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Carbohydrate sulfotransferase 2 (EC 2.8.2.-) (Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 2) (GST-2) (N-acetylglucosamine 6-O-sulfotransferase 1) (GlcNAc6ST-1) (Gn6ST-1)

 CHST2_HUMAN             Reviewed;         530 AA.
Q9Y4C5; D3DNG5; Q2M370; Q9GZN5; Q9UED5; Q9Y6F2;
15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 2.
28-FEB-2018, entry version 132.
RecName: Full=Carbohydrate sulfotransferase 2;
EC=2.8.2.-;
AltName: Full=Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 2;
Short=GST-2;
AltName: Full=N-acetylglucosamine 6-O-sulfotransferase 1;
Short=GlcNAc6ST-1;
Short=Gn6ST-1;
Name=CHST2; Synonyms=GN6ST;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, ALTERNATIVE
INITIATION, AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=9722682; DOI=10.1093/oxfordjournals.jbchem.a022164;
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.;
"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.";
J. Biochem. 124:670-678(1998).
[2]
SEQUENCE REVISION.
Uchimura K., Muramatsu H., Muramatsu T.;
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Umbilical vein endothelial cell;
PubMed=10049591; DOI=10.1006/geno.1998.5653;
Li X., Tedder T.F.;
"CHST1 and CHST2 sulfotransferases expressed by human vascular
endothelial cells: cDNA cloning, expression, and chromosomal
localization.";
Genomics 55:345-347(1999).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND FUNCTION.
TISSUE=Placenta;
PubMed=11042394; DOI=10.1016/S0304-4165(00)00136-7;
Sakaguchi H., Kitagawa H., Sugahara K.;
"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.";
Biochim. Biophys. Acta 1523:269-276(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=11310842;
Li X., Tu L., Murphy P.G., Kadono T., Steeber D.A., Tedder T.F.;
"CHST1 and CHST2 sulfotransferase expression by vascular endothelial
cells regulates shear-resistant leukocyte rolling via L-selectin.";
J. Leukoc. Biol. 69:565-574(2001).
[8]
BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ARG-174; ARG-296;
LYS-304; ARG-332 AND ARG-341.
PubMed=12501187; DOI=10.1021/bi0269557;
Grunwell J.R., Rath V.L., Rasmussen J., Cabrilo Z., Bertozzi C.R.;
"Characterization and mutagenesis of Gal/GlcNAc-6-O-
sulfotransferases.";
Biochemistry 41:15590-15600(2002).
[9]
SUBSTRATE SPECIFICITY.
PubMed=11726653; DOI=10.1074/jbc.M106587200;
Uchimura K., El-Fasakhany F.M., Hori M., Hemmerich S., Blink S.E.,
Kansas G.S., Kanamori A., Kumamoto K., Kannagi R., Muramatsu T.;
"Specificities of N-acetylglucosamine-6-O-sulfotransferases in
relation to L-selectin ligand synthesis and tumor-associated enzyme
expression.";
J. Biol. Chem. 277:3979-3984(2002).
[10]
SUBCELLULAR LOCATION.
PubMed=12855678; DOI=10.1074/jbc.M304928200;
de Graffenried C.L., Bertozzi C.R.;
"Golgi localization of carbohydrate sulfotransferases is a determinant
of L-selectin ligand biosynthesis.";
J. Biol. Chem. 278:40282-40295(2003).
[11]
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.
PubMed=15632306; DOI=10.1093/jb/mvh162;
Chen L., Ichihara-Tanaka K., Muramatsu T.;
"Role of the carboxyl-terminal region in the activity of N-
acetylglucosamine 6-o-sulfotransferase-1.";
J. Biochem. 136:659-664(2004).
[12]
SUBUNIT, AND MUTAGENESIS OF CYS-59 AND CYS-86.
PubMed=15220337; DOI=10.1074/jbc.M405709200;
de Graffenried C.L., Bertozzi C.R.;
"The stem region of the sulfotransferase GlcNAc6ST-1 is a determinant
of substrate specificity.";
J. Biol. Chem. 279:40035-40043(2004).
[13]
GLYCOSYLATION AT ASN-243; ASN-457 AND ASN-475, LACK OF GLYCOSYLATION
AT ASN-152, AND MUTAGENESIS OF ASN-457 AND ASN-475.
PubMed=19571171; DOI=10.1093/glycob/cwp092;
Desko M.M., Gross D.A., Kohler J.J.;
"Effects of N-glycosylation on the activity and localization of
GlcNAc-6-sulfotransferase 1.";
Glycobiology 19:1068-1077(2009).
[14]
SUBCELLULAR LOCATION, SUBUNIT, AND ALTERNATIVE INITIATION.
PubMed=22260995; DOI=10.1369/0022155412437613;
Fujiwara M., Kobayashi M., Hoshino H., Uchimura K., Nakada T.,
Masumoto J., Sakai Y., Fukuda M., Nakayama J.;
"Expression of long-form N-acetylglucosamine-6-O-sulfotransferase 1 in
human high endothelial venules.";
J. Histochem. Cytochem. 60:397-407(2012).
-!- 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.
{ECO:0000269|PubMed:11042394}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=3.9 uM for PAPS {ECO:0000269|PubMed:12501187};
KM=1.4 mM for BetaBnO-GlcNAc {ECO:0000269|PubMed:12501187};
-!- SUBUNIT: Homodimer; disulfide-linked. Homodimerization is not
essential for enzyme activity. {ECO:0000269|PubMed:15220337,
ECO:0000269|PubMed:22260995}.
-!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
membrane {ECO:0000269|PubMed:12855678,
ECO:0000269|PubMed:22260995}; Single-pass type II membrane protein
{ECO:0000269|PubMed:12855678, ECO:0000269|PubMed:22260995}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=1;
IsoId=Q9Y4C5-1; Sequence=Displayed;
Name=2;
IsoId=Q9Y4C5-2; Sequence=VSP_018887;
Note=Higher levels of expression compared to isoform 1 when
expressed in HeLa cells. Exhibits similar intracellular
GlcNAc-6-O-sulfation activity.;
-!- 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. {ECO:0000269|PubMed:10049591,
ECO:0000269|PubMed:11310842, ECO:0000269|PubMed:9722682}.
-!- INDUCTION: Up-regulated upon cytokine activation.
{ECO:0000269|PubMed:11310842}.
-!- PTM: Glycosylation at Asn-475 is required for catalytic activity.
{ECO:0000269|PubMed:19571171}.
-!- SIMILARITY: Belongs to the sulfotransferase 1 family.
Gal/GlcNAc/GalNAc subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA34265.2; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAB16886.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAB16887.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AB014679; BAA34265.2; ALT_INIT; mRNA.
EMBL; AB014680; BAA34266.2; -; mRNA.
EMBL; AF083066; AAD20981.1; -; mRNA.
EMBL; AB021124; BAB16886.1; ALT_INIT; mRNA.
EMBL; AB021125; BAB16887.1; ALT_INIT; Genomic_DNA.
EMBL; CH471052; EAW78952.1; -; Genomic_DNA.
EMBL; CH471052; EAW78953.1; -; Genomic_DNA.
EMBL; BC105010; AAI05011.1; -; mRNA.
EMBL; BC105012; AAI05013.1; -; mRNA.
CCDS; CCDS3129.1; -. [Q9Y4C5-1]
RefSeq; NP_004258.2; NM_004267.4. [Q9Y4C5-1]
UniGene; Hs.529249; -.
UniGene; Hs.8786; -.
ProteinModelPortal; Q9Y4C5; -.
SMR; Q9Y4C5; -.
STRING; 9606.ENSP00000307911; -.
iPTMnet; Q9Y4C5; -.
PhosphoSitePlus; Q9Y4C5; -.
BioMuta; CHST2; -.
DMDM; 61212252; -.
PaxDb; Q9Y4C5; -.
PeptideAtlas; Q9Y4C5; -.
PRIDE; Q9Y4C5; -.
DNASU; 9435; -.
Ensembl; ENST00000309575; ENSP00000307911; ENSG00000175040. [Q9Y4C5-1]
GeneID; 9435; -.
KEGG; hsa:9435; -.
CTD; 9435; -.
DisGeNET; 9435; -.
EuPathDB; HostDB:ENSG00000175040.5; -.
GeneCards; CHST2; -.
HGNC; HGNC:1970; CHST2.
HPA; HPA013620; -.
MIM; 603798; gene.
neXtProt; NX_Q9Y4C5; -.
OpenTargets; ENSG00000175040; -.
PharmGKB; PA26502; -.
eggNOG; ENOG410IIA6; Eukaryota.
eggNOG; ENOG4111DKG; LUCA.
GeneTree; ENSGT00530000062902; -.
HOGENOM; HOG000261614; -.
HOVERGEN; HBG050949; -.
InParanoid; Q9Y4C5; -.
KO; K04745; -.
OMA; MGGPADY; -.
OrthoDB; EOG091G0V3Y; -.
PhylomeDB; Q9Y4C5; -.
TreeFam; TF342871; -.
BioCyc; MetaCyc:ENSG00000175040-MONOMER; -.
Reactome; R-HSA-2022854; Keratan sulfate biosynthesis.
SABIO-RK; Q9Y4C5; -.
ChiTaRS; CHST2; human.
GeneWiki; CHST2; -.
GenomeRNAi; 9435; -.
PRO; PR:Q9Y4C5; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000175040; -.
CleanEx; HS_CHST2; -.
ExpressionAtlas; Q9Y4C5; baseline and differential.
Genevisible; Q9Y4C5; HS.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
GO; GO:0031228; C:intrinsic component of Golgi membrane; NAS:UniProtKB.
GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
GO; GO:0001517; F:N-acetylglucosamine 6-O-sulfotransferase activity; IDA:UniProtKB.
GO; GO:0008146; F:sulfotransferase activity; TAS:ProtInc.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
GO; GO:0018146; P:keratan sulfate biosynthetic process; TAS:Reactome.
GO; GO:0007275; P:multicellular organism development; TAS:ProtInc.
GO; GO:0006044; P:N-acetylglucosamine metabolic process; IDA:UniProtKB.
GO; GO:0006790; P:sulfur compound metabolic process; IDA:UniProtKB.
InterPro; IPR016469; Carbohydrate_sulfotransferase.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR000863; Sulfotransferase_dom.
Pfam; PF00685; Sulfotransfer_1; 1.
PIRSF; PIRSF005883; Carbohydrate_sulfotransferase; 1.
SUPFAM; SSF52540; SSF52540; 3.
1: Evidence at protein level;
Alternative initiation; Carbohydrate metabolism; Complete proteome;
Disulfide bond; Glycoprotein; Golgi apparatus; Inflammatory response;
Membrane; Reference proteome; Signal-anchor; Transferase;
Transmembrane; Transmembrane helix.
CHAIN 1 530 Carbohydrate sulfotransferase 2.
/FTId=PRO_0000085186.
TOPO_DOM 1 54 Cytoplasmic. {ECO:0000255}.
TRANSMEM 55 75 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 76 530 Lumenal. {ECO:0000255}.
NP_BIND 173 179 PAPS. {ECO:0000305}.
NP_BIND 332 340 PAPS. {ECO:0000305}.
SITE 152 152 Not glycosylated.
{ECO:0000269|PubMed:19571171}.
CARBOHYD 243 243 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19571171}.
CARBOHYD 457 457 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19571171}.
CARBOHYD 475 475 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19571171}.
VAR_SEQ 1 47 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_018887.
MUTAGEN 59 59 C->S: Does not affect homodimerization.
Abolishes homodimerization but not enzyme
activity; when associated with S-39.
{ECO:0000269|PubMed:15220337}.
MUTAGEN 86 86 C->S: Induces migration in both
homodimeric and monomeric forms.
Abolishes homodimerization but not enzyme
activity; when associated with S-12.
{ECO:0000269|PubMed:15220337}.
MUTAGEN 174 174 R->A: Induces a strong decrease in enzyme
activity. {ECO:0000269|PubMed:12501187}.
MUTAGEN 296 296 R->A: Induces a strong decrease in enzyme
activity. {ECO:0000269|PubMed:12501187}.
MUTAGEN 304 304 K->A: Loss of function.
{ECO:0000269|PubMed:12501187}.
MUTAGEN 332 332 R->A: Loss of function.
{ECO:0000269|PubMed:12501187}.
MUTAGEN 341 341 R->A: Induces a strong decrease in enzyme
activity. {ECO:0000269|PubMed:12501187}.
MUTAGEN 457 457 N->A: Reduced localization in the Golgi.
{ECO:0000269|PubMed:19571171}.
MUTAGEN 475 475 N->A: Unable to sulfate the sialyl Lewis
X tetrasaccharide.
{ECO:0000269|PubMed:19571171}.
MUTAGEN 518 518 K->A: Has weak or no effect.
{ECO:0000269|PubMed:15632306}.
MUTAGEN 519 519 D->A: Has weak or no effect.
{ECO:0000269|PubMed:15632306}.
MUTAGEN 520 520 L->A: Has weak or no effect.
{ECO:0000269|PubMed:15632306}.
MUTAGEN 521 521 S->A: No effect.
{ECO:0000269|PubMed:15632306}.
MUTAGEN 522 522 K->A: No effect.
{ECO:0000269|PubMed:15632306}.
MUTAGEN 523 523 T->A: Has weak or no effect.
{ECO:0000269|PubMed:15632306}.
MUTAGEN 524 524 L->A,T: Induces a strong decrease in
enzyme activity.
{ECO:0000269|PubMed:15632306}.
MUTAGEN 525 525 L->A: Induces a strong decrease in enzyme
activity. {ECO:0000269|PubMed:15632306}.
MUTAGEN 525 525 L->T: Has weak or no effect.
{ECO:0000269|PubMed:15632306}.
MUTAGEN 526 526 R->A: Has weak or no effect.
{ECO:0000269|PubMed:15632306}.
MUTAGEN 527 527 K->A: No effect.
{ECO:0000269|PubMed:15632306}.
MUTAGEN 528 528 P->A: Has weak or no effect.
{ECO:0000269|PubMed:15632306}.
MUTAGEN 529 529 R->A: No effect.
{ECO:0000269|PubMed:15632306}.
MUTAGEN 530 530 L->A,T: Induces a strong decrease in
enzyme activity.
{ECO:0000269|PubMed:15632306}.
CONFLICT 8 8 A -> V (in Ref. 4; BAB16887).
{ECO:0000305}.
SEQUENCE 530 AA; 57857 MW; A82CA227B9D5651B CRC64;
MSRSPQRALP PGALPRLLQA APAAAPRALL PQWPRRPGRR WPASPLGMKV FRRKALVLCA
GYALLLVLTM LNLLDYKWHK EPLQQCNPDG PLGAAAGAAG GSWGRPGPPP AGPPRAHARL
DLRTPYRPPA AAVGAAPAAA AGMAGVAAPP GNGTRGTGGV GDKRQLVYVF TTWRSGSSFF
GELFNQNPEV FFLYEPVWHV WQKLYPGDAV SLQGAARDML SALYRCDLSV FQLYSPAGSG
GRNLTTLGIF GAATNKVVCS SPLCPAYRKE VVGLVDDRVC KKCPPQRLAR FEEECRKYRT
LVIKGVRVFD VAVLAPLLRD PALDLKVIHL VRDPRAVASS RIRSRHGLIR ESLQVVRSRD
PRAHRMPFLE AAGHKLGAKK EGVGGPADYH ALGAMEVICN SMAKTLQTAL QPPDWLQGHY
LVVRYEDLVG DPVKTLRRVY DFVGLLVSPE MEQFALNMTS GSGSSSKPFV VSARNATQAA
NAWRTALTFQ QIKQVEEFCY QPMAVLGYER VNSPEEVKDL SKTLLRKPRL


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CHST6 CHST4 Gene carbohydrate (N-acetylglucosamine 6-O) sulfotransferase 4
CHST9 CHST7 Gene carbohydrate (N-acetylglucosamine 6-O) sulfotransferase 7
GWB-9446C9 Anti- CHST4 (carbohydrate (N-acetylglucosamine 6-O) sulfotransferase 4) Antibody


 

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