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{{Infobox_gene}}
{{PBB_Controls
'''Polypeptide N-acetylgalactosaminyltransferase 1''' is an [[enzyme]] that in [[human]]s is encoded by the ''GALNT1'' [[gene]].<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="pmid12199709">{{cite journal |vauthors=Tenno M, Toba S, Kezdy FJ, Elhammer AP, Kurosaka A | title = Identification of two cysteine residues involved in the binding of UDP-GalNAc to UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1 (GalNAc-T1) | journal = Eur J Biochem | volume = 269 | issue = 17 | pages = 4308–16 |date=Aug 2002 | pmid = 12199709 | pmc =  | doi =10.1046/j.1432-1033.2002.03123.x }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: GALNT1 UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 1 (GalNAc-T1)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2589| accessdate = }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_GALNT1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1xhb.
| PDB = {{PDB2|1xhb}}
| Name = UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 1 (GalNAc-T1)
| HGNCid = 4123
| Symbol = GALNT1
| AltSymbols =; GALNAC-T1
| OMIM = 602273
| ECnumber =
| Homologene = 8469
| MGIid = 894693
  | GeneAtlas_image1 = PBB_GE_GALNT1_201722_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_GALNT1_201723_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_GALNT1_201724_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 = 2589
    | Hs_Ensembl = ENSG00000141429
    | Hs_RefseqProtein = NP_065207
    | Hs_RefseqmRNA = NM_020474
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 18
    | Hs_GenLoc_start = 31488599
    | Hs_GenLoc_end = 31545792
    | Hs_Uniprot = Q10472
    | Mm_EntrezGene = 14423
    | Mm_Ensembl = ENSMUSG00000000420
    | Mm_RefseqmRNA = NM_013814
    | Mm_RefseqProtein = NP_038842
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 18
    | Mm_GenLoc_start = 24348451
    | Mm_GenLoc_end = 24428655
    | Mm_Uniprot = Q3UFE4
  }}
}}
'''UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 1 (GalNAc-T1)''', also known as '''GALNT1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GALNT1 UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 1 (GalNAc-T1)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2589| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = This gene encodes a member of the UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes. GalNAc-Ts initiate mucin-type O-linked glycosylation in the Golgi apparatus by catalyzing the transfer of GalNAc to serine and threonine residues on target proteins. They are characterized by an N-terminal transmembrane domain, a stem region, a lumenal catalytic domain containing a GT1 motif and Gal/GalNAc transferase motif, and a C-terminal ricin/lectin-like domain. GalNAc-Ts have different, but overlapping, substrate specificities and patterns of expression. Transcript variants derived from this gene that utilize alternative polyA signals have been described in the literature.<ref name="entrez">{{cite web | title = Entrez Gene: GALNT1 UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 1 (GalNAc-T1)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2589| accessdate = }}</ref>
| summary_text = This gene encodes a member of the UDP-N-acetyl-alpha-D-[[galactosamine]]:[[polypeptide]] N-[[acetylgalactosamine|acetylgalactosaminyltransferase]] (GalNAc-T) family of enzymes. GalNAc-Ts initiate [[mucin]]-type O-linked [[glycosylation]] in the [[Golgi apparatus]] by [[catalysis|catalyzing]] the transfer of GalNAc to [[serine]] and [[threonine]] residues on target [[protein]]s. They are characterized by an [[N-terminus|N-terminal]] transmembrane domain, a stem region, a lumenal catalytic domain containing a GT1 motif and Gal/GalNAc [[transferase]] motif, and a C-terminal [[ricin]]/[[lectin]]-like domain. GalNAc-Ts have different, but overlapping, [[Substrate specificity|substrate specificities]] and patterns of expression. Transcript variants derived from this gene that utilize alternative polyA signals have been described in the literature.<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=Paulson JC, Colley KJ |title=Glycosyltransferases. Structure, localization, and control of cell type-specific glycosylation. |journal=J. Biol. Chem. |volume=264 |issue= 30 |pages= 17615-8 |year= 1989 |pmid= 2681181 |doi=  }}
*{{cite journal  |vauthors=Paulson JC, Colley KJ |title=Glycosyltransferases. Structure, localization, and control of cell type-specific glycosylation. |journal=J. Biol. Chem. |volume=264 |issue= 30 |pages= 17615–8 |year= 1989 |pmid= 2681181 |doi=  }}
*{{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=Meurer JA, Naylor JM, Baker CA |title=cDNA cloning, expression, and chromosomal localization of a human UDP-GalNAc:polypeptide, N-acetylgalactosaminyltransferase. |journal=J. Biochem. |volume=118 |issue= 3 |pages= 568–74 |year= 1996 |pmid= 8690719 |doi=  |display-authors=etal}}
*{{cite journal  | author=Meurer JA, Naylor JM, Baker CA, ''et al.'' |title=cDNA cloning, expression, and chromosomal localization of a human UDP-GalNAc:polypeptide, N-acetylgalactosaminyltransferase. |journal=J. Biochem. |volume=118 |issue= 3 |pages= 568-74 |year= 1996 |pmid= 8690719 |doi=  }}
*{{cite journal  |vauthors=Meurer JA, Drong RF, Homa FL |title=Organization of a human UDP-GalNAc:polypeptide, N-acetylgalactosaminyltransferase gene and a related processed pseudogene. |journal=Glycobiology |volume=6 |issue= 2 |pages= 231–41 |year= 1996 |pmid= 8727794 |doi=10.1093/glycob/6.2.231 |display-authors=etal}}
*{{cite journal  | author=Meurer JA, Drong RF, Homa FL, ''et al.'' |title=Organization of a human UDP-GalNAc:polypeptide, N-acetylgalactosaminyltransferase gene and a related processed pseudogene. |journal=Glycobiology |volume=6 |issue= 2 |pages= 231-41 |year= 1996 |pmid= 8727794 |doi=  }}
*{{cite journal  |vauthors=Takai S, Hinoda Y, Adachi T |title=A human UDP-GalNAc: polypeptide, N-acetylgalactosaminyltransferase type 1 gene is located at the chromosomal region 18q12.1. |journal=Hum. Genet. |volume=99 |issue= 3 |pages= 293–4 |year= 1997 |pmid= 9050910 |doi=10.1007/s004390050359 |display-authors=etal}}
*{{cite journal  | author=Takai S, Hinoda Y, Adachi T, ''et al.'' |title=A human UDP-GalNAc: polypeptide, N-acetylgalactosaminyltransferase type 1 gene is located at the chromosomal region 18q12.1. |journal=Hum. Genet. |volume=99 |issue= 3 |pages= 293-4 |year= 1997 |pmid= 9050910 |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=Bennett EP, Weghuis DO, Merkx G |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=10.1093/glycob/8.6.547 |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  |title=Toward a complete human genome sequence. |journal=Genome Res. |volume=8 |issue= 11 |pages= 1097–108 |year= 1999 |pmid= 9847074 |doi=  10.1101/gr.8.11.1097}}
*{{cite journal  | author= |title=Toward a complete human genome sequence. |journal=Genome Res. |volume=8 |issue= 11 |pages= 1097-108 |year= 1999 |pmid= 9847074 |doi=  }}
*{{cite journal  |vauthors=Tenno M, Saeki A, Kézdy FJ |title=The lectin domain of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1 is involved in O-glycosylation of a polypeptide with multiple acceptor sites. |journal=J. Biol. Chem. |volume=277 |issue= 49 |pages= 47088–96 |year= 2003 |pmid= 12364335 |doi= 10.1074/jbc.M207369200 |display-authors=etal}}
*{{cite journal  | author=Tenno M, Toba S, Kézdy FJ, ''et al.'' |title=Identification of two cysteine residues involved in the binding of UDP-GalNAc to UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1 (GalNAc-T1). |journal=Eur. J. Biochem. |volume=269 |issue= 17 |pages= 4308-16 |year= 2002 |pmid= 12199709 |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=Tenno M, Saeki A, Kézdy FJ, ''et al.'' |title=The lectin domain of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1 is involved in O-glycosylation of a polypeptide with multiple acceptor sites. |journal=J. Biol. Chem. |volume=277 |issue= 49 |pages= 47088-96 |year= 2003 |pmid= 12364335 |doi= 10.1074/jbc.M207369200 }}
*{{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=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=Brokx RD, Revers L, Zhang Q |title=Nuclear magnetic resonance-based dissection of a glycosyltransferase specificity for the mucin MUC1 tandem repeat. |journal=Biochemistry |volume=42 |issue= 47 |pages= 13817–25 |year= 2004 |pmid= 14636048 |doi= 10.1021/bi0353070 |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=Brokx RD, Revers L, Zhang Q, ''et al.'' |title=Nuclear magnetic resonance-based dissection of a glycosyltransferase specificity for the mucin MUC1 tandem repeat. |journal=Biochemistry |volume=42 |issue= 47 |pages= 13817-25 |year= 2004 |pmid= 14636048 |doi= 10.1021/bi0353070 }}
*{{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 }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=2589}}
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{{gene-18-stub}}
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Latest revision as of 09:03, 9 January 2019

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

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

Polypeptide N-acetylgalactosaminyltransferase 1 is an enzyme that in humans is encoded by the GALNT1 gene.[1][2][3]

This gene encodes a member of the UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes. GalNAc-Ts initiate mucin-type O-linked glycosylation in the Golgi apparatus by catalyzing the transfer of GalNAc to serine and threonine residues on target proteins. They are characterized by an N-terminal transmembrane domain, a stem region, a lumenal catalytic domain containing a GT1 motif and Gal/GalNAc transferase motif, and a C-terminal ricin/lectin-like domain. GalNAc-Ts have different, but overlapping, substrate specificities and patterns of expression. Transcript variants derived from this gene that utilize alternative polyA signals have been described in the literature.[3]

References

  1. ↑ 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.
  2. ↑ Tenno M, Toba S, Kezdy FJ, Elhammer AP, Kurosaka A (Aug 2002). "Identification of two cysteine residues involved in the binding of UDP-GalNAc to UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1 (GalNAc-T1)". Eur J Biochem. 269 (17): 4308–16. doi:10.1046/j.1432-1033.2002.03123.x. PMID 12199709.
  3. ↑ 3.0 3.1 "Entrez Gene: GALNT1 UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 1 (GalNAc-T1)".

Further reading

  • Paulson JC, Colley KJ (1989). "Glycosyltransferases. Structure, localization, and control of cell type-specific glycosylation". J. Biol. Chem. 264 (30): 17615–8. PMID 2681181.
  • Bennett EP, Hassan H, Clausen H (1996). "cDNA cloning and expression of a novel human UDP-N-acetyl-alpha-D-galactosamine. Polypeptide N-acetylgalactosaminyltransferase, GalNAc-t3". J. Biol. Chem. 271 (29): 17006–12. doi:10.1074/jbc.271.29.17006. PMID 8663203.
  • Meurer JA, Naylor JM, Baker CA, et al. (1996). "cDNA cloning, expression, and chromosomal localization of a human UDP-GalNAc:polypeptide, N-acetylgalactosaminyltransferase". J. Biochem. 118 (3): 568–74. PMID 8690719.
  • Meurer JA, Drong RF, Homa FL, et al. (1996). "Organization of a human UDP-GalNAc:polypeptide, N-acetylgalactosaminyltransferase gene and a related processed pseudogene". Glycobiology. 6 (2): 231–41. doi:10.1093/glycob/6.2.231. PMID 8727794.
  • Takai S, Hinoda Y, Adachi T, et al. (1997). "A human UDP-GalNAc: polypeptide, N-acetylgalactosaminyltransferase type 1 gene is located at the chromosomal region 18q12.1". Hum. Genet. 99 (3): 293–4. doi:10.1007/s004390050359. PMID 9050910.
  • Wandall HH, Hassan H, Mirgorodskaya E, et al. (1997). "Substrate specificities of three members of the human UDP-N-acetyl-alpha-D-galactosamine:Polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1, -T2, and -T3". J. Biol. Chem. 272 (38): 23503–14. doi:10.1074/jbc.272.38.23503. PMID 9295285.
  • Müller S, Goletz S, Packer N, et al. (1997). "Localization of O-glycosylation sites on glycopeptide fragments from lactation-associated MUC1. All putative sites within the tandem repeat are glycosylation targets in vivo". J. Biol. Chem. 272 (40): 24780–93. doi:10.1074/jbc.272.40.24780. PMID 9312074.
  • Röttger S, White J, Wandall HH, et al. (1998). "Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus". J. Cell Sci. 111 (1): 45–60. PMID 9394011.
  • Bennett EP, Weghuis DO, Merkx G, et al. (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.
  • "Toward a complete human genome sequence". Genome Res. 8 (11): 1097–108. 1999. doi:10.1101/gr.8.11.1097. PMID 9847074.
  • Tenno M, Saeki A, Kézdy FJ, et al. (2003). "The lectin domain of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1 is involved in O-glycosylation of a polypeptide with multiple acceptor sites". J. Biol. Chem. 277 (49): 47088–96. doi:10.1074/jbc.M207369200. PMID 12364335.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Kinarsky L, Suryanarayanan G, Prakash O, et al. (2004). "Conformational studies on the MUC1 tandem repeat glycopeptides: implication for the enzymatic O-glycosylation of the mucin protein core". Glycobiology. 13 (12): 929–39. doi:10.1093/glycob/cwg109. PMID 12925576.
  • Brokx RD, Revers L, Zhang Q, et al. (2004). "Nuclear magnetic resonance-based dissection of a glycosyltransferase specificity for the mucin MUC1 tandem repeat". Biochemistry. 42 (47): 13817–25. doi:10.1021/bi0353070. PMID 14636048.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.


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