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P15291 (B4GT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-1,4-galactosyltransferase 1

Short name=Beta-1,4-GalTase 1
Short name=Beta4Gal-T1
Short name=b4Gal-T1
EC=2.4.1.-
Alternative name(s):
UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 1
UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 1

Cleaved into the following chain:

  1. Processed beta-1,4-galactosyltransferase 1

Including the following 4 domains:

  1. Lactose synthase A protein
    EC=2.4.1.22
  2. N-acetyllactosamine synthase
    EC=2.4.1.90
    Alternative name(s):
    Nal synthase
  3. Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase
    EC=2.4.1.38
  4. Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase
    EC=2.4.1.-
Gene names
Name:B4GALT1
Synonyms:GGTB2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length398 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.12 Ref.17

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. Ref.12 Ref.17

Catalytic activity

UDP-alpha-D-galactose + D-glucose = UDP + lactose. Ref.12 Ref.17

UDP-alpha-D-galactose + N-acetyl-beta-D-glucosaminylglycopeptide = UDP + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminylglycopeptide. Ref.12 Ref.17

UDP-alpha-D-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine. Ref.12 Ref.17

Cofactor

Manganese. Ref.17 Ref.18 Ref.19

Pathway

Protein modification; protein glycosylation.

Subunit structure

Homodimer; and heterodimer with alpha-lactalbumin to form lactose synthase. Ref.14

Subcellular location

Isoform Long: Golgi apparatusGolgi stack membrane; Single-pass type II membrane protein. Cell membrane; Single-pass type II membrane protein. Cell surface. Note: Found in trans cisternae of Golgi. Ref.13

Isoform Short: Golgi apparatusGolgi stack membrane; Single-pass type II membrane protein. Note: Found in trans cisternae of Golgi. Ref.13

Processed beta-1,4-galactosyltransferase 1: Secreted. Note: Soluble form found in body fluids. Ref.13

Tissue specificity

Ubiquitously expressed, but at very low levels in fetal and adult brain.

Post-translational modification

The soluble form derives from the membrane forms by proteolytic processing.

Involvement in 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Sequence similarities

Belongs to the glycosyltransferase 7 family.

Ontologies

Keywords
   Cellular componentCell membrane
Golgi apparatus
Membrane
Secreted
   Coding sequence diversityAlternative initiation
Polymorphism
   DiseaseCongenital disorder of glycosylation
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   LigandManganese
Metal-binding
   Molecular functionGlycosyltransferase
Transferase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processNotch signaling pathway

Traceable author statement. Source: Reactome

acute inflammatory response

Inferred from electronic annotation. Source: Ensembl

angiogenesis involved in wound healing

Inferred from electronic annotation. Source: Ensembl

binding of sperm to zona pellucida

Traceable author statement. Source: Reactome

branching morphogenesis of an epithelial tube

Inferred from electronic annotation. Source: Ensembl

carbohydrate metabolic process

Traceable author statement. Source: Reactome

cell adhesion

Inferred from electronic annotation. Source: Ensembl

cellular protein metabolic process

Traceable author statement. Source: Reactome

development of secondary sexual characteristics

Inferred from electronic annotation. Source: Ensembl

epithelial cell development

Inferred from electronic annotation. Source: Ensembl

extracellular matrix organization

Inferred from electronic annotation. Source: Ensembl

galactose metabolic process

Inferred from electronic annotation. Source: Ensembl

glycosaminoglycan metabolic process

Traceable author statement. Source: Reactome

keratan sulfate biosynthetic process

Traceable author statement. Source: Reactome

keratan sulfate metabolic process

Traceable author statement. Source: Reactome

lactose biosynthetic process

Inferred from electronic annotation. Source: Ensembl

leukocyte migration

Inferred from electronic annotation. Source: Ensembl

mammary gland development

Inferred from electronic annotation. Source: Ensembl

multicellular organism reproduction

Traceable author statement. Source: Reactome

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

oligosaccharide biosynthetic process

Inferred from direct assay Ref.12. Source: UniProtKB

penetration of zona pellucida

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process involved in mammary gland involution

Inferred from electronic annotation. Source: Ensembl

positive regulation of epithelial cell proliferation involved in wound healing

Inferred from electronic annotation. Source: Ensembl

post-translational protein modification

Traceable author statement. Source: Reactome

protein N-linked glycosylation

Inferred from direct assay Ref.17. Source: UniProtKB

protein N-linked glycosylation via asparagine

Traceable author statement. Source: Reactome

regulation of acrosome reaction

Inferred from electronic annotation. Source: Ensembl

regulation of cellular component movement

Inferred from electronic annotation. Source: Ensembl

single fertilization

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 10900002. Source: UniProtKB

Golgi cisterna membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

Golgi membrane

Traceable author statement. Source: Reactome

Golgi trans cisterna

Inferred from direct assay PubMed 6121819. Source: UniProtKB

basolateral plasma membrane

Inferred from direct assay PubMed 3917437. Source: UniProtKB

brush border membrane

Inferred from direct assay PubMed 3917437. Source: UniProtKB

desmosome

Inferred from direct assay PubMed 3917437. Source: UniProtKB

external side of plasma membrane

Inferred from direct assay PubMed 3917437. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 19199708. Source: UniProt

glycocalyx

Inferred from direct assay PubMed 3917437. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionN-acetyllactosamine synthase activity

Inferred from direct assay Ref.12PubMed 33805. Source: UniProtKB

UDP-galactosyltransferase activity

Inferred from direct assay PubMed 3917437. Source: UniProtKB

alpha-tubulin binding

Inferred from direct assay Ref.14. Source: UniProtKB

beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity

Inferred from direct assay Ref.17PubMed 33805. Source: UniProtKB

beta-tubulin binding

Inferred from physical interaction Ref.14. Source: UniProtKB

galactosyltransferase activity

Non-traceable author statement Ref.6. Source: UniProtKB

lactose synthase activity

Inferred from direct assay PubMed 33805. Source: UniProtKB

manganese ion binding

Inferred from direct assay Ref.17. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay Ref.14. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform Long (identifier: P15291-1)

Also known as: Cell surface;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Short (identifier: P15291-2)

Also known as: Golgi complex;

The sequence of this isoform differs from the canonical sequence as follows:
     1-13: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 398398Beta-1,4-galactosyltransferase 1
PRO_0000012278
Chain? – 398Processed beta-1,4-galactosyltransferase 1PRO_0000296229

Regions

Topological domain1 – 2424Cytoplasmic Potential
Transmembrane25 – 4420Helical; Signal-anchor for type II membrane protein; Potential
Topological domain45 – 398354Lumenal Potential
Region183 – 1875UDP-alpha-D-galactose binding
Region222 – 2243UDP-alpha-D-galactose binding By similarity
Region249 – 2502UDP-alpha-D-galactose binding
Region312 – 3154N-acetyl-D-glucosamine binding
Region343 – 3464UDP-alpha-D-galactose binding

Sites

Metal binding2501Manganese
Metal binding3431Manganese; via tele nitrogen
Binding site3101UDP-alpha-D-galactose
Binding site3551N-acetyl-D-glucosamine
Site77 – 782Cleavage; to produce soluble form

Amino acid modifications

Glycosylation1131N-linked (GlcNAc...) Potential
Disulfide bond130 ↔ 172 Ref.17 Ref.18
Disulfide bond243 ↔ 262 Ref.17 Ref.18

Natural variations

Alternative sequence1 – 1313Missing in isoform Short.
VSP_018802
Natural variant211R → W.
Corresponds to variant rs1065764 [ dbSNP | Ensembl ].
VAR_054019
Natural variant2571H → R.
Corresponds to variant rs9169 [ dbSNP | Ensembl ].
VAR_054020

Experimental info

Mutagenesis2821Y → G: Reduction in N-acetylglucosamine binding. Ref.12
Mutagenesis2851Y → F: No change in enzymatic activity. Ref.12
Mutagenesis3071Y → G: Reduction in N-acetylglucosamine and UDP-galactose binding. Ref.12
Mutagenesis3081W → G: Reduction in N-acetylglucosamine binding. Ref.12
Mutagenesis3101W → G: Reduction in N-acetylglucosamine binding. Ref.12
Mutagenesis3401M → H: Favors the closed conformation of the enzyme. Ref.17
Sequence conflict101G → R in CAA31611. Ref.4
Sequence conflict101G → R in BAA06188. Ref.5
Sequence conflict111Missing in AAA35936. Ref.1
Sequence conflict111Missing in AAB00776. Ref.3
Sequence conflict111Missing in AAA68220. Ref.6
Sequence conflict31 – 322AL → VW in AAA35936. Ref.1
Sequence conflict31 – 322AL → VW in AAA35937. Ref.1
Sequence conflict31 – 322AL → VW in AAA68220. Ref.6
Sequence conflict351G → R in CAA31611. Ref.4
Sequence conflict761E → D in BAA06188. Ref.5
Sequence conflict91 – 11525SSQPR…ASNLT → GKHAKSSFKQFLLQIKELSN PIDLD in AAA68219. Ref.6
Sequence conflict2121Y → YGIY in CAA32247. Ref.1
Sequence conflict2121Y → YGIY in AAB00776. Ref.3
Sequence conflict2601Y → D in AAA68218. Ref.6
Sequence conflict2921L → S in BAA06188. Ref.5
Sequence conflict3371R → T in BAA06188. Ref.5
Sequence conflict340 – 3412MI → PA in AAA68220. Ref.6

Secondary structure

............................................ 398
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Long (Cell surface) [UniParc].

Last modified October 17, 2006. Version 5.
Checksum: 29B224C83C61E165

FASTA39843,920
        10         20         30         40         50         60 
MRLREPLLSG SAAMPGASLQ RACRLLVAVC ALHLGVTLVY YLAGRDLSRL PQLVGVSTPL 

        70         80         90        100        110        120 
QGGSNSAAAI GQSSGELRTG GARPPPPLGA SSQPRPGGDS SPVVDSGPGP ASNLTSVPVP 

       130        140        150        160        170        180 
HTTALSLPAC PEESPLLVGP MLIEFNMPVD LELVAKQNPN VKMGGRYAPR DCVSPHKVAI 

       190        200        210        220        230        240 
IIPFRNRQEH LKYWLYYLHP VLQRQQLDYG IYVINQAGDT IFNRAKLLNV GFQEALKDYD 

       250        260        270        280        290        300 
YTCFVFSDVD LIPMNDHNAY RCFSQPRHIS VAMDKFGFSL PYVQYFGGVS ALSKQQFLTI 

       310        320        330        340        350        360 
NGFPNNYWGW GGEDDDIFNR LVFRGMSISR PNAVVGRCRM IRHSRDKKNE PNPQRFDRIA 

       370        380        390 
HTKETMLSDG LNSLTYQVLD VQRYPLYTQI TVDIGTPS 

« Hide

Isoform Short (Golgi complex) [UniParc].

Checksum: A28CB67033107C83
Show »

FASTA38542,538

References

« Hide 'large scale' references
[1]"Identification of the full-length coding sequence for human galactosyltransferase (beta-N-acetylglucosaminide: beta 1,4-galactosyltransferase)."
Masri K.A., Appert H.E., Fukuda M.N.
Biochem. Biophys. Res. Commun. 157:657-663(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Near identity of HeLa cell galactosyltransferase with the human placental enzyme."
Watzele G., Berger E.G.
Nucleic Acids Res. 18:7174-7174(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Genomic structure and expression of human beta-1,4-galactosyltransferase."
Mengle-Gaw L., McCoy-Haman M.F., Tiemeier D.C.
Biochem. Biophys. Res. Commun. 176:1269-1276(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Complementary DNA cloning for galactosyltransferase associated with tumor and determination of antigenic epitopes recognized by specific monoclonal antibodies."
Uejima T., Uemura M., Nozawa S., Narimatsu H.
Cancer Res. 52:6158-6163(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[5]"The beta 1, 4-galactosyltransferase gene is post-transcriptionally regulated during differentiation of mouse F9 teratocarcinoma cells."
Kudo T., Narimatsu H.
Glycobiology 5:397-403(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[6]"Analysis of the sequences of human beta-1,4-galactosyltransferase cDNA clones."
Chatterjee S.K., Mukerjee S., Tripathi P.K.
Int. J. Biochem. Cell Biol. 27:329-336(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fetal liver.
[7]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
Tissue: Testis.
[8]"DNA sequence and analysis of human chromosome 9."
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. expand/collapse author list , 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.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"Isolation of a cDNA coding for human galactosyltransferase."
Appert H.E., Rutherford T.J., Tarr G.E., Wiest J.S., Thomford N.R., McCorquodale D.J.
Biochem. Biophys. Res. Commun. 139:163-168(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 138-398, PARTIAL PROTEIN SEQUENCE.
[11]"Isolation of galactosyltransferase from human milk and the determination of its N-terminal amino acid sequence."
Appert H.E., Rutherford T.J., Tarr G.E., Thomford N.R., McCorquodale D.J.
Biochem. Biophys. Res. Commun. 138:224-229(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 78-94.
[12]"Analysis of the substrate binding sites of human galactosyltransferase by protein engineering."
Aoki D., Appert H.E., Johnson D., Wong S.S., Fukuda M.N.
EMBO J. 9:3171-3178(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 274-326, CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF TYR-282; TYR-285; TYR-307; TRP-308 AND TRP-310.
[13]"Evidence for a molecular distinction between Golgi and cell surface forms of beta 1,4-galactosyltransferase."
Lopez L.C., Youakim A., Evans S.C., Shur B.D.
J. Biol. Chem. 266:15984-15991(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE INITIATION, SUBCELLULAR LOCATION.
[14]"Golgi retention mechanism of beta-1,4-galactosyltransferase. Membrane-spanning domain-dependent homodimerization and association with alpha- and beta-tubulins."
Yamaguchi N., Fukuda M.N.
J. Biol. Chem. 270:12170-12176(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[15]"Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions."
Amado M., Almeida R., Schwientek T., Clausen H.
Biochim. Biophys. Acta 1473:35-53(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[16]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"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."
Ramasamy V., Ramakrishnan B., Boeggeman E., Ratner D.M., Seeberger P.H., Qasba P.K.
J. Mol. Biol. 353:53-67(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: 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, DISULFIDE BONDS.
[18]"Structural snapshots of beta-1,4-galactosyltransferase-I along the kinetic pathway."
Ramakrishnan B., Ramasamy V., Qasba P.K.
J. Mol. Biol. 357:1619-1633(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 126-397 OF MUTANT HIS-340 IN COMPLEX WITH MANGANESE IONS AND UDP, COFACTOR, DISULFIDE BONDS.
[19]"Deoxygenated disaccharide analogs as specific inhibitors of beta1-4-galactosyltransferase 1 and selectin-mediated tumor metastasis."
Brown J.R., Yang F., Sinha A., Ramakrishnan B., Tor Y., Qasba P.K., Esko J.D.
J. Biol. Chem. 284:4952-4959(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 126-398 IN COMPLEX WITH MANGANESE IONS AND N-ACETYL-D-GLUCOSAMINE, COFACTOR.
+Additional computationally mapped references.

Web resources

GeneReviews
GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Beta-1,4-galactosyltransferase 1

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X14085 mRNA. Translation: CAA32247.1.
M22921 mRNA. Translation: AAA35936.1.
M22921 mRNA. Translation: AAA35937.1.
X55415 mRNA. Translation: CAA39073.1.
X55415 mRNA. Translation: CAA39074.1.
M70432 expand/collapse EMBL AC list , M70427, M70428, M70429, M70430, M70431 Genomic DNA. Translation: AAB00776.1.
X13223 mRNA. Translation: CAA31611.1.
D29805 mRNA. Translation: BAA06188.1.
U10472 mRNA. Translation: AAA68218.1.
U10473 mRNA. Translation: AAA68219.1.
U10474 mRNA. Translation: AAA68220.1.
CH471071 Genomic DNA. Translation: EAW58520.1.
CH471071 Genomic DNA. Translation: EAW58521.1.
AK312797 mRNA. Translation: BAG35657.1.
AL161445 Genomic DNA. Translation: CAD13306.1.
M13701 mRNA. Translation: AAA35935.1.
PIRJQ1030.
RefSeqNP_001488.2. NM_001497.3.
UniGeneHs.272011.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2AE7X-ray2.00A/B/C126-397[»]
2AECX-ray2.00A/B/C126-397[»]
2AESX-ray2.00A/B/C126-397[»]
2AGDX-ray1.90A/B/C126-397[»]
2AH9X-ray2.00A/B/C126-397[»]
2FY7X-ray1.70A126-397[»]
2FYAX-ray1.90A126-397[»]
2FYBX-ray1.90A126-397[»]
3EE5X-ray2.20A/B/C126-398[»]
4EE3X-ray2.30A/B/C126-398[»]
4EE4X-ray1.95A/B/C126-398[»]
4EE5X-ray2.20A/B/C126-398[»]
4EEAX-ray2.00A/B/C126-398[»]
4EEGX-ray2.20A/B/C126-398[»]
4EEMX-ray2.20A/B/C126-398[»]
4EEOX-ray2.30A/B/C126-398[»]
4L41X-ray2.70C126-398[»]
ProteinModelPortalP15291.
SMRP15291. Positions 126-398.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108950. 11 interactions.
IntActP15291. 2 interactions.
MINTMINT-5004065.
STRING9606.ENSP00000369055.

Chemistry

BindingDBP15291.
ChEMBLCHEMBL4384.
DrugBankDB00141. N-Acetyl-D-glucosamine.

Protein family/group databases

CAZyGT7. Glycosyltransferase Family 7.

PTM databases

PhosphoSiteP15291.

Polymorphism databases

DMDM116241264.

Proteomic databases

PaxDbP15291.
PRIDEP15291.

Protocols and materials databases

DNASU2683.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000379731; ENSP00000369055; ENSG00000086062. [P15291-1]
GeneID2683.
KEGGhsa:2683.
UCSCuc003zsg.2. human. [P15291-1]

Organism-specific databases

CTD2683.
GeneCardsGC09M033100.
HGNCHGNC:924. B4GALT1.
HPAHPA010806.
HPA010807.
MIM137060. gene.
607091. phenotype.
neXtProtNX_P15291.
Orphanet79332. B4GALT1-CDG.
PharmGKBPA25223.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG327897.
HOVERGENHBG058334.
InParanoidP15291.
KOK07966.
OMAMSVSRPN.
OrthoDBEOG7060R0.
PhylomeDBP15291.
TreeFamTF312834.

Enzyme and pathway databases

BRENDA2.4.1.38. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_116125. Disease.
REACT_163848. Reproduction.
REACT_17015. Metabolism of proteins.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressP15291.
BgeeP15291.
CleanExHS_B4GALT1.
GenevestigatorP15291.

Family and domain databases

InterProIPR003859. Galactosyl_T.
IPR027791. Galactosyl_T_C.
IPR027995. Galactosyl_T_N.
[Graphical view]
PANTHERPTHR19300. PTHR19300. 1 hit.
PfamPF02709. Glyco_transf_7C. 1 hit.
PF13733. Glyco_transf_7N. 1 hit.
[Graphical view]
PRINTSPR02050. B14GALTRFASE.
ProtoNetSearch...

Other

ChiTaRSB4GALT1. human.
EvolutionaryTraceP15291.
GeneWikiB4GALT1.
GenomeRNAi2683.
NextBio10594.
PROP15291.
SOURCESearch...

Entry information

Entry nameB4GT1_HUMAN
AccessionPrimary (citable) accession number: P15291
Secondary accession number(s): B2R710 expand/collapse secondary AC list , D3DRL2, Q12909, Q12910, Q12911, Q14456, Q14509, Q14523
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: October 17, 2006
Last modified: April 16, 2014
This is version 162 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM