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Q8N428

- GLT16_HUMAN

UniProt

Q8N428 - GLT16_HUMAN

Protein

Polypeptide N-acetylgalactosaminyltransferase 16

Gene

GALNT16

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 2 (16 Aug 2004)
      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.1 Publication

    Catalytic activityi

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

    Cofactori

    Manganese.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

    Pathwayi

    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

    1. metal ion binding Source: UniProtKB-KW
    2. polypeptide N-acetylgalactosaminyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. protein glycosylation Source: UniProtKB-UniPathway

    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: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:23233. GALNT16.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. Golgi membrane Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134991608.

    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

    ArrayExpressiQ8N428.
    BgeeiQ8N428.
    CleanExiHS_GALNTL1.
    GenevestigatoriQ8N428.

    Organism-specific databases

    HPAiHPA059136.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000336729.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8N428.
    SMRiQ8N428. Positions 90-554.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 66CytoplasmicSequence Analysis
    Topological domaini27 – 558532LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei7 – 2620Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    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.
    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. Align

    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

    MRKIRANAIA ILTVAWILGT FYYLWQDNRA HAASSGGRGA QRAGRRSEQL    50
    REDRTIPLIV TGTPSKGFDE KAYLSAKQLK AGEDPYRQHA FNQLESDKLS 100
    PDRPIRDTRH YSCPSVSYSS DLPATSVIIT FHNEARSTLL RTVKSVLNRT 150
    PANLIQEIIL VDDFSSDPED CLLLTRIPKV KCLRNDRREG LIRSRVRGAD 200
    VAAATVLTFL DSHCEVNTEW LPPMLQRVKE DHTRVVSPII DVISLDNFAY 250
    LAASADLRGG FDWSLHFKWE QIPLEQKMTR TDPTRPIRTP VIAGGIFVID 300
    KSWFNHLGKY DAQMDIWGGE NFELSFRVWM CGGSLEIVPC SRVGHVFRKR 350
    HPYNFPEGNA LTYIRNTKRT AEVWMDEYKQ YYYEARPSAI GKAFGSVATR 400
    IEQRKKMNCK SFRWYLENVY PELTVPVKEA LPGIIKQGVN CLESQGQNTA 450
    GDFLLGMGIC RGSAKNPQPA QAWLFSDHLI QQQGKCLAAT STLMSSPGSP 500
    VILQMCNPRE GKQKWRRKGS FIQHSVSGLC LETKPAQLVT SKCQADAQAQ 550
    QWQLLPHT 558
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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]

    Polymorphism databases

    DMDMi51316024.

    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS32107.1. [Q8N428-1 ]
    RefSeqi NP_001161840.1. NM_001168368.1. [Q8N428-1 ]
    NP_065743.2. NM_020692.2. [Q8N428-1 ]
    UniGenei Hs.21035.

    3D structure databases

    ProteinModelPortali Q8N428.
    SMRi Q8N428. Positions 90-554.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000336729.

    Protein family/group databases

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

    PTM databases

    PhosphoSitei Q8N428.

    Polymorphism databases

    DMDMi 51316024.

    Proteomic databases

    MaxQBi Q8N428.
    PaxDbi Q8N428.
    PRIDEi Q8N428.

    Protocols and materials databases

    DNASUi 57452.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000337827 ; ENSP00000336729 ; ENSG00000100626 . [Q8N428-1 ]
    ENST00000448469 ; ENSP00000402970 ; ENSG00000100626 . [Q8N428-1 ]
    ENST00000553471 ; ENSP00000451420 ; ENSG00000100626 . [Q8N428-2 ]
    ENST00000553669 ; ENSP00000451200 ; ENSG00000100626 . [Q8N428-2 ]
    GeneIDi 57452.
    KEGGi hsa:57452.
    UCSCi uc001xla.2. human.
    uc001xlb.2. human. [Q8N428-1 ]

    Organism-specific databases

    CTDi 57452.
    GeneCardsi GC14P069725.
    HGNCi HGNC:23233. GALNT16.
    HPAi HPA059136.
    neXtProti NX_Q8N428.
    PharmGKBi PA134991608.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG239675.
    HOGENOMi HOG000038227.
    HOVERGENi HBG051699.
    InParanoidi Q8N428.
    KOi K00710.
    OMAi PEDCQLL.
    OrthoDBi EOG7J9VP2.
    PhylomeDBi Q8N428.
    TreeFami TF313267.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    Reactomei REACT_115606. O-linked glycosylation of mucins.

    Miscellaneous databases

    GenomeRNAii 57452.
    NextBioi 63624.
    PROi Q8N428.

    Gene expression databases

    ArrayExpressi Q8N428.
    Bgeei Q8N428.
    CleanExi HS_GALNTL1.
    Genevestigatori Q8N428.

    Family and domain databases

    Gene3Di 3.90.550.10. 1 hit.
    InterProi IPR027791. Galactosyl_T_C.
    IPR001173. Glyco_trans_2-like.
    IPR029044. Nucleotide-diphossugar_trans.
    IPR000772. Ricin_B_lectin.
    [Graphical view ]
    Pfami PF02709. Glyco_transf_7C. 1 hit.
    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. "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: October 1, 2014
    This is version 112 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3