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 B4GT1_HUMAN             Reviewed;         398 AA.
P15291; B2R710; D3DRL2; Q12909; Q12910; Q12911; Q14456; Q14509;
Q14523;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 5.
22-NOV-2017, entry version 197.
RecName: Full=Beta-1,4-galactosyltransferase 1;
Short=Beta-1,4-GalTase 1;
Short=Beta4Gal-T1;
Short=b4Gal-T1;
EC=2.4.1.-;
AltName: Full=UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 1;
AltName: Full=UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 1;
Includes:
RecName: Full=Lactose synthase A protein;
EC=2.4.1.22;
Includes:
RecName: Full=N-acetyllactosamine synthase;
EC=2.4.1.90;
AltName: Full=Nal synthase;
Includes:
RecName: Full=Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase;
EC=2.4.1.38;
Includes:
RecName: Full=Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase;
EC=2.4.1.-;
Contains:
RecName: Full=Processed beta-1,4-galactosyltransferase 1;
Name=B4GALT1; Synonyms=GGTB2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3144273; DOI=10.1016/S0006-291X(88)80300-0;
Masri K.A., Appert H.E., Fukuda M.N.;
"Identification of the full-length coding sequence for human
galactosyltransferase (beta-N-acetylglucosaminide: beta 1,4-
galactosyltransferase).";
Biochem. Biophys. Res. Commun. 157:657-663(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2124683; DOI=10.1093/nar/18.23.7174;
Watzele G., Berger E.G.;
"Near identity of HeLa cell galactosyltransferase with the human
placental enzyme.";
Nucleic Acids Res. 18:7174-7174(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1903938; DOI=10.1016/0006-291X(91)90423-5;
Mengle-Gaw L., McCoy-Haman M.F., Tiemeier D.C.;
"Genomic structure and expression of human beta-1,4-
galactosyltransferase.";
Biochem. Biophys. Res. Commun. 176:1269-1276(1991).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
PubMed=1384956;
Uejima T., Uemura M., Nozawa S., Narimatsu H.;
"Complementary DNA cloning for galactosyltransferase associated with
tumor and determination of antigenic epitopes recognized by specific
monoclonal antibodies.";
Cancer Res. 52:6158-6163(1992).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
PubMed=7579794; DOI=10.1093/glycob/5.4.397;
Kudo T., Narimatsu H.;
"The beta 1, 4-galactosyltransferase gene is post-transcriptionally
regulated during differentiation of mouse F9 teratocarcinoma cells.";
Glycobiology 5:397-403(1995).
[6]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fetal liver;
PubMed=7540104; DOI=10.1016/1357-2725(94)00062-G;
Chatterjee S.K., Mukerjee S., Tripathi P.K.;
"Analysis of the sequences of human beta-1,4-galactosyltransferase
cDNA clones.";
Int. J. Biochem. Cell Biol. 27:329-336(1995).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
TISSUE=Testis;
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).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[9]
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.
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 138-398, AND PARTIAL PROTEIN SEQUENCE.
PubMed=3094506; DOI=10.1016/S0006-291X(86)80094-8;
Appert H.E., Rutherford T.J., Tarr G.E., Wiest J.S., Thomford N.R.,
McCorquodale D.J.;
"Isolation of a cDNA coding for human galactosyltransferase.";
Biochem. Biophys. Res. Commun. 139:163-168(1986).
[11]
PROTEIN SEQUENCE OF 78-94.
PubMed=3091013; DOI=10.1016/0006-291X(86)90269-X;
Appert H.E., Rutherford T.J., Tarr G.E., Thomford N.R.,
McCorquodale D.J.;
"Isolation of galactosyltransferase from human milk and the
determination of its N-terminal amino acid sequence.";
Biochem. Biophys. Res. Commun. 138:224-229(1986).
[12]
PROTEIN SEQUENCE OF 274-326, CATALYTIC ACTIVITY, FUNCTION, AND
MUTAGENESIS OF TYR-282; TYR-285; TYR-307; TRP-308 AND TRP-310.
PubMed=2120039;
Aoki D., Appert H.E., Johnson D., Wong S.S., Fukuda M.N.;
"Analysis of the substrate binding sites of human
galactosyltransferase by protein engineering.";
EMBO J. 9:3171-3178(1990).
[13]
ALTERNATIVE INITIATION, AND SUBCELLULAR LOCATION.
PubMed=1714903;
Lopez L.C., Youakim A., Evans S.C., Shur B.D.;
"Evidence for a molecular distinction between Golgi and cell surface
forms of beta 1,4-galactosyltransferase.";
J. Biol. Chem. 266:15984-15991(1991).
[14]
SUBUNIT.
PubMed=7744867; DOI=10.1074/jbc.270.20.12170;
Yamaguchi N., Fukuda M.N.;
"Golgi retention mechanism of beta-1,4-galactosyltransferase.
Membrane-spanning domain-dependent homodimerization and association
with alpha- and beta-tubulins.";
J. Biol. Chem. 270:12170-12176(1995).
[15]
REVIEW.
PubMed=10580128; DOI=10.1016/S0304-4165(99)00168-3;
Amado M., Almeida R., Schwientek T., Clausen H.;
"Identification and characterization of large galactosyltransferase
gene families: galactosyltransferases for all functions.";
Biochim. Biophys. Acta 1473:35-53(1999).
[16]
INVOLVEMENT IN CDG2D.
PubMed=11901181; DOI=10.1172/JCI0214010;
Hansske B., Thiel C., Luebke T., Hasilik M., Hoening S., Peters V.,
Heidemann P.H., Hoffmann G.F., Berger E.G., von Figura K., Koerner C.;
"Deficiency of UDP-galactose:N-acetylglucosamine beta-1,4-
galactosyltransferase I causes the congenital disorder of
glycosylation type IId.";
J. Clin. Invest. 109:725-733(2002).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[19]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 126-397 OF MUTANT HIS-340 IN
COMPLEX WITH MANGANESE IONS AND N-ACETYL-D-GLUCOSAMINE, CATALYTIC
ACTIVITY, FUNCTION, COFACTOR, MUTAGENESIS OF MET-340, AND DISULFIDE
BONDS.
PubMed=16157350; DOI=10.1016/j.jmb.2005.07.050;
Ramasamy V., Ramakrishnan B., Boeggeman E., Ratner D.M.,
Seeberger P.H., Qasba P.K.;
"Oligosaccharide preferences of beta1,4-galactosyltransferase-I:
crystal structures of Met340His mutant of human beta1,4-
galactosyltransferase-I with a pentasaccharide and trisaccharides of
the N-glycan moiety.";
J. Mol. Biol. 353:53-67(2005).
[20]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 126-397 OF MUTANT HIS-340 IN
COMPLEX WITH MANGANESE IONS AND UDP, COFACTOR, AND DISULFIDE BONDS.
PubMed=16497331; DOI=10.1016/j.jmb.2006.01.088;
Ramakrishnan B., Ramasamy V., Qasba P.K.;
"Structural snapshots of beta-1,4-galactosyltransferase-I along the
kinetic pathway.";
J. Mol. Biol. 357:1619-1633(2006).
[21]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 126-398 IN COMPLEX WITH
MANGANESE IONS AND N-ACETYL-D-GLUCOSAMINE, AND COFACTOR.
PubMed=19106107; DOI=10.1074/jbc.M805782200;
Brown J.R., Yang F., Sinha A., Ramakrishnan B., Tor Y., Qasba P.K.,
Esko J.D.;
"Deoxygenated disaccharide analogs as specific inhibitors of beta1-4-
galactosyltransferase 1 and selectin-mediated tumor metastasis.";
J. Biol. Chem. 284:4952-4959(2009).
-!- FUNCTION: The Golgi complex form catalyzes the production of
lactose in the lactating mammary gland and could also be
responsible for the synthesis of complex-type N-linked
oligosaccharides in many glycoproteins as well as the carbohydrate
moieties of glycolipids.
-!- FUNCTION: The cell surface form functions as a recognition
molecule during a variety of cell to cell and cell to matrix
interactions, as those occurring during development and egg
fertilization, by binding to specific oligosaccharide ligands on
opposing cells or in the extracellular matrix.
-!- CATALYTIC ACTIVITY: UDP-alpha-D-galactose + D-glucose = UDP +
lactose.
-!- CATALYTIC ACTIVITY: UDP-alpha-D-galactose + N-acetyl-beta-D-
glucosaminylglycopeptide = UDP + beta-D-galactosyl-(1->4)-N-
acetyl-beta-D-glucosaminylglycopeptide.
-!- CATALYTIC ACTIVITY: UDP-alpha-D-galactose + N-acetyl-D-glucosamine
= UDP + N-acetyllactosamine.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:16157350,
ECO:0000269|PubMed:16497331, ECO:0000269|PubMed:19106107};
-!- PATHWAY: Protein modification; protein glycosylation.
-!- SUBUNIT: Homodimer; and heterodimer with alpha-lactalbumin to form
lactose synthase. Interacts (via N-terminal cytoplasmic domain)
with UBE2Q1 (via N-terminus); the interaction is direct (By
similarity). {ECO:0000250|UniProtKB:P15535,
ECO:0000269|PubMed:16157350, ECO:0000269|PubMed:16497331,
ECO:0000269|PubMed:19106107, ECO:0000269|PubMed:7744867}.
-!- SUBCELLULAR LOCATION: Isoform Long: Golgi apparatus, Golgi stack
membrane {ECO:0000269|PubMed:1714903}; Single-pass type II
membrane protein. Cell membrane {ECO:0000269|PubMed:1714903};
Single-pass type II membrane protein. Cell surface
{ECO:0000269|PubMed:1714903}. Cell projection, filopodium
{ECO:0000250|UniProtKB:P15535}. Note=Found in trans cisternae of
Golgi but is mainly localized at the plasma membrane
(PubMed:1714903). B4GALT1 cell surface expression is regulated by
UBE2Q1 (By similarity). {ECO:0000250|UniProtKB:P15535,
ECO:0000269|PubMed:1714903}.
-!- SUBCELLULAR LOCATION: Isoform Short: Golgi apparatus, Golgi stack
membrane {ECO:0000269|PubMed:1714903}; Single-pass type II
membrane protein. Note=Found in trans cisternae of Golgi.
{ECO:0000269|PubMed:1714903}.
-!- SUBCELLULAR LOCATION: Processed beta-1,4-galactosyltransferase 1:
Secreted {ECO:0000303|PubMed:2120039}. Note=Soluble form found in
body fluids. {ECO:0000303|PubMed:2120039}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=Long; Synonyms=Cell surface;
IsoId=P15291-1; Sequence=Displayed;
Name=Short; Synonyms=Golgi complex;
IsoId=P15291-2; Sequence=VSP_018802;
-!- TISSUE SPECIFICITY: Ubiquitously expressed, but at very low levels
in fetal and adult brain.
-!- PTM: The soluble form derives from the membrane forms by
proteolytic processing.
-!- DISEASE: Congenital disorder of glycosylation 2D (CDG2D)
[MIM:607091]: A multisystem disorder caused by a defect in
glycoprotein biosynthesis and characterized by under-glycosylated
serum glycoproteins. Congenital disorders of glycosylation result
in a wide variety of clinical features, such as defects in the
nervous system development, psychomotor retardation, dysmorphic
features, hypotonia, coagulation disorders, and immunodeficiency.
The broad spectrum of features reflects the critical role of N-
glycoproteins during embryonic development, differentiation, and
maintenance of cell functions. {ECO:0000269|PubMed:11901181}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the glycosyltransferase 7 family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
Note=Beta-1,4-galactosyltransferase 1;
URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_436";
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EMBL; X14085; CAA32247.1; -; mRNA.
EMBL; M22921; AAA35936.1; -; mRNA.
EMBL; M22921; AAA35937.1; -; mRNA.
EMBL; X55415; CAA39073.1; -; mRNA.
EMBL; X55415; CAA39074.1; -; mRNA.
EMBL; M70432; AAB00776.1; -; Genomic_DNA.
EMBL; M70427; AAB00776.1; JOINED; Genomic_DNA.
EMBL; M70428; AAB00776.1; JOINED; Genomic_DNA.
EMBL; M70429; AAB00776.1; JOINED; Genomic_DNA.
EMBL; M70430; AAB00776.1; JOINED; Genomic_DNA.
EMBL; M70431; AAB00776.1; JOINED; Genomic_DNA.
EMBL; X13223; CAA31611.1; -; mRNA.
EMBL; D29805; BAA06188.1; -; mRNA.
EMBL; U10472; AAA68218.1; -; mRNA.
EMBL; U10473; AAA68219.1; -; mRNA.
EMBL; U10474; AAA68220.1; -; mRNA.
EMBL; CH471071; EAW58520.1; -; Genomic_DNA.
EMBL; CH471071; EAW58521.1; -; Genomic_DNA.
EMBL; AK312797; BAG35657.1; -; mRNA.
EMBL; AL161445; CAD13306.1; -; Genomic_DNA.
EMBL; M13701; AAA35935.1; -; mRNA.
CCDS; CCDS6535.1; -. [P15291-1]
PIR; JQ1030; JQ1030.
RefSeq; NP_001488.2; NM_001497.3. [P15291-1]
UniGene; Hs.272011; -.
PDB; 2AE7; X-ray; 2.00 A; A/B/C=126-398.
PDB; 2AEC; X-ray; 2.00 A; A/B/C=126-398.
PDB; 2AES; X-ray; 2.00 A; A/B/C=126-398.
PDB; 2AGD; X-ray; 1.90 A; A/B/C=126-398.
PDB; 2AH9; X-ray; 2.00 A; A/B/C=126-398.
PDB; 2FY7; X-ray; 1.70 A; A=126-398.
PDB; 2FYA; X-ray; 1.90 A; A=126-398.
PDB; 2FYB; X-ray; 1.90 A; A=126-398.
PDB; 3EE5; X-ray; 2.20 A; A/B/C=126-398.
PDB; 4EE3; X-ray; 2.30 A; A/B/C=126-398.
PDB; 4EE4; X-ray; 1.95 A; A/B/C=126-398.
PDB; 4EE5; X-ray; 2.20 A; A/B/C=126-398.
PDB; 4EEA; X-ray; 2.00 A; A/B/C=126-398.
PDB; 4EEG; X-ray; 2.20 A; A/B/C=126-398.
PDB; 4EEM; X-ray; 2.20 A; A/B/C=126-398.
PDB; 4EEO; X-ray; 2.30 A; A/B/C=126-398.
PDB; 4L41; X-ray; 2.70 A; C=126-398.
PDBsum; 2AE7; -.
PDBsum; 2AEC; -.
PDBsum; 2AES; -.
PDBsum; 2AGD; -.
PDBsum; 2AH9; -.
PDBsum; 2FY7; -.
PDBsum; 2FYA; -.
PDBsum; 2FYB; -.
PDBsum; 3EE5; -.
PDBsum; 4EE3; -.
PDBsum; 4EE4; -.
PDBsum; 4EE5; -.
PDBsum; 4EEA; -.
PDBsum; 4EEG; -.
PDBsum; 4EEM; -.
PDBsum; 4EEO; -.
PDBsum; 4L41; -.
ProteinModelPortal; P15291; -.
SMR; P15291; -.
BioGrid; 108950; 28.
IntAct; P15291; 4.
MINT; MINT-5004065; -.
STRING; 9606.ENSP00000369055; -.
BindingDB; P15291; -.
ChEMBL; CHEMBL4384; -.
DrugBank; DB03814; 2-(N-Morpholino)-Ethanesulfonic Acid.
DrugBank; DB03013; Di(N-Acetyl-D-Glucosamine).
DrugBank; DB03501; Galactose-uridine-5'-diphosphate.
DrugBank; DB00141; N-Acetyl-D-glucosamine.
DrugBank; DB03685; Uridine-5'-Monophosphate.
CAZy; GT7; Glycosyltransferase Family 7.
iPTMnet; P15291; -.
PhosphoSitePlus; P15291; -.
SwissPalm; P15291; -.
BioMuta; B4GALT1; -.
DMDM; 116241264; -.
EPD; P15291; -.
MaxQB; P15291; -.
PaxDb; P15291; -.
PeptideAtlas; P15291; -.
PRIDE; P15291; -.
DNASU; 2683; -.
Ensembl; ENST00000379731; ENSP00000369055; ENSG00000086062. [P15291-1]
GeneID; 2683; -.
KEGG; hsa:2683; -.
UCSC; uc003zsg.3; human. [P15291-1]
CTD; 2683; -.
DisGeNET; 2683; -.
EuPathDB; HostDB:ENSG00000086062.12; -.
GeneCards; B4GALT1; -.
GeneReviews; B4GALT1; -.
HGNC; HGNC:924; B4GALT1.
HPA; HPA010806; -.
HPA; HPA010807; -.
MalaCards; B4GALT1; -.
MIM; 137060; gene.
MIM; 607091; phenotype.
neXtProt; NX_P15291; -.
OpenTargets; ENSG00000086062; -.
Orphanet; 79332; B4GALT1-CDG.
PharmGKB; PA25223; -.
eggNOG; KOG3916; Eukaryota.
eggNOG; ENOG410ZYYA; LUCA.
GeneTree; ENSGT00760000119140; -.
HOVERGEN; HBG058334; -.
InParanoid; P15291; -.
KO; K07966; -.
OMA; AHTRETM; -.
OrthoDB; EOG091G0P66; -.
PhylomeDB; P15291; -.
TreeFam; TF312834; -.
BioCyc; MetaCyc:HS01519-MONOMER; -.
BRENDA; 2.4.1.133; 2681.
BRENDA; 2.4.1.38; 2681.
Reactome; R-HSA-1300644; Interaction With The Zona Pellucida.
Reactome; R-HSA-1912420; Pre-NOTCH Processing in Golgi.
Reactome; R-HSA-2022854; Keratan sulfate biosynthesis.
Reactome; R-HSA-3656244; Defective B4GALT1 causes B4GALT1-CDG (CDG-2d).
Reactome; R-HSA-4793953; Defective B4GALT1 causes B4GALT1-CDG (CDG-2d).
Reactome; R-HSA-5653890; Lactose synthesis.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-975577; N-Glycan antennae elongation.
UniPathway; UPA00378; -.
ChiTaRS; B4GALT1; human.
EvolutionaryTrace; P15291; -.
GeneWiki; B4GALT1; -.
GenomeRNAi; 2683; -.
PRO; PR:P15291; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000086062; -.
CleanEx; HS_B4GALT1; -.
ExpressionAtlas; P15291; baseline and differential.
Genevisible; P15291; HS.
GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
GO; GO:0031526; C:brush border membrane; IDA:UniProtKB.
GO; GO:0030057; C:desmosome; IDA:UniProtKB.
GO; GO:0009897; C:external side of plasma membrane; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0000138; C:Golgi trans cisterna; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
GO; GO:0043014; F:alpha-tubulin binding; IDA:UniProtKB.
GO; GO:0003831; F:beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity; IDA:UniProtKB.
GO; GO:0048487; F:beta-tubulin binding; IPI:UniProtKB.
GO; GO:0008092; F:cytoskeletal protein binding; IEA:Ensembl.
GO; GO:0008378; F:galactosyltransferase activity; NAS:UniProtKB.
GO; GO:0004461; F:lactose synthase activity; IDA:UniProtKB.
GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
GO; GO:0003945; F:N-acetyllactosamine synthase activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0035250; F:UDP-galactosyltransferase activity; IDA:UniProtKB.
GO; GO:0002526; P:acute inflammatory response; IEA:Ensembl.
GO; GO:0060055; P:angiogenesis involved in wound healing; IEA:Ensembl.
GO; GO:0007339; P:binding of sperm to zona pellucida; TAS:Reactome.
GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IEA:Ensembl.
GO; GO:0007155; P:cell adhesion; IEA:Ensembl.
GO; GO:0045136; P:development of secondary sexual characteristics; IEA:Ensembl.
GO; GO:0002064; P:epithelial cell development; IEA:Ensembl.
GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
GO; GO:0006012; P:galactose metabolic process; IEA:Ensembl.
GO; GO:0018146; P:keratan sulfate biosynthetic process; TAS:Reactome.
GO; GO:0005989; P:lactose biosynthetic process; TAS:Reactome.
GO; GO:0050900; P:leukocyte migration; IEA:Ensembl.
GO; GO:0030879; P:mammary gland development; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0009312; P:oligosaccharide biosynthetic process; IDA:UniProtKB.
GO; GO:0007341; P:penetration of zona pellucida; IEA:Ensembl.
GO; GO:0060058; P:positive regulation of apoptotic process involved in mammary gland involution; IEA:Ensembl.
GO; GO:0060054; P:positive regulation of epithelial cell proliferation involved in wound healing; IEA:Ensembl.
GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
GO; GO:0006487; P:protein N-linked glycosylation; IDA:UniProtKB.
GO; GO:0060046; P:regulation of acrosome reaction; IEA:Ensembl.
GO; GO:0051270; P:regulation of cellular component movement; IEA:Ensembl.
Gene3D; 3.90.550.10; -; 1.
InterPro; IPR003859; Galactosyl_T.
InterPro; IPR027791; Galactosyl_T_C.
InterPro; IPR027995; Galactosyl_T_N.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
PANTHER; PTHR19300; PTHR19300; 1.
Pfam; PF02709; Glyco_transf_7C; 1.
Pfam; PF13733; Glyco_transf_7N; 1.
PRINTS; PR02050; B14GALTRFASE.
SUPFAM; SSF53448; SSF53448; 1.
1: Evidence at protein level;
3D-structure; Alternative initiation; Cell membrane; Cell projection;
Complete proteome; Congenital disorder of glycosylation;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Glycosyltransferase; Golgi apparatus; Manganese; Membrane;
Metal-binding; Polymorphism; Reference proteome; Secreted;
Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 398 Beta-1,4-galactosyltransferase 1.
/FTId=PRO_0000012278.
CHAIN ? 398 Processed beta-1,4-galactosyltransferase
1.
/FTId=PRO_0000296229.
TOPO_DOM 1 24 Cytoplasmic. {ECO:0000255}.
TRANSMEM 25 44 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 45 398 Lumenal. {ECO:0000255}.
REGION 183 187 UDP-alpha-D-galactose binding.
REGION 222 224 UDP-alpha-D-galactose binding.
{ECO:0000250}.
REGION 249 250 UDP-alpha-D-galactose binding.
REGION 312 315 N-acetyl-D-glucosamine binding.
REGION 343 346 UDP-alpha-D-galactose binding.
METAL 250 250 Manganese.
METAL 343 343 Manganese; via tele nitrogen.
BINDING 310 310 UDP-alpha-D-galactose.
{ECO:0000269|PubMed:16497331}.
BINDING 355 355 N-acetyl-D-glucosamine.
{ECO:0000269|PubMed:16157350,
ECO:0000269|PubMed:19106107}.
SITE 77 78 Cleavage; to produce soluble form.
CARBOHYD 113 113 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 130 172
DISULFID 243 262
VAR_SEQ 1 13 Missing (in isoform Short).
{ECO:0000305}.
/FTId=VSP_018802.
VARIANT 21 21 R -> W (in dbSNP:rs1065764).
/FTId=VAR_054019.
VARIANT 257 257 H -> R (in dbSNP:rs9169).
/FTId=VAR_054020.
MUTAGEN 282 282 Y->G: Reduction in N-acetylglucosamine
binding. {ECO:0000269|PubMed:2120039}.
MUTAGEN 285 285 Y->F: No change in enzymatic activity.
{ECO:0000269|PubMed:2120039}.
MUTAGEN 307 307 Y->G: Reduction in N-acetylglucosamine
and UDP-galactose binding.
{ECO:0000269|PubMed:2120039}.
MUTAGEN 308 308 W->G: Reduction in N-acetylglucosamine
binding. {ECO:0000269|PubMed:2120039}.
MUTAGEN 310 310 W->G: Reduction in N-acetylglucosamine
binding. {ECO:0000269|PubMed:2120039}.
MUTAGEN 340 340 M->H: Favors the closed conformation of
the enzyme.
{ECO:0000269|PubMed:16157350}.
CONFLICT 10 10 G -> R (in Ref. 4; CAA31611 and 5;
BAA06188). {ECO:0000305}.
CONFLICT 11 11 Missing (in Ref. 1; AAA35936, 3; AAB00776
and 6; AAA68220). {ECO:0000305}.
CONFLICT 31 32 AL -> VW (in Ref. 1; AAA35936/AAA35937
and 6; AAA68220). {ECO:0000305}.
CONFLICT 35 35 G -> R (in Ref. 4; CAA31611).
{ECO:0000305}.
CONFLICT 76 76 E -> D (in Ref. 5; BAA06188).
{ECO:0000305}.
CONFLICT 91 115 SSQPRPGGDSSPVVDSGPGPASNLT -> GKHAKSSFKQFL
LQIKELSNPIDLD (in Ref. 6; AAA68219).
{ECO:0000305}.
CONFLICT 212 212 Y -> YGIY (in Ref. 1; CAA32247 and 3;
AAB00776). {ECO:0000305}.
CONFLICT 260 260 Y -> D (in Ref. 6; AAA68218).
{ECO:0000305}.
CONFLICT 292 292 L -> S (in Ref. 5; BAA06188).
{ECO:0000305}.
CONFLICT 337 337 R -> T (in Ref. 5; BAA06188).
{ECO:0000305}.
CONFLICT 340 341 MI -> PA (in Ref. 6; AAA68220).
{ECO:0000305}.
HELIX 151 157 {ECO:0000244|PDB:2FY7}.
TURN 163 165 {ECO:0000244|PDB:2FY7}.
STRAND 170 173 {ECO:0000244|PDB:2FY7}.
STRAND 177 186 {ECO:0000244|PDB:2FY7}.
HELIX 188 204 {ECO:0000244|PDB:2FY7}.
STRAND 208 216 {ECO:0000244|PDB:2FY7}.
STRAND 218 220 {ECO:0000244|PDB:2FY7}.
HELIX 224 238 {ECO:0000244|PDB:2FY7}.
STRAND 243 247 {ECO:0000244|PDB:2FY7}.
STRAND 251 255 {ECO:0000244|PDB:2FY7}.
HELIX 274 276 {ECO:0000244|PDB:2FY7}.
STRAND 288 293 {ECO:0000244|PDB:2FY7}.
HELIX 294 299 {ECO:0000244|PDB:2FY7}.
STRAND 309 312 {ECO:0000244|PDB:2AGD}.
HELIX 313 323 {ECO:0000244|PDB:2FY7}.
TURN 333 335 {ECO:0000244|PDB:2FY7}.
STRAND 337 340 {ECO:0000244|PDB:2FY7}.
HELIX 347 349 {ECO:0000244|PDB:4L41}.
HELIX 359 365 {ECO:0000244|PDB:2FY7}.
TURN 366 368 {ECO:0000244|PDB:2FY7}.
HELIX 371 373 {ECO:0000244|PDB:2FY7}.
STRAND 377 384 {ECO:0000244|PDB:2FY7}.
STRAND 387 393 {ECO:0000244|PDB:2FY7}.
SEQUENCE 398 AA; 43920 MW; 29B224C83C61E165 CRC64;
MRLREPLLSG SAAMPGASLQ RACRLLVAVC ALHLGVTLVY YLAGRDLSRL PQLVGVSTPL
QGGSNSAAAI GQSSGELRTG GARPPPPLGA SSQPRPGGDS SPVVDSGPGP ASNLTSVPVP
HTTALSLPAC PEESPLLVGP MLIEFNMPVD LELVAKQNPN VKMGGRYAPR DCVSPHKVAI
IIPFRNRQEH LKYWLYYLHP VLQRQQLDYG IYVINQAGDT IFNRAKLLNV GFQEALKDYD
YTCFVFSDVD LIPMNDHNAY RCFSQPRHIS VAMDKFGFSL PYVQYFGGVS ALSKQQFLTI
NGFPNNYWGW GGEDDDIFNR LVFRGMSISR PNAVVGRCRM IRHSRDKKNE PNPQRFDRIA
HTKETMLSDG LNSLTYQVLD VQRYPLYTQI TVDIGTPS


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