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Q9Y4C5

- CHST2_HUMAN

UniProt

Q9Y4C5 - CHST2_HUMAN

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Protein
Carbohydrate sulfotransferase 2
Gene
CHST2, GN6ST
Organism
Homo sapiens (Human)
Status
Reviewed - 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-GlcNAc

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei152 – 1521Not glycosylated

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi173 – 1797PAPS Inferred
Nucleotide bindingi332 – 3409PAPS Inferred

GO - Molecular functioni

  1. N-acetylglucosamine 6-O-sulfotransferase activity Source: UniProtKB
  2. sulfotransferase activity Source: ProtInc

GO - Biological processi

  1. N-acetylglucosamine metabolic process Source: UniProtKB
  2. carbohydrate metabolic process Source: Reactome
  3. glycosaminoglycan metabolic process Source: Reactome
  4. inflammatory response Source: ProtInc
  5. keratan sulfate biosynthetic process Source: Reactome
  6. keratan sulfate metabolic process Source: Reactome
  7. multicellular organismal development Source: ProtInc
  8. small molecule metabolic process Source: Reactome
  9. sulfur compound metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Carbohydrate metabolism, Inflammatory response

Enzyme and pathway databases

ReactomeiREACT_121120. 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
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:1970. CHST2.

Subcellular locationi

Golgi apparatustrans-Golgi network membrane; Single-pass type II membrane protein 2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5454Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei55 – 7521Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini76 – 530455Lumenal Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. Golgi membrane Source: Reactome
  2. integral component of membrane Source: UniProtKB-KW
  3. intrinsic component of Golgi membrane Source: UniProtKB
  4. trans-Golgi network Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi59 – 591C → S: Does not affect homodimerization. Abolishes homodimerization but not enzyme activity; when associated with S-39. 1 Publication
Mutagenesisi86 – 861C → S: Induces migration in both homodimeric and monomeric forms. Abolishes homodimerization but not enzyme activity; when associated with S-12. 1 Publication
Mutagenesisi174 – 1741R → A: Induces a strong decrease in enzyme activity. 1 Publication
Mutagenesisi296 – 2961R → A: Induces a strong decrease in enzyme activity. 1 Publication
Mutagenesisi304 – 3041K → A: Loss of function. 1 Publication
Mutagenesisi332 – 3321R → A: Loss of function. 1 Publication
Mutagenesisi341 – 3411R → A: Induces a strong decrease in enzyme activity. 1 Publication
Mutagenesisi457 – 4571N → A: Reduced localization in the Golgi. 1 Publication
Mutagenesisi475 – 4751N → A: Unable to sulfate the sialyl Lewis X tetrasaccharide. 1 Publication
Mutagenesisi518 – 5181K → A: Has weak or no effect. 1 Publication
Mutagenesisi519 – 5191D → A: Has weak or no effect. 1 Publication
Mutagenesisi520 – 5201L → A: Has weak or no effect. 1 Publication
Mutagenesisi521 – 5211S → A: No effect. 1 Publication
Mutagenesisi522 – 5221K → A: No effect. 1 Publication
Mutagenesisi523 – 5231T → A: Has weak or no effect. 1 Publication
Mutagenesisi524 – 5241L → A or T: Induces a strong decrease in enzyme activity. 1 Publication
Mutagenesisi525 – 5251L → A: Induces a strong decrease in enzyme activity. 1 Publication
Mutagenesisi525 – 5251L → T: Has weak or no effect. 1 Publication
Mutagenesisi526 – 5261R → A: Has weak or no effect. 1 Publication
Mutagenesisi527 – 5271K → A: No effect. 1 Publication
Mutagenesisi528 – 5281P → A: Has weak or no effect. 1 Publication
Mutagenesisi529 – 5291R → A: No effect. 1 Publication
Mutagenesisi530 – 5301L → A or T: Induces a strong decrease in enzyme activity. 1 Publication

Organism-specific databases

PharmGKBiPA26502.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 530530Carbohydrate sulfotransferase 2
PRO_0000085186Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi243 – 2431N-linked (GlcNAc...)1 Publication
Glycosylationi457 – 4571N-linked (GlcNAc...)1 Publication
Glycosylationi475 – 4751N-linked (GlcNAc...)1 Publication

Post-translational modificationi

Glycosylation at Asn-475 is required for catalytic activity.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9Y4C5.
PRIDEiQ9Y4C5.

PTM databases

PhosphoSiteiQ9Y4C5.

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

BgeeiQ9Y4C5.
CleanExiHS_CHST2.
GenevestigatoriQ9Y4C5.

Organism-specific databases

HPAiHPA013313.

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. Positions 417-501.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG67451.
HOGENOMiHOG000261614.
HOVERGENiHBG050949.
InParanoidiQ9Y4C5.
KOiK04745.
OMAiMGGPADY.
OrthoDBiEOG7RZ5S0.
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. Align

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

MSRSPQRALP PGALPRLLQA APAAAPRALL PQWPRRPGRR WPASPLGMKV    50
FRRKALVLCA GYALLLVLTM LNLLDYKWHK EPLQQCNPDG PLGAAAGAAG 100
GSWGRPGPPP AGPPRAHARL DLRTPYRPPA AAVGAAPAAA AGMAGVAAPP 150
GNGTRGTGGV GDKRQLVYVF TTWRSGSSFF GELFNQNPEV FFLYEPVWHV 200
WQKLYPGDAV SLQGAARDML SALYRCDLSV FQLYSPAGSG GRNLTTLGIF 250
GAATNKVVCS SPLCPAYRKE VVGLVDDRVC KKCPPQRLAR FEEECRKYRT 300
LVIKGVRVFD VAVLAPLLRD PALDLKVIHL VRDPRAVASS RIRSRHGLIR 350
ESLQVVRSRD PRAHRMPFLE AAGHKLGAKK EGVGGPADYH ALGAMEVICN 400
SMAKTLQTAL QPPDWLQGHY LVVRYEDLVG DPVKTLRRVY DFVGLLVSPE 450
MEQFALNMTS GSGSSSKPFV VSARNATQAA NAWRTALTFQ QIKQVEEFCY 500
QPMAVLGYER VNSPEEVKDL SKTLLRKPRL 530
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 BAA34265.2 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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4747Missing in isoform 2.
VSP_018887Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81A → V in BAB16887. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
UCSCiuc003evm.3. human. [Q9Y4C5-1]

Polymorphism databases

DMDMi61212252.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS3129.1. [Q9Y4C5-1 ]
RefSeqi NP_004258.2. NM_004267.4. [Q9Y4C5-1 ]
UniGenei Hs.529249.
Hs.8786.

3D structure databases

ProteinModelPortali Q9Y4C5.
SMRi Q9Y4C5. Positions 417-501.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000307911.

PTM databases

PhosphoSitei Q9Y4C5.

Polymorphism databases

DMDMi 61212252.

Proteomic databases

PaxDbi Q9Y4C5.
PRIDEi Q9Y4C5.

Protocols and materials databases

DNASUi 9435.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000309575 ; ENSP00000307911 ; ENSG00000175040 . [Q9Y4C5-1 ]
GeneIDi 9435.
KEGGi hsa:9435.
UCSCi uc003evm.3. human. [Q9Y4C5-1 ]

Organism-specific databases

CTDi 9435.
GeneCardsi GC03P142838.
HGNCi HGNC:1970. CHST2.
HPAi HPA013313.
MIMi 603798. gene.
neXtProti NX_Q9Y4C5.
PharmGKBi PA26502.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG67451.
HOGENOMi HOG000261614.
HOVERGENi HBG050949.
InParanoidi Q9Y4C5.
KOi K04745.
OMAi MGGPADY.
OrthoDBi EOG7RZ5S0.
PhylomeDBi Q9Y4C5.
TreeFami TF342871.

Enzyme and pathway databases

Reactomei REACT_121120. Keratan sulfate biosynthesis.
SABIO-RK Q9Y4C5.

Miscellaneous databases

ChiTaRSi CHST2. human.
GeneWikii CHST2.
GenomeRNAii 9435.
NextBioi 35332.
PROi Q9Y4C5.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y4C5.
CleanExi HS_CHST2.
Genevestigatori Q9Y4C5.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi IPR016469. Carbohydrate_sulfotransferase.
IPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view ]
Pfami PF00685. Sulfotransfer_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF005883. Carbohydrate_sulfotransferase. 1 hit.
SUPFAMi SSF52540. SSF52540. 3 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

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: September 3, 2014
This is version 107 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

External Data

Dasty 3

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