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O60512 (B4GT3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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 3

Short name=Beta-1,4-GalTase 3
Short name=Beta4Gal-T3
Short name=b4Gal-T3
EC=2.4.1.-
Alternative name(s):
UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 3
UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 3

Including the following 3 domains:

  1. N-acetyllactosamine synthase
    EC=2.4.1.90
    Alternative name(s):
    Nal synthase
  2. Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase
    EC=2.4.1.38
  3. Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase
    EC=2.4.1.-
Gene names
Name:B4GALT3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length393 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids.

Catalytic activity

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

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

Cofactor

Manganese By similarity.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Golgi apparatusGolgi stack membrane; Single-pass type II membrane protein. Note: Trans cisternae of Golgi stack.

Tissue specificity

Found in various tissues. Highest expression in placenta, prostate, testis, ovary, intestine and muscle, and in fetal brain.

Sequence similarities

Belongs to the glycosyltransferase 7 family.

Biophysicochemical properties

Kinetic parameters:

KM=63 µM for GlcNAc-B-S-pNP Ref.3

Ontologies

Keywords
   Cellular componentGolgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   LigandManganese
Metal-binding
   Molecular functionGlycosyltransferase
Transferase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

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

post-translational protein modification

Traceable author statement. Source: Reactome

protein N-linked glycosylation via asparagine

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentGolgi apparatus

Inferred from direct assay. Source: HPA

Golgi cisterna membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

Golgi membrane

Traceable author statement. Source: Reactome

cytoplasm

Inferred from direct assay. Source: HPA

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708. Source: UniProt

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionN-acetyllactosamine synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

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

Inferred from electronic annotation. Source: UniProtKB-EC

galactosyltransferase activity

Traceable author statement Ref.1. Source: ProtInc

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O60512-1)

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 2 (identifier: O60512-2)

The sequence of this isoform differs from the canonical sequence as follows:
     116-145: PAGCEPRSRTAIIVPHRAREHHLRLLLYHL → PAALPPAPLLAAPAACLWHLCHPPGWKWNI
     146-393: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 393393Beta-1,4-galactosyltransferase 3
PRO_0000080537

Regions

Topological domain1 – 1010Cytoplasmic Potential
Transmembrane11 – 3121Helical; Signal-anchor for type II membrane protein; Potential
Topological domain32 – 393362Lumenal Potential
Region130 – 1345UDP-alpha-D-galactose binding By similarity
Region169 – 1713UDP-alpha-D-galactose binding By similarity
Region196 – 1972UDP-alpha-D-galactose binding By similarity
Region260 – 2634N-acetyl-D-glucosamine binding By similarity
Region291 – 2933UDP-alpha-D-galactose binding By similarity

Sites

Metal binding1971Manganese By similarity
Metal binding2911Manganese; via tele nitrogen By similarity
Binding site2261UDP-alpha-D-galactose By similarity
Binding site2581UDP-alpha-D-galactose By similarity
Binding site3031N-acetyl-D-glucosamine By similarity

Amino acid modifications

Glycosylation571N-linked (GlcNAc...) Potential
Glycosylation1661N-linked (GlcNAc...) Potential
Glycosylation3371N-linked (GlcNAc...) Potential
Glycosylation3851N-linked (GlcNAc...) Potential
Disulfide bond77 ↔ 119 By similarity
Disulfide bond190 ↔ 209 By similarity

Natural variations

Alternative sequence116 – 14530PAGCE…LLYHL → PAALPPAPLLAAPAACLWHL CHPPGWKWNI in isoform 2.
VSP_014106
Alternative sequence146 – 393248Missing in isoform 2.
VSP_014107

Experimental info

Sequence conflict641A → R in AAC39734. Ref.2
Sequence conflict1121G → A in AAC39734. Ref.2
Sequence conflict2231K → S in AAC39734. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 21, 2005. Version 2.
Checksum: CA0BF955F95ED1F4

FASTA39343,928
        10         20         30         40         50         60 
MLRRLLERPC TLALLVGSQL AVMMYLSLGG FRSLSALFGR DQGPTFDYSH PRDVYSNLSH 

        70         80         90        100        110        120 
LPGAPGGPPA PQGLPYCPER SPLLVGPVSV SFSPVPSLAE IVERNPRVEP GGRYRPAGCE 

       130        140        150        160        170        180 
PRSRTAIIVP HRAREHHLRL LLYHLHPFLQ RQQLAYGIYV IHQAGNGTFN RAKLLNVGVR 

       190        200        210        220        230        240 
EALRDEEWDC LFLHDVDLLP ENDHNLYVCD PRGPRHVAVA MNKFGYSLPY PQYFGGVSAL 

       250        260        270        280        290        300 
TPDQYLKMNG FPNEYWGWGG EDDDIATRVR LAGMKISRPP TSVGHYKMVK HRGDKGNEEN 

       310        320        330        340        350        360 
PHRFDLLVRT QNSWTQDGMN SLTYQLLARE LGPLYTNITA DIGTDPRGPR APSGPRYPPG 

       370        380        390 
SSQAFRQEML QRRPPARPGP LSTANHTALR GSH 

« Hide

Isoform 2 [UniParc].

Checksum: 4231F9B50756A99C
Show »

FASTA14515,654

References

« Hide 'large scale' references
[1]"A family of human beta4-galactosyltransferases. Cloning and expression of two novel UDP-galactose:beta-n-acetylglucosamine beta1, 4-galactosyltransferases, beta4Gal-T2 and beta4Gal-T3."
Almeida R., Amado M., David L., Levery S.B., Holmes E.H., Merkx G., van Kessel A.G., Rygaard E., Hassan H., Bennett E., Clausen H.
J. Biol. Chem. 272:31979-31991(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"The expanding beta 4-galactosyltransferase gene family: messages from the databanks."
Lo N.-W., Shaper J.H., Pevsner J., Shaper N.L.
Glycobiology 8:517-526(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Galactosylation of N-linked oligosaccharides by human beta-1,4-galactosyltransferases I, II, III, IV, V, and VI expressed in Sf-9 cells."
Guo S., Sato T., Shirane K., Furukawa K.
Glycobiology 11:813-820(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), BIOPHYSICOCHEMICAL PROPERTIES.
[4]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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].
[6]"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 2).
Tissue: Ovary.
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain, Eye and Lymph.
[8]"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.
+Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Beta-1,4-galactosyltransferase 3

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y12509 mRNA. Translation: CAA73111.1.
AF038661 mRNA. Translation: AAC39734.1.
AB024435 mRNA. Translation: BAA75820.1.
AL590714 Genomic DNA. Translation: CAH72145.1.
AK023311 mRNA. Translation: BAB14520.1.
CH471121 Genomic DNA. Translation: EAW52628.1.
CH471121 Genomic DNA. Translation: EAW52629.1.
CH471121 Genomic DNA. Translation: EAW52630.1.
CH471121 Genomic DNA. Translation: EAW52631.1.
CH471121 Genomic DNA. Translation: EAW52632.1.
BC000276 mRNA. Translation: AAH00276.1.
BC006099 mRNA. Translation: AAH06099.1.
BC009985 mRNA. Translation: AAH09985.1.
RefSeqNP_001186802.1. NM_001199873.1.
NP_001186803.1. NM_001199874.1.
NP_003770.1. NM_003779.3.
XP_005245623.1. XM_005245566.1.
UniGeneHs.321231.
Hs.741821.

3D structure databases

ProteinModelPortalO60512.
SMRO60512. Positions 74-344.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114246. 3 interactions.
IntActO60512. 5 interactions.
MINTMINT-1371449.
STRING9606.ENSP00000320965.

Chemistry

DrugBankDB00141. N-Acetyl-D-glucosamine.

Protein family/group databases

CAZyGT7. Glycosyltransferase Family 7.

PTM databases

PhosphoSiteO60512.

Proteomic databases

PaxDbO60512.
PRIDEO60512.

Protocols and materials databases

DNASU8703.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000319769; ENSP00000320965; ENSG00000158850. [O60512-1]
ENST00000367998; ENSP00000356977; ENSG00000158850. [O60512-1]
GeneID8703.
KEGGhsa:8703.
UCSCuc001fyq.2. human. [O60512-1]

Organism-specific databases

CTD8703.
GeneCardsGC01M161141.
H-InvDBHIX0159958.
HGNCHGNC:926. B4GALT3.
HPAHPA010793.
MIM604014. gene.
neXtProtNX_O60512.
PharmGKBPA25225.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG327897.
HOGENOMHOG000231027.
HOVERGENHBG058334.
InParanoidO60512.
KOK07968.
OMAALFGREQ.
OrthoDBEOG7060R0.
PhylomeDBO60512.
TreeFamTF312834.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
REACT_17015. Metabolism of proteins.
UniPathwayUPA00378.

Gene expression databases

BgeeO60512.
CleanExHS_B4GALT3.
GenevestigatorO60512.

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

GeneWikiB4GALT3.
GenomeRNAi8703.
NextBio32631.
PROO60512.
SOURCESearch...

Entry information

Entry nameB4GT3_HUMAN
AccessionPrimary (citable) accession number: O60512
Secondary accession number(s): D3DVG3 expand/collapse secondary AC list , O60910, Q9BPZ4, Q9H8T2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: June 21, 2005
Last modified: April 16, 2014
This is version 128 of the entry and version 2 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM