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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Alpha-2,8-sialyltransferase 8B''' is an [[enzyme]] that in humans is encoded by the ''ST8SIA2'' [[gene]].<ref name="pmid7559389">{{cite journal | vauthors = Scheidegger EP, Sternberg LR, Roth J, Lowe JB | title = A human STX cDNA confers polysialic acid expression in mammalian cells | journal = The Journal of Biological Chemistry | volume = 270 | issue = 39 | pages = 22685–8 | date = September 1995 | pmid = 7559389 | pmc = | doi = 10.1074/jbc.270.39.22685 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ST8SIA2 ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8128| 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 = ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 2
| HGNCid = 10870
| Symbol = ST8SIA2
| AltSymbols =; HsT19690; MGC116854; MGC116857; SIAT8B; ST8SIA-II; STX
| OMIM = 602546
| ECnumber = 
| Homologene = 4384
| MGIid = 106020
| GeneAtlas_image1 = PBB_GE_ST8SIA2_221285_at_tn.png
| Function = {{GNF_GO|id=GO:0003828 |text = alpha-N-acetylneuraminate alpha-2,8-sialyltransferase activity}} {{GNF_GO|id=GO:0008373 |text = 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:0005975 |text = carbohydrate metabolic process}} {{GNF_GO|id=GO:0006486 |text = protein amino acid glycosylation}} {{GNF_GO|id=GO:0006491 |text = N-glycan processing}} {{GNF_GO|id=GO:0007399 |text = nervous system development}} {{GNF_GO|id=GO:0009312 |text = oligosaccharide biosynthetic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 8128
    | Hs_Ensembl = ENSG00000140557
    | Hs_RefseqProtein = NP_006002
    | Hs_RefseqmRNA = NM_006011
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 15
    | Hs_GenLoc_start = 90738144
    | Hs_GenLoc_end = 90812962
    | Hs_Uniprot = Q92186
    | Mm_EntrezGene = 20450
    | Mm_Ensembl = ENSMUSG00000025789
    | Mm_RefseqmRNA = NM_009181
    | Mm_RefseqProtein = NP_033207
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 7
    | Mm_GenLoc_start = 73812635
    | Mm_GenLoc_end = 73887187
    | Mm_Uniprot = Q4VA47
  }}
}}
'''ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 2''', also known as '''ST8SIA2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ST8SIA2 ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8128| 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 is thought to catalyze the transfer of [[sialic acid]] from CMP-sialic acid to N-linked oligosaccharides and glycoproteins. The encoded protein may be found in the Golgi apparatus and may be involved in the production of polysialic acid, a modulator of the adhesive properties of neural cell adhesion molecule (NCAM1). This protein is a member of glycosyltransferase family 29.<ref name="entrez" />
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a type II membrane protein that is thought to catalyze the transfer of sialic acid from CMP-sialic acid to N-linked oligosaccharides and glycoproteins. The encoded protein may be found in the Golgi apparatus and may be involved in the production of polysialic acid, a modulator of the adhesive properties of neural cell adhesion molecule (NCAM1). This protein is a member of glycosyltransferase family 29.<ref name="entrez">{{cite web | title = Entrez Gene: ST8SIA2 ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8128| accessdate = }}</ref>
}}


==References==
== References ==
{{reflist|2}}
{{reflist}}
==Further reading==
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Munro S | title = An investigation of the role of transmembrane domains in Golgi protein retention | journal = The EMBO Journal | volume = 14 | issue = 19 | pages = 4695–704 | date = October 1995 | pmid = 7588599 | pmc = 394566 | doi =  }}
| citations =
* {{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 = July 1994 | pmid = 8027041 | doi =  }}
*{{cite journal | author=Scheidegger EP, Sternberg LR, Roth J, Lowe JB |title=A human STX cDNA confers polysialic acid expression in mammalian cells. |journal=J. Biol. Chem. |volume=270 |issue= 39 |pages= 22685-8 |year= 1995 |pmid= 7559389 |doi=  }}
* {{cite journal | vauthors = Kojima N, Tachida Y, Yoshida Y, Tsuji S | title = Characterization of mouse ST8Sia II (STX) as a neural cell adhesion molecule-specific polysialic acid synthase. Requirement of core alpha1,6-linked fucose and a polypeptide chain for polysialylation | journal = The Journal of Biological Chemistry | volume = 271 | issue = 32 | pages = 19457–63 | date = August 1996 | pmid = 8702635 | doi = 10.1074/jbc.271.32.19457 }}
*{{cite journal  | author=Munro S |title=An investigation of the role of transmembrane domains in Golgi protein retention. |journal=EMBO J. |volume=14 |issue= 19 |pages= 4695-704 |year= 1995 |pmid= 7588599 |doi=  }}
* {{cite journal | vauthors = Angata K, Nakayama J, Fredette B, Chong K, Ranscht B, Fukuda M | title = 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 | journal = The Journal of Biological Chemistry | volume = 272 | issue = 11 | pages = 7182–90 | date = March 1997 | pmid = 9054414 | doi = 10.1074/jbc.272.11.7182 }}
*{{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 | vauthors = Close BE, Colley KJ | title = In vivo autopolysialylation and localization of the polysialyltransferases PST and STX | journal = The Journal of Biological Chemistry | volume = 273 | issue = 51 | pages = 34586–93 | date = December 1998 | pmid = 9852130 | doi = 10.1074/jbc.273.51.34586 }}
*{{cite journal | author=Kojima N, Tachida Y, Yoshida Y, Tsuji S |title=Characterization of mouse ST8Sia II (STX) as a neural cell adhesion molecule-specific polysialic acid synthase. Requirement of core alpha1,6-linked fucose and a polypeptide chain for polysialylation. |journal=J. Biol. Chem. |volume=271 |issue= 32 |pages= 19457-63 |year= 1996 |pmid= 8702635 |doi= }}
* {{cite journal | vauthors = Angata K, Suzuki M, McAuliffe J, Ding Y, Hindsgaul O, Fukuda M | title = 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 | journal = The Journal of Biological Chemistry | volume = 275 | issue = 24 | pages = 18594–601 | date = June 2000 | pmid = 10766765 | doi = 10.1074/jbc.M910204199 }}
*{{cite journal | author=Angata K, Nakayama J, Fredette B, ''et al.'' |title=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. |journal=J. Biol. Chem. |volume=272 |issue= 11 |pages= 7182-90 |year= 1997 |pmid= 9054414 |doi= }}
* {{cite journal | vauthors = Close BE, Wilkinson JM, Bohrer TJ, Goodwin CP, Broom LJ, Colley KJ | title = The polysialyltransferase ST8Sia II/STX: posttranslational processing and role of autopolysialylation in the polysialylation of neural cell adhesion molecule | journal = Glycobiology | volume = 11 | issue = 11 | pages = 997–1008 | date = November 2001 | pmid = 11744634 | doi = 10.1093/glycob/11.11.997 }}
*{{cite journal | author=Close BE, Colley KJ |title=In vivo autopolysialylation and localization of the polysialyltransferases PST and STX. |journal=J. Biol. Chem. |volume=273 |issue= 51 |pages= 34586-93 |year= 1999 |pmid= 9852130 |doi= }}
* {{cite journal | vauthors = Angata K, Suzuki M, Fukuda M | title = ST8Sia II and ST8Sia IV polysialyltransferases exhibit marked differences in utilizing various acceptors containing oligosialic acid and short polysialic acid. The basis for cooperative polysialylation by two enzymes | journal = The Journal of Biological Chemistry | volume = 277 | issue = 39 | pages = 36808–17 | date = September 2002 | pmid = 12138100 | doi = 10.1074/jbc.M204632200 }}
*{{cite journal | author=Angata K, Suzuki M, McAuliffe J, ''et al.'' |title=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. |journal=J. Biol. Chem. |volume=275 |issue= 24 |pages= 18594-601 |year= 2000 |pmid= 10766765 |doi= 10.1074/jbc.M910204199 }}
* {{cite journal | vauthors = Lazzell DR, Belizaire R, Thakur P, Sherry DM, Janz R | title = SV2B regulates synaptotagmin 1 by direct interaction | journal = The Journal of Biological Chemistry | volume = 279 | issue = 50 | pages = 52124–31 | date = December 2004 | pmid = 15466855 | doi = 10.1074/jbc.M407502200 }}
*{{cite journal | author=Close BE, Wilkinson JM, Bohrer TJ, ''et al.'' |title=The polysialyltransferase ST8Sia II/STX: posttranslational processing and role of autopolysialylation in the polysialylation of neural cell adhesion molecule. |journal=Glycobiology |volume=11 |issue= 11 |pages= 997-1008 |year= 2002 |pmid= 11744634 |doi= }}
* {{cite journal | vauthors = Beecken WD, Engl T, Ogbomo H, Relja B, Cinatl J, Bereiter-Hahn J, Oppermann E, Jonas D, Blaheta RA | title = Valproic acid modulates NCAM polysialylation and polysialyltransferase mRNA expression in human tumor cells | journal = International Immunopharmacology | volume = 5 | issue = 4 | pages = 757–69 | date = April 2005 | pmid = 15710344 | doi = 10.1016/j.intimp.2004.12.009 }}
*{{cite journal | author=Angata K, Suzuki M, Fukuda M |title=ST8Sia II and ST8Sia IV polysialyltransferases exhibit marked differences in utilizing various acceptors containing oligosialic acid and short polysialic acid. The basis for cooperative polysialylation by two enzymes. |journal=J. Biol. Chem. |volume=277 |issue= 39 |pages= 36808-17 |year= 2002 |pmid= 12138100 |doi= 10.1074/jbc.M204632200 }}
* {{cite journal | vauthors = Arai M, Yamada K, Toyota T, Obata N, Haga S, Yoshida Y, Nakamura K, Minabe Y, Ujike H, Sora I, Ikeda K, Mori N, Yoshikawa T, Itokawa M | title = Association between polymorphisms in the promoter region of the sialyltransferase 8B (SIAT8B) gene and schizophrenia | journal = Biological Psychiatry | volume = 59 | issue = 7 | pages = 652–9 | date = April 2006 | pmid = 16229822 | doi = 10.1016/j.biopsych.2005.08.016 }}
*{{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  |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 }}
*{{cite journal  | author=Clark HF, Gurney AL, Abaya E, ''et al.'' |title=The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. |journal=Genome Res. |volume=13 |issue= 10 |pages= 2265-70 |year= 2003 |pmid= 12975309 |doi= 10.1101/gr.1293003 }}
*{{cite journal  | author=Lazzell DR, Belizaire R, Thakur P, ''et al.'' |title=SV2B regulates synaptotagmin 1 by direct interaction. |journal=J. Biol. Chem. |volume=279 |issue= 50 |pages= 52124-31 |year= 2005 |pmid= 15466855 |doi= 10.1074/jbc.M407502200 }}
*{{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=Beecken WD, Engl T, Ogbomo H, ''et al.'' |title=Valproic acid modulates NCAM polysialylation and polysialyltransferase mRNA expression in human tumor cells. |journal=Int. Immunopharmacol. |volume=5 |issue= 4 |pages= 757-69 |year= 2005 |pmid= 15710344 |doi= 10.1016/j.intimp.2004.12.009 }}
*{{cite journal | author=Arai M, Yamada K, Toyota T, ''et al.'' |title=Association between polymorphisms in the promoter region of the sialyltransferase 8B (SIAT8B) gene and schizophrenia. |journal=Biol. Psychiatry |volume=59 |issue= 7 |pages= 652-9 |year= 2006 |pmid= 16229822 |doi= 10.1016/j.biopsych.2005.08.016 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{gene-15-stub}}
{{WikiDoc Sources}}

Latest revision as of 12:45, 9 January 2019

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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

Alpha-2,8-sialyltransferase 8B is an enzyme that in humans is encoded by the ST8SIA2 gene.[1][2]

Function

The protein encoded by this gene is a type II membrane protein that is thought to catalyze the transfer of sialic acid from CMP-sialic acid to N-linked oligosaccharides and glycoproteins. The encoded protein may be found in the Golgi apparatus and may be involved in the production of polysialic acid, a modulator of the adhesive properties of neural cell adhesion molecule (NCAM1). This protein is a member of glycosyltransferase family 29.[2]

References

  1. ↑ Scheidegger EP, Sternberg LR, Roth J, Lowe JB (September 1995). "A human STX cDNA confers polysialic acid expression in mammalian cells". The Journal of Biological Chemistry. 270 (39): 22685–8. doi:10.1074/jbc.270.39.22685. PMID 7559389.
  2. ↑ 2.0 2.1 "Entrez Gene: ST8SIA2 ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 2".

Further reading

  • Munro S (October 1995). "An investigation of the role of transmembrane domains in Golgi protein retention". The EMBO Journal. 14 (19): 4695–704. PMC 394566. PMID 7588599.
  • Kitagawa H, Paulson JC (July 1994). "Differential expression of five sialyltransferase genes in human tissues". The Journal of Biological Chemistry. 269 (27): 17872–8. PMID 8027041.
  • Kojima N, Tachida Y, Yoshida Y, Tsuji S (August 1996). "Characterization of mouse ST8Sia II (STX) as a neural cell adhesion molecule-specific polysialic acid synthase. Requirement of core alpha1,6-linked fucose and a polypeptide chain for polysialylation". The Journal of Biological Chemistry. 271 (32): 19457–63. doi:10.1074/jbc.271.32.19457. PMID 8702635.
  • Angata K, Nakayama J, Fredette B, Chong K, Ranscht B, Fukuda M (March 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". The Journal of Biological Chemistry. 272 (11): 7182–90. doi:10.1074/jbc.272.11.7182. PMID 9054414.
  • Close BE, Colley KJ (December 1998). "In vivo autopolysialylation and localization of the polysialyltransferases PST and STX". The Journal of Biological Chemistry. 273 (51): 34586–93. doi:10.1074/jbc.273.51.34586. PMID 9852130.
  • Angata K, Suzuki M, McAuliffe J, Ding Y, Hindsgaul O, Fukuda M (June 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". The Journal of Biological Chemistry. 275 (24): 18594–601. doi:10.1074/jbc.M910204199. PMID 10766765.
  • Close BE, Wilkinson JM, Bohrer TJ, Goodwin CP, Broom LJ, Colley KJ (November 2001). "The polysialyltransferase ST8Sia II/STX: posttranslational processing and role of autopolysialylation in the polysialylation of neural cell adhesion molecule". Glycobiology. 11 (11): 997–1008. doi:10.1093/glycob/11.11.997. PMID 11744634.
  • Angata K, Suzuki M, Fukuda M (September 2002). "ST8Sia II and ST8Sia IV polysialyltransferases exhibit marked differences in utilizing various acceptors containing oligosialic acid and short polysialic acid. The basis for cooperative polysialylation by two enzymes". The Journal of Biological Chemistry. 277 (39): 36808–17. doi:10.1074/jbc.M204632200. PMID 12138100.
  • Lazzell DR, Belizaire R, Thakur P, Sherry DM, Janz R (December 2004). "SV2B regulates synaptotagmin 1 by direct interaction". The Journal of Biological Chemistry. 279 (50): 52124–31. doi:10.1074/jbc.M407502200. PMID 15466855.
  • Beecken WD, Engl T, Ogbomo H, Relja B, Cinatl J, Bereiter-Hahn J, Oppermann E, Jonas D, Blaheta RA (April 2005). "Valproic acid modulates NCAM polysialylation and polysialyltransferase mRNA expression in human tumor cells". International Immunopharmacology. 5 (4): 757–69. doi:10.1016/j.intimp.2004.12.009. PMID 15710344.
  • Arai M, Yamada K, Toyota T, Obata N, Haga S, Yoshida Y, Nakamura K, Minabe Y, Ujike H, Sora I, Ikeda K, Mori N, Yoshikawa T, Itokawa M (April 2006). "Association between polymorphisms in the promoter region of the sialyltransferase 8B (SIAT8B) gene and schizophrenia". Biological Psychiatry. 59 (7): 652–9. doi:10.1016/j.biopsych.2005.08.016. PMID 16229822.
  • Szabo R, Skropeta D, et al. (2017). "Advancement of Sialyltransferase Inhibitors: Therapeutic Challenges and Opportunities". Med. Res. Rev. 37: 210–270. doi:10.1002/med.21407.
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