GALNT3: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''Polypeptide N-acetylgalactosaminyltransferase 3''' is an [[enzyme]] that in humans is encoded by the ''GALNT3'' [[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="pmid15133511">{{cite journal |vauthors=Topaz O, Shurman DL, Bergman R, Indelman M, Ratajczak P, Mizrachi M, Khamaysi Z, Behar D, Petronius D, Friedman V, Zelikovic I, Raimer S, Metzker A, Richard G, Sprecher E | title = Mutations in GALNT3, encoding a protein involved in O-linked glycosylation, cause familial tumoral calcinosis | journal = Nat Genet | volume = 36 | issue = 6 | pages = 579–81 |date=May 2004 | pmid = 15133511 | pmc =  | doi = 10.1038/ng1358 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: GALNT3 UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 3 (GalNAc-T3)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2591| accessdate = }}</ref>
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{{GNF_Protein_box
| image =
| image_source = 
| PDB =
| Name = UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 3 (GalNAc-T3)
| HGNCid = 4125
| Symbol = GALNT3
| AltSymbols =; DKFZp686C10199; GalNAc-T3; HFTC; HHS; MGC61909
| OMIM = 601756
| ECnumber =
| Homologene = 55827
| MGIid = 894695
  | GeneAtlas_image1 = PBB_GE_GALNT3_203397_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_GALNT3_203398_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:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
  | Process = {{GNF_GO|id=GO:0005975 |text = carbohydrate metabolic process}}  
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2591
    | Hs_Ensembl = ENSG00000115339
    | Hs_RefseqProtein = NP_004473
    | Hs_RefseqmRNA = NM_004482
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 2
    | Hs_GenLoc_start = 166311691
    | Hs_GenLoc_end = 166335456
    | Hs_Uniprot = Q14435
    | Mm_EntrezGene = 14425
    | Mm_Ensembl = ENSMUSG00000026994
    | Mm_RefseqmRNA = NM_015736
    | Mm_RefseqProtein = NP_056551
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 2
    | Mm_GenLoc_start = 65883605
    | Mm_GenLoc_end = 65925632
    | Mm_Uniprot = Q3UXL2
  }}
}}
'''UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 3 (GalNAc-T3)''', also known as '''GALNT3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GALNT3 UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 3 (GalNAc-T3)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2591| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = This gene encodes UDP-GalNAc transferase 3, 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 is regulated by a repertoire of GalNAc-transferases.  The protein encoded by this gene is highly homologous to other family members, however the enzymes have different substrate specificities.<ref name="entrez">{{cite web | title = Entrez Gene: GALNT3 UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 3 (GalNAc-T3)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2591| accessdate = }}</ref>
| summary_text = This gene encodes UDP-GalNAc transferase 3, a member of the [[GalNAc transferase]] 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]] is regulated by a repertoire of GalNAc-transferases.  The protein encoded by this gene is highly [[Homologous protein|homologous]] to other family members; however, the enzymes have different substrate specificities.<ref name="entrez" />
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{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=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=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  | author=Wandall HH |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 |name-list-format=vanc| author2=Hassan H  | author3=Mirgorodskaya E  | display-authors=| last4=Kristensen | first4=AK  | last5=Roepstorff  | first5=| last6=Bennett  | first6=EP  | last7=Nielsen  | first7=PA  | last8=Hollingsworth  | first8=MA  | last9=Burchell  | first9=J }}
*{{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  | author=Röttger S |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=  |name-list-format=vanc| author2=White J  | author3=Wandall HH  | display-authors=3  | last4=Olivo  | first4=JC  | last5=Stark  | first5=| last6=Bennett  | first6=EP  | last7=Whitehouse | first7=C | last8=Berger  | first8=EG  | last9=Clausen  | first9=H }}
*{{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  | author=Mandel U |title=Expression of polypeptide GalNAc-transferases in stratified epithelia and squamous cell carcinomas: immunohistological evaluation using monoclonal antibodies to three members of the GalNAc-transferase family |journal=Glycobiology |volume=9 |issue= 1 |pages= 43–52 |year= 1999 |pmid= 9884405 |doi=10.1093/glycob/9.1.43 |name-list-format=vanc| author2=Hassan H  | author3=Therkildsen MH  | display-authors=| last4=Rygaard  | first4=| last5=Jakobsen  | first5=MH  | last6=Juhl  | first6=BR | last7=Dabelsteen  | first7=E  | last8=Clausen  | first8=H  }}
*{{cite journal | author=Mandel U, Hassan H, Therkildsen MH, ''et al.'' |title=Expression of polypeptide GalNAc-transferases in stratified epithelia and squamous cell carcinomas: immunohistological evaluation using monoclonal antibodies to three members of the GalNAc-transferase family. |journal=Glycobiology |volume=9 |issue= 1 |pages= 43-52 |year= 1999 |pmid= 9884405 |doi}}
*{{cite journal  | author=Dosaka-Akita H |title=N-acetylgalactosaminyl transferase-3 is a potential new marker for non-small cell lung cancers |journal=Br. J. Cancer |volume=87 |issue= 7 |pages= 751–5 |year= 2002 |pmid= 12232759 |doi= 10.1038/sj.bjc.6600536 | pmc=2364253 |name-list-format=vanc| author2=Kinoshita I  | author3=Yamazaki K | display-authors=3  | last4=Izumi  | first4=H  | last5=Itoh  | first5=| last6=Katoh  | first6=| last7=Nishimura  | first7=| last8=Matsuo | first8=K  | last9=Yamada  | first9=Y }}
*{{cite journal | author=Dosaka-Akita H, Kinoshita I, Yamazaki K, ''et al.'' |title=N-acetylgalactosaminyl transferase-3 is a potential new marker for non-small cell lung cancers. |journal=Br. J. Cancer |volume=87 |issue= 7 |pages= 751-5 |year= 2002 |pmid= 12232759 |doi= 10.1038/sj.bjc.6600536 }}
*{{cite journal  | author=Strausberg RL |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  |name-list-format=vanc| author2=Feingold EA  | author3=Grouse LH  | display-authors=3 | last4=Derge  | first4=JG  | last5=Klausner  | first5=RD  | last6=Collins  | first6=FS  | last7=Wagner  | first7=L  | last8=Shenmen  | first8=CM  | last9=Schuler  | first9=GD }}
*{{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=Argüeso P |title=The cell-layer- and cell-type-specific distribution of GalNAc-transferases in the ocular surface epithelia is altered during keratinization |journal=Invest. Ophthalmol. Vis. Sci. |volume=44 |issue= 1 |pages= 86–92 |year= 2003 |pmid= 12506059 |doi=10.1167/iovs.02-0181 |name-list-format=vanc| author2=Tisdale A  | author3=Mandel U | display-authors=| last4=Letko  | first4=| last5=Foster  | first5=CS  | last6=Gipson  | first6=IK  }}
*{{cite journal | author=Argüeso P, Tisdale A, Mandel U, ''et al.'' |title=The cell-layer- and cell-type-specific distribution of GalNAc-transferases in the ocular surface epithelia is altered during keratinization. |journal=Invest. Ophthalmol. Vis. Sci. |volume=44 |issue= 1 |pages= 86-92 |year= 2003 |pmid= 12506059 |doi=  }}
*{{cite journal  | author=Onitsuka K |title=Prognostic significance of UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-3 (GalNAc-T3) expression in patients with gastric carcinoma |journal=Cancer Sci. |volume=94 |issue= 1 |pages= 32–6 |year= 2003 |pmid= 12708471 |doi=10.1111/j.1349-7006.2003.tb01348.x |name-list-format=vanc| author2=Shibao K | author3=Nakayama Y  | display-authors=3 | last4=Minagawa  | first4=Noritaka  | last5=Hirata  | first5=Keiji  | last6=Izumi  | first6=Hiroto  | last7=Matsuo  | first7=Ken-Ichi  | last8=Nagata  | first8=Naoki  | last9=Kitazato  | first9=Kenji  }}
*{{cite journal | author=Onitsuka K, Shibao K, Nakayama Y, ''et al.'' |title=Prognostic significance of UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-3 (GalNAc-T3) expression in patients with gastric carcinoma. |journal=Cancer Sci. |volume=94 |issue= 1 |pages= 32-6 |year= 2003 |pmid= 12708471 |doi}}
*{{cite journal  | author=Yamamoto S |title=Expression of uridine diphosphate N-acetyl-alpha-D-galactosamine: polypeptide N-acetylgalactosaminyl transferase 3 in adenocarcinoma of the pancreas |journal=Pathobiology |volume=71 |issue= 1 |pages= 12–8 |year= 2004 |pmid= 14555840 |doi= 10.1159/000072957 |name-list-format=vanc| author2=Nakamori S  | author3=Tsujie M  | display-authors=3  | last4=Takahashi  | first4=Yuji  | last5=Nagano  | first5=Hiroaki  | last6=Dono  | first6=Keizo  | last7=Umeshita  | first7=Koji  | last8=Sakon  | first8=Masato  | last9=Tomita  | first9=Yasuhiko }}
*{{cite journal  | author=Yamamoto S, Nakamori S, Tsujie M, ''et al.'' |title=Expression of uridine diphosphate N-acetyl-alpha-D-galactosamine: polypeptide N-acetylgalactosaminyl transferase 3 in adenocarcinoma of the pancreas. |journal=Pathobiology |volume=71 |issue= 1 |pages= 12-8 |year= 2004 |pmid= 14555840 |doi= 10.1159/000072957 }}
*{{cite journal  | author=Gu C |title=Low expression of polypeptide GalNAc N-acetylgalactosaminyl transferase-3 in lung adenocarcinoma: impact on poor prognosis and early recurrence |journal=Br. J. Cancer |volume=90 |issue= 2 |pages= 436–42 |year= 2004 |pmid= 14735190 |doi= 10.1038/sj.bjc.6601531 | pmc=2409559  |name-list-format=vanc| author2=Oyama T  | author3=Osaki T  | display-authors=| last4=Li  | first4=| last5=Takenoyama  | first5=M  | last6=Izumi | first6=H  | last7=Sugio  | first7=K  | last8=Kohno  | first8=K  | last9=Yasumoto  | first9=K }}
*{{cite journal | author=Gu C, Oyama T, Osaki T, ''et al.'' |title=Low expression of polypeptide GalNAc N-acetylgalactosaminyl transferase-3 in lung adenocarcinoma: impact on poor prognosis and early recurrence. |journal=Br. J. Cancer |volume=90 |issue= 2 |pages= 436-42 |year= 2004 |pmid= 14735190 |doi= 10.1038/sj.bjc.6601531 }}
*{{cite journal  | author=Miyahara N |title=Expression of UDP-N-acetyl-alpha-D-galactosamine-polypeptide N-acetylgalactosaminyltransferase isozyme 3 in the subserosal layer correlates with postsurgical survival of pathological tumor stage 2 carcinoma of the gallbladder |journal=Clin. Cancer Res. |volume=10 |issue= 6 |pages= 2090–9 |year= 2004 |pmid= 15041730 |doi=10.1158/1078-0432.CCR-1024-03  |name-list-format=vanc| author2=Shoda J  | author3=Kawamoto T  | display-authors=3  | last4=Furukawa  | first4=M  | last5=Ueda  | first5=T  | last6=Todoroki  | first6=T  | last7=Tanaka  | first7=N  | last8=Matsuo  | first8=K  | last9=Yamada  | first9=Y  }}
*{{cite journal  | author=Miyahara N, Shoda J, Kawamoto T, ''et al.'' |title=Expression of UDP-N-acetyl-alpha-D-galactosamine-polypeptide N-acetylgalactosaminyltransferase isozyme 3 in the subserosal layer correlates with postsurgical survival of pathological tumor stage 2 carcinoma of the gallbladder. |journal=Clin. Cancer Res. |volume=10 |issue= 6 |pages= 2090-9 |year= 2004 |pmid= 15041730 |doi=  }}
*{{cite journal  | author=Gerhard DS |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  |name-list-format=vanc| author2=Wagner L  | author3=Feingold EA  | display-authors=3  | last4=Shenmen  | first4=CM  | last5=Grouse  | first5=LH  | last6=Schuler  | first6=G  | last7=Klein  | first7=SL  | last8=Old  | first8=S  | last9=Rasooly  | first9=R }}
*{{cite journal | author=Topaz O, Shurman DL, Bergman R, ''et al.'' |title=Mutations in GALNT3, encoding a protein involved in O-linked glycosylation, cause familial tumoral calcinosis. |journal=Nat. Genet. |volume=36 |issue= 6 |pages= 579-81 |year= 2004 |pmid= 15133511 |doi= 10.1038/ng1358 }}
*{{cite journal  |vauthors=Ishikawa M, Kitayama J, Kohno K, Nagawa H |title=The expression pattern of UDP-N-acetyl-alpha-D-galactosamine-polypeptide N-acetyl-galactosaminyl transferase-3 in squamous cell carcinoma of the esophagus |journal=Pathobiology |volume=72 |issue= 3 |pages= 139–45 |year= 2005 |pmid= 15860931 |doi= 10.1159/000084117 }}
*{{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=Kimura K |title=Diversification of transcriptional modulation: Large-scale identification and characterization of putative alternative promoters of human genes |journal=Genome Res. |volume=16 |issue= 1 |pages= 55–65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406  | pmc=1356129  |name-list-format=vanc| author2=Wakamatsu A  | author3=Suzuki Y  | display-authors=3  | last4=Ota  | first4=T  | last5=Nishikawa  | first5=T  | last6=Yamashita  | first6=R  | last7=Yamamoto  | first7=J  | last8=Sekine  | first8=M  | last9=Tsuritani  | first9=K }}
*{{cite journal | author=Ishikawa M, Kitayama J, Kohno K, Nagawa H |title=The expression pattern of UDP-N-acetyl-alpha-D-galactosamine-polypeptide N-acetyl-galactosaminyl transferase-3 in squamous cell carcinoma of the esophagus. |journal=Pathobiology |volume=72 |issue= 3 |pages= 139-45 |year= 2005 |pmid= 15860931 |doi= 10.1159/000084117 }}
*{{cite journal  | author=Kato K |title=Polypeptide GalNAc-transferase T3 and familial tumoral calcinosis. Secretion of fibroblast growth factor 23 requires O-glycosylation |journal=J. Biol. Chem. |volume=281 |issue= 27 |pages= 18370–7 |year= 2006 |pmid= 16638743 |doi= 10.1074/jbc.M602469200  |name-list-format=vanc| author2=Jeanneau C  | author3=Tarp MA  | display-authors=3  | last4=Benet-Pagès  | first4=A  | last5=Lorenz-Depiereux  | first5=B  | last6=Bennett  | first6=EP  | last7=Mandel  | first7=U  | last8=Strom  | first8=TM  | last9=Clausen  | first9=H }}
*{{cite journal  | author=Kimura K, Wakamatsu A, Suzuki Y, ''et al.'' |title=Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. |journal=Genome Res. |volume=16 |issue= 1 |pages= 55-65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406 }}
*{{cite journal  | author=Ichikawa S |title=Tumoral calcinosis presenting with eyelid calcifications due to novel missense mutations in the glycosyl transferase domain of the GALNT3 gene |journal=J. Clin. Endocrinol. Metab. |volume=91 |issue= 11 |pages= 4472–5 |year= 2007 |pmid= 16940445 |doi= 10.1210/jc.2006-1247  |name-list-format=vanc| author2=Imel EA  | author3=Sorenson AH  | display-authors=3  | last4=Severe  | first4=R.  | last5=Knudson  | first5=P.  | last6=Harris  | first6=G. J.  | last7=Shaker  | first7=J. L.  | last8=Econs  | first8=M. J. }}
*{{cite journal | author=Kato K, Jeanneau C, Tarp MA, ''et al.'' |title=Polypeptide GalNAc-transferase T3 and familial tumoral calcinosis. Secretion of fibroblast growth factor 23 requires O-glycosylation. |journal=J. Biol. Chem. |volume=281 |issue= 27 |pages= 18370-7 |year= 2006 |pmid= 16638743 |doi= 10.1074/jbc.M602469200 }}
*{{cite journal  |vauthors=Barbieri AM, Filopanti M, Bua G, Beck-Peccoz P |title=Two novel nonsense mutations in GALNT3 gene are responsible for familial tumoral calcinosis |journal=J. Hum. Genet. |volume=52 |issue= 5 |pages= 464–8 |year= 2007 |pmid= 17351710 |doi= 10.1007/s10038-007-0126-5 }}
*{{cite journal  | author=Ichikawa S, Imel EA, Sorenson AH, ''et al.'' |title=Tumoral calcinosis presenting with eyelid calcifications due to novel missense mutations in the glycosyl transferase domain of the GALNT3 gene. |journal=J. Clin. Endocrinol. Metab. |volume=91 |issue= 11 |pages= 4472-5 |year= 2007 |pmid= 16940445 |doi= 10.1210/jc.2006-1247 }}
*{{cite journal  | author=Inoue T |title=Expression of GalNAc-T3 and its relationships with clinicopathological factors in 61 extrahepatic bile duct carcinomas analyzed using stepwise sections - special reference to its association with lymph node metastases- |journal=Mod. Pathol. |volume=20 |issue= 2 |pages= 267–76 |year= 2007 |pmid= 17361208 |doi= 10.1038/modpathol.3800700  |name-list-format=vanc| author2=Eguchi T  | author3=Oda Y  | display-authors=3  | last4=Nishiyama  | first4=Kenichi  | last5=Fujii  | first5=Kei  | last6=Izumi  | first6=Hiroto  | last7=Kohno  | first7=Kimitoshi  | last8=Yamaguchi  | first8=Koji  | last9=Tanaka  | first9=Masao }}
*{{cite journal | author=Barbieri AM, Filopanti M, Bua G, Beck-Peccoz P |title=Two novel nonsense mutations in GALNT3 gene are responsible for familial tumoral calcinosis. |journal=J. Hum. Genet. |volume=52 |issue= 5 |pages= 464-8 |year= 2007 |pmid= 17351710 |doi= 10.1007/s10038-007-0126-5 }}
*{{cite journal | author=Inoue T, Eguchi T, Oda Y, ''et al.'' |title=Expression of GalNAc-T3 and its relationships with clinicopathological factors in 61 extrahepatic bile duct carcinomas analyzed using stepwise sections - special reference to its association with lymph node metastases-. |journal=Mod. Pathol. |volume=20 |issue= 2 |pages= 267-76 |year= 2007 |pmid= 17361208 |doi= 10.1038/modpathol.3800700 }}
}}
}}
{{refend}}
{{refend}}


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Latest revision as of 04:29, 15 February 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
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Polypeptide N-acetylgalactosaminyltransferase 3 is an enzyme that in humans is encoded by the GALNT3 gene.[1][2][3]

This gene encodes UDP-GalNAc transferase 3, a member of the GalNAc transferase 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 is regulated by a repertoire of GalNAc-transferases. The protein encoded by this gene is highly homologous to other family members; however, the enzymes have different substrate specificities.[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. Topaz O, Shurman DL, Bergman R, Indelman M, Ratajczak P, Mizrachi M, Khamaysi Z, Behar D, Petronius D, Friedman V, Zelikovic I, Raimer S, Metzker A, Richard G, Sprecher E (May 2004). "Mutations in GALNT3, encoding a protein involved in O-linked glycosylation, cause familial tumoral calcinosis". Nat Genet. 36 (6): 579–81. doi:10.1038/ng1358. PMID 15133511.
  3. 3.0 3.1 "Entrez Gene: GALNT3 UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 3 (GalNAc-T3)".

Further reading