GenomeNet

Database: UniProt/SWISS-PROT UniProt/TrEMBL
Entry: B3GT4_HUMAN Q5STJ7_HUMAN B3KQP5_HUMAN
LinkDB: B3GT4_HUMAN Q5STJ7_HUMAN B3KQP5_HUMAN
Original site: B3GT4_HUMAN Q5STJ7_HUMAN B3KQP5_HUMAN 
ID   B3GT4_HUMAN             Reviewed;         378 AA.
AC   O96024;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-OCT-2017, entry version 133.
DE   RecName: Full=Beta-1,3-galactosyltransferase 4;
DE            Short=Beta-1,3-GalTase 4;
DE            Short=Beta3Gal-T4;
DE            Short=Beta3GalT4;
DE            Short=GalT4;
DE            Short=b3Gal-T4;
DE            EC=2.4.1.62 {ECO:0000269|PubMed:9582303};
DE   AltName: Full=Gal-T2;
DE   AltName: Full=Ganglioside galactosyltransferase;
DE   AltName: Full=UDP-galactose:beta-N-acetyl-galactosamine-beta-1,3-galactosyltransferase;
GN   Name=B3GALT4; Synonyms=GALT4;
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], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Fetal brain;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=10663566; DOI=10.1007/s002510050012;
RA   Shiina T., Kikkawa E., Iwasaki H., Kaneko M., Narimatsu H., Sasaki K.,
RA   Bahram S., Inoko H.;
RT   "The beta 1,3-galactosyltransferase-4 (b3Gal-T4) gene is located in
RT   the centromeric segment of the human MHC class II region.";
RL   Immunogenetics 51:75-78(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA   Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA   Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA   Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA   Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA   Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA   Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA   Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA   Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA   Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA   Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA   Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA   Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA   McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA   Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA   Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA   Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA   Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA   Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA   Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA   Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA   Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA   Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA   Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Fetal 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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Involved in GM1/GD1B/GA1 ganglioside biosynthesis.
CC       {ECO:0000269|PubMed:9582303}.
CC   -!- CATALYTIC ACTIVITY: UDP-alpha-D-galactose + an N-acetyl-beta-D-
CC       galactosaminyl-(1->4)-(alpha-N-acetylneuraminyl-(2->3))-beta-D-
CC       galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide = UDP + a beta-
CC       D-galactosyl-(1->3)-N-acetyl-beta-D-galactosaminyl-(1->4)-(alpha-
CC       N-acetylneuraminyl-(2->3))-beta-D-galactosyl-(1->4)-beta-D-
CC       glucosyl-(1<->1)-ceramide. {ECO:0000269|PubMed:9582303}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type
CC       II membrane protein.
CC   -!- TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle and
CC       pancreas and, to a lesser extent, in brain, placenta, kidney,
CC       liver and lung. {ECO:0000269|PubMed:10663566,
CC       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 4;
CC       URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_431";
DR   EMBL; Y15061; CAA75345.1; -; mRNA.
DR   EMBL; AL031228; CAA20230.1; -; Genomic_DNA.
DR   EMBL; AB026730; BAA88988.1; -; mRNA.
DR   EMBL; BC032574; AAH32574.1; -; mRNA.
DR   CCDS; CCDS34425.1; -.
DR   RefSeq; NP_003773.1; NM_003782.3.
DR   UniGene; Hs.534375; -.
DR   ProteinModelPortal; O96024; -.
DR   BioGrid; 114248; 3.
DR   IntAct; O96024; 4.
DR   MINT; MINT-1387639; -.
DR   STRING; 9606.ENSP00000390784; -.
DR   SwissLipids; SLP:000000772; -.
DR   CAZy; GT31; Glycosyltransferase Family 31.
DR   iPTMnet; O96024; -.
DR   PhosphoSitePlus; O96024; -.
DR   BioMuta; B3GALT4; -.
DR   PaxDb; O96024; -.
DR   PeptideAtlas; O96024; -.
DR   PRIDE; O96024; -.
DR   DNASU; 8705; -.
DR   Ensembl; ENST00000383209; ENSP00000372696; ENSG00000206285.
DR   Ensembl; ENST00000415322; ENSP00000394876; ENSG00000226936.
DR   Ensembl; ENST00000419471; ENSP00000398660; ENSG00000235155.
DR   Ensembl; ENST00000430971; ENSP00000414880; ENSG00000236802.
DR   Ensembl; ENST00000451237; ENSP00000390784; ENSG00000235863.
DR   GeneID; 8705; -.
DR   KEGG; hsa:8705; -.
DR   CTD; 8705; -.
DR   DisGeNET; 8705; -.
DR   EuPathDB; HostDB:ENSG00000235863.3; -.
DR   GeneCards; B3GALT4; -.
DR   HGNC; HGNC:919; B3GALT4.
DR   HPA; HPA043001; -.
DR   MIM; 603095; gene.
DR   neXtProt; NX_O96024; -.
DR   OpenTargets; ENSG00000235863; -.
DR   PharmGKB; PA25212; -.
DR   eggNOG; KOG2287; Eukaryota.
DR   eggNOG; ENOG410ZZ1B; LUCA.
DR   GeneTree; ENSGT00760000118879; -.
DR   HOGENOM; HOG000064523; -.
DR   HOVERGEN; HBG050651; -.
DR   InParanoid; O96024; -.
DR   KO; K00715; -.
DR   OMA; PFCSWLQ; -.
DR   OrthoDB; EOG091G0AXM; -.
DR   PhylomeDB; O96024; -.
DR   TreeFam; TF318639; -.
DR   BRENDA; 2.4.1.62; 2681.
DR   UniPathway; UPA00378; -.
DR   GeneWiki; B3GALT4; -.
DR   GenomeRNAi; 8705; -.
DR   PRO; PR:O96024; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   Bgee; ENSG00000235863; -.
DR   CleanEx; HS_B3GALT4; -.
DR   ExpressionAtlas; O96024; baseline and differential.
DR   Genevisible; O96024; HS.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0047915; F:ganglioside galactosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008499; F:UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity; IDA:BHF-UCL.
DR   GO; GO:0001574; P:ganglioside biosynthetic process; IDA:BHF-UCL.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR002659; Glyco_trans_31.
DR   PANTHER; PTHR11214; PTHR11214; 1.
DR   Pfam; PF01762; Galactosyl_T; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW   Membrane; Reference proteome; Signal-anchor; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    378       Beta-1,3-galactosyltransferase 4.
FT                                /FTId=PRO_0000219160.
FT   TOPO_DOM      1      8       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM      9     19       Helical; Signal-anchor for type II
FT                                membrane protein. {ECO:0000255}.
FT   TOPO_DOM     20    378       Lumenal. {ECO:0000255}.
FT   CARBOHYD    149    149       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
SQ   SEQUENCE   378 AA;  41537 MW;  4E55DFC72AE96213 CRC64;
     MQLRLFRRLL LAALLLVIVW TLFGPSGLGE ELLSLSLASL LPAPASPGPP LALPRLLIPN
     QEACSGPGAP PFLLILVCTA PENLNQRNAI RASWGGLREA RGLRVQTLFL LGEPNAQHPV
     WGSQGSDLAS ESAAQGDILQ AAFQDSYRNL TLKTLSGLNW AEKHCPMARY VLKTDDDVYV
     NVPELVSELV LRGGRWGQWE RSTEPQREAE QEGGQVLHSE EVPLLYLGRV HWRVNPSRTP
     GGRHRVSEEQ WPHTWGPFPP YASGTGYVLS ASAVQLILKV ASRAPLLPLE DVFVGVSARR
     GGLAPTQCVK LAGATHYPLD RCCYGKFLLT SHRLDPWKMQ EAWKLVGGSD GERTAPFCSW
     FQGVLGILRC RAIAWLQS
//
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Ontology (7)   
   GO (6)   
   CAZY (1)   
Disease (1)   
   OMIM (1)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (20)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   UniGene (1)   
   HGNC (1)   
   ENSEMBL-UP (15)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (4)   
   EMBL (4)   
Protein domain (3)   
   InterPro (1)   
   Pfam (1)   
   PROSITE (1)   
Literature (4)   
   PubMed (4)   
Enzyme (1)   
   BRENDA (1)   
All databases (42)   

Download RDF
ID   Q5STJ7_HUMAN            Unreviewed;       378 AA.
AC   Q5STJ7;
DT   10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2005, sequence version 1.
DT   25-OCT-2017, entry version 109.
DE   RecName: Full=Hexosyltransferase {ECO:0000256|RuleBase:RU363063};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU363063};
GN   Name=B3GALT4 {ECO:0000313|EMBL:ACN81315.1};
GN   ORFNames=hCG_17511 {ECO:0000313|EMBL:EAX03700.1};
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 {ECO:0000313|EMBL:ACN81315.1};
RN   [1] {ECO:0000313|EMBL:EAX03700.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=11181995; DOI=10.1126/science.1058040;
RA   Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G.,
RA   Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D.,
RA   Amanatides P., Ballew R.M., Huson D.H., Wortman J.R., Zhang Q.,
RA   Kodira C.D., Zheng X.H., Chen L., Skupski M., Subramanian G.,
RA   Thomas P.D., Zhang J., Gabor Miklos G.L., Nelson C., Broder S.,
RA   Clark A.G., Nadeau J., McKusick V.A., Zinder N., Levine A.J.,
RA   Roberts R.J., Simon M., Slayman C., Hunkapiller M., Bolanos R.,
RA   Delcher A., Dew I., Fasulo D., Flanigan M., Florea L., Halpern A.,
RA   Hannenhalli S., Kravitz S., Levy S., Mobarry C., Reinert K.,
RA   Remington K., Abu-Threideh J., Beasley E., Biddick K., Bonazzi V.,
RA   Brandon R., Cargill M., Chandramouliswaran I., Charlab R.,
RA   Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K.,
RA   Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z.,
RA   Guan P., Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A.,
RA   Lai Z., Lei Y., Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V.,
RA   Milshina N., Moore H.M., Naik A.K., Narayan V.A., Neelam B.,
RA   Nusskern D., Rusch D.B., Salzberg S., Shao W., Shue B., Sun J.,
RA   Wang Z., Wang A., Wang X., Wang J., Wei M., Wides R., Xiao C., Yan C.,
RA   Yao A., Ye J., Zhan M., Zhang W., Zhang H., Zhao Q., Zheng L.,
RA   Zhong F., Zhong W., Zhu S., Zhao S., Gilbert D., Baumhueter S.,
RA   Spier G., Carter C., Cravchik A., Woodage T., Ali F., An H., Awe A.,
RA   Baldwin D., Baden H., Barnstead M., Barrow I., Beeson K., Busam D.,
RA   Carver A., Center A., Cheng M.L., Curry L., Danaher S., Davenport L.,
RA   Desilets R., Dietz S., Dodson K., Doup L., Ferriera S., Garg N.,
RA   Gluecksmann A., Hart B., Haynes J., Haynes C., Heiner C., Hladun S.,
RA   Hostin D., Houck J., Howland T., Ibegwam C., Johnson J., Kalush F.,
RA   Kline L., Koduru S., Love A., Mann F., May D., McCawley S.,
RA   McIntosh T., McMullen I., Moy M., Moy L., Murphy B., Nelson K.,
RA   Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M.,
RA   Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C.,
RA   Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N.,
RA   Tse S., Vech C., Wang G., Wetter J., Williams S., Williams M.,
RA   Windsor S., Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F.,
RA   Guigo R., Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A.,
RA   Mi H., Lazareva B., Hatton T., Narechania A., Diemer K.,
RA   Muruganujan A., Guo N., Sato S., Bafna V., Istrail S., Lippert R.,
RA   Schwartz R., Walenz B., Yooseph S., Allen D., Basu A., Baxendale J.,
RA   Blick L., Caminha M., Carnes-Stine J., Caulk P., Chiang Y.H.,
RA   Coyne M., Dahlke C., Mays A., Dombroski M., Donnelly M., Ely D.,
RA   Esparham S., Fosler C., Gire H., Glanowski S., Glasser K., Glodek A.,
RA   Gorokhov M., Graham K., Gropman B., Harris M., Heil J., Henderson S.,
RA   Hoover J., Jennings D., Jordan C., Jordan J., Kasha J., Kagan L.,
RA   Kraft C., Levitsky A., Lewis M., Liu X., Lopez J., Ma D., Majoros W.,
RA   McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N., Nodell M.,
RA   Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J.,
RA   Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E.,
RA   Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.;
RT   "The sequence of the human genome.";
RL   Science 291:1304-1351(2001).
RN   [2] {ECO:0000313|EMBL:CAG33374.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:EAX03700.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:BAG38014.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Synovial membrane tissue {ECO:0000313|EMBL:BAG38014.1};
RA   Wakamatsu A., Yamamoto J., Kimura K., Kaida T., Tsuchiya K., Iida Y.,
RA   Takayama Y., Murakawa K., Kanehori K., Andoh T., Kagawa N., Sato R.,
RA   Kawamura Y., Tanaka S., Kisu Y., Sugano S., Goshima N., Nomura N.,
RA   Isogai T.;
RT   "NEDO functional analysis of protein and research application
RT   project.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:ACN81315.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Rieder M.J., Bertucci C., Stanaway I.B., Johnson E.J., Swanson J.E.,
RA   Siegel D.L., da Ponte S.H., Igartua C., Patterson K., Nickerson D.A.;
RL   Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|EMBL:AQY76665.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Norman P.J., Norberg S.J., Nemat-Gorgani N., Ronaghi M., Parham P.;
RT   "CDS alleles of MHC region genes derived from homozygous
RT   individuals.";
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000256|RuleBase:RU363063}; Single-pass type II membrane
CC       protein {ECO:0000256|RuleBase:RU363063}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC       {ECO:0000256|RuleBase:RU363063}.
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DR   EMBL; FJ525877; ACN81315.1; -; Genomic_DNA.
DR   EMBL; KY500161; AQY76665.1; -; Genomic_DNA.
DR   EMBL; KY500162; AQY76666.1; -; Genomic_DNA.
DR   EMBL; AK315647; BAG38014.1; -; mRNA.
DR   EMBL; CR457093; CAG33374.1; -; mRNA.
DR   EMBL; CH471081; EAX03700.1; -; Genomic_DNA.
DR   RefSeq; NP_003773.1; NM_003782.3.
DR   UniGene; Hs.534375; -.
DR   CAZy; GT31; Glycosyltransferase Family 31.
DR   DNASU; 8705; -.
DR   GeneID; 8705; -.
DR   KEGG; hsa:8705; -.
DR   UCSC; uc003odr.4; human.
DR   CTD; 8705; -.
DR   EuPathDB; HostDB:ENSG00000235863.3; -.
DR   PharmGKB; PA25212; -.
DR   eggNOG; KOG2287; Eukaryota.
DR   eggNOG; ENOG410ZZ1B; LUCA.
DR   HOVERGEN; HBG050651; -.
DR   KO; K00715; -.
DR   OMA; PFCSWLQ; -.
DR   OrthoDB; EOG091G0AXM; -.
DR   GenomeRNAi; 8705; -.
DR   Bgee; ENSG00000235863; -.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008378; F:galactosyltransferase activity; IEA:InterPro.
DR   GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR   InterPro; IPR002659; Glyco_trans_31.
DR   PANTHER; PTHR11214; PTHR11214; 1.
DR   Pfam; PF01762; Galactosyl_T; 1.
PE   2: Evidence at transcript level;
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU363063,
KW   ECO:0000256|SAAS:SAAS00100863, ECO:0000313|EMBL:ACN81315.1};
KW   Golgi apparatus {ECO:0000256|RuleBase:RU363063,
KW   ECO:0000256|SAAS:SAAS00100862};
KW   Membrane {ECO:0000256|SAAS:SAAS00100854};
KW   Transferase {ECO:0000256|SAAS:SAAS00100874,
KW   ECO:0000313|EMBL:ACN81315.1};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00100864};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00100856}.
SQ   SEQUENCE   378 AA;  41537 MW;  4E55DFC72AE96213 CRC64;
     MQLRLFRRLL LAALLLVIVW TLFGPSGLGE ELLSLSLASL LPAPASPGPP LALPRLLIPN
     QEACSGPGAP PFLLILVCTA PENLNQRNAI RASWGGLREA RGLRVQTLFL LGEPNAQHPV
     WGSQGSDLAS ESAAQGDILQ AAFQDSYRNL TLKTLSGLNW AEKHCPMARY VLKTDDDVYV
     NVPELVSELV LRGGRWGQWE RSTEPQREAE QEGGQVLHSE EVPLLYLGRV HWRVNPSRTP
     GGRHRVSEEQ WPHTWGPFPP YASGTGYVLS ASAVQLILKV ASRAPLLPLE DVFVGVSARR
     GGLAPTQCVK LAGATHYPLD RCCYGKFLLT SHRLDPWKMQ EAWKLVGGSD GERTAPFCSW
     FQGVLGILRC RAIAWLQS
//
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Ontology (5)   
   GO (4)   
   CAZY (1)   
Gene (4)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   UniGene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (6)   
   EMBL (6)   
Protein domain (2)   
   InterPro (1)   
   Pfam (1)   
Literature (1)   
   PubMed (1)   
All databases (19)   

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ID   B3KQP5_HUMAN            Unreviewed;       378 AA.
AC   B3KQP5;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   05-JUL-2017, entry version 45.
DE   RecName: Full=Hexosyltransferase {ECO:0000256|RuleBase:RU363063};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU363063};
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 {ECO:0000313|EMBL:BAG52107.1};
RN   [1] {ECO:0000313|EMBL:BAG52107.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA   Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA   Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA   Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA   Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA   Isogai T.;
RT   "Signal sequence and keyword trap in silico for selection of full-
RT   length human cDNAs encoding secretion or membrane proteins from oligo-
RT   capped cDNA libraries.";
RL   DNA Res. 12:117-126(2005).
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000256|RuleBase:RU363063}; Single-pass type II membrane
CC       protein {ECO:0000256|RuleBase:RU363063}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC       {ECO:0000256|RuleBase:RU363063}.
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DR   EMBL; AK075312; BAG52107.1; -; mRNA.
DR   RefSeq; NP_003773.1; NM_003782.3.
DR   UniGene; Hs.534375; -.
DR   PaxDb; B3KQP5; -.
DR   PRIDE; B3KQP5; -.
DR   DNASU; 8705; -.
DR   GeneID; 8705; -.
DR   KEGG; hsa:8705; -.
DR   CTD; 8705; -.
DR   PharmGKB; PA25212; -.
DR   eggNOG; KOG2287; Eukaryota.
DR   eggNOG; ENOG410ZZ1B; LUCA.
DR   HOVERGEN; HBG050651; -.
DR   KO; K00715; -.
DR   GenomeRNAi; 8705; -.
DR   Genevisible; B3KQP5; HS.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008378; F:galactosyltransferase activity; IEA:InterPro.
DR   GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR   InterPro; IPR002659; Glyco_trans_31.
DR   PANTHER; PTHR11214; PTHR11214; 1.
DR   Pfam; PF01762; Galactosyl_T; 1.
PE   2: Evidence at transcript level;
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU363063,
KW   ECO:0000256|SAAS:SAAS00100863, ECO:0000313|EMBL:BAG52107.1};
KW   Golgi apparatus {ECO:0000256|RuleBase:RU363063,
KW   ECO:0000256|SAAS:SAAS00100862};
KW   Membrane {ECO:0000256|SAAS:SAAS00100854};
KW   Transferase {ECO:0000256|SAAS:SAAS00100874,
KW   ECO:0000313|EMBL:BAG52107.1};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00100864};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00100856}.
SQ   SEQUENCE   378 AA;  41438 MW;  BB5A6FC8954C78B9 CRC64;
     MQLRLFRRLL LAALLLVIVW TLFGPSGLGE ELLSLSLASL LPAPASPGPP LALPRLLIPN
     QEACSGPGAP PFLLILVCTA PENLNQRNAI RASWGGLREA RGLRVQTLFL LGEPNAQHPV
     WGSQGSDLAS ESAAQGDILQ AAFQDSYRNL TLKTLSGLNW AEKHCPMARY VLKTDDDVYV
     NVPELVSELV LRGGRWGQWE GSTEPQREAE QEGGQVLHSE EVPLLYLGRV HWRVNPSRTP
     GGRHRVSEEQ WPHTWGPFPP YASGTGYVLS ASAVQLILKV ASRAPLLPLE DVFVGVSARR
     GGLAPTQCVK LAGATHYPLD RCCYGKFLLT SHRLDPWKMQ EAWKLVGGSD GERTAPFCSW
     FQGVLGILRC RAIAWLQS
//
  All links  
Ontology (4)   
   GO (4)   
Gene (4)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   UniGene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (2)   
   InterPro (1)   
   Pfam (1)   
Literature (1)   
   PubMed (1)   
All databases (13)   

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