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Protein

Polypeptide N-acetylgalactosaminyltransferase 16

Gene

GALNT16

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.1 Publication

Catalytic activityi

UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.1 Publication

Cofactori

Mn2+By similarity

Kineticsi

  1. KM=251 µM for Muc5AC1 Publication
  2. KM=310 µM for Muc5AC-31 Publication
  3. KM=390 µM for Muc5AC-131 Publication
  4. KM=332 µM for EA21 Publication

    Pathway: 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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei163 – 1631SubstrateBy similarity
    Binding sitei188 – 1881SubstrateBy similarity
    Metal bindingi211 – 2111ManganeseBy similarity
    Binding sitei212 – 2121SubstrateBy similarity
    Metal bindingi213 – 2131ManganeseBy similarity
    Binding sitei317 – 3171SubstrateBy similarity
    Metal bindingi345 – 3451ManganeseBy similarity
    Binding sitei348 – 3481SubstrateBy similarity
    Binding sitei351 – 3511SubstrateBy similarity
    Binding sitei353 – 3531SubstrateBy similarity

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Ligandi

    Lectin, Manganese, Metal-binding

    Enzyme and pathway databases

    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 16 (EC:2.4.1.41)
    Alternative name(s):
    Polypeptide GalNAc transferase 16
    Short name:
    GalNAc-T16
    Polypeptide GalNAc transferase-like protein 1
    Short name:
    GalNAc-T-like protein 1
    Short name:
    pp-GaNTase-like protein 1
    Polypeptide N-acetylgalactosaminyltransferase-like protein 1
    Protein-UDP acetylgalactosaminyltransferase-like protein 1
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 1
    Gene namesi
    Name:GALNT16
    Synonyms:GALNTL1, KIAA1130
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:23233. GALNT16.

    Subcellular locationi

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 66CytoplasmicSequence Analysis
    Transmembranei7 – 2620Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST
    Topological domaini27 – 558532LumenalSequence AnalysisAdd
    BLAST

    GO - Cellular componenti

    • extracellular exosome Source: UniProtKB
    • Golgi membrane Source: UniProtKB-SubCell
    • integral component of membrane Source: UniProtKB-KW
    Complete GO annotation...

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134991608.

    Polymorphism and mutation databases

    BioMutaiGALNT16.
    DMDMi51316024.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 558558Polypeptide N-acetylgalactosaminyltransferase 16PRO_0000059135Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi113 ↔ 340PROSITE-ProRule annotation
    Disulfide bondi331 ↔ 409PROSITE-ProRule annotation
    Disulfide bondi441 ↔ 460PROSITE-ProRule annotation
    Disulfide bondi486 ↔ 506PROSITE-ProRule annotation
    Disulfide bondi530 ↔ 543PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    MaxQBiQ8N428.
    PaxDbiQ8N428.
    PRIDEiQ8N428.

    PTM databases

    PhosphoSiteiQ8N428.

    Expressioni

    Gene expression databases

    BgeeiQ8N428.
    CleanExiHS_GALNTL1.
    ExpressionAtlasiQ8N428. baseline and differential.
    GenevisibleiQ8N428. HS.

    Organism-specific databases

    HPAiHPA059136.

    Interactioni

    Protein-protein interaction databases

    BioGridi121524. 2 interactions.
    STRINGi9606.ENSP00000336729.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8N428.
    SMRiQ8N428. Positions 68-554.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini428 – 555128Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni122 – 227106Catalytic subdomain AAdd
    BLAST
    Regioni286 – 34863Catalytic 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 binds to GalNAc and contributes to the glycopeptide specificity.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.
    InParanoidiQ8N428.
    KOiK00710.
    OMAiPEDCQLL.
    OrthoDBiEOG7J9VP2.
    PhylomeDBiQ8N428.
    TreeFamiTF313267.

    Family and domain databases

    Gene3Di3.90.550.10. 1 hit.
    InterProiIPR027791. Galactosyl_T_C.
    IPR001173. Glyco_trans_2-like.
    IPR029044. Nucleotide-diphossugar_trans.
    IPR000772. Ricin_B_lectin.
    [Graphical view]
    PfamiPF02709. Glyco_transf_7C. 1 hit.
    PF00535. 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.

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

    Isoform 1 (identifier: Q8N428-1) [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
    MRKIRANAIA ILTVAWILGT FYYLWQDNRA HAASSGGRGA QRAGRRSEQL
    60 70 80 90 100
    REDRTIPLIV TGTPSKGFDE KAYLSAKQLK AGEDPYRQHA FNQLESDKLS
    110 120 130 140 150
    PDRPIRDTRH YSCPSVSYSS DLPATSVIIT FHNEARSTLL RTVKSVLNRT
    160 170 180 190 200
    PANLIQEIIL VDDFSSDPED CLLLTRIPKV KCLRNDRREG LIRSRVRGAD
    210 220 230 240 250
    VAAATVLTFL DSHCEVNTEW LPPMLQRVKE DHTRVVSPII DVISLDNFAY
    260 270 280 290 300
    LAASADLRGG FDWSLHFKWE QIPLEQKMTR TDPTRPIRTP VIAGGIFVID
    310 320 330 340 350
    KSWFNHLGKY DAQMDIWGGE NFELSFRVWM CGGSLEIVPC SRVGHVFRKR
    360 370 380 390 400
    HPYNFPEGNA LTYIRNTKRT AEVWMDEYKQ YYYEARPSAI GKAFGSVATR
    410 420 430 440 450
    IEQRKKMNCK SFRWYLENVY PELTVPVKEA LPGIIKQGVN CLESQGQNTA
    460 470 480 490 500
    GDFLLGMGIC RGSAKNPQPA QAWLFSDHLI QQQGKCLAAT STLMSSPGSP
    510 520 530 540 550
    VILQMCNPRE GKQKWRRKGS FIQHSVSGLC LETKPAQLVT SKCQADAQAQ

    QWQLLPHT
    Length:558
    Mass (Da):63,074
    Last modified:August 16, 2004 - v2
    Checksum:iFF35C5606B5291B8
    GO
    Isoform 2 (identifier: Q8N428-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         514-558: KWRRKGSFIQHSVSGLCLETKPAQLVTSKCQADAQAQQWQLLPHT → VSLLASGPEAQQPEGPCLRVADLGRRAPD

    Show »
    Length:542
    Mass (Da):60,972
    Checksum:i1E517B517B2568A9
    GO

    Sequence cautioni

    The sequence BAA86444.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti201 – 2011V → M.2 Publications
    Corresponds to variant rs12879377 [ dbSNP | Ensembl ].
    VAR_055848
    Natural varianti497 – 4971P → S.
    Corresponds to variant rs59840366 [ dbSNP | Ensembl ].
    VAR_061195

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei514 – 55845KWRRK…LLPHT → VSLLASGPEAQQPEGPCLRV ADLGRRAPD in isoform 2. 2 PublicationsVSP_011231Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB032956 mRNA. Translation: BAA86444.1. Different initiation.
    AB078143 mRNA. Translation: BAD93178.1.
    AK289745 mRNA. Translation: BAF82434.1.
    CH471061 Genomic DNA. Translation: EAW80987.1.
    BC036812 mRNA. Translation: AAH36812.2.
    BC098578 mRNA. Translation: AAH98578.1.
    CCDSiCCDS32107.1. [Q8N428-1]
    RefSeqiNP_001161840.1. NM_001168368.1. [Q8N428-1]
    NP_065743.2. NM_020692.2. [Q8N428-1]
    UniGeneiHs.21035.

    Genome annotation databases

    EnsembliENST00000337827; ENSP00000336729; ENSG00000100626. [Q8N428-1]
    ENST00000448469; ENSP00000402970; ENSG00000100626. [Q8N428-1]
    ENST00000553471; ENSP00000451420; ENSG00000100626. [Q8N428-2]
    ENST00000553669; ENSP00000451200; ENSG00000100626. [Q8N428-2]
    GeneIDi57452.
    KEGGihsa:57452.
    UCSCiuc001xla.2. human.
    uc001xlb.2. human. [Q8N428-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    GGDB

    GlycoGene database

    Functional Glycomics Gateway - GTase

    Putative polypeptide N-acetylgalactosaminyltransferase-like protein 1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB032956 mRNA. Translation: BAA86444.1. Different initiation.
    AB078143 mRNA. Translation: BAD93178.1.
    AK289745 mRNA. Translation: BAF82434.1.
    CH471061 Genomic DNA. Translation: EAW80987.1.
    BC036812 mRNA. Translation: AAH36812.2.
    BC098578 mRNA. Translation: AAH98578.1.
    CCDSiCCDS32107.1. [Q8N428-1]
    RefSeqiNP_001161840.1. NM_001168368.1. [Q8N428-1]
    NP_065743.2. NM_020692.2. [Q8N428-1]
    UniGeneiHs.21035.

    3D structure databases

    ProteinModelPortaliQ8N428.
    SMRiQ8N428. Positions 68-554.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi121524. 2 interactions.
    STRINGi9606.ENSP00000336729.

    Protein family/group databases

    CAZyiCBM13. Carbohydrate-Binding Module Family 13.
    GT27. Glycosyltransferase Family 27.

    PTM databases

    PhosphoSiteiQ8N428.

    Polymorphism and mutation databases

    BioMutaiGALNT16.
    DMDMi51316024.

    Proteomic databases

    MaxQBiQ8N428.
    PaxDbiQ8N428.
    PRIDEiQ8N428.

    Protocols and materials databases

    DNASUi57452.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000337827; ENSP00000336729; ENSG00000100626. [Q8N428-1]
    ENST00000448469; ENSP00000402970; ENSG00000100626. [Q8N428-1]
    ENST00000553471; ENSP00000451420; ENSG00000100626. [Q8N428-2]
    ENST00000553669; ENSP00000451200; ENSG00000100626. [Q8N428-2]
    GeneIDi57452.
    KEGGihsa:57452.
    UCSCiuc001xla.2. human.
    uc001xlb.2. human. [Q8N428-1]

    Organism-specific databases

    CTDi57452.
    GeneCardsiGC14P069725.
    HGNCiHGNC:23233. GALNT16.
    HPAiHPA059136.
    MIMi615132. gene.
    neXtProtiNX_Q8N428.
    PharmGKBiPA134991608.
    HUGEiSearch...
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiNOG239675.
    GeneTreeiENSGT00760000118828.
    HOGENOMiHOG000038227.
    HOVERGENiHBG051699.
    InParanoidiQ8N428.
    KOiK00710.
    OMAiPEDCQLL.
    OrthoDBiEOG7J9VP2.
    PhylomeDBiQ8N428.
    TreeFamiTF313267.

    Enzyme and pathway databases

    UniPathwayiUPA00378.
    ReactomeiREACT_115606. O-linked glycosylation of mucins.

    Miscellaneous databases

    GenomeRNAii57452.
    NextBioi63624.
    PROiQ8N428.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ8N428.
    CleanExiHS_GALNTL1.
    ExpressionAtlasiQ8N428. baseline and differential.
    GenevisibleiQ8N428. HS.

    Family and domain databases

    Gene3Di3.90.550.10. 1 hit.
    InterProiIPR027791. Galactosyl_T_C.
    IPR001173. Glyco_trans_2-like.
    IPR029044. Nucleotide-diphossugar_trans.
    IPR000772. Ricin_B_lectin.
    [Graphical view]
    PfamiPF02709. Glyco_transf_7C. 1 hit.
    PF00535. 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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain."
      Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.
      DNA Res. 6:329-336(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    2. "Cloning and Characterization of New Member of Human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, Designated GalNAc-T16."
      Guo J., Zhang Y., Chen L., Narimatsu H.
      Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Fetal brain.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT MET-201.
      Tissue: Brain.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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 1), VARIANT MET-201.
      Tissue: Brain and Chondrosarcoma.
    6. "UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferases: completion of the family tree."
      Raman J., Guan Y., Perrine C.L., Gerken T.A., Tabak L.A.
      Glycobiology 22:768-777(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiGLT16_HUMAN
    AccessioniPrimary (citable) accession number: Q8N428
    Secondary accession number(s): Q4KMG3, Q58A55, Q9ULT9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: August 16, 2004
    Last modified: June 24, 2015
    This is version 119 of the entry and version 2 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 14
      Human chromosome 14: 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.