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
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi173 – 1797PAPSBy similarity
Nucleotide bindingi332 – 3409PAPSBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Carbohydrate metabolism, Inflammatory response

Enzyme and pathway databases

ReactomeiREACT_346228. Keratan sulfate biosynthesis.

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:Gst2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1891160. Chst2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5454CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei55 – 7521Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini76 – 530455LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice are impaired in the elaboration of sialyl 6-sulfo Lewis X in HEV. Lymphocyte homing to peripheral lymph nodes, mesenteric lymph nodes, and Peyer patches are significantly reduced.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 530530Carbohydrate sulfotransferase 2PRO_0000085187Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ80WV3.
PaxDbiQ80WV3.
PRIDEiQ80WV3.

PTM databases

PhosphoSiteiQ80WV3.

Expressioni

Tissue specificityi

In brain, it is expressed in pyramidal cells in the CA3 subregion of the hippocampus, cerebellar nucleus and Purkinje cells.2 Publications

Gene expression databases

BgeeiQ80WV3.
CleanExiMM_CHST2.
ExpressionAtlasiQ80WV3. baseline and differential.
GenevisibleiQ80WV3. MM.

Interactioni

Subunit structurei

Homodimer; disulfide-linked. Homodimerization is not essential for enzyme activity (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000040775.

Structurei

3D structure databases

ProteinModelPortaliQ80WV3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG67451.
GeneTreeiENSGT00530000062902.
HOGENOMiHOG000261614.
HOVERGENiHBG050949.
InParanoidiQ80WV3.
KOiK04745.
OMAiMGGPADY.
OrthoDBiEOG7RZ5S0.
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.

Sequencei

Sequence statusi: Complete.

Q80WV3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRSSPRALP PGALPRPLPA APAAVQRALL PPWPRRAGRR WPASPLGMKV
60 70 80 90 100
FRRKALVLCA GYALLLVLTM LNLLDYKWHK EPLQQCNPDG PLGAAVGAAG
110 120 130 140 150
AGWGRPGSPP AAPPRAHSRM DPRTPYRPPA AGVGAVPAAA AGSAGAAASL
160 170 180 190 200
GNATRGTRGG 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 VAVLAPLLKD PALDLKVIHL VRDPRAVASS RIRSRHGLIR
360 370 380 390 400
ESLQVVRSRD PRAHRMPFLE AAGHKLGAKK EGMGGPADYH 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):57,828
Last modified:July 27, 2011 - v3
Checksum:i275363BF15440730
GO

Sequence cautioni

The sequence AAH51963.2 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAA32137.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAA32139.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAD16775.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti301 – 3011L → V in BAA32137 (PubMed:9712885).Curated
Sequence conflicti301 – 3011L → V in BAA32139 (PubMed:9712885).Curated
Sequence conflicti301 – 3011L → V in BAA32138 (PubMed:9712885).Curated
Sequence conflicti301 – 3011L → V in BAD16775 (PubMed:15175329).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB011451 mRNA. Translation: BAA32137.1. Different initiation.
AB011452 mRNA. Translation: BAA32138.1.
AB011452 mRNA. Translation: BAA32139.1. Different initiation.
AB125058 Genomic DNA. Translation: BAD16775.1. Different initiation.
AC144813 Genomic DNA. No translation available.
BC051963 mRNA. Translation: AAH51963.2. Different initiation.
CCDSiCCDS52888.1.
RefSeqiNP_061233.2. NM_018763.2.
UniGeneiMm.212446.

Genome annotation databases

EnsembliENSMUST00000036267; ENSMUSP00000040775; ENSMUSG00000033350.
GeneIDi54371.
KEGGimmu:54371.
UCSCiuc009raz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB011451 mRNA. Translation: BAA32137.1. Different initiation.
AB011452 mRNA. Translation: BAA32138.1.
AB011452 mRNA. Translation: BAA32139.1. Different initiation.
AB125058 Genomic DNA. Translation: BAD16775.1. Different initiation.
AC144813 Genomic DNA. No translation available.
BC051963 mRNA. Translation: AAH51963.2. Different initiation.
CCDSiCCDS52888.1.
RefSeqiNP_061233.2. NM_018763.2.
UniGeneiMm.212446.

3D structure databases

ProteinModelPortaliQ80WV3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000040775.

PTM databases

PhosphoSiteiQ80WV3.

Proteomic databases

MaxQBiQ80WV3.
PaxDbiQ80WV3.
PRIDEiQ80WV3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000036267; ENSMUSP00000040775; ENSMUSG00000033350.
GeneIDi54371.
KEGGimmu:54371.
UCSCiuc009raz.2. mouse.

Organism-specific databases

CTDi9435.
MGIiMGI:1891160. Chst2.

Phylogenomic databases

eggNOGiNOG67451.
GeneTreeiENSGT00530000062902.
HOGENOMiHOG000261614.
HOVERGENiHBG050949.
InParanoidiQ80WV3.
KOiK04745.
OMAiMGGPADY.
OrthoDBiEOG7RZ5S0.
TreeFamiTF342871.

Enzyme and pathway databases

ReactomeiREACT_346228. Keratan sulfate biosynthesis.

Miscellaneous databases

ChiTaRSiChst2. mouse.
NextBioi311174.
PROiQ80WV3.
SOURCEiSearch...

Gene expression databases

BgeeiQ80WV3.
CleanExiMM_CHST2.
ExpressionAtlasiQ80WV3. baseline and differential.
GenevisibleiQ80WV3. MM.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and characterization of an N-acetylglucosamine-6-O-sulfotransferase."
    Uchimura K., Muramatsu H., Kadomatsu K., Fan Q.-W., Kurosawa N., Mitsuoka C., Kannagi R., Habuchi O., Muramatsu T.
    J. Biol. Chem. 273:22577-22583(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Tissue: Embryo.
  2. "N-acetylglucosamine 6-O-sulfotransferase-1 regulates expression of L-selectin ligands and lymphocyte homing."
    Uchimura K., Kadomatsu K., El-Fasakhany F.M., Singer M.S., Izawa M., Kannagi R., Takeda N., Rosen S.D., Muramatsu T.
    J. Biol. Chem. 279:35001-35008(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE, FUNCTION.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "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].
    Strain: C57BL/6.
    Tissue: Brain.
  5. "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: TISSUE SPECIFICITY.

Entry informationi

Entry nameiCHST2_MOUSE
AccessioniPrimary (citable) accession number: Q80WV3
Secondary accession number(s): E9QNG2, O88276, Q794G9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: July 27, 2011
Last modified: June 24, 2015
This is version 99 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

It is uncertain whether Met-1 or Met-48 is the initiator.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.