 PMID 9451034 Taniguchi A Morishima T Tsujita Y Matsumoto Y Matsumoto K Jan 2003 Genomic structure expression and transcriptional regulation of human Gal beta 1 3 GalNAc alpha 2 3 sialyltransferase gene Biochemical and Biophysical Research Communications 300 2 570 6 doi 10 1016 S0006 291X 02 02899 1 PMID 12504121 Taniguchi A Saito K Kubota T Matsumoto K Apr 2003 Characterization of the promoter region of the human Galbeta1 3 4 GlcNAc alpha2 3 sialyltransferase III hST3Gal III gene Biochimica et Biophysica Acta BBA Gene Structure and Expression 1626 1 3 92 6 doi 10 1016 s0167 4781 03 00021 6 PMID 12697334 Saito S Aoki H Ito A Ueno S Wada T Mitsuzuka K Satoh M Arai Y Miyagi T Jul 2003 Human alpha2 3 sialyltransferase ST3Gal II is a stage specific embryonic antigen 4 synthase The Journal of Biological Chemistry 278 29 26474 9 doi 10 1074 jbc M213223200 PMID 12716912 Grahn A Barkhordar GS Larson G Mar 2002 Cloning and sequencing of nineteen transcript isoforms of the human alpha2 3 sialyltransferase gene ST3Gal III its genomic organisation and expression in human tissues Glycoconjugate Journal 19 3 197 210 doi 10 1023 A 1024253808424 PMID 12815231 S2CID 23897339 Gretschel S Haensch W Schlag PM Kemmner W 2003 Clinical relevance of sialyltransferases ST6GAL I and ST3GAL III in gastric cancer Oncology 65 2 139 45 doi 10 1159 000072339 PMID 12931020 S2CID 6438454 Jeanneau C Chazalet V Auge C Soumpasis DM Harduin Lepers A Delannoy P Imberty A Breton C Apr 2004 Structure function analysis of the human sialyltransferase ST3Gal I role of n glycosylation and a novel conserved sialylmotif The Journal of Biological Chemistry 279 14 13461 8 doi 10 1074 jbc M311764200 PMID 14722111 Grahn A Barkhordar GS Larson G 2005 Identification of seven new alpha2 3 sialyltransferase III ST3Gal III transcripts from human foetal brain Glycoconjugate Journal 20 7 8 493 500 doi 10 1023 B GLYC 0000038295 87747 0b PMID 15316282 S2CID 1544031 Van Dyken SJ Green RS Marth JD Feb 2007 Structural and mechanistic features of protein O glycosylation linked to CD8 T cell apoptosis Molecular and Cellular Biology 27 3 1096 111 doi 10 1128 MCB 01750 06 PMC 1800694 PMID 17101770 Hu H Eggers K Chen W Garshasbi M Motazacker MM Wrogemann K Kahrizi K Tzschach A Hosseini M Bahman I Hucho T Muhlenhoff M Gerardy Schahn R Najmabadi H Ropers HH Kuss AW Sep 2011 ST3GAL3 mutations impair the development of higher cognitive functions American Journal of Human Genetics 89 3 407 14 doi 10 1016 j ajhg 2011 08 008 PMC 3169827 PMID 21907012 Szabo R Skropeta D et al 2017 Advancement of Sialyltransferase Inhibitors Therapeutic Challenges and Opportunities Med Res Rev 37 2 210 270 doi 10 1002 med 21407 PMID 27678392 S2CID 26280291 nbsp This article on a gene on human chromosome 1 is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title ST3GAL3 amp oldid 1194587581, wikipedia, wiki, book, books, library,
