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Protein

Polypeptide N-acetylgalactosaminyltransferase 1

Gene

GALNT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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 Muc7.1 Publication

Catalytic activityi

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

Cofactori

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei156SubstrateBy similarity1
Binding sitei186SubstrateBy similarity1
Metal bindingi209ManganeseBy similarity1
Metal bindingi211ManganeseBy similarity1
Binding sitei316SubstrateBy similarity1
Metal bindingi344ManganeseBy similarity1
Binding sitei347SubstrateBy similarity1
Binding sitei352SubstrateBy similarity1

GO - Molecular functioni

  • carbohydrate binding Source: UniProtKB-KW
  • manganese ion binding Source: BHF-UCL
  • polypeptide N-acetylgalactosaminyltransferase activity Source: UniProtKB

GO - Biological processi

  • O-glycan processing Source: Reactome
  • protein O-linked glycosylation Source: UniProtKB
  • protein O-linked glycosylation via serine Source: BHF-UCL
  • protein O-linked glycosylation via threonine Source: BHF-UCL

Keywordsi

Molecular functionGlycosyltransferase, Transferase
LigandLectin, Manganese, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS06826-MONOMER
BRENDAi2.4.1.41 2681
ReactomeiR-HSA-6811436 COPI-independent Golgi-to-ER retrograde traffic
R-HSA-913709 O-linked glycosylation of mucins
SABIO-RKiQ10472
UniPathwayiUPA00378

Protein family/group databases

CAZyiCBM13 Carbohydrate-Binding Module Family 13
GT27 Glycosyltransferase Family 27

Names & Taxonomyi

Protein namesi
Recommended 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
Cleaved into the following chain:
Gene namesi
Name:GALNT1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 18

Organism-specific databases

EuPathDBiHostDB:ENSG00000141429.13
HGNCiHGNC:4123 GALNT1
MIMi602273 gene
neXtProtiNX_Q10472

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 8CytoplasmicSequence analysis8
Transmembranei9 – 28Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST20
Topological domaini29 – 559LumenalSequence analysisAdd BLAST531

Keywords - Cellular componenti

Golgi apparatus, Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi2589
OpenTargetsiENSG00000141429
PharmGKBiPA30054

Polymorphism and mutation databases

BioMutaiGALNT1
DMDMi1709558

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002233871 – 559Polypeptide N-acetylgalactosaminyltransferase 1Add BLAST559
ChainiPRO_000001225741 – 559Polypeptide N-acetylgalactosaminyltransferase 1 soluble formAdd BLAST519

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi95N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi106 ↔ 339PROSITE-ProRule annotation
Disulfide bondi330 ↔ 408PROSITE-ProRule annotation
Disulfide bondi442 ↔ 459PROSITE-ProRule annotation
Disulfide bondi482 ↔ 497PROSITE-ProRule annotation
Disulfide bondi523 ↔ 540PROSITE-ProRule annotation
Glycosylationi552N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ10472
MaxQBiQ10472
PaxDbiQ10472
PeptideAtlasiQ10472
PRIDEiQ10472
ProteomicsDBi58855
58856 [Q10472-2]

PTM databases

iPTMnetiQ10472
PhosphoSitePlusiQ10472
SwissPalmiQ10472

Expressioni

Tissue specificityi

Widely expressed. Expressed in all tissues tested.1 Publication

Gene expression databases

BgeeiENSG00000141429
CleanExiHS_GALNT1
ExpressionAtlasiQ10472 baseline and differential
GenevisibleiQ10472 HS

Organism-specific databases

HPAiHPA012628

Interactioni

Protein-protein interaction databases

BioGridi108861, 10 interactors
IntActiQ10472, 4 interactors
MINTiQ10472
STRINGi9606.ENSP00000269195

Structurei

3D structure databases

ProteinModelPortaliQ10472
SMRiQ10472
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini429 – 551Ricin B-type lectinPROSITE-ProRule annotationAdd BLAST123

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni115 – 225Catalytic subdomain AAdd BLAST111
Regioni285 – 347Catalytic subdomain BAdd BLAST63

Domaini

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).By similarity

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3736 Eukaryota
ENOG410XPMK LUCA
GeneTreeiENSGT00760000118828
HOGENOMiHOG000038227
HOVERGENiHBG051699
InParanoidiQ10472
KOiK00710
OMAiIKHDRKT
OrthoDBiEOG091G085O
PhylomeDBiQ10472
TreeFamiTF313267

Family and domain databases

CDDicd00161 RICIN, 1 hit
Gene3Di3.90.550.10, 1 hit
InterProiView protein in InterPro
IPR001173 Glyco_trans_2-like
IPR029044 Nucleotide-diphossugar_trans
IPR035992 Ricin_B-like_lectins
IPR000772 Ricin_B_lectin
PfamiView protein in Pfam
PF00535 Glycos_transf_2, 1 hit
PF00652 Ricin_B_lectin, 1 hit
SMARTiView protein in SMART
SM00458 RICIN, 1 hit
SUPFAMiSSF50370 SSF50370, 1 hit
SSF53448 SSF53448, 1 hit
PROSITEiView protein in PROSITE
PS50231 RICIN_B_LECTIN, 1 hit

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q10472-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MRKFAYCKVV LATSLIWVLL DMFLLLYFSE CNKCDEKKER GLPAGDVLEP
60 70 80 90 100
VQKPHEGPGE MGKPVVIPKE DQEKMKEMFK INQFNLMASE MIALNRSLPD
110 120 130 140 150
VRLEGCKTKV YPDNLPTTSV VIVFHNEAWS TLLRTVHSVI NRSPRHMIEE
160 170 180 190 200
IVLVDDASER DFLKRPLESY VKKLKVPVHV IRMEQRSGLI RARLKGAAVS
210 220 230 240 250
KGQVITFLDA HCECTVGWLE PLLARIKHDR RTVVCPIIDV ISDDTFEYMA
260 270 280 290 300
GSDMTYGGFN WKLNFRWYPV PQREMDRRKG DRTLPVRTPT MAGGLFSIDR
310 320 330 340 350
DYFQEIGTYD AGMDIWGGEN LEISFRIWQC GGTLEIVTCS HVGHVFRKAT
360 370 380 390 400
PYTFPGGTGQ IINKNNRRLA EVWMDEFKNF FYIISPGVTK VDYGDISSRV
410 420 430 440 450
GLRHKLQCKP FSWYLENIYP DSQIPRHYFS LGEIRNVETN QCLDNMARKE
460 470 480 490 500
NEKVGIFNCH GMGGNQVFSY TANKEIRTDD LCLDVSKLNG PVTMLKCHHL
510 520 530 540 550
KGNQLWEYDP VKLTLQHVNS NQCLDKATEE DSQVPSIRDC NGSRSQQWLL

RNVTLPEIF
Length:559
Mass (Da):64,219
Last modified:October 1, 1996 - v1
Checksum:iCD68118CB201EE5B
GO
Isoform 2 (identifier: Q10472-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     106-559: Missing.

Note: No experimental confirmation available.
Show »
Length:105
Mass (Da):12,046
Checksum:i01BE501BD11331AF
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_033946414Y → D. Corresponds to variant dbSNP:rs34304568Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_011200106 – 559Missing in isoform 2. 1 PublicationAdd BLAST454

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U41514 mRNA Translation: AAC50327.1
X85018 mRNA Translation: CAA59380.1
BC047746 mRNA Translation: AAH47746.1
S82597 Genomic DNA Translation: AAD14406.1
CCDSiCCDS11915.1 [Q10472-1]
PIRiJC4223
RefSeqiNP_065207.2, NM_020474.3 [Q10472-1]
XP_005258296.1, XM_005258239.3 [Q10472-1]
XP_016881181.1, XM_017025692.1 [Q10472-1]
UniGeneiHs.514806

Genome annotation databases

EnsembliENST00000269195; ENSP00000269195; ENSG00000141429 [Q10472-1]
ENST00000591081; ENSP00000466411; ENSG00000141429 [Q10472-2]
ENST00000591924; ENSP00000465699; ENSG00000141429 [Q10472-2]
GeneIDi2589
KEGGihsa:2589
UCSCiuc002kza.3 human [Q10472-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiGALT1_HUMAN
AccessioniPrimary (citable) accession number: Q10472
Secondary accession number(s): Q86TJ7, Q9UM86
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 18, 2018
This is version 172 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

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