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Q9HCQ5

- GALT9_HUMAN

UniProt

Q9HCQ5 - GALT9_HUMAN

Protein

Polypeptide N-acetylgalactosaminyltransferase 9

Gene

GALNT9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 3 (03 Apr 2007)
      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. Does not glycosylate apomucin or SDC3.

    Catalytic activityi

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

    Cofactori

    Manganese.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei191 – 1911SubstrateBy similarity
    Binding sitei222 – 2221SubstrateBy similarity
    Metal bindingi245 – 2451ManganeseBy similarity
    Metal bindingi247 – 2471ManganeseBy similarity
    Metal bindingi377 – 3771ManganeseBy similarity
    Binding sitei380 – 3801SubstrateBy similarity
    Binding sitei385 – 3851SubstrateBy similarity

    GO - Molecular functioni

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

    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

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Ligandi

    Lectin, Manganese, Metal-binding

    Enzyme and pathway databases

    BRENDAi2.4.1.41. 2681.
    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 9 (EC:2.4.1.41)
    Alternative name(s):
    Polypeptide GalNAc transferase 9
    Short name:
    GalNAc-T9
    Short name:
    pp-GaNTase 9
    Protein-UDP acetylgalactosaminyltransferase 9
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9
    Gene namesi
    Name:GALNT9
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:4131. GALNT9.

    Subcellular locationi

    GO - Cellular componenti

    1. Golgi membrane Source: Reactome
    2. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28544.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 603603Polypeptide N-acetylgalactosaminyltransferase 9PRO_0000059120Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi141 ↔ 372PROSITE-ProRule annotation
    Disulfide bondi363 ↔ 442PROSITE-ProRule annotation
    Glycosylationi460 – 4601N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi477 ↔ 493PROSITE-ProRule annotation
    Disulfide bondi525 ↔ 540PROSITE-ProRule annotation
    Disulfide bondi567 ↔ 587PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ9HCQ5.
    PRIDEiQ9HCQ5.

    Expressioni

    Tissue specificityi

    Specifically expressed in brain. Not expressed in heart, placenta, lung, liver, skeletal muscle, kidney, pancreas, spleen, thymus, prostate, testis, ovary, small intestine, colon and leukocyte. In brain, it is expressed in cerebellum, frontal lobe, temporal lobe, putamen and spinal cord, weakly expressed in cerebral cortex. Not expressed in medulla and occipital pole.1 Publication

    Gene expression databases

    ArrayExpressiQ9HCQ5.
    BgeeiQ9HCQ5.
    CleanExiHS_GALNT9.
    GenevestigatoriQ9HCQ5.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000380488.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9HCQ5.
    SMRiQ9HCQ5. Positions 105-596.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 66CytoplasmicSequence Analysis
    Topological domaini30 – 603574LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei7 – 2923Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini464 – 600137Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni150 – 261112Catalytic subdomain AAdd
    BLAST
    Regioni318 – 38063Catalytic 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

    eggNOGiNOG250827.
    HOGENOMiHOG000038228.
    HOVERGENiHBG051699.
    InParanoidiQ9HCQ5.
    KOiK00710.
    PhylomeDBiQ9HCQ5.
    TreeFamiTF313267.

    Family and domain databases

    Gene3Di3.90.550.10. 1 hit.
    InterProiIPR001173. Glyco_trans_2-like.
    IPR029044. Nucleotide-diphossugar_trans.
    IPR000772. Ricin_B_lectin.
    IPR001202. WW_dom.
    [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.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9HCQ5-1) [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

    MAVARKIRTL LTVNILVFVG IVLFSVYCRL QGRSQELVRI VSGDRRVRSR    50
    HAKVGTLGDR EAILQRLDHL EEVVYNQLNG LAKPIGLVEG PGGLGQGGLA 100
    ATLRDDGQEA EGKYEEYGYN AQLSDRISLD RSIPDYRPRK CRQMSYAQDL 150
    PQVSVVFIFV NEALSVILRS VHSVVNHTPS QLLKEVILVD DNSDNVELKF 200
    NLDQYVNKRY PGLVKIVRNS RREGLIRARL QGWKAATAPV VGFFDAHVEF 250
    NTGWAEPALS RIREDRRRIV LPAIDNIKYS TFEVQQYANA AHGYNWGLRC 300
    MYIIPPQDWL DRGDESAPIR TPAMIGCSFV VDREYFGDIG LLDPGMEVYG 350
    GENVELGMRV WQCGGSMEVL PCSRVAHIER TRKPYNNDID YYAKRNALRA 400
    AEVWMDDFKS HVYMAWNIPM SNPGVDFGDV SERLALRQRL KCRSFKWYLE 450
    NVYPEMRVYN NTLTYGEVRN SKASAYCLDQ GAEDGDRAIL YPCHGMSSQL 500
    VRYSADGLLQ LGPLGSTAFL PDSKCLVDDG TGRMPTLKKC EDVARPTQRL 550
    WDFTQSGPIV SRATGRCLEV EMSKDANFGL RLVVQRCSGQ KWMIRNWIKH 600
    ARH 603
    Length:603
    Mass (Da):68,359
    Last modified:April 3, 2007 - v3
    Checksum:i4B5888733D8577CF
    GO
    Isoform 2 (identifier: Q9HCQ5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-366: Missing.

    Show »
    Length:237
    Mass (Da):27,211
    Checksum:i5484F64E65F6F6DA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti539 – 5391K → R in BAB13699. (PubMed:10978536)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 366366Missing in isoform 2. 2 PublicationsVSP_011206Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB040672 mRNA. Translation: BAB13699.2.
    AF458594 mRNA. Translation: AAM49722.1.
    BC093817 mRNA. Translation: AAH93817.2.
    BC093819 mRNA. Translation: AAH93819.2.
    CCDSiCCDS41866.1. [Q9HCQ5-2]
    RefSeqiNP_001116108.1. NM_001122636.1.
    NP_068580.2. NM_021808.3. [Q9HCQ5-2]
    UniGeneiHs.301062.
    Hs.658249.

    Genome annotation databases

    EnsembliENST00000397325; ENSP00000380488; ENSG00000182870. [Q9HCQ5-2]
    ENST00000541995; ENSP00000440544; ENSG00000182870. [Q9HCQ5-2]
    GeneIDi50614.
    KEGGihsa:50614.
    UCSCiuc001uka.3. human. [Q9HCQ5-2]

    Polymorphism databases

    DMDMi143811393.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    GGDB

    GlycoGene database

    Functional Glycomics Gateway - GTase

    Polypeptide N-acetylgalactosaminyltransferase 9

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB040672 mRNA. Translation: BAB13699.2 .
    AF458594 mRNA. Translation: AAM49722.1 .
    BC093817 mRNA. Translation: AAH93817.2 .
    BC093819 mRNA. Translation: AAH93819.2 .
    CCDSi CCDS41866.1. [Q9HCQ5-2 ]
    RefSeqi NP_001116108.1. NM_001122636.1.
    NP_068580.2. NM_021808.3. [Q9HCQ5-2 ]
    UniGenei Hs.301062.
    Hs.658249.

    3D structure databases

    ProteinModelPortali Q9HCQ5.
    SMRi Q9HCQ5. Positions 105-596.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000380488.

    Protein family/group databases

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

    Polymorphism databases

    DMDMi 143811393.

    Proteomic databases

    PaxDbi Q9HCQ5.
    PRIDEi Q9HCQ5.

    Protocols and materials databases

    DNASUi 50614.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000397325 ; ENSP00000380488 ; ENSG00000182870 . [Q9HCQ5-2 ]
    ENST00000541995 ; ENSP00000440544 ; ENSG00000182870 . [Q9HCQ5-2 ]
    GeneIDi 50614.
    KEGGi hsa:50614.
    UCSCi uc001uka.3. human. [Q9HCQ5-2 ]

    Organism-specific databases

    CTDi 50614.
    GeneCardsi GC12M132680.
    HGNCi HGNC:4131. GALNT9.
    MIMi 606251. gene.
    neXtProti NX_Q9HCQ5.
    PharmGKBi PA28544.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG250827.
    HOGENOMi HOG000038228.
    HOVERGENi HBG051699.
    InParanoidi Q9HCQ5.
    KOi K00710.
    PhylomeDBi Q9HCQ5.
    TreeFami TF313267.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    BRENDAi 2.4.1.41. 2681.
    Reactomei REACT_115606. O-linked glycosylation of mucins.

    Miscellaneous databases

    GenomeRNAii 50614.
    NextBioi 53114.
    PROi Q9HCQ5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9HCQ5.
    Bgeei Q9HCQ5.
    CleanExi HS_GALNT9.
    Genevestigatori Q9HCQ5.

    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.
    IPR001202. WW_dom.
    [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. "Brain-specific expression of a novel human UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T9)."
      Toba S., Tenno M., Konishi M., Mikami T., Itoh N., Kurosaka A.
      Biochim. Biophys. Acta 1493:264-268(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Brain.
    2. Guo J.H., Zan Q., Yu L.
      Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Kidney.
    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: Colon.
    4. "Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen."
      Zhang Y., Iwasaki H., Wang H., Kudo T., Kalka T.B., Hennet T., Kubota T., Cheng L., Inaba N., Gotoh M., Togayachi A., Guo J.-M., Hisatomi H., Nakajima K., Nishihara S., Nakamura M., Marth J.D., Narimatsu H.
      J. Biol. Chem. 278:573-584(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME ACTIVITY.

    Entry informationi

    Entry nameiGALT9_HUMAN
    AccessioniPrimary (citable) accession number: Q9HCQ5
    Secondary accession number(s): Q52LR8, Q6NT54, Q8NFR1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: April 3, 2007
    Last modified: October 1, 2014
    This is version 114 of the entry and version 3 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 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3