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Q10472

- GALT1_HUMAN

UniProt

Q10472 - GALT1_HUMAN

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Protein

Polypeptide N-acetylgalactosaminyltransferase 1

Gene

GALNT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei156 – 1561SubstrateBy similarity
Binding sitei186 – 1861SubstrateBy similarity
Metal bindingi209 – 2091ManganeseBy similarity
Metal bindingi211 – 2111ManganeseBy similarity
Binding sitei316 – 3161SubstrateBy similarity
Metal bindingi344 – 3441ManganeseBy similarity
Binding sitei347 – 3471SubstrateBy similarity
Binding sitei352 – 3521SubstrateBy similarity

GO - Molecular functioni

  1. carbohydrate binding Source: UniProtKB-KW
  2. manganese ion binding Source: BHF-UCL
  3. polypeptide N-acetylgalactosaminyltransferase activity Source: BHF-UCL

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. O-glycan processing Source: Reactome
  3. post-translational protein modification Source: Reactome
  4. protein O-linked glycosylation Source: UniProtKB
  5. protein O-linked glycosylation via serine Source: BHF-UCL
  6. protein O-linked glycosylation via threonine Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Lectin, Manganese, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS06826-MONOMER.
ReactomeiREACT_115606. O-linked glycosylation of mucins.
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
ProteomesiUP000005640: Chromosome 18

Organism-specific databases

HGNCiHGNC:4123. GALNT1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 88CytoplasmicSequence Analysis
Transmembranei9 – 2820Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini29 – 559531LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
  2. Golgi membrane Source: Reactome
  3. integral component of membrane Source: UniProtKB-KW
  4. membrane Source: UniProtKB
  5. perinuclear region of cytoplasm Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30054.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 559559Polypeptide N-acetylgalactosaminyltransferase 1PRO_0000223387Add
BLAST
Chaini41 – 559519Polypeptide N-acetylgalactosaminyltransferase 1 soluble formPRO_0000012257Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi95 – 951N-linked (GlcNAc...)Sequence Analysis
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
Glycosylationi552 – 5521N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ10472.
PaxDbiQ10472.
PeptideAtlasiQ10472.
PRIDEiQ10472.

PTM databases

PhosphoSiteiQ10472.

Expressioni

Tissue specificityi

Widely expressed. Expressed in all tissues tested.1 Publication

Gene expression databases

BgeeiQ10472.
CleanExiHS_GALNT1.
ExpressionAtlasiQ10472. baseline and differential.
GenevestigatoriQ10472.

Organism-specific databases

HPAiHPA012628.

Interactioni

Protein-protein interaction databases

BioGridi108861. 6 interactions.
IntActiQ10472. 1 interaction.
STRINGi9606.ENSP00000269195.

Structurei

3D structure databases

ProteinModelPortaliQ10472.
SMRiQ10472. Positions 95-553.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini429 – 551123Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni115 – 225111Catalytic subdomain AAdd
BLAST
Regioni285 – 34763Catalytic subdomain BAdd
BLAST

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

Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG239675.
GeneTreeiENSGT00760000118828.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
InParanoidiQ10472.
KOiK00710.
OMAiIKHDRKT.
OrthoDBiEOG7J9VP2.
PhylomeDBiQ10472.
TreeFamiTF313267.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTiSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 1 hit.
SSF53448. SSF53448. 1 hit.
PROSITEiPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]

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. Align

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti414 – 4141Y → D.
Corresponds to variant rs34304568 [ dbSNP | Ensembl ].
VAR_033946

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei106 – 559454Missing in isoform 2. 1 PublicationVSP_011200Add
BLAST

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_005258239.1. [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.
UCSCiuc002kyz.4. human. [Q10472-1]
uc002kza.2. human. [Q10472-2]

Polymorphism databases

DMDMi1709558.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 1

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 .
CCDSi CCDS11915.1. [Q10472-1 ]
PIRi JC4223.
RefSeqi NP_065207.2. NM_020474.3. [Q10472-1 ]
XP_005258296.1. XM_005258239.1. [Q10472-1 ]
UniGenei Hs.514806.

3D structure databases

ProteinModelPortali Q10472.
SMRi Q10472. Positions 95-553.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108861. 6 interactions.
IntActi Q10472. 1 interaction.
STRINGi 9606.ENSP00000269195.

Protein family/group databases

CAZyi CBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

PTM databases

PhosphoSitei Q10472.

Polymorphism databases

DMDMi 1709558.

Proteomic databases

MaxQBi Q10472.
PaxDbi Q10472.
PeptideAtlasi Q10472.
PRIDEi Q10472.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000269195 ; ENSP00000269195 ; ENSG00000141429 . [Q10472-1 ]
ENST00000591081 ; ENSP00000466411 ; ENSG00000141429 . [Q10472-2 ]
ENST00000591924 ; ENSP00000465699 ; ENSG00000141429 . [Q10472-2 ]
GeneIDi 2589.
KEGGi hsa:2589.
UCSCi uc002kyz.4. human. [Q10472-1 ]
uc002kza.2. human. [Q10472-2 ]

Organism-specific databases

CTDi 2589.
GeneCardsi GC18P033161.
HGNCi HGNC:4123. GALNT1.
HPAi HPA012628.
MIMi 602273. gene.
neXtProti NX_Q10472.
PharmGKBi PA30054.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG239675.
GeneTreei ENSGT00760000118828.
HOGENOMi HOG000038227.
HOVERGENi HBG051699.
InParanoidi Q10472.
KOi K00710.
OMAi IKHDRKT.
OrthoDBi EOG7J9VP2.
PhylomeDBi Q10472.
TreeFami TF313267.

Enzyme and pathway databases

UniPathwayi UPA00378 .
BioCyci MetaCyc:HS06826-MONOMER.
Reactomei REACT_115606. O-linked glycosylation of mucins.

Miscellaneous databases

ChiTaRSi GALNT1. human.
GeneWikii GALNT1.
GenomeRNAii 2589.
NextBioi 10241.
PROi Q10472.
SOURCEi Search...

Gene expression databases

Bgeei Q10472.
CleanExi HS_GALNT1.
ExpressionAtlasi Q10472. baseline and differential.
Genevestigatori Q10472.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
InterProi IPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view ]
Pfami PF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view ]
SMARTi SM00458. RICIN. 1 hit.
[Graphical view ]
SUPFAMi SSF50370. SSF50370. 1 hit.
SSF53448. SSF53448. 1 hit.
PROSITEi PS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGALT1_HUMAN
AccessioniPrimary (citable) accession number: Q10472
Secondary accession number(s): Q86TJ7, Q9UM86
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 26, 2014
This is version 143 of the entry and version 1 of the sequence. [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

External Data

Dasty 3