BioPAX pathway converted from "N-Glycan antennae elongation" in the Reactome database. N-Glycan antennae elongation N-Glycan antennae elongation This event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a> 2.4.1.145 Addition of GlcNAc to position 4 by N-acetylglucosaminyltransferase (GnT)-IV Addition of GlcNAc to position 4 by N-acetylglucosaminyltransferase (GnT)-IV This event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a> Reactome DB_ID: 975910 1 Golgi lumen GO 0005796 N-glycan [ChEBI:59520] N-glycan Reactome http://www.reactome.org ChEBI 59520 Reactome DB_ID: 914003 1 UDP-N-acetyl-alpha-D-glucosamine(2-) [ChEBI:57705] UDP-N-acetyl-alpha-D-glucosamine(2-) UDP-N-acetyl-alpha-D-glucosamine dianion UDP-N-acetyl-alpha-D-glucosamine uridine 5'-[3-(acetamido-2-deoxy-alpha-D-glucopyranosyl) diphosphate] ChEBI 57705 Reactome DB_ID: 981616 1 Glycoprotein with GlcNAc in position 4 [Golgi lumen] Glycoprotein with GlcNAc in position 4 PHYSIOL-LEFT-TO-RIGHT ACTIVATION Converted from EntitySet in Reactome Reactome DB_ID: 10559883 Golgi membrane GO 0000139 MGAT4s [Golgi membrane] Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntity MGAT4A [Golgi membrane] MGAT4B [Golgi membrane] MGAT4C [Golgi membrane] Gallus gallus NCBI Taxonomy 9031 UniProt Q5F407 UniProt A0A1D5PP75 UniProt R4GKF3 GO 0008454 GO molecular function Reactome Database ID Release 81 10559884 Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10559884 Reactome Database ID Release 81 10559886 Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10559886 Reactome R-GGA-975903 1 Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-GGA-975903.1 N-acetylglucosaminyltransferase (GnT)-IV catalyzes the addition of GlcNAc beta,1,4 on the GlcNAc beta1,2 Man,alpha1,3 arm of both complex and hybrid N-glycans (Oguri S et al, 2006). Two human GnT-IV isozymes have been characterized (MGAT4A, MGAT4B) , plus a putative MGAT4C on chromosome 2 (Furukawa T et al, 1999). Aberrant expression of MGAT4A or MGAT4B is associated with pancreatic cancer (Ide Y et al, 2006; Kudo T et al , 2007) 17006639 Pubmed 2006 Kinetic properties and substrate specificities of two recombinant human N-acetylglucosaminyltransferase-IV isozymes Oguri, S Yoshida, A Minowa, MT Takeuchi, M Glycoconj J 23:473-80 17488527 Pubmed 2007 N-glycan alterations are associated with drug resistance in human hepatocellular carcinoma Kudo, T Nakagawa, H Takahashi, M Hamaguchi, J Kamiyama, N Yokoo, H Nakanishi, K Nakagawa, T Kamiyama, T Deguchi, K Nishimura, S Todo, S Mol Cancer 6:32 16434023 Pubmed 2006 Aberrant expression of N-acetylglucosaminyltransferase-IVa and IVb (GnT-IVa and b) in pancreatic cancer Ide, Y Miyoshi, E Nakagawa, T Gu, J Tanemura, M Nishida, T Ito, T Yamamoto, H Kozutsumi, Y Taniguchi, N Biochem Biophys Res Commun 341:478-82 10570912 Pubmed 1999 Cloning and characterization of the human UDP-N-acetylglucosamine: alpha-1,3-D-mannoside beta-1,4-N-acetylglucosaminyltransferase IV-homologue (hGnT-IV-H) gene Furukawa, T Youssef, EM Yatsuoka, T Yokoyama, T Makino, N Inoue, H Fukushige, S Hoshi, M Hayashi, Y Sunamura, M Horii, A J Hum Genet 44:397-401 inferred by electronic annotation IEA GO IEA 2.4.1.155 Addition of GlcNAc to position 5 by MGAT5 Addition of GlcNAc to position 5 by MGAT5 This event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a> Reactome DB_ID: 975910 1 Reactome DB_ID: 914003 1 Reactome DB_ID: 981617 1 Glycoprotein with GlcNAc in position 5 [Golgi lumen] Glycoprotein with GlcNAc in position 5 PHYSIOL-LEFT-TO-RIGHT ACTIVATION Reactome DB_ID: 10559890 UniProt:F1NEL5 MGAT5 UniProt F1NEL5 Chain Coordinates 1 EQUAL 741 EQUAL GO 0030144 GO molecular function Reactome Database ID Release 81 10559891 Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10559891 Reactome Database ID Release 81 10559893 Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10559893 Reactome R-GGA-975916 1 Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-GGA-975916.1 N-acetylglucosaminyltransferase (GnT)-V catalyzes the addition of GlcNAc beta 1,4 on the GlcNAc beta1,2 Man,alpha1,6 arm of complex type N-Glycans (Park C et al, 1999; Granowski M et al, 2000; Wang L et al, 2007). The activity of MGAT5 competes with MGAT3 (Pinho SS et al, 2009) and is associated with gastric cancer (Tian H et al, 2008) and multiple sclerosis (Brynedal B et al, 2010). 10395745 Pubmed 1999 Characterization of UDP-N-acetylglucosamine:alpha-6-d-mannoside beta-1,6-N-acetylglucosaminyltransferase V from a human hepatoma cell line Hep3B Park, C Jin, UH Lee, YC Cho, TJ Kim, CH Arch Biochem Biophys 367:281-8 16924681 Pubmed 2007 Increase in beta1-6 GlcNAc branching caused by N-acetylglucosaminyltransferase V directs integrin beta1 stability in human hepatocellular carcinoma cell line SMMC-7721 Wang, L Liang, Y Li, Z Cai, X Zhang, W Wu, G Jin, J Fang, Z Yang, Y Zha, X J Cell Biochem 100:230-41 20117844 Pubmed 2010 MGAT5 alters the severity of multiple sclerosis Brynedal, B Wojcik, J Esposito, F Debailleul, V Yaouanq, J Martinelli-Boneschi, F Edan, G Comi, G Hillert, J Abderrahim, H J Neuroimmunol 220:120-4 18931531 Pubmed 2008 The implication of N-acetylglucosaminyltransferase V expression in gastric cancer Tian, H Miyoshi, E Kawaguchi, N Shaker, M Ito, Y Taniguchi, N Tsujimoto, M Matsuura, N Pathobiology 75:288-94 19403558 Pubmed 2009 The role of N-acetylglucosaminyltransferase III and V in the post-transcriptional modifications of E-cadherin Pinho, SS Reis, CA Paredes, J Magalhães, AM Ferreira, AC Figueiredo, J Xiaogang, W Carneiro, F Gärtner, F Seruca, R Hum Mol Genet 18:2599-608 10700233 Pubmed 2000 Suppression of tumor growth and metastasis in Mgat5-deficient mice Granovsky, M Fata, J Pawling, J Muller, WJ Khokha, R Dennis, JW Nat Med 6:306-12 inferred by electronic annotation IEA GO IEA 2.4.1.38 Addition of galactose by beta 4-galactosyltransferases Addition of galactose by beta 4-galactosyltransferases This event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a> Reactome DB_ID: 975910 1 Reactome DB_ID: 735682 1 UDP-D-galactose(2-) [ChEBI:58439] UDP-D-galactose(2-) uridine 5'-[3-(D-galactopyranosyl) diphosphate] UDP-D-galactose dianion ChEBI 58439 Reactome DB_ID: 981618 1 Glycoprotein with galactose [Golgi lumen] Glycoprotein with galactose PHYSIOL-LEFT-TO-RIGHT ACTIVATION Converted from EntitySet in Reactome Reactome DB_ID: 10559931 B4GALT1-6 homodimers [Golgi membrane] Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntity GO 0003831 GO molecular function Reactome Database ID Release 81 10559932 Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10559932 Reactome Database ID Release 81 10559934 Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10559934 Reactome R-GGA-975919 1 Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-GGA-975919.1 Addition of a galactose residue on N-acetylglucosamine. The family of beta 4-galactosyltransferases is composed by at least six known members with different K(m) and acceptor specifities (Guo S et al, 2001) and probably originated by duplication (Lo NW et al, 1998). B4GALT1 is associated with Congenital Disorder of Glycosylation of type IId (Hansske B et al, 2002), and is expressed as two splicing isoforms of which only one is localizated in the Golgi system (Lopez LC et al, 1991; Schaub BE et al, 2006). B4GALT2 is key in the regulation of proteins involved in neuronal development (Sasaki N et <br>al, 2005). 11588157 Pubmed 2001 Galactosylation of N-linked oligosaccharides by human beta-1,4-galactosyltransferases I, II, III, IV, V, and VI expressed in Sf-9 cells Guo, S Sato, T Shirane, K Furukawa, K Glycobiology 11:813-20 9597550 Pubmed 1998 The expanding beta 4-galactosyltransferase gene family: messages from the databanks Lo, NW Shaper, JH Pevsner, J Shaper, NL Glycobiology 8:517-26 11901181 Pubmed 2002 Deficiency of UDP-galactose:N-acetylglucosamine beta-1,4-galactosyltransferase I causes the congenital disorder of glycosylation type IId Hansske, B Thiel, C Lübke, T Hasilik, M Höning, S Peters, V Heidemann, PH Hoffmann, GF Berger, EG von Figura, K Körner, C J Clin Invest 109:725-33 17021253 Pubmed 2006 Transition of galactosyltransferase 1 from trans-Golgi cisterna to the trans-Golgi network is signal mediated Schaub, BE Berger, B Berger, EG Rohrer, J Mol Biol Cell 17:5153-62 1714903 Pubmed 1991 Evidence for a molecular distinction between Golgi and cell surface forms of beta 1,4-galactosyltransferase Lopez, LC Youakim, A Evans, SC Shur, BD J Biol Chem 266:15984-91 15939404 Pubmed 2005 beta4GalT-II is a key regulator of glycosylation of the proteins involved in neuronal development Sasaki, N Manya, H Okubo, R Kobayashi, K Ishida, Hiroko Toda, T Endo, T Nishihara, S Biochem Biophys Res Commun 333:131-7 inferred by electronic annotation IEA GO IEA 2.4.99.1 ST6GAL1 transfers Neu5Ac to terminal Gal of N-glycans ST6GAL1 transfers Neu5Ac to terminal Gal of N-glycans Addition of alpha-2,6-sialic acid to terminal galactose of N-glycans by ST6GAL1 This event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a> Reactome DB_ID: 975910 1 Reactome DB_ID: 975925 1 N-acetylneuraminic acid [ChEBI:17012] N-acetylneuraminic acid ChEBI 17012 Reactome DB_ID: 981615 1 Glycoprotein-Neu5Ac [Golgi lumen] Glycoprotein-Neu5Ac PHYSIOL-LEFT-TO-RIGHT ACTIVATION Reactome DB_ID: 10559866 UniProt:F1NRE4 ST6GAL1 UniProt F1NRE4 1 EQUAL 406 EQUAL GO 0003835 GO molecular function Reactome Database ID Release 81 10559867 Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10559867 Reactome Database ID Release 81 10559869 Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10559869 Reactome R-GGA-975902 1 Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-GGA-975902.1 Addition of sialic acid to galactose-containing N-glycan. Sialic acid is usually found at terminal positions of the N-glycan. This imparts a negative charge at neutral pH which affects the chemico-physical and biological properties of the N-glycans (for review, see Schauer 2000); moreover, this modification can lead to the addition of extraordinarily long antennae such as polysialic acid (hundreds of sials) or polylactosamine repeats (dozens of disaccharide repeats) (Harduin-Lepers 2001), while the number of modifications on the antennae of N-glycans is usually lower.<br>There are over 20 sialyltransferases known in humans, 5 of which are known to act on N-glycans. Beta-galactoside alpha-2,6-sialyltransferase 1 (ST6GAL1) is the only sialyltransferase known to transfer sialic acid to galactose on N-Glycans (Dall'Olio 2000). A second beta-galactoside alpha-2,6-sialyltransferase has been characterized, but this enzyme acts mainly on oligosaccharides (Krzewinski-Recchi et al. 2003). Neu5Ac can also be added via an alpha-2,3-linkage to galactose on N-glycans by CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4 (ST3GAL4) (Ellies et al. 2002). ST8Sia II (ST8SIA2), ST8Sia III (ST8SIA3), and ST8Sia IV (ST8SIA6) have alpha-2,8-activity (Angata et al. 1997, Angata et al. 2000, Angata & Fuduka 2003). 11530204 Pubmed 2001 The human sialyltransferase family Harduin-Lepers, A Vallejo-Ruiz, V Krzewinski-Recchi, MA Samyn-Petit, B Julien, S Delannoy, P Biochimie 83:727-37 11425186 Pubmed 2000 The sialyl-alpha2,6-lactosaminyl-structure: biosynthesis and functional role Dall'Olio, F Glycoconj J 17:669-76 12603328 Pubmed 2003 Identification and functional expression of a second human beta-galactoside alpha2,6-sialyltransferase, ST6Gal II Krzewinski-Recchi, MA Julien, S Juliant, S Teintenier-Lelièvre, M Samyn-Petit, B Montiel, MD Mir, AM Cerutti, M Harduin-Lepers, A Delannoy, P Eur J Biochem 270:950-61 12765789 Pubmed 2003 Polysialyltransferases: major players in polysialic acid synthesis on the neural cell adhesion molecule Angata, K Fukuda, M Biochimie 85:195-206 12097641 Pubmed 2002 Sialyltransferase ST3Gal-IV operates as a dominant modifier of hemostasis by concealing asialoglycoprotein receptor ligands Ellies, LG Ditto, D Levy, GG Wahrenbrock, M Ginsburg, D Varki, A Le, DT Marth, JD Proc Natl Acad Sci U S A 99:10042-7 11421344 Pubmed 2000 Achievements and challenges of sialic acid research Schauer, R Glycoconj J 17:485-99 10766765 Pubmed 2000 Differential biosynthesis of polysialic acid on neural cell adhesion molecule (NCAM) and oligosaccharide acceptors by three distinct alpha 2,8-sialyltransferases, ST8Sia IV (PST), ST8Sia II (STX), and ST8Sia III Angata, K Suzuki, M McAuliffe, J Ding, Y Hindsgaul, O Fukuda, M J Biol Chem 275:18594-601 9054414 Pubmed 1997 Human STX polysialyltransferase forms the embryonic form of the neural cell adhesion molecule. Tissue-specific expression, neurite outgrowth, and chromosomal localization in comparison with another polysialyltransferase, PST Angata, K Nakayama, J Fredette, B Chong, K Ranscht, B Fukuda, M J Biol Chem 272:7182-90 inferred by electronic annotation IEA GO IEA 2.4.99.8 ST8SIA2,3,6 transfer Neu5Ac to terminal Gal of N-glycans ST8SIA2,3,6 transfer Neu5Ac to terminal Gal of N-glycans Addition of alpha-2,8-sialic acid to N-glycan over a galactose by ST8SIAs This event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a> Reactome DB_ID: 975910 1 Reactome DB_ID: 975925 1 Reactome DB_ID: 981615 1 PHYSIOL-LEFT-TO-RIGHT ACTIVATION Converted from EntitySet in Reactome Reactome DB_ID: 10562979 ST8SIA2,3,6 [Golgi membrane] Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntity ST8SIA6 [Golgi membrane] SIAT8C [Golgi membrane] ST8SIA2 [Golgi membrane] UniProt A0A1D5PEI3 UniProt Q6ZXD0 UniProt F1NIM6 GO 0003828 GO molecular function Reactome Database ID Release 81 10562980 Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10562980 Reactome Database ID Release 81 10562982 Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10562982 Reactome R-GGA-1022133 1 Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-GGA-1022133.1 Addition of sialic acid (Neu5Ac) to galactose-containing N-glycan. Sialic acid is usually found at terminal positions of the N-glycan. This imparts a negative charge at neutral pH which affects the chemico-physical and biological properties of the N-glycans (for a review, see Schauer 2000); moreover, this modification can lead to the addition of extraordinarily long antennae such as polysialic acid (hundreds of sials) or polylactosamine repeats (dozens of disaccharide repeats) (Harduin-Lepers 2001), while the number of modifications on the antennae of N-glycans is usually lower.<br>There are over 20 sialyltransferases known in humans, 5 of which are known to act on N-glycans. Beta-galactoside alpha-2,6-sialyltransferase 1<br>(ST6GAL1) is the only sialyltransferase known to transfer Neu5Ac to Gal on N-Glycans (Dall'Olio 2000). A second beta-galactoside alpha-2,6-sialyltransferase has been characterized, but this enzyme acts mainly on oligosaccharides (Krzewinski-Recchi et al. 2003). Neu5Ac can also be added via an alpha-2,3-linkage to Gal on N-glycans by CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4 (ST3GAL4) (Ellies et al. 2002). ST8Sia II (ST8SIA2), ST8Sia III (ST8SIA3), and ST8Sia IV (ST8SIA6) have alpha-2,8-activity (Angata et al. 1997, Angata et al. 2000, Angata & Fuduka 2003). inferred by electronic annotation IEA GO IEA 2.4.99.4 ST3GAL4 transfers Neu5Ac to terminal Gal of N-glycans ST3GAL4 transfers Neu5Ac to terminal Gal of N-glycans Addition of alpha-2,3-sialic acid to N-glycan over a galactose by ST3GAL4 This event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a> Reactome DB_ID: 975910 1 Reactome DB_ID: 975925 1 Reactome DB_ID: 981615 1 PHYSIOL-LEFT-TO-RIGHT ACTIVATION Reactome DB_ID: 10560207 UniProt:A0A1D5PWH2 C20orf173 UniProt A0A1D5PWH2 1 EQUAL 333 EQUAL GO 0003836 GO molecular function Reactome Database ID Release 81 10562963 Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10562963 Reactome Database ID Release 81 10562965 Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10562965 Reactome R-GGA-1022129 1 Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-GGA-1022129.1 Addition of sialic acid (Neu5Ac) to galactose-containing N-glycan. Neu5Ac is usually found at terminal positions of the N-glycan. This imparts a negative charge at neutral pH which affects the chemico-physical and biological properties of the N-glycans (for a review, see Schauer 2000); moreover, this modification can lead to the addition of extraordinarily long antennae such as polysialic acid (hundreds of sials) or polylactosamine repeats (dozens of disaccharide repeats) (Harduin-Lepers 2001), while the number of modifications on the antennae of N-glycans is usually lower.<br>There are over 20 sialyltransferases known in humans, 5 of which are known to act on N-glycans. Beta-galactoside alpha-2,6-sialyltransferase 1 (ST6GAL1) is the only sialyltransferase known to transfer Neu5Ac to galactose (Gal) on N-Glycans (Dall'Olio 2000). A second beta-Galactoside alpha-2,6-sialyltransferase has been characterized, but this enzyme acts mainly on oligosaccharides (Krzewinski-Recchi et al. 2003). Neu5Ac can also be added via an alpha-2,3-linkage to Gal on N-glycans by CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4 (ST3GAL4) (Ellies et al. 2002). ST8Sia II (ST8SIA2), ST8Sia III (ST8SIA3), and ST8Sia IV (ST8SIA6) have alpha-2,8-activity (Angata et al. 1997, Angata et al. 2000; Angata & Fuduka 2003). inferred by electronic annotation IEA GO IEA Reactome Database ID Release 81 10616921 Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10616921 Reactome R-GGA-975577 1 Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-GGA-975577.1 N-glycans are further modified after the commitment to Complex or Hybrid N-glycans. The exact structure of the network of metabolic reactions involved is complex and not yet validated experimentally. Here we will show a generic reaction for each of the genes known to be involved in N-Glycosylation.<br>For a better annotation of the reactions and genes involved in the synthesis of Complex and Hybrid N-glycans we recommend the GlycoGene Database (Ito H. et al, 2010) (http://riodb.ibase.aist.go.jp/rcmg/ggdb/textsearch.jsp) for annotations of genes, and the Consortium for Functional Genomics (http://riodb.ibase.aist.go.jp/rcmg/ggdb/textsearch.jsp) for annotation of Glycan structures and reactions. Moreover, a computationally inferred prediction for the structure of this network is available through the software GlycoVis (Hossler P. et. al. 2006). 20816477 Pubmed 2010 In vitro and in vivo enzymatic syntheses and mass spectrometric database for N-glycans and o-glycans Ito, H Chiba, Y Kameyama, A Sato, T Narimatsu, H Methods Enzymol 478:127-49 16807922 Pubmed 2006 GlycoVis: visualizing glycan distribution in the protein N-glycosylation pathway in mammalian cells Hossler, P Goh, LT Lee, MM Hu, WS Biotechnol Bioeng 95:946-60 inferred by electronic annotation IEA GO IEA