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Protein

Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2

Gene

ST6GALNAC2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the transfer of N-acetylneuraminyl groups onto glycan chains in glycoproteins.2 Publications

Miscellaneous

Aberrant O-galactosylation of IgA1 molecules plays a role in the development and progression of IgA nephropathy (IgAN). Genetic interactions of C1GALT1 and ST6GALNAC2 variants influence IgA1 O-glycosylation, disease predisposition, and disease severity, and may contribute to the polygenic nature of IgAN.

Catalytic activityi

CMP-N-acetylneuraminate + glycano-(1->3)-(N-acetyl-alpha-D-galactosaminyl)-glycoprotein = CMP + glycano-((2->6)-alpha-N-acetylneuraminyl)-(N-acetyl-D-galactosaminyl)-glycoprotein.2 Publications

Kineticsi

  1. KM=130 µM for CMP-N-acetylneuraminate1 Publication
  2. KM=104 µM for CMP-N-acetylneuraminate1 Publication

    Pathwayi: protein glycosylation

    This protein is involved in the pathway protein glycosylation, which is part of Protein modification.2 Publications
    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)DescriptionActionsGraphical viewLength
    Binding sitei156CMP-N-acetylneuraminateCombined sources1 Publication1
    Binding sitei179CMP-N-acetylneuraminateCombined sources1 Publication1
    Binding sitei304CMP-N-acetylneuraminateCombined sources1 Publication1
    Binding sitei336CMP-N-acetylneuraminateCombined sources1 Publication1

    GO - Molecular functioni

    GO - Biological processi

    • O-glycan processing Source: Reactome
    • oligosaccharide metabolic process Source: GO_Central
    • protein glycosylation Source: UniProtKB
    • protein N-linked glycosylation via asparagine Source: GO_Central
    • protein O-linked glycosylation Source: UniProtKB
    • protein sialylation Source: UniProtKB
    • sialylation Source: GO_Central

    Keywordsi

    Molecular functionGlycosyltransferase, Transferase

    Enzyme and pathway databases

    BRENDAi2.4.99.3 2681
    ReactomeiR-HSA-4085001 Sialic acid metabolism
    R-HSA-977068 Termination of O-glycan biosynthesis
    UniPathwayiUPA00378

    Protein family/group databases

    CAZyiGT29 Glycosyltransferase Family 29

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2 (EC:2.4.99.32 Publications)
    Alternative name(s):
    GalNAc alpha-2,6-sialyltransferase II
    ST6GalNAc II1 Publication
    Short name:
    ST6GalNAcII1 Publication
    SThM
    Sialyltransferase 7B
    Short name:
    SIAT7-B
    Gene namesi
    Name:ST6GALNAC2
    Synonyms:SIAT7B, SIATL1, STHM
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 17

    Organism-specific databases

    EuPathDBiHostDB:ENSG00000070731.9
    HGNCiHGNC:10867 ST6GALNAC2
    MIMi610137 gene
    neXtProtiNX_Q9UJ37

    Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Topology

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Topological domaini1 – 7CytoplasmicSequence analysis7
    Transmembranei8 – 28Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
    Topological domaini29 – 374LumenalSequence analysisAdd BLAST346

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Organism-specific databases

    DisGeNETi10610
    OpenTargetsiENSG00000070731
    PharmGKBiPA35769

    Polymorphism and mutation databases

    BioMutaiST6GALNAC2
    DMDMi21759448

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001492721 – 374Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2Add BLAST374

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Disulfide bondi66 ↔ 148Combined sources1 Publication
    Glycosylationi85N-linked (GlcNAc...) asparagineCombined sources1 Publication1
    Glycosylationi130N-linked (GlcNAc...) asparagineCombined sources1 Publication1
    Disulfide bondi151 ↔ 317Combined sources1 Publication
    Glycosylationi161N-linked (GlcNAc...) asparagineCombined sources1 Publication1

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    EPDiQ9UJ37
    MaxQBiQ9UJ37
    PaxDbiQ9UJ37
    PeptideAtlasiQ9UJ37
    PRIDEiQ9UJ37
    ProteomicsDBi84582

    PTM databases

    iPTMnetiQ9UJ37
    PhosphoSitePlusiQ9UJ37

    Expressioni

    Tissue specificityi

    Expressed in skeletal muscle, heart, kidney, placenta, lung and leukocytes.1 Publication

    Gene expression databases

    BgeeiENSG00000070731
    CleanExiHS_ST6GALNAC2
    ExpressionAtlasiQ9UJ37 baseline and differential
    GenevisibleiQ9UJ37 HS

    Organism-specific databases

    HPAiHPA048849

    Interactioni

    Protein-protein interaction databases

    BioGridi115856, 1 interactor
    IntActiQ9UJ37, 1 interactor
    MINTiQ9UJ37
    STRINGi9606.ENSP00000225276

    Structurei

    Secondary structure

    1374
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi70 – 76Combined sources7
    Helixi78 – 81Combined sources4
    Helixi94 – 96Combined sources3
    Helixi99 – 105Combined sources7
    Helixi110 – 112Combined sources3
    Helixi119 – 128Combined sources10
    Helixi132 – 135Combined sources4
    Beta strandi150 – 154Combined sources5
    Helixi158 – 160Combined sources3
    Turni161 – 163Combined sources3
    Helixi166 – 171Combined sources6
    Beta strandi172 – 180Combined sources9
    Turni184 – 186Combined sources3
    Helixi187 – 190Combined sources4
    Beta strandi195 – 199Combined sources5
    Helixi201 – 210Combined sources10
    Turni212 – 215Combined sources4
    Beta strandi226 – 229Combined sources4
    Helixi234 – 245Combined sources12
    Turni253 – 256Combined sources4
    Helixi259 – 263Combined sources5
    Turni269 – 271Combined sources3
    Beta strandi272 – 275Combined sources4
    Helixi277 – 286Combined sources10
    Helixi305 – 316Combined sources12
    Beta strandi318 – 324Combined sources7
    Helixi328 – 332Combined sources5
    Beta strandi339 – 341Combined sources3
    Helixi353 – 365Combined sources13

    3D structure databases

    ProteinModelPortaliQ9UJ37
    SMRiQ9UJ37
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyltransferase 29 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiKOG2692 Eukaryota
    ENOG410XT8P LUCA
    GeneTreeiENSGT00760000119095
    HOGENOMiHOG000231097
    HOVERGENiHBG056467
    InParanoidiQ9UJ37
    KOiK06616
    OMAiDKGDRPH
    OrthoDBiEOG091G09FL
    PhylomeDBiQ9UJ37
    TreeFamiTF354325

    Family and domain databases

    Gene3Di3.90.1480.20, 1 hit
    InterProiView protein in InterPro
    IPR001675 Glyco_trans_29
    IPR038578 GT29-like_sf
    IPR012163 Sialyl_trans
    PfamiView protein in Pfam
    PF00777 Glyco_transf_29, 1 hit
    PIRSFiPIRSF005557 Sialyl_trans, 1 hit

    Sequencei

    Sequence statusi: Complete.

    Q9UJ37-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MGLPRGSFFW LLLLLTAACS GLLFALYFSA VQRYPGPAAG ARDTTSFEAF
    60 70 80 90 100
    FQSKASNSWT GKGQACRHLL HLAIQRHPHF RGLFNLSIPV LLWGDLFTPA
    110 120 130 140 150
    LWDRLSQHKA PYGWRGLSHQ VIASTLSLLN GSESAKLFAP PRDTPPKCIR
    160 170 180 190 200
    CAVVGNGGIL NGSRQGPNID AHDYVFRLNG AVIKGFERDV GTKTSFYGFT
    210 220 230 240 250
    VNTMKNSLVS YWNLGFTSVP QGQDLQYIFI PSDIRDYVML RSAILGVPVP
    260 270 280 290 300
    EGLDKGDRPH AYFGPEASAS KFKLLHPDFI SYLTERFLKS KLINTHFGDL
    310 320 330 340 350
    YMPSTGALML LTALHTCDQV SAYGFITSNY WKFSDHYFER KMKPLIFYAN
    360 370
    HDLSLEAALW RDLHKAGILQ LYQR
    Length:374
    Mass (Da):41,939
    Last modified:May 1, 2000 - v1
    Checksum:iE0BD439E4C6BB427
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti11L → V in AAA52228 (Ref. 2) Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ251053 mRNA Translation: CAB61434.1
    U14550 mRNA Translation: AAA52228.1
    BT019972 mRNA Translation: AAV38775.1
    BC040455 mRNA Translation: AAH40455.1
    CCDSiCCDS11747.1
    RefSeqiNP_006447.2, NM_006456.2
    UniGeneiHs.592105

    Genome annotation databases

    EnsembliENST00000225276; ENSP00000225276; ENSG00000070731
    GeneIDi10610
    KEGGihsa:10610
    UCSCiuc002jsg.5 human

    Similar proteinsi

    Entry informationi

    Entry nameiSIA7B_HUMAN
    AccessioniPrimary (citable) accession number: Q9UJ37
    Secondary accession number(s): Q12971
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 11, 2002
    Last sequence update: May 1, 2000
    Last modified: July 18, 2018
    This is version 144 of the entry and version 1 of the sequence. See 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

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