GenomeNet

Database: UniProt/SWISS-PROT
Entry: B3GT1_HUMAN
LinkDB: B3GT1_HUMAN
Original site: B3GT1_HUMAN 
ID   B3GT1_HUMAN             Reviewed;         326 AA.
AC   Q9Y5Z6; D3DPB8; Q53SS2;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   05-DEC-2018, entry version 132.
DE   RecName: Full=Beta-1,3-galactosyltransferase 1;
DE            Short=Beta-1,3-GalTase 1;
DE            Short=Beta3Gal-T1;
DE            Short=Beta3GalT1;
DE            EC=2.4.1.86 {ECO:0000269|PubMed:9582303};
DE   AltName: Full=UDP-galactose:beta-N-acetyl-glucosamine-beta-1,3-galactosyltransferase 1;
GN   Name=B3GALT1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Colon adenocarcinoma;
RX   PubMed=10356986; DOI=10.1016/S0014-5793(99)00547-5;
RA   Bardoni A., Valli M., Trinchera M.;
RT   "Differential expression of beta1,3galactosyltransferases in human
RT   colon cells derived from adenocarcinomas or normal mucosa.";
RL   FEBS Lett. 451:75-80(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15014171; DOI=10.1093/molbev/msh100;
RA   Kitano T., Liu Y.-H., Ueda S., Saitou N.;
RT   "Human-specific amino acid changes found in 103 protein-coding
RT   genes.";
RL   Mol. Biol. Evol. 21:936-944(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX   PubMed=9582303; DOI=10.1074/jbc.273.21.12770;
RA   Amado M., Almeida R., Carneiro F., Levery S.B., Holmes E.H.,
RA   Nomoto M., Hollingsworth M.A., Hassan H., Schwientek T., Nielsen P.A.,
RA   Bennett E.P., Clausen H.;
RT   "A family of human beta3-galactosyltransferases. Characterization of
RT   four members of a UDP-galactose:beta-N-acetyl-glucosamine/beta-N-
RT   acetyl-galactosamine beta-1,3-galactosyltransferase family.";
RL   J. Biol. Chem. 273:12770-12778(1998).
CC   -!- FUNCTION: Beta-1,3-galactosyltransferase that transfers galactose
CC       from UDP-alpha-D-galactose to substrates with a terminal beta-N-
CC       acetylglucosamine (beta-GlcNAc) residue. Involved in the
CC       biosynthesis of the carbohydrate moieties of glycolipids and
CC       glycoproteins. Inactive towards substrates with terminal alpha-N-
CC       acetylglucosamine (alpha-GlcNAc) or alpha-N-acetylgalactosamine
CC       (alpha-GalNAc) residues. {ECO:0000269|PubMed:9582303}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-
CC         galactose = a beta-D-galactosyl-(1->3)-N-acetyl-beta-D-
CC         glucosaminyl derivative + H(+) + UDP; Xref=Rhea:RHEA:53432,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:61631,
CC         ChEBI:CHEBI:66914, ChEBI:CHEBI:133506; EC=2.4.1.86;
CC         Evidence={ECO:0000269|PubMed:9582303};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=90 uM for UDP-alpha-D-galactose {ECO:0000269|PubMed:9582303};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305};
CC       Single-pass type II membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Detected in brain and colon mucosa and to a
CC       lesser extent in colon adenocarcinoma cells.
CC       {ECO:0000269|PubMed:10356986, ECO:0000269|PubMed:9582303}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC       Note=Beta-1,3-galactosyltransferase 1;
CC       URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_429";
DR   EMBL; AF117222; AAD23451.1; -; mRNA.
DR   EMBL; AB041407; BAA94492.1; -; Genomic_DNA.
DR   EMBL; AC016723; AAY15002.1; -; Genomic_DNA.
DR   EMBL; CH471058; EAX11307.1; -; Genomic_DNA.
DR   EMBL; BC101545; AAI01546.1; -; mRNA.
DR   EMBL; BC104813; AAI04814.1; -; mRNA.
DR   CCDS; CCDS2227.1; -.
DR   RefSeq; NP_066191.1; NM_020981.3.
DR   RefSeq; XP_005246988.1; XM_005246931.3.
DR   RefSeq; XP_006712882.1; XM_006712819.3.
DR   RefSeq; XP_011510387.1; XM_011512085.2.
DR   UniGene; Hs.735833; -.
DR   ProteinModelPortal; Q9Y5Z6; -.
DR   SMR; Q9Y5Z6; -.
DR   BioGrid; 114251; 1.
DR   STRING; 9606.ENSP00000303740; -.
DR   BindingDB; Q9Y5Z6; -.
DR   ChEMBL; CHEMBL2321634; -.
DR   SwissLipids; SLP:000000774; -.
DR   CAZy; GT31; Glycosyltransferase Family 31.
DR   iPTMnet; Q9Y5Z6; -.
DR   PhosphoSitePlus; Q9Y5Z6; -.
DR   BioMuta; B3GALT1; -.
DR   DMDM; 61212254; -.
DR   EPD; Q9Y5Z6; -.
DR   PaxDb; Q9Y5Z6; -.
DR   PeptideAtlas; Q9Y5Z6; -.
DR   PRIDE; Q9Y5Z6; -.
DR   ProteomicsDB; 86553; -.
DR   DNASU; 8708; -.
DR   Ensembl; ENST00000392690; ENSP00000376456; ENSG00000172318.
DR   GeneID; 8708; -.
DR   KEGG; hsa:8708; -.
DR   UCSC; uc061pgb.1; human.
DR   CTD; 8708; -.
DR   DisGeNET; 8708; -.
DR   EuPathDB; HostDB:ENSG00000172318.5; -.
DR   GeneCards; B3GALT1; -.
DR   HGNC; HGNC:916; B3GALT1.
DR   MIM; 603093; gene.
DR   neXtProt; NX_Q9Y5Z6; -.
DR   OpenTargets; ENSG00000172318; -.
DR   PharmGKB; PA25209; -.
DR   eggNOG; KOG2287; Eukaryota.
DR   eggNOG; ENOG410ZZ1B; LUCA.
DR   GeneTree; ENSGT00940000156219; -.
DR   HOGENOM; HOG000059604; -.
DR   HOVERGEN; HBG101354; -.
DR   InParanoid; Q9Y5Z6; -.
DR   KO; K07819; -.
DR   OMA; HPYQNSG; -.
DR   OrthoDB; EOG091G0AXM; -.
DR   PhylomeDB; Q9Y5Z6; -.
DR   TreeFam; TF318639; -.
DR   BioCyc; MetaCyc:ENSG00000172318-MONOMER; -.
DR   BRENDA; 2.4.1.134; 2681.
DR   UniPathway; UPA00378; -.
DR   ChiTaRS; B3GALT1; human.
DR   GenomeRNAi; 8708; -.
DR   PRO; PR:Q9Y5Z6; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   Bgee; ENSG00000172318; Expressed in 74 organ(s), highest expression level in caudate nucleus.
DR   CleanEx; HS_B3GALT1; -.
DR   Genevisible; Q9Y5Z6; HS.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR   GO; GO:0008376; F:acetylgalactosaminyltransferase activity; IBA:GO_Central.
DR   GO; GO:0047275; F:glucosaminylgalactosylglucosylceramide beta-galactosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008499; F:UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0006682; P:galactosylceramide biosynthetic process; IDA:BHF-UCL.
DR   GO; GO:0030259; P:lipid glycosylation; IDA:UniProtKB.
DR   GO; GO:0009312; P:oligosaccharide biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0006486; P:protein glycosylation; IBA:GO_Central.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR   InterPro; IPR002659; Glyco_trans_31.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR11214; PTHR11214; 1.
DR   Pfam; PF01762; Galactosyl_T; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW   Manganese; Membrane; Reference proteome; Signal-anchor; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    326       Beta-1,3-galactosyltransferase 1.
FT                                /FTId=PRO_0000219145.
FT   TOPO_DOM      1      6       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM      7     26       Helical; Signal-anchor for type II
FT                                membrane protein. {ECO:0000255}.
FT   TOPO_DOM     27    326       Lumenal. {ECO:0000255}.
FT   CARBOHYD     47     47       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    151    151       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
SQ   SEQUENCE   326 AA;  37993 MW;  83271E99B2EE74F5 CRC64;
     MASKVSCLYV LTVVCWASAL WYLSITRPTS SYTGSKPFSH LTVARKNFTF GNIRTRPINP
     HSFEFLINEP NKCEKNIPFL VILISTTHKE FDARQAIRET WGDENNFKGI KIATLFLLGK
     NADPVLNQMV EQESQIFHDI IVEDFIDSYH NLTLKTLMGM RWVATFCSKA KYVMKTDSDI
     FVNMDNLIYK LLKPSTKPRR RYFTGYVING GPIRDVRSKW YMPRDLYPDS NYPPFCSGTG
     YIFSADVAEL IYKTSLHTRL LHLEDVYVGL CLRKLGIHPF QNSGFNHWKM AYSLCRYRRV
     ITVHQISPEE MHRIWNDMSS KKHLRC
//
DBGET integrated database retrieval system