CHST2_HUMAN
ID CHST2_HUMAN Reviewed; 530 AA.
AC Q9Y4C5; D3DNG5; Q2M370; Q9GZN5; Q9UED5; Q9Y6F2;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Carbohydrate sulfotransferase 2;
DE EC=2.8.2.- {ECO:0000269|PubMed:11726653};
DE AltName: Full=Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 2;
DE Short=GST-2;
DE AltName: Full=N-acetylglucosamine 6-O-sulfotransferase 1;
DE Short=GlcNAc6ST-1;
DE Short=Gn6ST-1;
GN Name=CHST2; Synonyms=GN6ST;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, ALTERNATIVE INITIATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9722682; DOI=10.1093/oxfordjournals.jbchem.a022164;
RA Uchimura K., Muramatsu H., Kaname T., Ogawa H., Yamakawa T., Fan Q.-W.,
RA Mitsuoka C., Kannagi R., Habuchi O., Yokoyama I., Yamamura K., Ozaki T.,
RA Nakagawara A., Kadomatsu K., Muramatsu T.;
RT "Human N-acetylglucosamine-6-O-sulfotransferase involved in the
RT biosynthesis of 6-sulfo sialyl Lewis X: molecular cloning, chromosomal
RT mapping, and expression in various organs and tumor cells.";
RL J. Biochem. 124:670-678(1998).
RN [2]
RP SEQUENCE REVISION.
RA Uchimura K., Muramatsu H., Muramatsu T.;
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Umbilical vein endothelial cell;
RX PubMed=10049591; DOI=10.1006/geno.1998.5653;
RA Li X., Tedder T.F.;
RT "CHST1 and CHST2 sulfotransferases expressed by human vascular endothelial
RT cells: cDNA cloning, expression, and chromosomal localization.";
RL Genomics 55:345-347(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND FUNCTION.
RC TISSUE=Placenta;
RX PubMed=11042394; DOI=10.1016/s0304-4165(00)00136-7;
RA Sakaguchi H., Kitagawa H., Sugahara K.;
RT "Functional expression and genomic structure of human N-acetylglucosamine-
RT 6-O-sulfotransferase that transfers sulfate to b-N-acetylglucosamine at the
RT nonreducing end of an N-acetyllactosamine sequence.";
RL Biochim. Biophys. Acta 1523:269-276(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=11310842;
RA Li X., Tu L., Murphy P.G., Kadono T., Steeber D.A., Tedder T.F.;
RT "CHST1 and CHST2 sulfotransferase expression by vascular endothelial cells
RT regulates shear-resistant leukocyte rolling via L-selectin.";
RL J. Leukoc. Biol. 69:565-574(2001).
RN [8]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ARG-174; ARG-296;
RP LYS-304; ARG-332 AND ARG-341.
RX PubMed=12501187; DOI=10.1021/bi0269557;
RA Grunwell J.R., Rath V.L., Rasmussen J., Cabrilo Z., Bertozzi C.R.;
RT "Characterization and mutagenesis of Gal/GlcNAc-6-O-sulfotransferases.";
RL Biochemistry 41:15590-15600(2002).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND PATHWAY.
RX PubMed=11726653; DOI=10.1074/jbc.m106587200;
RA Uchimura K., El-Fasakhany F.M., Hori M., Hemmerich S., Blink S.E.,
RA Kansas G.S., Kanamori A., Kumamoto K., Kannagi R., Muramatsu T.;
RT "Specificities of N-acetylglucosamine-6-O-sulfotransferases in relation to
RT L-selectin ligand synthesis and tumor-associated enzyme expression.";
RL J. Biol. Chem. 277:3979-3984(2002).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=12855678; DOI=10.1074/jbc.m304928200;
RA de Graffenried C.L., Bertozzi C.R.;
RT "Golgi localization of carbohydrate sulfotransferases is a determinant of
RT L-selectin ligand biosynthesis.";
RL J. Biol. Chem. 278:40282-40295(2003).
RN [11]
RP MUTAGENESIS OF LYS-518; ASP-519; LEU-520; SER-521; LYS-522; THR-523;
RP LEU-524; LEU-525; ARG-526; LYS-527; PRO-528; ARG-529 AND LEU-530.
RX PubMed=15632306; DOI=10.1093/jb/mvh162;
RA Chen L., Ichihara-Tanaka K., Muramatsu T.;
RT "Role of the carboxyl-terminal region in the activity of N-
RT acetylglucosamine 6-o-sulfotransferase-1.";
RL J. Biochem. 136:659-664(2004).
RN [12]
RP SUBUNIT, AND MUTAGENESIS OF CYS-59 AND CYS-86.
RX PubMed=15220337; DOI=10.1074/jbc.m405709200;
RA de Graffenried C.L., Bertozzi C.R.;
RT "The stem region of the sulfotransferase GlcNAc6ST-1 is a determinant of
RT substrate specificity.";
RL J. Biol. Chem. 279:40035-40043(2004).
RN [13]
RP GLYCOSYLATION AT ASN-243; ASN-457 AND ASN-475, LACK OF GLYCOSYLATION AT
RP ASN-152, AND MUTAGENESIS OF ASN-457 AND ASN-475.
RX PubMed=19571171; DOI=10.1093/glycob/cwp092;
RA Desko M.M., Gross D.A., Kohler J.J.;
RT "Effects of N-glycosylation on the activity and localization of GlcNAc-6-
RT sulfotransferase 1.";
RL Glycobiology 19:1068-1077(2009).
RN [14]
RP SUBCELLULAR LOCATION, SUBUNIT, AND ALTERNATIVE INITIATION.
RX PubMed=22260995; DOI=10.1369/0022155412437613;
RA Fujiwara M., Kobayashi M., Hoshino H., Uchimura K., Nakada T., Masumoto J.,
RA Sakai Y., Fukuda M., Nakayama J.;
RT "Expression of long-form N-acetylglucosamine-6-O-sulfotransferase 1 in
RT human high endothelial venules.";
RL J. Histochem. Cytochem. 60:397-407(2012).
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC (PAPS) as sulfonate donor to catalyze the transfer of sulfate to
CC position 6 of non-reducing N-acetylglucosamine (GlcNAc) residues within
CC keratan-like structures on N-linked glycans and within mucin-associated
CC glycans that can ultimately serve as SELL ligands. SELL ligands are
CC present in high endothelial cells (HEVs) and play a central role in
CC lymphocyte homing at sites of inflammation. Participates in
CC biosynthesis of the SELL ligand sialyl 6-sulfo Lewis X and in
CC lymphocyte homing to Peyer patches. Has no activity toward O-linked
CC sugars. Its substrate specificity may be influenced by its subcellular
CC location. Sulfates GlcNAc residues at terminal, non-reducing ends of
CC oligosaccharide chains. {ECO:0000269|PubMed:11042394,
CC ECO:0000269|PubMed:11726653}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + 3-O-{N-acetyl-beta-D-
CC glucosaminyl-(1->3)-beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC galactosaminyl}-L-threonyl-[protein] = 3-O-{6-O-sulfo-N-acetyl-beta-
CC D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC galactosaminyl}-L-threonyl-[protein] + adenosine 3',5'-bisphosphate +
CC H(+); Xref=Rhea:RHEA:67856, Rhea:RHEA-COMP:17368, Rhea:RHEA-
CC COMP:17369, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:176489, ChEBI:CHEBI:176492;
CC Evidence={ECO:0000250|UniProtKB:Q80WV3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67857;
CC Evidence={ECO:0000250|UniProtKB:Q80WV3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + 3-O-{N-acetyl-beta-D-
CC glucosaminyl-(1->3)-beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC galactosaminyl}-L-seryl-[protein] = 3-O-{6-O-sulfo-N-acetyl-beta-D-
CC glucosaminyl-(1->3)-beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC galactosaminyl}-L-seryl-[protein] + adenosine 3',5'-bisphosphate +
CC H(+); Xref=Rhea:RHEA:67860, Rhea:RHEA-COMP:17365, Rhea:RHEA-
CC COMP:17366, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:176490, ChEBI:CHEBI:176491;
CC Evidence={ECO:0000250|UniProtKB:Q80WV3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67861;
CC Evidence={ECO:0000250|UniProtKB:Q80WV3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + 3-O-{beta-D-galactosyl-(1->3)-[N-
CC acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-
CC L-threonyl-[protein] = 3-O-{beta-D-galactosyl-(1->3)-[6-O-sulfo-N-
CC acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-
CC L-threonyl-[protein] + adenosine 3',5'-bisphosphate + H(+);
CC Xref=Rhea:RHEA:67864, Rhea:RHEA-COMP:14420, Rhea:RHEA-COMP:17370,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:139607, ChEBI:CHEBI:176493;
CC Evidence={ECO:0000269|PubMed:11726653};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67865;
CC Evidence={ECO:0000305|PubMed:11726653};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + 3-O-{beta-D-galactosyl-(1->3)-[N-
CC acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-
CC L-seryl-[protein] = 3-O-{beta-D-galactosyl-(1->3)-[6-O-sulfo-N-
CC acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-
CC L-seryl-[protein] + adenosine 3',5'-bisphosphate + H(+);
CC Xref=Rhea:RHEA:67868, Rhea:RHEA-COMP:14419, Rhea:RHEA-COMP:17367,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:139605, ChEBI:CHEBI:176494;
CC Evidence={ECO:0000269|PubMed:11726653};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67869;
CC Evidence={ECO:0000305|PubMed:11726653};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.9 uM for PAPS {ECO:0000269|PubMed:12501187};
CC KM=1.4 mM for BetaBnO-GlcNAc {ECO:0000269|PubMed:12501187};
CC -!- PATHWAY: Protein modification; carbohydrate sulfation.
CC {ECO:0000269|PubMed:11726653}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Homodimerization is not essential
CC for enzyme activity. {ECO:0000269|PubMed:15220337,
CC ECO:0000269|PubMed:22260995}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:12855678, ECO:0000269|PubMed:22260995}; Single-pass
CC type II membrane protein {ECO:0000269|PubMed:12855678,
CC ECO:0000269|PubMed:22260995}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y4C5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y4C5-2; Sequence=VSP_018887;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in bone marrow,
CC peripheral blood leukocytes, spleen, brain, spinal cord, ovary and
CC placenta. Expressed by high endothelial cells (HEVs) and leukocytes.
CC {ECO:0000269|PubMed:10049591, ECO:0000269|PubMed:11310842,
CC ECO:0000269|PubMed:9722682}.
CC -!- INDUCTION: Up-regulated upon cytokine activation.
CC {ECO:0000269|PubMed:11310842}.
CC -!- PTM: Glycosylation at Asn-475 is required for catalytic activity.
CC {ECO:0000269|PubMed:19571171}.
CC -!- MISCELLANEOUS: [Isoform 2]: Higher levels of expression compared to
CC isoform 1 when expressed in HeLa cells. Exhibits similar intracellular
CC GlcNAc-6-O-sulfation activity. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. Gal/GlcNAc/GalNAc
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34265.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB16886.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB16887.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB014679; BAA34265.2; ALT_INIT; mRNA.
DR EMBL; AB014680; BAA34266.2; -; mRNA.
DR EMBL; AF083066; AAD20981.1; -; mRNA.
DR EMBL; AB021124; BAB16886.1; ALT_INIT; mRNA.
DR EMBL; AB021125; BAB16887.1; ALT_INIT; Genomic_DNA.
DR EMBL; CH471052; EAW78952.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78953.1; -; Genomic_DNA.
DR EMBL; BC105010; AAI05011.1; -; mRNA.
DR EMBL; BC105012; AAI05013.1; -; mRNA.
DR CCDS; CCDS3129.1; -. [Q9Y4C5-1]
DR RefSeq; NP_004258.2; NM_004267.4. [Q9Y4C5-1]
DR AlphaFoldDB; Q9Y4C5; -.
DR BioGRID; 114826; 13.
DR STRING; 9606.ENSP00000307911; -.
DR GlyGen; Q9Y4C5; 3 sites.
DR iPTMnet; Q9Y4C5; -.
DR PhosphoSitePlus; Q9Y4C5; -.
DR BioMuta; CHST2; -.
DR DMDM; 61212252; -.
DR EPD; Q9Y4C5; -.
DR jPOST; Q9Y4C5; -.
DR MassIVE; Q9Y4C5; -.
DR PaxDb; Q9Y4C5; -.
DR PeptideAtlas; Q9Y4C5; -.
DR PRIDE; Q9Y4C5; -.
DR ProteomicsDB; 86161; -. [Q9Y4C5-1]
DR ProteomicsDB; 86162; -. [Q9Y4C5-2]
DR Antibodypedia; 2653; 228 antibodies from 26 providers.
DR DNASU; 9435; -.
DR Ensembl; ENST00000309575.5; ENSP00000307911.3; ENSG00000175040.6. [Q9Y4C5-1]
DR GeneID; 9435; -.
DR KEGG; hsa:9435; -.
DR MANE-Select; ENST00000309575.5; ENSP00000307911.3; NM_004267.5; NP_004258.2.
DR CTD; 9435; -.
DR DisGeNET; 9435; -.
DR GeneCards; CHST2; -.
DR HGNC; HGNC:1970; CHST2.
DR HPA; ENSG00000175040; Tissue enhanced (brain).
DR MIM; 603798; gene.
DR neXtProt; NX_Q9Y4C5; -.
DR OpenTargets; ENSG00000175040; -.
DR PharmGKB; PA26502; -.
DR VEuPathDB; HostDB:ENSG00000175040; -.
DR eggNOG; ENOG502QTSD; Eukaryota.
DR GeneTree; ENSGT00940000161292; -.
DR HOGENOM; CLU_028381_1_0_1; -.
DR InParanoid; Q9Y4C5; -.
DR OMA; YCHQPMA; -.
DR PhylomeDB; Q9Y4C5; -.
DR TreeFam; TF342871; -.
DR BioCyc; MetaCyc:ENSG00000175040-MON; -.
DR PathwayCommons; Q9Y4C5; -.
DR Reactome; R-HSA-2022854; Keratan sulfate biosynthesis.
DR SABIO-RK; Q9Y4C5; -.
DR UniPathway; UPA00353; -.
DR BioGRID-ORCS; 9435; 8 hits in 1077 CRISPR screens.
DR ChiTaRS; CHST2; human.
DR GeneWiki; CHST2; -.
DR GenomeRNAi; 9435; -.
DR Pharos; Q9Y4C5; Tbio.
DR PRO; PR:Q9Y4C5; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9Y4C5; protein.
DR Bgee; ENSG00000175040; Expressed in decidua and 182 other tissues.
DR ExpressionAtlas; Q9Y4C5; baseline and differential.
DR Genevisible; Q9Y4C5; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031228; C:intrinsic component of Golgi membrane; NAS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0001517; F:N-acetylglucosamine 6-O-sulfotransferase activity; IDA:UniProtKB.
DR GO; GO:0008146; F:sulfotransferase activity; TAS:ProtInc.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR GO; GO:0018146; P:keratan sulfate biosynthetic process; TAS:Reactome.
DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; IDA:UniProtKB.
DR GO; GO:1903238; P:positive regulation of leukocyte tethering or rolling; ISS:UniProtKB.
DR GO; GO:0006790; P:sulfur compound metabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR016469; Carbohydrate_sulfotransferase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000863; Sulfotransferase_dom.
DR Pfam; PF00685; Sulfotransfer_1; 1.
DR PIRSF; PIRSF005883; Carbohydrate_sulfotransferase; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; Carbohydrate metabolism; Disulfide bond;
KW Glycoprotein; Golgi apparatus; Inflammatory response; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..530
FT /note="Carbohydrate sulfotransferase 2"
FT /id="PRO_0000085186"
FT TOPO_DOM 1..54
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..530
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 89..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 173..179
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000305"
FT BINDING 332..340
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000305"
FT SITE 152
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:19571171"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19571171"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19571171"
FT CARBOHYD 475
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19571171"
FT VAR_SEQ 1..47
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_018887"
FT MUTAGEN 59
FT /note="C->S: Does not affect homodimerization. Abolishes
FT homodimerization but not enzyme activity; when associated
FT with S-39."
FT /evidence="ECO:0000269|PubMed:15220337"
FT MUTAGEN 86
FT /note="C->S: Induces migration in both homodimeric and
FT monomeric forms. Abolishes homodimerization but not enzyme
FT activity; when associated with S-12."
FT /evidence="ECO:0000269|PubMed:15220337"
FT MUTAGEN 174
FT /note="R->A: Induces a strong decrease in enzyme activity."
FT /evidence="ECO:0000269|PubMed:12501187"
FT MUTAGEN 296
FT /note="R->A: Induces a strong decrease in enzyme activity."
FT /evidence="ECO:0000269|PubMed:12501187"
FT MUTAGEN 304
FT /note="K->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:12501187"
FT MUTAGEN 332
FT /note="R->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:12501187"
FT MUTAGEN 341
FT /note="R->A: Induces a strong decrease in enzyme activity."
FT /evidence="ECO:0000269|PubMed:12501187"
FT MUTAGEN 457
FT /note="N->A: Reduced localization in the Golgi."
FT /evidence="ECO:0000269|PubMed:19571171"
FT MUTAGEN 475
FT /note="N->A: Unable to sulfate the sialyl Lewis X
FT tetrasaccharide."
FT /evidence="ECO:0000269|PubMed:19571171"
FT MUTAGEN 518
FT /note="K->A: Has weak or no effect."
FT /evidence="ECO:0000269|PubMed:15632306"
FT MUTAGEN 519
FT /note="D->A: Has weak or no effect."
FT /evidence="ECO:0000269|PubMed:15632306"
FT MUTAGEN 520
FT /note="L->A: Has weak or no effect."
FT /evidence="ECO:0000269|PubMed:15632306"
FT MUTAGEN 521
FT /note="S->A: No effect."
FT /evidence="ECO:0000269|PubMed:15632306"
FT MUTAGEN 522
FT /note="K->A: No effect."
FT /evidence="ECO:0000269|PubMed:15632306"
FT MUTAGEN 523
FT /note="T->A: Has weak or no effect."
FT /evidence="ECO:0000269|PubMed:15632306"
FT MUTAGEN 524
FT /note="L->A,T: Induces a strong decrease in enzyme
FT activity."
FT /evidence="ECO:0000269|PubMed:15632306"
FT MUTAGEN 525
FT /note="L->A: Induces a strong decrease in enzyme activity."
FT /evidence="ECO:0000269|PubMed:15632306"
FT MUTAGEN 525
FT /note="L->T: Has weak or no effect."
FT /evidence="ECO:0000269|PubMed:15632306"
FT MUTAGEN 526
FT /note="R->A: Has weak or no effect."
FT /evidence="ECO:0000269|PubMed:15632306"
FT MUTAGEN 527
FT /note="K->A: No effect."
FT /evidence="ECO:0000269|PubMed:15632306"
FT MUTAGEN 528
FT /note="P->A: Has weak or no effect."
FT /evidence="ECO:0000269|PubMed:15632306"
FT MUTAGEN 529
FT /note="R->A: No effect."
FT /evidence="ECO:0000269|PubMed:15632306"
FT MUTAGEN 530
FT /note="L->A,T: Induces a strong decrease in enzyme
FT activity."
FT /evidence="ECO:0000269|PubMed:15632306"
FT CONFLICT 8
FT /note="A -> V (in Ref. 4; BAB16887)"
FT /evidence="ECO:0000305"
SQ 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
