Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3 (EC 2.4.1.135) (Beta-1,3-glucuronyltransferase 3) (Glucuronosyltransferase I) (GlcAT-I) (UDP-GlcUA:Gal beta-1,3-Gal-R glucuronyltransferase) (GlcUAT-I)

 B3GA3_HUMAN             Reviewed;         335 AA.
O94766; B7ZAB3; Q96I06; Q9UEP0;
01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
26-APR-2004, sequence version 2.
25-OCT-2017, entry version 173.
RecName: Full=Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3;
EC=2.4.1.135 {ECO:0000269|PubMed:25893793};
AltName: Full=Beta-1,3-glucuronyltransferase 3;
AltName: Full=Glucuronosyltransferase I;
Short=GlcAT-I;
AltName: Full=UDP-GlcUA:Gal beta-1,3-Gal-R glucuronyltransferase;
Short=GlcUAT-I;
Name=B3GAT3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHARACTERIZATION.
TISSUE=Placenta;
PubMed=9506957; DOI=10.1074/jbc.273.12.6615;
Kitagawa H., Tone Y., Tamura J., Neumann K.W., Ogawa T., Oka S.,
Kawasaki T., Sugahara K.;
"Molecular cloning and expression of glucuronyltransferase I involved
in the biosynthesis of the glycosaminoglycan-protein linkage region of
proteoglycans.";
J. Biol. Chem. 273:6615-6618(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION, AND
MUTAGENESIS.
PubMed=10842173; DOI=10.1074/jbc.M002182200;
Ouzzine M., Gulberti S., Netter P., Magdalou J., Fournel-Gigleux S.;
"Structure/function of the human Ga1beta1,3-glucuronosyltransferase.
Dimerization and functional activity are mediated by two crucial
cysteine residues.";
J. Biol. Chem. 275:28254-28260(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Eye, and Skin;
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 9-335 (ISOFORM 1).
TISSUE=Brain;
PubMed=9927678; DOI=10.1073/pnas.96.3.974;
Herman T., Horvitz H.R.;
"Three proteins involved in Caenorhabditis elegans vulval invagination
are similar to components of a glycosylation pathway.";
Proc. Natl. Acad. Sci. U.S.A. 96:974-979(1999).
[7]
CHARACTERIZATION.
PubMed=10526176; DOI=10.1016/S0014-5793(99)01287-9;
Tone Y., Kitagawa H., Imiya K., Oka S., Kawasaki T., Sugahara K.;
"Characterization of recombinant human glucuronyltransferase I
involved in the biosynthesis of the glycosaminoglycan-protein linkage
region of proteoglycans.";
FEBS Lett. 459:415-420(1999).
[8]
SUBCELLULAR LOCATION, VARIANT JDSCD GLN-277, CHARACTERIZATION OF
VARIANT JDSCD GLN-277, AND INVOLVEMENT IN JDSCD.
PubMed=21763480; DOI=10.1016/j.ajhg.2011.05.021;
Baasanjav S., Al-Gazali L., Hashiguchi T., Mizumoto S., Fischer B.,
Horn D., Seelow D., Ali B.R., Aziz S.A., Langer R., Saleh A.A.,
Becker C., Nurnberg G., Cantagrel V., Gleeson J.G., Gomez D.,
Michel J.B., Stricker S., Lindner T.H., Nurnberg P., Sugahara K.,
Mundlos S., Hoffmann K.;
"Faulty initiation of proteoglycan synthesis causes cardiac and joint
defects.";
Am. J. Hum. Genet. 89:15-27(2011).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10]
FUNCTION, INTERACTION WITH PXYLP1, AND MUTAGENESIS OF GLU-281.
PubMed=24425863; DOI=10.1074/jbc.M113.520536;
Koike T., Izumikawa T., Sato B., Kitagawa H.;
"Identification of phosphatase that dephosphorylates xylose in the
glycosaminoglycan-protein linkage region of proteoglycans.";
J. Biol. Chem. 289:6695-6708(2014).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[12]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 76-335 IN COMPLEX WITH
UDP-GLUCURONIC ACID AND GALACTOSE MOIETY OF SUBSTRATE GLYCOPROTEIN.
TISSUE=Liver;
PubMed=10946001; DOI=10.1074/jbc.M007399200;
Pedersen L.C., Tsuchida K., Kitagawa H., Sugahara K., Darden T.A.,
Negishi M.;
"Heparan/chondroitin sulfate biosynthesis. Structure and mechanism of
human glucuronyltransferase I.";
J. Biol. Chem. 275:34580-34585(2000).
[13]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 76-335 IN COMPLEX WITH
UDP-GLUCURONIC ACID, AND ACTIVE SITE.
PubMed=11950836; DOI=10.1074/jbc.M112343200;
Pedersen L.C., Darden T.A., Negishi M.;
"Crystal structure of beta 1,3-glucuronyltransferase I in complex with
active donor substrate UDP-GlcUA.";
J. Biol. Chem. 277:21869-21873(2002).
[14]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 76-335 IN COMPLEX WITH
URIDINE-5'-DIPHOSPHATE AND GALACTOSE MOIETY OF SUBSTRATE GLYCOPROTEIN.
PubMed=18400750; DOI=10.1074/jbc.M709556200;
Tone Y., Pedersen L.C., Yamamoto T., Izumikawa T., Kitagawa H.,
Nishihara J., Tamura J., Negishi M., Sugahara K.;
"2-o-phosphorylation of xylose and 6-O-sulfation of galactose in the
protein linkage region of glycosaminoglycans influence the
glucuronyltransferase-I activity involved in the linkage region
synthesis.";
J. Biol. Chem. 283:16801-16807(2008).
[15]
VARIANT JDSCD GLN-277.
PubMed=24668659; DOI=10.1002/ajmg.a.36487;
von Oettingen J.E., Tan W.H., Dauber A.;
"Skeletal dysplasia, global developmental delay, and multiple
congenital anomalies in a 5-year-old boy-report of the second family
with B3GAT3 mutation and expansion of the phenotype.";
Am. J. Med. Genet. A 164A:1580-1586(2014).
[16]
VARIANT JDSCD SER-223.
PubMed=26086840; DOI=10.1002/ajmg.a.37209;
Jones K.L., Schwarze U., Adam M.P., Byers P.H., Mefford H.C.;
"A homozygous B3GAT3 mutation causes a severe syndrome with multiple
fractures, expanding the phenotype of linkeropathy syndromes.";
Am. J. Med. Genet. A 167A:2691-2696(2015).
[17]
VARIANT JDSCD LEU-140, CHARACTERIZATION OF VARIANT JDSCD LEU-140,
FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
PubMed=25893793; DOI=10.1007/s00439-015-1549-2;
Budde B.S., Mizumoto S., Kogawa R., Becker C., Altmueller J.,
Thiele H., Rueschendorf F., Toliat M.R., Kaleschke G., Haemmerle J.M.,
Hoehne W., Sugahara K., Nuernberg P., Kennerknecht I.;
"Skeletal dysplasia in a consanguineous clan from the island of
Nias/Indonesia is caused by a novel mutation in B3GAT3.";
Hum. Genet. 134:691-704(2015).
-!- FUNCTION: Glycosaminoglycans biosynthesis (PubMed:25893793).
Involved in forming the linkage tetrasaccharide present in heparan
sulfate and chondroitin sulfate. Transfers a glucuronic acid
moiety from the uridine diphosphate-glucuronic acid (UDP-GlcUA) to
the common linkage region trisaccharide Gal-beta-1,3-Gal-beta-1,4-
Xyl covalently bound to a Ser residue at the glycosaminylglycan
attachment site of proteoglycans. Can also play a role in the
biosynthesis of l2/HNK-1 carbohydrate epitope on glycoproteins.
Shows strict specificity for Gal-beta-1,3-Gal-beta-1,4-Xyl,
exhibiting negligible incorporation into other galactoside
substrates including Galbeta1-3Gal beta1-O-benzyl, Galbeta1-
4GlcNAc and Galbeta1-4Glc. Stimulates 2-phosphoxylose phosphatase
activity of PXYLP1 in presence of uridine diphosphate-glucuronic
acid (UDP-GlcUA) during completion of linkage region formation
(PubMed:24425863). {ECO:0000269|PubMed:24425863,
ECO:0000269|PubMed:25893793}.
-!- CATALYTIC ACTIVITY: UDP-alpha-D-glucuronate + [protein]-3-O-(beta-
D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-
serine = UDP + [protein]-3-O-(beta-D-GlcA-(1->3)-beta-D-Gal-
(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-serine.
{ECO:0000269|PubMed:25893793}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
-!- ENZYME REGULATION: Inhibited by EDTA.
-!- PATHWAY: Protein modification; protein glycosylation.
-!- SUBUNIT: Homodimer; disulfide-linked. Interacts with PXYLP1; the
interaction increases the 2-phosphoxylose phosphatase activity of
PXYLP1 during completion of linkage region formation in a B3GAT3-
mediated manner. {ECO:0000269|PubMed:10946001,
ECO:0000269|PubMed:11950836, ECO:0000269|PubMed:18400750,
ECO:0000269|PubMed:24425863}.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane
{ECO:0000269|PubMed:21763480}; Single-pass type II membrane
protein {ECO:0000269|PubMed:21763480}. Golgi apparatus, cis-Golgi
network {ECO:0000269|PubMed:21763480,
ECO:0000269|PubMed:25893793}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O94766-1; Sequence=Displayed;
Name=2;
IsoId=O94766-2; Sequence=VSP_056347;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous (but weakly expressed in all
tissues examined).
-!- PTM: N-glycosylated.
-!- DISEASE: Multiple joint dislocations, short stature, and
craniofacial dysmorphism with or without congenital heart defects
(JDSCD) [MIM:245600]: An autosomal recessive disease characterized
by dysmorphic facies, bilateral dislocations of the elbows, hips,
and knees, clubfeet, and short stature, as well as cardiovascular
defects. {ECO:0000269|PubMed:21763480,
ECO:0000269|PubMed:24668659, ECO:0000269|PubMed:25893793,
ECO:0000269|PubMed:26086840}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the glycosyltransferase 43 family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB009598; BAA34537.1; -; mRNA.
EMBL; AK316228; BAH14599.1; -; mRNA.
EMBL; AP001458; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC007906; AAH07906.1; -; mRNA.
EMBL; BC071961; AAH71961.1; -; mRNA.
EMBL; AJ005865; CAA06742.1; -; mRNA.
CCDS; CCDS76418.1; -. [O94766-2]
CCDS; CCDS8025.1; -. [O94766-1]
RefSeq; NP_001275652.1; NM_001288723.1. [O94766-2]
RefSeq; NP_036332.2; NM_012200.3. [O94766-1]
UniGene; Hs.502759; -.
PDB; 1FGG; X-ray; 2.30 A; A/B=76-335.
PDB; 1KWS; X-ray; 2.10 A; A/B=76-335.
PDB; 3CU0; X-ray; 1.90 A; A/B=76-335.
PDBsum; 1FGG; -.
PDBsum; 1KWS; -.
PDBsum; 3CU0; -.
ProteinModelPortal; O94766; -.
SMR; O94766; -.
BioGrid; 117620; 25.
IntAct; O94766; 2.
STRING; 9606.ENSP00000265471; -.
DrugBank; DB03041; UDP-alpha-D-glucuronic acid.
DrugBank; DB03435; Uridine-5'-Diphosphate.
CAZy; GT43; Glycosyltransferase Family 43.
BioMuta; B3GAT3; -.
EPD; O94766; -.
MaxQB; O94766; -.
PaxDb; O94766; -.
PeptideAtlas; O94766; -.
PRIDE; O94766; -.
DNASU; 26229; -.
Ensembl; ENST00000265471; ENSP00000265471; ENSG00000149541. [O94766-1]
Ensembl; ENST00000534026; ENSP00000432474; ENSG00000149541. [O94766-2]
GeneID; 26229; -.
KEGG; hsa:26229; -.
UCSC; uc001ntw.3; human. [O94766-1]
CTD; 26229; -.
DisGeNET; 26229; -.
EuPathDB; HostDB:ENSG00000149541.9; -.
GeneCards; B3GAT3; -.
HGNC; HGNC:923; B3GAT3.
HPA; HPA051328; -.
MalaCards; B3GAT3; -.
MIM; 245600; phenotype.
MIM; 606374; gene.
neXtProt; NX_O94766; -.
OpenTargets; ENSG00000149541; -.
Orphanet; 284139; Larsen-like syndrome, B3GAT3 type.
PharmGKB; PA25217; -.
eggNOG; KOG1476; Eukaryota.
eggNOG; ENOG410XP79; LUCA.
GeneTree; ENSGT00390000017640; -.
HOVERGEN; HBG050650; -.
InParanoid; O94766; -.
KO; K10158; -.
OMA; FHTAWEP; -.
OrthoDB; EOG091G0G8P; -.
PhylomeDB; O94766; -.
TreeFam; TF313522; -.
BioCyc; MetaCyc:HS07624-MONOMER; -.
BRENDA; 2.4.1.135; 2681.
Reactome; R-HSA-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
SABIO-RK; O94766; -.
UniPathway; UPA00378; -.
ChiTaRS; B3GAT3; human.
EvolutionaryTrace; O94766; -.
GeneWiki; B3GAT3; -.
GenomeRNAi; 26229; -.
PRO; PR:O94766; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000149541; -.
CleanEx; HS_B3GAT3; -.
ExpressionAtlas; O94766; baseline and differential.
Genevisible; O94766; HS.
GO; GO:0005801; C:cis-Golgi network; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0015018; F:galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity; IBA:GO_Central.
GO; GO:0015020; F:glucuronosyltransferase activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0072542; F:protein phosphatase activator activity; IDA:UniProtKB.
GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
GO; GO:0030204; P:chondroitin sulfate metabolic process; IBA:GO_Central.
GO; GO:0050650; P:chondroitin sulfate proteoglycan biosynthetic process; IDA:MGI.
GO; GO:0050651; P:dermatan sulfate proteoglycan biosynthetic process; IDA:MGI.
GO; GO:0006024; P:glycosaminoglycan biosynthetic process; IDA:UniProtKB.
GO; GO:0030203; P:glycosaminoglycan metabolic process; TAS:Reactome.
GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IDA:MGI.
GO; GO:0043085; P:positive regulation of catalytic activity; IDA:UniProtKB.
GO; GO:0090316; P:positive regulation of intracellular protein transport; IMP:UniProtKB.
GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
CDD; cd00218; GlcAT-I; 1.
Gene3D; 3.90.550.10; -; 1.
InterPro; IPR005027; Glyco_trans_43.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
PANTHER; PTHR10896; PTHR10896; 1.
Pfam; PF03360; Glyco_transf_43; 1.
SUPFAM; SSF53448; SSF53448; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Disease mutation; Disulfide bond; Glycoprotein; Golgi apparatus;
Manganese; Membrane; Metal-binding; Reference proteome; Signal-anchor;
Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 335 Galactosylgalactosylxylosylprotein 3-
beta-glucuronosyltransferase 3.
/FTId=PRO_0000195176.
TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}.
TRANSMEM 8 28 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 29 335 Lumenal. {ECO:0000255}.
NP_BIND 82 84 UDP-glucuronate binding.
NP_BIND 194 196 UDP-glucuronate binding.
NP_BIND 308 310 UDP-glucuronate binding.
REGION 243 252 Interaction with galactose moiety of
substrate glycoprotein.
ACT_SITE 281 281 Proton donor/acceptor.
{ECO:0000269|PubMed:11950836}.
METAL 196 196 Manganese.
BINDING 113 113 UDP-glucuronate.
BINDING 156 156 UDP-glucuronate.
BINDING 161 161 UDP-glucuronate.
SITE 227 227 Interaction with galactose moiety of
substrate glycoprotein.
SITE 318 318 Interaction with galactose moiety of
substrate glycoprotein.
CARBOHYD 300 300 N-linked (GlcNAc...) asparagine.
DISULFID 33 33 Interchain.
VAR_SEQ 304 335 VLVWHTRTEKPKMKQEEQLQRQGRGSDPAIEV -> TESRC
VTQAGVQ (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056347.
VARIANT 140 140 P -> L (in JDSCD; reduced
glucuronyltransferase activity; patient
fibroblasts have decreased levels of
dermatan sulfate, chondroitin sulfate and
heparan sulfate proteoglycans;
dbSNP:rs879255269).
{ECO:0000269|PubMed:25893793}.
/FTId=VAR_075370.
VARIANT 223 223 G -> S (in JDSCD; unknown pathological
significance; dbSNP:rs372487178).
{ECO:0000269|PubMed:26086840}.
/FTId=VAR_075371.
VARIANT 277 277 R -> Q (in JDSCD; reduced
glucuronyltransferase activity; patient
fibroblasts have decreased levels of
dermatan sulfate, chondroitin sulfate and
heparan sulfate proteoglycans;
dbSNP:rs387906937).
{ECO:0000269|PubMed:21763480,
ECO:0000269|PubMed:24668659}.
/FTId=VAR_066624.
MUTAGEN 33 33 C->A: Loss of dimer formation and reduced
activity. {ECO:0000269|PubMed:10842173}.
MUTAGEN 281 281 E->A: Absence of enzymatic activity in
presence of uridine diphosphate-
glucuronic acid (UDP-GlcUA). Does not
increase PXYLP1-induced 2-phosphoxylose
phosphatase activity in presence of
uridine diphosphate-glucuronic acid (UDP-
GlcUA). {ECO:0000269|PubMed:24425863,
ECO:0000303|PubMed:24425863}.
MUTAGEN 301 301 C->A: Enzyme inactivation and loss of
glycosylation.
{ECO:0000269|PubMed:10842173}.
CONFLICT 204 204 F -> S (in Ref. 1; BAA34537).
{ECO:0000305}.
STRAND 76 83 {ECO:0000244|PDB:3CU0}.
HELIX 89 100 {ECO:0000244|PDB:3CU0}.
STRAND 103 116 {ECO:0000244|PDB:3CU0}.
HELIX 119 128 {ECO:0000244|PDB:3CU0}.
STRAND 130 136 {ECO:0000244|PDB:3CU0}.
HELIX 158 168 {ECO:0000244|PDB:3CU0}.
STRAND 174 177 {ECO:0000244|PDB:3CU0}.
STRAND 188 192 {ECO:0000244|PDB:3CU0}.
STRAND 197 199 {ECO:0000244|PDB:3CU0}.
HELIX 201 207 {ECO:0000244|PDB:3CU0}.
STRAND 211 215 {ECO:0000244|PDB:3CU0}.
STRAND 218 221 {ECO:0000244|PDB:3CU0}.
STRAND 224 232 {ECO:0000244|PDB:3CU0}.
STRAND 235 240 {ECO:0000244|PDB:3CU0}.
HELIX 253 255 {ECO:0000244|PDB:3CU0}.
STRAND 256 259 {ECO:0000244|PDB:3CU0}.
HELIX 260 265 {ECO:0000244|PDB:3CU0}.
HELIX 280 285 {ECO:0000244|PDB:3CU0}.
TURN 286 288 {ECO:0000244|PDB:3CU0}.
HELIX 291 293 {ECO:0000244|PDB:3CU0}.
HELIX 298 301 {ECO:0000244|PDB:3CU0}.
HELIX 317 323 {ECO:0000244|PDB:3CU0}.
TURN 324 326 {ECO:0000244|PDB:3CU0}.
SEQUENCE 335 AA; 37122 MW; 5EC45408597F1C0F CRC64;
MKLKLKNVFL AYFLVSIAGL LYALVQLGQP CDCLPPLRAA AEQLRQKDLR ISQLQAELRR
PPPAPAQPPE PEALPTIYVV TPTYARLVQK AELVRLSQTL SLVPRLHWLL VEDAEGPTPL
VSGLLAASGL LFTHLVVLTP KAQRLREGEP GWVHPRGVEQ RNKALDWLRG RGGAVGGEKD
PPPPGTQGVV YFADDDNTYS RELFEEMRWT RGVSVWPVGL VGGLRFEGPQ VQDGRVVGFH
TAWEPSRPFP VDMAGFAVAL PLLLDKPNAQ FDSTAPRGHL ESSLLSHLVD PKDLEPRAAN
CTRVLVWHTR TEKPKMKQEE QLQRQGRGSD PAIEV


Related products :

Catalog number Product name Quantity
20-272-191908 CD57 - Mouse monoclonal [VC1.1] to CD57; EC 2.4.1.135; Beta-1.3-glucuronyltransferase 1; Glucuronosyltransferase-P; GlcAT-P; UDP-GlcUA glycoprotein beta-1.3-glucuronyltransferase; GlcUAT-P Monoclonal 0.2 mg
B3GAT3 B3GAT1 Gene beta-1,3-glucuronyltransferase 1 (glucuronosyltransferase P)
B3GNT1 B3GAT2 Gene beta-1,3-glucuronyltransferase 2 (glucuronosyltransferase S)
B3GNT2 B3GAT3 Gene beta-1,3-glucuronyltransferase 3 (glucuronosyltransferase I)
CSB-EL002496RA Rat beta-1,3-glucuronyltransferase 1 (glucuronosyltransferase P) (B3GAT1) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL002497RA Rat beta-1,3-glucuronyltransferase 2 (glucuronosyltransferase S) (B3GAT2) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL002497DO Dog beta-1,3-glucuronyltransferase 2 (glucuronosyltransferase S) (B3GAT2) ELISA kit, Species Dog, Sample Type serum, plasma 96T
CSB-EL002496DO Dog beta-1,3-glucuronyltransferase 1 (glucuronosyltransferase P) (B3GAT1) ELISA kit, Species Dog, Sample Type serum, plasma 96T
CSB-EL002496MO Mouse beta-1,3-glucuronyltransferase 1 (glucuronosyltransferase P) (B3GAT1) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL002496HU Human beta-1,3-glucuronyltransferase 1 (glucuronosyltransferase P) (B3GAT1) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL002498HU Human beta-1,3-glucuronyltransferase 3 (glucuronosyltransferase I) (B3GAT3) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL002497HU Human beta-1,3-glucuronyltransferase 2 (glucuronosyltransferase S) (B3GAT2) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL002498MO Mouse beta-1,3-glucuronyltransferase 3 (glucuronosyltransferase I) (B3GAT3) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL002497MO Mouse beta-1,3-glucuronyltransferase 2 (glucuronosyltransferase S) (B3GAT2) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
E1079m Dog ELISA Kit FOR Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2 96T
E1060p Rat ELISA Kit FOR Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1 96T
B3GA1_MOUSE Mouse ELISA Kit FOR Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1 96T
CSB-EL002497RA Rat Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2(B3GAT2) ELISA kit 96T
CSB-EL002496RA Rat Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1(B3GAT1) ELISA kit 96T
E2012m Mouse ELISA Kit FOR Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2 96T
CSB-EL002496DO Dog Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1(B3GAT1) ELISA kit 96T
CSB-EL002497DO Dog Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2(B3GAT2) ELISA kit 96T
CSB-EL002497RA Rat Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2(B3GAT2) ELISA kit SpeciesRat 96T
CSB-EL002497MO Mouse Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2(B3GAT2) ELISA kit 96T
CSB-EL002496MO Mouse Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1(B3GAT1) ELISA kit 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur