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Q10472 (GALT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polypeptide N-acetylgalactosaminyltransferase 1

EC=2.4.1.41
Alternative name(s):
Polypeptide GalNAc transferase 1
Short name=GalNAc-T1
Short name=pp-GaNTase 1
Protein-UDP acetylgalactosaminyltransferase 1
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1
Gene names
Name:GALNT1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length559 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b and Muc7. Ref.5

Catalytic activity

UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.

Cofactor

Manganese.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Polypeptide N-acetylgalactosaminyltransferase 1: Golgi apparatusGolgi stack membrane; Single-pass type II membrane protein Ref.6.

Polypeptide N-acetylgalactosaminyltransferase 1 soluble form: Secreted.

Tissue specificity

Widely expressed. Expressed in all tissues tested. Ref.2

Domain

There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding By similarity.

The ricin B-type lectin domain directs the glycopeptide specificity. It is required in the glycopeptide specificity of enzyme activity but not for activity with naked peptide substrates, suggesting that it triggers the catalytic domain to act on GalNAc-glycopeptide substrates By similarity.

Sequence similarities

Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily.

Contains 1 ricin B-type lectin domain.

Ontologies

Keywords
   Cellular componentGolgi apparatus
Membrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   LigandLectin
Manganese
Metal-binding
   Molecular functionGlycosyltransferase
Transferase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processO-glycan processing

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

post-translational protein modification

Traceable author statement. Source: Reactome

protein O-linked glycosylation

Inferred from sequence or structural similarity. Source: UniProtKB

protein O-linked glycosylation via serine

Inferred from direct assay Ref.5. Source: BHF-UCL

protein O-linked glycosylation via threonine

Inferred from direct assay Ref.5. Source: BHF-UCL

   Cellular_componentGolgi cisterna membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

Golgi membrane

Traceable author statement. Source: Reactome

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

perinuclear region of cytoplasm

Inferred from direct assay PubMed 12506059. Source: BHF-UCL

   Molecular_functionmanganese ion binding

Inferred from direct assay Ref.5. Source: BHF-UCL

polypeptide N-acetylgalactosaminyltransferase activity

Inferred from direct assay Ref.5. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q10472-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q10472-2)

The sequence of this isoform differs from the canonical sequence as follows:
     106-559: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 559559Polypeptide N-acetylgalactosaminyltransferase 1
PRO_0000223387
Chain41 – 559519Polypeptide N-acetylgalactosaminyltransferase 1 soluble form
PRO_0000012257

Regions

Topological domain1 – 88Cytoplasmic Potential
Transmembrane9 – 2820Helical; Signal-anchor for type II membrane protein; Potential
Topological domain29 – 559531Lumenal Potential
Domain429 – 551123Ricin B-type lectin
Region115 – 225111Catalytic subdomain A
Region285 – 34763Catalytic subdomain B

Sites

Metal binding2091Manganese By similarity
Metal binding2111Manganese By similarity
Metal binding3441Manganese By similarity
Binding site1561Substrate By similarity
Binding site1861Substrate By similarity
Binding site3161Substrate By similarity
Binding site3471Substrate By similarity
Binding site3521Substrate By similarity

Amino acid modifications

Glycosylation951N-linked (GlcNAc...) Potential
Glycosylation5521N-linked (GlcNAc...) Potential
Disulfide bond106 ↔ 339 By similarity
Disulfide bond330 ↔ 408 By similarity
Disulfide bond442 ↔ 459 By similarity
Disulfide bond482 ↔ 497 By similarity
Disulfide bond523 ↔ 540 By similarity

Natural variations

Alternative sequence106 – 559454Missing in isoform 2.
VSP_011200
Natural variant4141Y → D.
Corresponds to variant rs34304568 [ dbSNP | Ensembl ].
VAR_033946

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: CD68118CB201EE5B

FASTA55964,219
        10         20         30         40         50         60 
MRKFAYCKVV LATSLIWVLL DMFLLLYFSE CNKCDEKKER GLPAGDVLEP VQKPHEGPGE 

        70         80         90        100        110        120 
MGKPVVIPKE DQEKMKEMFK INQFNLMASE MIALNRSLPD VRLEGCKTKV YPDNLPTTSV 

       130        140        150        160        170        180 
VIVFHNEAWS TLLRTVHSVI NRSPRHMIEE IVLVDDASER DFLKRPLESY VKKLKVPVHV 

       190        200        210        220        230        240 
IRMEQRSGLI RARLKGAAVS KGQVITFLDA HCECTVGWLE PLLARIKHDR RTVVCPIIDV 

       250        260        270        280        290        300 
ISDDTFEYMA GSDMTYGGFN WKLNFRWYPV PQREMDRRKG DRTLPVRTPT MAGGLFSIDR 

       310        320        330        340        350        360 
DYFQEIGTYD AGMDIWGGEN LEISFRIWQC GGTLEIVTCS HVGHVFRKAT PYTFPGGTGQ 

       370        380        390        400        410        420 
IINKNNRRLA EVWMDEFKNF FYIISPGVTK VDYGDISSRV GLRHKLQCKP FSWYLENIYP 

       430        440        450        460        470        480 
DSQIPRHYFS LGEIRNVETN QCLDNMARKE NEKVGIFNCH GMGGNQVFSY TANKEIRTDD 

       490        500        510        520        530        540 
LCLDVSKLNG PVTMLKCHHL KGNQLWEYDP VKLTLQHVNS NQCLDKATEE DSQVPSIRDC 

       550 
NGSRSQQWLL RNVTLPEIF 

« Hide

Isoform 2 [UniParc].

Checksum: 01BE501BD11331AF
Show »

FASTA10512,046

References

« Hide 'large scale' references
[1]"cDNA cloning, expression, and chromosomal localization of a human UDP-GalNAc:polypeptide, N-acetylgalactosaminyltransferase."
Meurer J.A., Naylor J.M., Baker C.A., Thomsen D.R., Homa F.L., Elhammer A.P.
J. Biochem. 118:568-574(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1).
Tissue: Salivary gland.
[2]"Purification and cDNA cloning of a human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase."
White T., Bennett E.P., Takio K., Soerensen T., Bonding N., Clausen H.
J. Biol. Chem. 270:24156-24165(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: PNS.
[4]"Organization of a human UDP-GalNAc:polypeptide, N-acetylgalactosaminyltransferase gene and a related processed pseudogene."
Meurer J.A., Drong R.F., Homa F.L., Slightom J.L., Elhammer A.P.
Glycobiology 6:231-241(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 512-559 (ISOFORM 1).
[5]"Substrate specificities of three members of the human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1, -T2, and -T3."
Wandall H.H., Hassan H., Mirgorodskaya E., Kristensen A.K., Roepstorff P., Bennett E.P., Nielsen P.A., Hollingsworth M.A., Burchell J., Taylor-Papadimitriou J., Clausen H.
J. Biol. Chem. 272:23503-23514(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus."
Roettger S., White J., Wandall H.H., Olivo J.-C., Stark A., Bennett E.P., Whitehouse C., Berger E.G., Clausen H., Nilsson T.
J. Cell Sci. 111:45-60(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[7]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 1

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U41514 mRNA. Translation: AAC50327.1.
X85018 mRNA. Translation: CAA59380.1.
BC047746 mRNA. Translation: AAH47746.1.
S82597 Genomic DNA. Translation: AAD14406.1.
CCDSCCDS11915.1. [Q10472-1]
PIRJC4223.
RefSeqNP_065207.2. NM_020474.3. [Q10472-1]
XP_005258296.1. XM_005258239.1. [Q10472-1]
UniGeneHs.514806.

3D structure databases

ProteinModelPortalQ10472.
SMRQ10472. Positions 95-553.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108861. 3 interactions.
IntActQ10472. 1 interaction.
STRING9606.ENSP00000269195.

Protein family/group databases

CAZyCBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

PTM databases

PhosphoSiteQ10472.

Polymorphism databases

DMDM1709558.

Proteomic databases

MaxQBQ10472.
PaxDbQ10472.
PeptideAtlasQ10472.
PRIDEQ10472.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000269195; ENSP00000269195; ENSG00000141429. [Q10472-1]
ENST00000591081; ENSP00000466411; ENSG00000141429. [Q10472-2]
ENST00000591924; ENSP00000465699; ENSG00000141429. [Q10472-2]
GeneID2589.
KEGGhsa:2589.
UCSCuc002kyz.4. human. [Q10472-1]
uc002kza.2. human. [Q10472-2]

Organism-specific databases

CTD2589.
GeneCardsGC18P033161.
HGNCHGNC:4123. GALNT1.
HPAHPA012628.
MIM602273. gene.
neXtProtNX_Q10472.
PharmGKBPA30054.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG239675.
HOGENOMHOG000038227.
HOVERGENHBG051699.
InParanoidQ10472.
KOK00710.
OMAIKHDRKT.
OrthoDBEOG7J9VP2.
PhylomeDBQ10472.
TreeFamTF313267.

Enzyme and pathway databases

BioCycMetaCyc:HS06826-MONOMER.
ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ10472.
BgeeQ10472.
CleanExHS_GALNT1.
GenevestigatorQ10472.

Family and domain databases

Gene3D3.90.550.10. 1 hit.
InterProIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamPF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMSSF50370. SSF50370. 1 hit.
SSF53448. SSF53448. 1 hit.
PROSITEPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGALNT1. human.
GeneWikiGALNT1.
GenomeRNAi2589.
NextBio10241.
PROQ10472.
SOURCESearch...

Entry information

Entry nameGALT1_HUMAN
AccessionPrimary (citable) accession number: Q10472
Secondary accession number(s): Q86TJ7, Q9UM86
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 18

Human chromosome 18: entries, gene names and cross-references to MIM