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Q9BYG0 (B3GN5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 5

Short name=BGnT-5
Short name=Beta-1,3-Gn-T5
Short name=Beta-1,3-N-acetylglucosaminyltransferase 5
Short name=Beta3Gn-T5
EC=2.4.1.-
Alternative name(s):
Lactotriaosylceramide synthase
Short name=Lc(3)Cer synthase
Short name=Lc3 synthase
Gene names
Name:B3GNT5
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length378 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Beta-1,3-N-acetylglucosaminyltransferase that plays a key role in the synthesis of lacto- or neolacto-series carbohydrate chains on glycolipids, notably by participating in biosynthesis of HNK-1 and Lewis X carbohydrate structures. Has strong activity toward lactosylceramide (LacCer) and neolactotetraosylceramide (nLc4Cer; paragloboside), resulting in the synthesis of Lc3Cer and neolactopentaosylceramide (nLc5Cer), respectively. Probably plays a central role in regulating neolacto-series glycolipid synthesis during embryonic development.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein By similarity.

Tissue specificity

Widely expressed. Highly expressed in lung, colon, placenta, testis, pituitary gland and cerebellum. Weakly expressed in brain, liver, spleen, lymph node and thymus. Ref.1

Induction

Up-regulated by stimulation with retinoic acid and down-regulated with 12-O-tetradecanoylphorbol-13-acetate (TPA). Ref.1

Sequence similarities

Belongs to the glycosyltransferase 31 family.

Sequence caution

The sequence BAD92754.1 differs from that shown. Reason: Frameshift at position 347.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 378378UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 5
PRO_0000289209

Regions

Topological domain1 – 1414Cytoplasmic Potential
Transmembrane15 – 3521Helical; Signal-anchor for type II membrane protein; Potential
Topological domain36 – 378343Lumenal Potential

Amino acid modifications

Glycosylation591N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q9BYG0 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: E19BA966A5E12CD2

FASTA37844,053
        10         20         30         40         50         60 
MRMLVSGRRV KKWQLIIQLF ATCFLASLMF FWEPIDNHIV SHMKSYSYRY LINSYDFVND 

        70         80         90        100        110        120 
TLSLKHTSAG PRYQYLINHK EKCQAQDVLL LLFVKTAPEN YDRRSGIRRT WGNENYVRSQ 

       130        140        150        160        170        180 
LNANIKTLFA LGTPNPLEGE ELQRKLAWED QRYNDIIQQD FVDSFYNLTL KLLMQFSWAN 

       190        200        210        220        230        240 
TYCPHAKFLM TADDDIFIHM PNLIEYLQSL EQIGVQDFWI GRVHRGAPPI RDKSSKYYVS 

       250        260        270        280        290        300 
YEMYQWPAYP DYTAGAAYVI SGDVAAKVYE ASQTLNSSLY IDDVFMGLCA NKIGIVPQDH 

       310        320        330        340        350        360 
VFFSGEGKTP YHPCIYEKMM TSHGHLEDLQ DLWKNATDPK VKTISKGFFG QIYCRLMKII 

       370 
LLCKISYVDT YPCRAAFI 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of UDP-GlcNAc:lactosylceramide beta 1,3-N-acetylglucosaminyltransferase (beta 3Gn-T5), an essential enzyme for the expression of HNK-1 and Lewis X epitopes on glycolipids."
Togayachi A., Akashima T., Ookubo R., Kudo T., Nishihara S., Iwasaki H., Natsume A., Mio H., Inokuchi J., Irimura T., Sasaki K., Narimatsu H.
J. Biol. Chem. 276:22032-22040(2001) [PubMed: 11283017] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, TISSUE SPECIFICITY, INDUCTION.
[2]"Cloning of a mouse beta 1,3 N-acetylglucosaminyltransferase GlcNAc(beta 1,3)Gal(beta 1,4)Glc-ceramide synthase gene encoding the key regulator of lacto-series glycolipid biosynthesis."
Henion T.R., Zhou D., Wolfer D.P., Jungalwala F.B., Hennet T.
J. Biol. Chem. 276:30261-30269(2001) [PubMed: 11384981] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]Bennett E.P.
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[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]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
+Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Beta1,3-N-acetylglucosaminyltransferase 5

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB045278 mRNA. Translation: BAB40940.1.
AF368169 mRNA. Translation: AAK53403.1.
AJ304505 mRNA. Translation: CAC83093.1.
AB209517 mRNA. Translation: BAD92754.1. Frameshift.
CH471052 Genomic DNA. Translation: EAW78333.1.
CH471052 Genomic DNA. Translation: EAW78334.1.
CH471052 Genomic DNA. Translation: EAW78335.1.
CH471052 Genomic DNA. Translation: EAW78336.1.
BC028058 mRNA. Translation: AAH28058.1.
IPIIPI00012508.
RefSeqNP_114436.1. NM_032047.4.
UniGeneHs.718506.

3D structure databases

ProteinModelPortalQ9BYG0.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9BYG0. 1 interaction.
STRINGQ9BYG0.

Protein family/group databases

CAZyGT31. Glycosyltransferase Family 31.

Polymorphism databases

DMDM74733473.

Proteomic databases

PRIDEQ9BYG0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000326505; ENSP00000316173; ENSG00000176597.
ENST00000460419; ENSP00000420778; ENSG00000176597.
ENST00000465010; ENSP00000417868; ENSG00000176597.
GeneID84002.
KEGGhsa:84002.
UCSCuc003flk.1. human.

Organism-specific databases

CTD84002.
GeneCardsGC03P182971.
H-InvDBHIX0003898.
HGNCHGNC:15684. B3GNT5.
HPAHPA017292.
neXtProtNX_Q9BYG0.
PharmGKBPA25221.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG17451.
GeneTreeENSGT00560000076821.
HOGENOMHBG446090.
HOVERGENHBG101684.
InParanoidQ9BYG0.
OMAYTAGAAY.
OrthoDBEOG4PNXH6.
PhylomeDBQ9BYG0.

Enzyme and pathway databases

BRENDA2.4.1.206. 2681.

Gene expression databases

ArrayExpressQ9BYG0.
BgeeQ9BYG0.
CleanExHS_B3GNT5.
GenevestigatorQ9BYG0.

Family and domain databases

InterProIPR002659. Glyco_trans_31.
[Graphical view]
KOK03766.
PANTHERPTHR11214. Glyco_trans_31. 1 hit.
PfamPF01762. Galactosyl_T. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio73170.

Entry information

Entry nameB3GN5_HUMAN
AccessionPrimary (citable) accession number: Q9BYG0
Secondary accession number(s): D3DNS5 expand/collapse secondary AC list , Q59FE3, Q7L9Z5, Q8WWP9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: June 1, 2001
Last modified: January 25, 2012
This is version 77 of the entry and version 1 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

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families