Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Carbohydrate sulfotransferase 2

Gene

CHST2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine (GlcNAc) residues within keratan-like structures on N-linked glycans and within mucin-associated glycans that can ultimately serve as SELL ligands. SELL ligands are present in high endothelial cells (HEVs) and play a central role in lymphocyte homing at sites of inflammation. Participates in biosynthesis of the SELL ligand sialyl 6-sulfo Lewis X and in lymphocyte homing to Peyer patches. Has no activity toward O-linked sugars. Its substrate specificity may be influenced by its subcellular location. Sulfates GlcNAc residues at terminal, non-reducing ends of oligosaccharide chains.1 Publication

Kineticsi

  1. KM=3.9 µM for PAPS1 Publication
  2. KM=1.4 mM for BetaBnO-GlcNAc1 Publication

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi173 – 179PAPSCurated7
    Nucleotide bindingi332 – 340PAPSCurated9

    GO - Molecular functioni

    • N-acetylglucosamine 6-O-sulfotransferase activity Source: UniProtKB
    • sulfotransferase activity Source: ProtInc

    GO - Biological processi

    • carbohydrate metabolic process Source: UniProtKB-KW
    • inflammatory response Source: ProtInc
    • keratan sulfate biosynthetic process Source: Reactome
    • multicellular organism development Source: ProtInc
    • N-acetylglucosamine metabolic process Source: UniProtKB
    • sulfur compound metabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Carbohydrate metabolism, Inflammatory response

    Enzyme and pathway databases

    BioCyciZFISH:ENSG00000175040-MONOMER.
    ReactomeiR-HSA-2022854. Keratan sulfate biosynthesis.
    SABIO-RKQ9Y4C5.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carbohydrate sulfotransferase 2 (EC:2.8.2.-)
    Alternative name(s):
    Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 2
    Short name:
    GST-2
    N-acetylglucosamine 6-O-sulfotransferase 1
    Short name:
    GlcNAc6ST-1
    Short name:
    Gn6ST-1
    Gene namesi
    Name:CHST2
    Synonyms:GN6ST
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:1970. CHST2.

    Subcellular locationi

    Topology

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Topological domaini1 – 54CytoplasmicSequence analysisAdd BLAST54
    Transmembranei55 – 75Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
    Topological domaini76 – 530LumenalSequence analysisAdd BLAST455

    GO - Cellular componenti

    • Golgi membrane Source: Reactome
    • integral component of membrane Source: GO_Central
    • intrinsic component of Golgi membrane Source: UniProtKB
    • trans-Golgi network Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi59C → S: Does not affect homodimerization. Abolishes homodimerization but not enzyme activity; when associated with S-39. 1 Publication1
    Mutagenesisi86C → S: Induces migration in both homodimeric and monomeric forms. Abolishes homodimerization but not enzyme activity; when associated with S-12. 1 Publication1
    Mutagenesisi174R → A: Induces a strong decrease in enzyme activity. 1 Publication1
    Mutagenesisi296R → A: Induces a strong decrease in enzyme activity. 1 Publication1
    Mutagenesisi304K → A: Loss of function. 1 Publication1
    Mutagenesisi332R → A: Loss of function. 1 Publication1
    Mutagenesisi341R → A: Induces a strong decrease in enzyme activity. 1 Publication1
    Mutagenesisi457N → A: Reduced localization in the Golgi. 1 Publication1
    Mutagenesisi475N → A: Unable to sulfate the sialyl Lewis X tetrasaccharide. 1 Publication1
    Mutagenesisi518K → A: Has weak or no effect. 1 Publication1
    Mutagenesisi519D → A: Has weak or no effect. 1 Publication1
    Mutagenesisi520L → A: Has weak or no effect. 1 Publication1
    Mutagenesisi521S → A: No effect. 1 Publication1
    Mutagenesisi522K → A: No effect. 1 Publication1
    Mutagenesisi523T → A: Has weak or no effect. 1 Publication1
    Mutagenesisi524L → A or T: Induces a strong decrease in enzyme activity. 1 Publication1
    Mutagenesisi525L → A: Induces a strong decrease in enzyme activity. 1 Publication1
    Mutagenesisi525L → T: Has weak or no effect. 1 Publication1
    Mutagenesisi526R → A: Has weak or no effect. 1 Publication1
    Mutagenesisi527K → A: No effect. 1 Publication1
    Mutagenesisi528P → A: Has weak or no effect. 1 Publication1
    Mutagenesisi529R → A: No effect. 1 Publication1
    Mutagenesisi530L → A or T: Induces a strong decrease in enzyme activity. 1 Publication1

    Organism-specific databases

    DisGeNETi9435.
    OpenTargetsiENSG00000175040.
    PharmGKBiPA26502.

    Polymorphism and mutation databases

    BioMutaiCHST2.
    DMDMi61212252.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000851861 – 530Carbohydrate sulfotransferase 2Add BLAST530

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Glycosylationi243N-linked (GlcNAc...)1 Publication1
    Glycosylationi457N-linked (GlcNAc...)1 Publication1
    Glycosylationi475N-linked (GlcNAc...)1 Publication1

    Post-translational modificationi

    Glycosylation at Asn-475 is required for catalytic activity.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sitei152Not glycosylated1

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ9Y4C5.
    PeptideAtlasiQ9Y4C5.
    PRIDEiQ9Y4C5.

    PTM databases

    iPTMnetiQ9Y4C5.
    PhosphoSitePlusiQ9Y4C5.

    Expressioni

    Tissue specificityi

    Widely expressed. Highly expressed in bone marrow, peripheral blood leukocytes, spleen, brain, spinal cord, ovary and placenta. Expressed by high endothelial cells (HEVs) and leukocytes.3 Publications

    Inductioni

    Up-regulated upon cytokine activation.1 Publication

    Gene expression databases

    BgeeiENSG00000175040.
    CleanExiHS_CHST2.
    ExpressionAtlasiQ9Y4C5. baseline and differential.
    GenevisibleiQ9Y4C5. HS.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked. Homodimerization is not essential for enzyme activity.2 Publications

    Protein-protein interaction databases

    STRINGi9606.ENSP00000307911.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y4C5.
    SMRiQ9Y4C5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiENOG410IIA6. Eukaryota.
    ENOG4111DKG. LUCA.
    GeneTreeiENSGT00530000062902.
    HOGENOMiHOG000261614.
    HOVERGENiHBG050949.
    InParanoidiQ9Y4C5.
    KOiK04745.
    OMAiMGGPADY.
    OrthoDBiEOG091G0V3Y.
    PhylomeDBiQ9Y4C5.
    TreeFamiTF342871.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR016469. Carbohydrate_sulfotransferase.
    IPR027417. P-loop_NTPase.
    IPR000863. Sulfotransferase_dom.
    [Graphical view]
    PfamiPF00685. Sulfotransfer_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005883. Carbohydrate_sulfotransferase. 1 hit.
    SUPFAMiSSF52540. SSF52540. 3 hits.

    Sequences (2)i

    Sequence statusi: Complete.

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

    Isoform 1 (identifier: Q9Y4C5-1) [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
    MSRSPQRALP PGALPRLLQA APAAAPRALL PQWPRRPGRR WPASPLGMKV
    60 70 80 90 100
    FRRKALVLCA GYALLLVLTM LNLLDYKWHK EPLQQCNPDG PLGAAAGAAG
    110 120 130 140 150
    GSWGRPGPPP AGPPRAHARL DLRTPYRPPA AAVGAAPAAA AGMAGVAAPP
    160 170 180 190 200
    GNGTRGTGGV GDKRQLVYVF TTWRSGSSFF GELFNQNPEV FFLYEPVWHV
    210 220 230 240 250
    WQKLYPGDAV SLQGAARDML SALYRCDLSV FQLYSPAGSG GRNLTTLGIF
    260 270 280 290 300
    GAATNKVVCS SPLCPAYRKE VVGLVDDRVC KKCPPQRLAR FEEECRKYRT
    310 320 330 340 350
    LVIKGVRVFD VAVLAPLLRD PALDLKVIHL VRDPRAVASS RIRSRHGLIR
    360 370 380 390 400
    ESLQVVRSRD PRAHRMPFLE AAGHKLGAKK EGVGGPADYH ALGAMEVICN
    410 420 430 440 450
    SMAKTLQTAL QPPDWLQGHY LVVRYEDLVG DPVKTLRRVY DFVGLLVSPE
    460 470 480 490 500
    MEQFALNMTS GSGSSSKPFV VSARNATQAA NAWRTALTFQ QIKQVEEFCY
    510 520 530
    QPMAVLGYER VNSPEEVKDL SKTLLRKPRL
    Length:530
    Mass (Da):57,857
    Last modified:March 1, 2003 - v2
    Checksum:iA82CA227B9D5651B
    GO
    Isoform 2 (identifier: Q9Y4C5-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-47: Missing.

    Note: Higher levels of expression compared to isoform 1 when expressed in HeLa cells. Exhibits similar intracellular GlcNAc-6-O-sulfation activity.
    Show »
    Length:483
    Mass (Da):52,787
    Checksum:iE27797D44931BA18
    GO

    Sequence cautioni

    The sequence BAA34265 differs from that shown. Reason: Erroneous initiation.Curated
    The sequence BAB16886 differs from that shown. Reason: Erroneous initiation.Curated
    The sequence BAB16887 differs from that shown. Reason: Erroneous initiation.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti8A → V in BAB16887 (PubMed:11042394).Curated1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_0188871 – 47Missing in isoform 2. CuratedAdd BLAST47

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB014679 mRNA. Translation: BAA34265.2. Different initiation.
    AB014680 mRNA. Translation: BAA34266.2.
    AF083066 mRNA. Translation: AAD20981.1.
    AB021124 mRNA. Translation: BAB16886.1. Different initiation.
    AB021125 Genomic DNA. Translation: BAB16887.1. Different initiation.
    CH471052 Genomic DNA. Translation: EAW78952.1.
    CH471052 Genomic DNA. Translation: EAW78953.1.
    BC105010 mRNA. Translation: AAI05011.1.
    BC105012 mRNA. Translation: AAI05013.1.
    CCDSiCCDS3129.1. [Q9Y4C5-1]
    RefSeqiNP_004258.2. NM_004267.4. [Q9Y4C5-1]
    UniGeneiHs.529249.
    Hs.8786.

    Genome annotation databases

    EnsembliENST00000309575; ENSP00000307911; ENSG00000175040. [Q9Y4C5-1]
    GeneIDi9435.
    KEGGihsa:9435.

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB014679 mRNA. Translation: BAA34265.2. Different initiation.
    AB014680 mRNA. Translation: BAA34266.2.
    AF083066 mRNA. Translation: AAD20981.1.
    AB021124 mRNA. Translation: BAB16886.1. Different initiation.
    AB021125 Genomic DNA. Translation: BAB16887.1. Different initiation.
    CH471052 Genomic DNA. Translation: EAW78952.1.
    CH471052 Genomic DNA. Translation: EAW78953.1.
    BC105010 mRNA. Translation: AAI05011.1.
    BC105012 mRNA. Translation: AAI05013.1.
    CCDSiCCDS3129.1. [Q9Y4C5-1]
    RefSeqiNP_004258.2. NM_004267.4. [Q9Y4C5-1]
    UniGeneiHs.529249.
    Hs.8786.

    3D structure databases

    ProteinModelPortaliQ9Y4C5.
    SMRiQ9Y4C5.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi9606.ENSP00000307911.

    PTM databases

    iPTMnetiQ9Y4C5.
    PhosphoSitePlusiQ9Y4C5.

    Polymorphism and mutation databases

    BioMutaiCHST2.
    DMDMi61212252.

    Proteomic databases

    PaxDbiQ9Y4C5.
    PeptideAtlasiQ9Y4C5.
    PRIDEiQ9Y4C5.

    Protocols and materials databases

    DNASUi9435.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000309575; ENSP00000307911; ENSG00000175040. [Q9Y4C5-1]
    GeneIDi9435.
    KEGGihsa:9435.

    Organism-specific databases

    CTDi9435.
    DisGeNETi9435.
    GeneCardsiCHST2.
    HGNCiHGNC:1970. CHST2.
    MIMi603798. gene.
    neXtProtiNX_Q9Y4C5.
    OpenTargetsiENSG00000175040.
    PharmGKBiPA26502.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiENOG410IIA6. Eukaryota.
    ENOG4111DKG. LUCA.
    GeneTreeiENSGT00530000062902.
    HOGENOMiHOG000261614.
    HOVERGENiHBG050949.
    InParanoidiQ9Y4C5.
    KOiK04745.
    OMAiMGGPADY.
    OrthoDBiEOG091G0V3Y.
    PhylomeDBiQ9Y4C5.
    TreeFamiTF342871.

    Enzyme and pathway databases

    BioCyciZFISH:ENSG00000175040-MONOMER.
    ReactomeiR-HSA-2022854. Keratan sulfate biosynthesis.
    SABIO-RKQ9Y4C5.

    Miscellaneous databases

    ChiTaRSiCHST2. human.
    GeneWikiiCHST2.
    GenomeRNAii9435.
    PROiQ9Y4C5.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000175040.
    CleanExiHS_CHST2.
    ExpressionAtlasiQ9Y4C5. baseline and differential.
    GenevisibleiQ9Y4C5. HS.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR016469. Carbohydrate_sulfotransferase.
    IPR027417. P-loop_NTPase.
    IPR000863. Sulfotransferase_dom.
    [Graphical view]
    PfamiPF00685. Sulfotransfer_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005883. Carbohydrate_sulfotransferase. 1 hit.
    SUPFAMiSSF52540. SSF52540. 3 hits.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiCHST2_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y4C5
    Secondary accession number(s): D3DNG5
    , Q2M370, Q9GZN5, Q9UED5, Q9Y6F2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 15, 2005
    Last sequence update: March 1, 2003
    Last modified: November 2, 2016
    This is version 125 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 3
      Human chromosome 3: 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. SIMILARITY comments
      Index of protein domains and families

    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 one 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.