GALNT2: Difference between revisions

Jump to navigation Jump to search
VisualWikitext
WikiBot (talk | contribs)
Bots, Bureaucrats, bureaucrats, interwiki, nocaptcha, Administrators
57,550 edits
m Robot: Automated text replacement (-{{WikiDoc Cardiology Network Infobox}} +, -<references /> +{{reflist|2}}, -{{reflist}} +{{reflist|2}})
 
imported>Veryproicelandic
added some links, removed that flag...
 
(One intermediate revision by one other user not shown)
Line 1: Line 1:
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Polypeptide N-acetylgalactosaminyltransferase 2''' is an [[enzyme]] that in [[human]]s is encoded by the ''GALNT2'' [[gene]].<ref name="pmid9592121">{{cite journal |vauthors=Bennett EP, Weghuis DO, Merkx G, van Kessel AG, Eiberg H, Clausen H | title = Genomic organization and chromosomal localization of three members of the UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase family | journal = Glycobiology | volume = 8 | issue = 6 | pages = 547–55 |date=Jul 1998 | pmid = 9592121 | pmc =  | doi =10.1093/glycob/8.6.547 }}</ref><ref name="pmid7592619">{{cite journal |vauthors=White T, Bennett EP, Takio K, Sorensen T, Bonding N, Clausen H | title = Purification and cDNA cloning of a human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase | journal = J Biol Chem | volume = 270 | issue = 41 | pages = 24156–65 |date=Dec 1995 | pmid = 7592619 | pmc = | doi =10.1074/jbc.270.41.24156  }}</ref><ref name="entrez"/>
| 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. -->
{{GNF_Protein_box
| image = PBB_Protein_GALNT2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2ffu.
| PDB = {{PDB2|2ffu}}, {{PDB2|2ffv}}
| Name = UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2 (GalNAc-T2)
| HGNCid = 4124
| Symbol = GALNT2
| AltSymbols =; GalNAc-T2
| OMIM = 602274
| ECnumber =
| Homologene = 3297
| MGIid = 894694
  | GeneAtlas_image1 = PBB_GE_GALNT2_217788_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_GALNT2_217787_s_at_tn.png
  | Function = {{GNF_GO|id=GO:0004653 |text = polypeptide N-acetylgalactosaminyltransferase activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005529 |text = sugar binding}} {{GNF_GO|id=GO:0016757 |text = transferase activity, transferring glycosyl groups}} {{GNF_GO|id=GO:0030145 |text = manganese ion binding}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006493 |text = protein amino acid O-linked glycosylation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2590
    | Hs_Ensembl = ENSG00000143641
    | Hs_RefseqProtein = NP_004472
    | Hs_RefseqmRNA = NM_004481
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 228269579
    | Hs_GenLoc_end = 228484493
    | Hs_Uniprot = Q10471
    | Mm_EntrezGene = 108148
    | Mm_Ensembl = ENSMUSG00000031977
    | Mm_RefseqmRNA = NM_139272
    | Mm_RefseqProtein = NP_644678
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 8
    | Mm_GenLoc_start = 127117484
    | Mm_GenLoc_end = 127231812
    | Mm_Uniprot = Q3UA32
  }}
}}
'''UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2 (GalNAc-T2)''', also known as '''GALNT2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GALNT2 UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2 (GalNAc-T2)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2590| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = This gene encodes polypeptide N-acetylgalactosaminyltransferase 2, a member of the GalNAc-transferases family. This family transfers an N-acetyl galactosamine to the hydroxyl group of a serine or threonine residue in the first step of O-linked oligosaccharide biosynthesis. Individual GalNAc-transferases have distinct activities and initiation of O-glycosylation in a cell is regulated by a repertoire of GalNAc-transferases.<ref name="entrez">{{cite web | title = Entrez Gene: GALNT2 UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2 (GalNAc-T2)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2590| accessdate = }}</ref>
| summary_text = This gene encodes [[polypeptide]] [[N-acetylgalactosaminyltransferase II|N-acetylgalactosaminyltransferase 2]], a member of the GalNAc-[[transferase]]s family. This family transfers an N-acetyl [[galactosamine]] to the [[hydroxyl group]] of a [[serine]] or [[threonine]] residue in the first step of [[Olinked oligosaccharide|O-linked oligosaccharide]] [[biosynthesis]]. The localization site of this particular enzyme is preponderantly the [[Trans Golgi network|trans-Golgi]].<ref name="trans">{{cite web | title = African Swine Fever Virus Causes Microtubule-Dependent Dispersal of trans-Golgi Network| url = http://jvi.asm.org/cgi/reprint/80/22/11385.pdf| accessdate = }}</ref> Individual GalNAc-transferases have distinct activities, and initiation of [[O-glycosylation]] in a [[cell (biology)|cell]] is regulated by a repertoire of GalNAc-transferases.<ref name="entrez">{{cite web | title = Entrez Gene: GALNT2 UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2 (GalNAc-T2)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2590| accessdate = }}</ref>
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=White T, Bennett EP, Takio K, ''et al.'' |title=Purification and cDNA cloning of a human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase. |journal=J. Biol. Chem. |volume=270 |issue= 41 |pages= 24156-65 |year= 1995 |pmid= 7592619 |doi=  }}
*{{cite journal  |vauthors=Bennett EP, Hassan H, Clausen H |title=cDNA cloning and expression of a novel human UDP-N-acetyl-alpha-D-galactosamine. Polypeptide N-acetylgalactosaminyltransferase, GalNAc-t3. |journal=J. Biol. Chem. |volume=271 |issue= 29 |pages= 17006–12 |year= 1996 |pmid= 8663203 |doi=10.1074/jbc.271.29.17006 }}
*{{cite journal  | author=Bennett EP, Hassan H, Clausen H |title=cDNA cloning and expression of a novel human UDP-N-acetyl-alpha-D-galactosamine. Polypeptide N-acetylgalactosaminyltransferase, GalNAc-t3. |journal=J. Biol. Chem. |volume=271 |issue= 29 |pages= 17006-12 |year= 1996 |pmid= 8663203 |doi=  }}
*{{cite journal  |vauthors=Wandall HH, Hassan H, Mirgorodskaya E |title=Substrate specificities of three members of the human UDP-N-acetyl-alpha-D-galactosamine:Polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1, -T2, and -T3. |journal=J. Biol. Chem. |volume=272 |issue= 38 |pages= 23503–14 |year= 1997 |pmid= 9295285 |doi=10.1074/jbc.272.38.23503 |display-authors=etal}}
*{{cite journal  | author=Wandall HH, Hassan H, Mirgorodskaya E, ''et al.'' |title=Substrate specificities of three members of the human UDP-N-acetyl-alpha-D-galactosamine:Polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1, -T2, and -T3. |journal=J. Biol. Chem. |volume=272 |issue= 38 |pages= 23503-14 |year= 1997 |pmid= 9295285 |doi=  }}
*{{cite journal  |vauthors=Müller S, Goletz S, Packer N |title=Localization of O-glycosylation sites on glycopeptide fragments from lactation-associated MUC1. All putative sites within the tandem repeat are glycosylation targets in vivo. |journal=J. Biol. Chem. |volume=272 |issue= 40 |pages= 24780–93 |year= 1997 |pmid= 9312074 |doi=10.1074/jbc.272.40.24780 |display-authors=etal}}
*{{cite journal  | author=Müller S, Goletz S, Packer N, ''et al.'' |title=Localization of O-glycosylation sites on glycopeptide fragments from lactation-associated MUC1. All putative sites within the tandem repeat are glycosylation targets in vivo. |journal=J. Biol. Chem. |volume=272 |issue= 40 |pages= 24780-93 |year= 1997 |pmid= 9312074 |doi=  }}
*{{cite journal  |vauthors=Röttger S, White J, Wandall HH |title=Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus. |journal=J. Cell Sci. |volume=111 |issue=  1|pages= 45–60 |year= 1998 |pmid= 9394011 |doi=  |display-authors=etal}}
*{{cite journal  | author=Röttger S, White J, Wandall HH, ''et al.'' |title=Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus. |journal=J. Cell. Sci. |volume=111 ( Pt 1) |issue=  |pages= 45-60 |year= 1998 |pmid= 9394011 |doi=  }}
*{{cite journal  |vauthors=Mattu TS, Pleass RJ, Willis AC |title=The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fc alpha receptor interactions. |journal=J. Biol. Chem. |volume=273 |issue= 4 |pages= 2260–72 |year= 1998 |pmid= 9442070 |doi=10.1074/jbc.273.4.2260  |display-authors=etal}}
*{{cite journal  | author=Mattu TS, Pleass RJ, Willis AC, ''et al.'' |title=The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fc alpha receptor interactions. |journal=J. Biol. Chem. |volume=273 |issue= 4 |pages= 2260-72 |year= 1998 |pmid= 9442070 |doi= }}
*{{cite journal  |vauthors=Iwasaki H, Zhang Y, Tachibana K |title=Initiation of O-glycan synthesis in IgA1 hinge region is determined by a single enzyme, UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2. |journal=J. Biol. Chem. |volume=278 |issue= 8 |pages= 5613–21 |year= 2003 |pmid= 12438318 |doi= 10.1074/jbc.M211097200 |display-authors=etal}}
*{{cite journal  | author=Bennett EP, Weghuis DO, Merkx G, ''et al.'' |title=Genomic organization and chromosomal localization of three members of the UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase family. |journal=Glycobiology |volume=8 |issue= 6 |pages= 547-55 |year= 1998 |pmid= 9592121 |doi=  }}
*{{cite journal  |vauthors=Strausberg RL, Feingold EA, Grouse LH |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 | pmc=139241 |display-authors=etal}}
*{{cite journal  | author=Iwasaki H, Zhang Y, Tachibana K, ''et al.'' |title=Initiation of O-glycan synthesis in IgA1 hinge region is determined by a single enzyme, UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2. |journal=J. Biol. Chem. |volume=278 |issue= 8 |pages= 5613-21 |year= 2003 |pmid= 12438318 |doi= 10.1074/jbc.M211097200 }}
*{{cite journal  |vauthors=Marcos NT, Cruz A, Silva F |title=Polypeptide GalNAc-transferases, ST6GalNAc-transferase I, and ST3Gal-transferase I expression in gastric carcinoma cell lines |journal=J. Histochem. Cytochem. |volume=51 |issue= 6 |pages= 761–71 |year= 2003 |pmid= 12754287 |doi=10.1177/002215540305100607 |display-authors=etal}}
*{{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=Kinarsky L, Suryanarayanan G, Prakash O |title=Conformational studies on the MUC1 tandem repeat glycopeptides: implication for the enzymatic O-glycosylation of the mucin protein core |journal=Glycobiology |volume=13 |issue= 12 |pages= 929–39 |year= 2004 |pmid= 12925576 |doi= 10.1093/glycob/cwg109 |display-authors=etal}}
*{{cite journal  | author=Marcos NT, Cruz A, Silva F, ''et al.'' |title=Polypeptide GalNAc-transferases, ST6GalNAc-transferase I, and ST3Gal-transferase I expression in gastric carcinoma cell lines. |journal=J. Histochem. Cytochem. |volume=51 |issue= 6 |pages= 761-71 |year= 2003 |pmid= 12754287 |doi=  }}
*{{cite journal  |vauthors=Ota T, Suzuki Y, Nishikawa T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |display-authors=etal}}
*{{cite journal  | author=Kinarsky L, Suryanarayanan G, Prakash O, ''et al.'' |title=Conformational studies on the MUC1 tandem repeat glycopeptides: implication for the enzymatic O-glycosylation of the mucin protein core. |journal=Glycobiology |volume=13 |issue= 12 |pages= 929-39 |year= 2004 |pmid= 12925576 |doi= 10.1093/glycob/cwg109 }}
*{{cite journal  |vauthors=Gerhard DS, Wagner L, Feingold EA |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 | pmc=528928 |display-authors=etal}}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  |vauthors=Gregory SG, Barlow KF, McLay KE |title=The DNA sequence and biological annotation of human chromosome 1 |journal=Nature |volume=441 |issue= 7091 |pages= 315–21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727 |display-authors=etal}}
*{{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=Gregory SG, Barlow KF, McLay KE, ''et al.'' |title=The DNA sequence and biological annotation of human chromosome 1. |journal=Nature |volume=441 |issue= 7091 |pages= 315-21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727 }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=2590}}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


{{protein-stub}}
{{gene-1-stub}}
{{WikiDoc Sources}}

Latest revision as of 06:12, 25 July 2018

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

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

Polypeptide N-acetylgalactosaminyltransferase 2 is an enzyme that in humans is encoded by the GALNT2 gene.[1][2][3]

This gene encodes polypeptide N-acetylgalactosaminyltransferase 2, a member of the GalNAc-transferases family. This family transfers an N-acetyl galactosamine to the hydroxyl group of a serine or threonine residue in the first step of O-linked oligosaccharide biosynthesis. The localization site of this particular enzyme is preponderantly the trans-Golgi.[4] Individual GalNAc-transferases have distinct activities, and initiation of O-glycosylation in a cell is regulated by a repertoire of GalNAc-transferases.[3]

References

  1. ↑ Bennett EP, Weghuis DO, Merkx G, van Kessel AG, Eiberg H, Clausen H (Jul 1998). "Genomic organization and chromosomal localization of three members of the UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase family". Glycobiology. 8 (6): 547–55. doi:10.1093/glycob/8.6.547. PMID 9592121.
  2. ↑ White T, Bennett EP, Takio K, Sorensen T, Bonding N, Clausen H (Dec 1995). "Purification and cDNA cloning of a human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase". J Biol Chem. 270 (41): 24156–65. doi:10.1074/jbc.270.41.24156. PMID 7592619.
  3. ↑ 3.0 3.1 "Entrez Gene: GALNT2 UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2 (GalNAc-T2)".
  4. ↑ "African Swine Fever Virus Causes Microtubule-Dependent Dispersal of trans-Golgi Network" (PDF).

Further reading


Retrieved from "https://www.wikidoc.org/index.php?title=GALNT2&oldid=1530733"