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Q10472

- GALT1_HUMAN

UniProt

Q10472 - GALT1_HUMAN

Protein

Polypeptide N-acetylgalactosaminyltransferase 1

Gene

GALNT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    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

    Manganese.

    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. manganese ion binding Source: BHF-UCL
    2. 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

    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

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell
    2. Golgi cisterna membrane Source: UniProtKB-SubCell
    3. Golgi membrane Source: Reactome
    4. integral component of membrane Source: UniProtKB-KW
    5. membrane Source: UniProtKB
    6. perinuclear region of cytoplasm Source: BHF-UCL

    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

    ArrayExpressiQ10472.
    BgeeiQ10472.
    CleanExiHS_GALNT1.
    GenevestigatoriQ10472.

    Organism-specific databases

    HPAiHPA012628.

    Interactioni

    Protein-protein interaction databases

    BioGridi108861. 3 interactions.
    IntActiQ10472. 1 interaction.
    STRINGi9606.ENSP00000269195.

    Structurei

    3D structure databases

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

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 88CytoplasmicSequence Analysis
    Topological domaini29 – 559531LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei9 – 2820Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    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.
    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

    MRKFAYCKVV LATSLIWVLL DMFLLLYFSE CNKCDEKKER GLPAGDVLEP    50
    VQKPHEGPGE MGKPVVIPKE DQEKMKEMFK INQFNLMASE MIALNRSLPD 100
    VRLEGCKTKV YPDNLPTTSV VIVFHNEAWS TLLRTVHSVI NRSPRHMIEE 150
    IVLVDDASER DFLKRPLESY VKKLKVPVHV IRMEQRSGLI RARLKGAAVS 200
    KGQVITFLDA HCECTVGWLE PLLARIKHDR RTVVCPIIDV ISDDTFEYMA 250
    GSDMTYGGFN WKLNFRWYPV PQREMDRRKG DRTLPVRTPT MAGGLFSIDR 300
    DYFQEIGTYD AGMDIWGGEN LEISFRIWQC GGTLEIVTCS HVGHVFRKAT 350
    PYTFPGGTGQ IINKNNRRLA EVWMDEFKNF FYIISPGVTK VDYGDISSRV 400
    GLRHKLQCKP FSWYLENIYP DSQIPRHYFS LGEIRNVETN QCLDNMARKE 450
    NEKVGIFNCH GMGGNQVFSY TANKEIRTDD LCLDVSKLNG PVTMLKCHHL 500
    KGNQLWEYDP VKLTLQHVNS NQCLDKATEE DSQVPSIRDC NGSRSQQWLL 550
    RNVTLPEIF 559
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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. 3 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.
    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

    ArrayExpressi Q10472.
    Bgeei Q10472.
    CleanExi HS_GALNT1.
    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

    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: October 1, 2014
    This is version 141 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