Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9Y4C5 (CHST2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:CHST2
Synonyms:GN6ST
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length530 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4

Subunit structure

Homodimer; disulfide-linked. Homodimerization is not essential for enzyme activity. Ref.12 Ref.14

Subcellular location

Golgi apparatustrans-Golgi network membrane; Single-pass type II membrane protein Ref.10 Ref.14.

Tissue specificity

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. Ref.1 Ref.3 Ref.7

Induction

Up-regulated upon cytokine activation. Ref.7

Post-translational modification

Glycosylation at Asn-475 is required for catalytic activity.

Sequence similarities

Belongs to the sulfotransferase 1 family. Gal/GlcNAc/GalNAc subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=3.9 µM for PAPS Ref.8

KM=1.4 mM for BetaBnO-GlcNAc

Sequence caution

The sequence BAA34265.2 differs from that shown. Reason: Erroneous initiation.

The sequence BAB16886.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAB16887.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Inflammatory response
   Cellular componentGolgi apparatus
Membrane
   Coding sequence diversityAlternative initiation
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   Molecular functionTransferase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processN-acetylglucosamine metabolic process

Inferred from direct assay Ref.1. Source: UniProtKB

carbohydrate metabolic process

Traceable author statement. Source: Reactome

glycosaminoglycan metabolic process

Traceable author statement. Source: Reactome

inflammatory response

Traceable author statement Ref.3. Source: ProtInc

keratan sulfate biosynthetic process

Traceable author statement. Source: Reactome

keratan sulfate metabolic process

Traceable author statement. Source: Reactome

multicellular organismal development

Traceable author statement Ref.1. Source: ProtInc

small molecule metabolic process

Traceable author statement. Source: Reactome

sulfur compound metabolic process

Inferred from direct assay Ref.1. Source: UniProtKB

   Cellular_componentGolgi membrane

Traceable author statement. Source: Reactome

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

intrinsic component of Golgi membrane

Non-traceable author statement Ref.10. Source: UniProtKB

trans-Golgi network

Inferred from direct assay Ref.10. Source: UniProtKB

   Molecular_functionN-acetylglucosamine 6-O-sulfotransferase activity

Inferred from direct assay Ref.4Ref.1. Source: UniProtKB

sulfotransferase activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform 1 (identifier: Q9Y4C5-1)

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.
Isoform 2 (identifier: Q9Y4C5-2)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 530530Carbohydrate sulfotransferase 2
PRO_0000085186

Regions

Topological domain1 – 5454Cytoplasmic Potential
Transmembrane55 – 7521Helical; Signal-anchor for type II membrane protein; Potential
Topological domain76 – 530455Lumenal Potential
Nucleotide binding173 – 1797PAPS Probable
Nucleotide binding332 – 3409PAPS Probable

Sites

Site1521Not glycosylated

Amino acid modifications

Glycosylation2431N-linked (GlcNAc...) Ref.13
Glycosylation4571N-linked (GlcNAc...) Ref.13
Glycosylation4751N-linked (GlcNAc...) Ref.13

Natural variations

Alternative sequence1 – 4747Missing in isoform 2.
VSP_018887

Experimental info

Mutagenesis591C → S: Does not affect homodimerization. Abolishes homodimerization but not enzyme activity; when associated with S-39. Ref.12
Mutagenesis861C → S: Induces migration in both homodimeric and monomeric forms. Abolishes homodimerization but not enzyme activity; when associated with S-12. Ref.12
Mutagenesis1741R → A: Induces a strong decrease in enzyme activity. Ref.8
Mutagenesis2961R → A: Induces a strong decrease in enzyme activity. Ref.8
Mutagenesis3041K → A: Loss of function. Ref.8
Mutagenesis3321R → A: Loss of function. Ref.8
Mutagenesis3411R → A: Induces a strong decrease in enzyme activity. Ref.8
Mutagenesis4571N → A: Reduced localization in the Golgi. Ref.13
Mutagenesis4751N → A: Unable to sulfate the sialyl Lewis X tetrasaccharide. Ref.13
Mutagenesis5181K → A: Has weak or no effect. Ref.11
Mutagenesis5191D → A: Has weak or no effect. Ref.11
Mutagenesis5201L → A: Has weak or no effect. Ref.11
Mutagenesis5211S → A: No effect. Ref.11
Mutagenesis5221K → A: No effect. Ref.11
Mutagenesis5231T → A: Has weak or no effect. Ref.11
Mutagenesis5241L → A or T: Induces a strong decrease in enzyme activity. Ref.11
Mutagenesis5251L → A: Induces a strong decrease in enzyme activity. Ref.11
Mutagenesis5251L → T: Has weak or no effect. Ref.11
Mutagenesis5261R → A: Has weak or no effect. Ref.11
Mutagenesis5271K → A: No effect. Ref.11
Mutagenesis5281P → A: Has weak or no effect. Ref.11
Mutagenesis5291R → A: No effect. Ref.11
Mutagenesis5301L → A or T: Induces a strong decrease in enzyme activity. Ref.11
Sequence conflict81A → V in BAB16887. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2003. Version 2.
Checksum: A82CA227B9D5651B

FASTA53057,857
        10         20         30         40         50         60 
MSRSPQRALP PGALPRLLQA APAAAPRALL PQWPRRPGRR WPASPLGMKV FRRKALVLCA 

        70         80         90        100        110        120 
GYALLLVLTM LNLLDYKWHK EPLQQCNPDG PLGAAAGAAG GSWGRPGPPP AGPPRAHARL 

       130        140        150        160        170        180 
DLRTPYRPPA AAVGAAPAAA AGMAGVAAPP GNGTRGTGGV GDKRQLVYVF TTWRSGSSFF 

       190        200        210        220        230        240 
GELFNQNPEV FFLYEPVWHV WQKLYPGDAV SLQGAARDML SALYRCDLSV FQLYSPAGSG 

       250        260        270        280        290        300 
GRNLTTLGIF GAATNKVVCS SPLCPAYRKE VVGLVDDRVC KKCPPQRLAR FEEECRKYRT 

       310        320        330        340        350        360 
LVIKGVRVFD VAVLAPLLRD PALDLKVIHL VRDPRAVASS RIRSRHGLIR ESLQVVRSRD 

       370        380        390        400        410        420 
PRAHRMPFLE AAGHKLGAKK EGVGGPADYH ALGAMEVICN SMAKTLQTAL QPPDWLQGHY 

       430        440        450        460        470        480 
LVVRYEDLVG DPVKTLRRVY DFVGLLVSPE MEQFALNMTS GSGSSSKPFV VSARNATQAA 

       490        500        510        520        530 
NAWRTALTFQ QIKQVEEFCY QPMAVLGYER VNSPEEVKDL SKTLLRKPRL 

« Hide

Isoform 2 [UniParc].

Checksum: E27797D44931BA18
Show »

FASTA48352,787

References

« Hide 'large scale' references
[1]"Human N-acetylglucosamine-6-O-sulfotransferase involved in the biosynthesis of 6-sulfo sialyl Lewis X: molecular cloning, chromosomal mapping, and expression in various organs and tumor cells."
Uchimura K., Muramatsu H., Kaname T., Ogawa H., Yamakawa T., Fan Q.-W., Mitsuoka C., Kannagi R., Habuchi O., Yokoyama I., Yamamura K., Ozaki T., Nakagawara A., Kadomatsu K., Muramatsu T.
J. Biochem. 124:670-678(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, ALTERNATIVE INITIATION, TISSUE SPECIFICITY.
Tissue: Brain.
[2]Uchimura K., Muramatsu H., Muramatsu T.
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"CHST1 and CHST2 sulfotransferases expressed by human vascular endothelial cells: cDNA cloning, expression, and chromosomal localization."
Li X., Tedder T.F.
Genomics 55:345-347(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Umbilical vein endothelial cell.
[4]"Functional expression and genomic structure of human N-acetylglucosamine-6-O-sulfotransferase that transfers sulfate to b-N-acetylglucosamine at the nonreducing end of an N-acetyllactosamine sequence."
Sakaguchi H., Kitagawa H., Sugahara K.
Biochim. Biophys. Acta 1523:269-276(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION.
Tissue: Placenta.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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].
Tissue: Brain.
[7]"CHST1 and CHST2 sulfotransferase expression by vascular endothelial cells regulates shear-resistant leukocyte rolling via L-selectin."
Li X., Tu L., Murphy P.G., Kadono T., Steeber D.A., Tedder T.F.
J. Leukoc. Biol. 69:565-574(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INDUCTION.
[8]"Characterization and mutagenesis of Gal/GlcNAc-6-O-sulfotransferases."
Grunwell J.R., Rath V.L., Rasmussen J., Cabrilo Z., Bertozzi C.R.
Biochemistry 41:15590-15600(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-174; ARG-296; LYS-304; ARG-332 AND ARG-341.
[9]"Specificities of N-acetylglucosamine-6-O-sulfotransferases in relation to L-selectin ligand synthesis and tumor-associated enzyme expression."
Uchimura K., El-Fasakhany F.M., Hori M., Hemmerich S., Blink S.E., Kansas G.S., Kanamori A., Kumamoto K., Kannagi R., Muramatsu T.
J. Biol. Chem. 277:3979-3984(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBSTRATE SPECIFICITY.
[10]"Golgi localization of carbohydrate sulfotransferases is a determinant of L-selectin ligand biosynthesis."
de Graffenried C.L., Bertozzi C.R.
J. Biol. Chem. 278:40282-40295(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[11]"Role of the carboxyl-terminal region in the activity of N-acetylglucosamine 6-o-sulfotransferase-1."
Chen L., Ichihara-Tanaka K., Muramatsu T.
J. Biochem. 136:659-664(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF LYS-518; ASP-519; LEU-520; SER-521; LYS-522; THR-523; LEU-524; LEU-525; ARG-526; LYS-527; PRO-528; ARG-529 AND LEU-530.
[12]"The stem region of the sulfotransferase GlcNAc6ST-1 is a determinant of substrate specificity."
de Graffenried C.L., Bertozzi C.R.
J. Biol. Chem. 279:40035-40043(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, MUTAGENESIS OF CYS-59 AND CYS-86.
[13]"Effects of N-glycosylation on the activity and localization of GlcNAc-6-sulfotransferase 1."
Desko M.M., Gross D.A., Kohler J.J.
Glycobiology 19:1068-1077(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-243; ASN-457 AND ASN-475, ABSENCE OF GLYCOSYLATION AT ASN-152, MUTAGENESIS OF ASN-457 AND ASN-475.
[14]"Expression of long-form N-acetylglucosamine-6-O-sulfotransferase 1 in human high endothelial venules."
Fujiwara M., Kobayashi M., Hoshino H., Uchimura K., Nakada T., Masumoto J., Sakai Y., Fukuda M., Nakayama J.
J. Histochem. Cytochem. 60:397-407(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, SUBUNIT, ALTERNATIVE INITIATION.
+Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS3129.1. [Q9Y4C5-1]
RefSeqNP_004258.2. NM_004267.4. [Q9Y4C5-1]
UniGeneHs.529249.
Hs.8786.

3D structure databases

ProteinModelPortalQ9Y4C5.
SMRQ9Y4C5. Positions 417-501.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000307911.

PTM databases

PhosphoSiteQ9Y4C5.

Polymorphism databases

DMDM61212252.

Proteomic databases

PaxDbQ9Y4C5.
PRIDEQ9Y4C5.

Protocols and materials databases

DNASU9435.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000309575; ENSP00000307911; ENSG00000175040. [Q9Y4C5-1]
GeneID9435.
KEGGhsa:9435.
UCSCuc003evm.3. human. [Q9Y4C5-1]

Organism-specific databases

CTD9435.
GeneCardsGC03P142838.
HGNCHGNC:1970. CHST2.
HPAHPA013313.
MIM603798. gene.
neXtProtNX_Q9Y4C5.
PharmGKBPA26502.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG67451.
HOGENOMHOG000261614.
HOVERGENHBG050949.
InParanoidQ9Y4C5.
KOK04745.
OMAMGGPADY.
OrthoDBEOG7RZ5S0.
PhylomeDBQ9Y4C5.
TreeFamTF342871.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
SABIO-RKQ9Y4C5.

Gene expression databases

BgeeQ9Y4C5.
CleanExHS_CHST2.
GenevestigatorQ9Y4C5.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR016469. Carbohydrate_sulfotransferase.
IPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view]
PfamPF00685. Sulfotransfer_1. 1 hit.
[Graphical view]
PIRSFPIRSF005883. Carbohydrate_sulfotransferase. 1 hit.
SUPFAMSSF52540. SSF52540. 3 hits.
ProtoNetSearch...

Other

ChiTaRSCHST2. human.
GeneWikiCHST2.
GenomeRNAi9435.
NextBio35332.
PROQ9Y4C5.
SOURCESearch...

Entry information

Entry nameCHST2_HUMAN
AccessionPrimary (citable) accession number: Q9Y4C5
Secondary accession number(s): D3DNG5 expand/collapse secondary AC list , Q2M370, Q9GZN5, Q9UED5, Q9Y6F2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM