GALNT1

Protein-coding gene in the species Homo sapiens

GALNT1

Available structures

PDB

Ortholog search: PDBe RCSB

List of PDB id codes
1XHB

Identifiers

Aliases

GALNT1, GALNAC-T1, polypeptide N-acetylgalactosaminyltransferase 1

External IDs

OMIM: 602273; MGI: 894693; HomoloGene: 8469; GeneCards: GALNT1; OMA:GALNT1 - orthologs

Gene location (Human)

Chr.	Chromosome 18 (human)^[1]

Band	18q12.2	Start	35,581,117 bp^[1]
Band	18q12.2	End	35,711,834 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 18 (mouse)^[2]

Band	18\|18 A2	Start	24,338,401 bp^[2]
Band	18\|18 A2	End	24,419,875 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

buccal mucosa cell

mucosa of pharynx

nipple

amniotic fluid

oral cavity

tibia

superior surface of tongue

lactiferous duct

retinal pigment epithelium

periodontal fiber

Top expressed in

endothelial cell of lymphatic vessel

molar

blood

proximal tubule

right kidney

cardiac muscle tissue of left ventricle

parotid gland

decidua

fossa

ciliary body

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	glycosyltransferase activity polypeptide N-acetylgalactosaminyltransferase activity transferase activity manganese ion binding metal ion binding carbohydrate binding
Cellular component	perinuclear region of cytoplasm integral component of membrane extracellular region Golgi cisterna membrane Golgi membrane Golgi apparatus membrane endoplasmic reticulum membrane
Biological process	protein glycosylation protein O-linked glycosylation via serine protein O-linked glycosylation via threonine O-glycan processing protein O-linked glycosylation
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


2589


14423

Ensembl


ENSG00000141429


ENSMUSG00000000420

UniProt


Q10472


O08912

RefSeq (mRNA)


NM_020474


NM_001160404 NM_013814 NM_001361200

RefSeq (protein)


NP_065207


NP_001153876 NP_038842 NP_001348129

Location (UCSC)

Chr 18: 35.58 – 35.71 Mb

Chr 18: 24.34 – 24.42 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Polypeptide N-acetylgalactosaminyltransferase 1 is an enzyme that in humans is encoded by the GALNT1 gene.^[5]^[6]^[7]

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.^[7]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000141429 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000000420 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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.
^ 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.
^ ^a ^b "Entrez Gene: GALNT1 UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 1 (GalNAc-T1)".

Paulson JC, Colley KJ (1989). "Glycosyltransferases. Structure, localization, and control of cell type-specific glycosylation". J. Biol. Chem. 264 (30): 17615–8. doi:10.1016/S0021-9258(19)84610-0. 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. doi:10.1093/oxfordjournals.jbchem.a124947. 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. S2CID 22965327.
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. doi:10.1242/jcs.111.1.45. 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.
Sanger Centre, The; Washington University Genome Sequencing Cente, The (1999). "Toward a complete human genome sequence". Genome Res. 8 (11): 1097–108. 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. Bibcode:2002PNAS...9916899M. 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. CiteSeerX 10.1.1.879.1929. 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.