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O54905 (B3GT2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 94. 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:
Beta-1,3-galactosyltransferase 2

Short name=Beta-1,3-GalTase 2
Short name=Beta3Gal-T2
Short name=Beta3GalT2
EC=2.4.1.-
Alternative name(s):
UDP-Gal:betaGlcNAc beta 1,3-galactosyltransferase-II
Gene names
Name:B3galt2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length422 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Beta-1,3-galactosyltransferase that transfers galactose from UDP-galactose to substrates with a terminal beta-N-acetylglucosamine (beta-GlcNAc) residue. Can also utilize substrates with a terminal galactose residue, albeit with lower efficiency. Involved in the biosynthesis of the carbohydrate moieties of glycolipids and glycoproteins. Ref.1

Cofactor

Manganese. Ref.1

Pathway

Protein modification; protein glycosylation.

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein Probable.

Tissue specificity

Detected in brain and heart. Ref.1

Sequence similarities

Belongs to the glycosyltransferase 31 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 422422Beta-1,3-galactosyltransferase 2
PRO_0000219151

Regions

Topological domain1 – 2020Cytoplasmic Potential
Transmembrane21 – 4323Helical; Signal-anchor for type II membrane protein; Potential
Topological domain44 – 422379Lumenal Potential

Amino acid modifications

Glycosylation751N-linked (GlcNAc...) Potential
Glycosylation981N-linked (GlcNAc...) Potential
Glycosylation1191N-linked (GlcNAc...) Potential
Glycosylation1761N-linked (GlcNAc...) Potential
Glycosylation2261N-linked (GlcNAc...) Potential

Natural variations

Natural variant441N → S in strain: HMI/Msf. Ref.4
Natural variant861V → A in strain: BLG2/Msf, MSM/Msf, SWN/Msf and NJL/Msf. Ref.4
Natural variant881P → S in strain: BLG2/Msf and NJL/Msf. Ref.4
Natural variant1001S → T in strain: CAST/Ei and HMI/Msf. Ref.4
Natural variant1241N → D in strain: BLG2/Msf, NJL/Msf, MSM/Msf and SWN/Msf. Ref.4

Experimental info

Sequence conflict951T → I in AAC53524. Ref.1
Sequence conflict3661H → R in BAC28688. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O54905 [UniParc].

Last modified March 15, 2005. Version 2.
Checksum: 58F5D3568143F4FB

FASTA42249,095
        10         20         30         40         50         60 
MLQWRRRHCC FAKMTWSPKR SLLRTPLTGV LSLVFLFAMF LFFNHHDWLP GRPGFKENPV 

        70         80         90        100        110        120 
TYTFRGFRST KSETNHSSLR TIWKEVAPQT LRPHTASNSS NTELSPQGVT GLQNTLSANG 

       130        140        150        160        170        180 
SIYNEKGTGH PNSYHFKYII NEPEKCQEKS PFLILLIAAE PGQIEARRAI RQTWGNETLA 

       190        200        210        220        230        240 
PGIQIIRVFL LGISIKLNGY LQHAIQEESR QYHDIIQQEY LDTYYNLTIK TLMGMNWVAT 

       250        260        270        280        290        300 
YCPHTPYVMK TDSDMFVNTE YLIHKLLKPD LPPRHNYFTG YLMRGYAPNR NKDSKWYMPP 

       310        320        330        340        350        360 
DLYPSERYPV FCSGTGYVFS GDLAEKIFKV SLGIRRLHLE DVYVGICLAK LRVDPVPPPN 

       370        380        390        400        410        420 
EFVFNHWRVS YSSCKYSHLI TSHQFQPSEL IKYWNHLQQN KHNACANAAK EKAGRYRHRK 


LH 

« Hide

References

« Hide 'large scale' references
[1]"Genomic cloning and expression of three murine UDP-galactose: beta-N-acetylglucosamine beta1,3-galactosyltransferase genes."
Hennet T., Dinter A., Kuhnert P., Mattu T.S., Rudd P.M., Berger E.G.
J. Biol. Chem. 273:58-65(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, COFACTOR, TISSUE SPECIFICITY.
Strain: 129/SvJ.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Cerebellum, Diencephalon and Hippocampus.
[3]"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].
Tissue: Olfactory epithelium.
[4]"Conspicuous differences among gene genealogies of 21 nuclear genes of five Mus musculus subspecies."
Liu Y., Kitano T., Koide T., Shiroishi T., Moriwaki K., Saitou N.
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 7-415, VARIANTS SER-44; ALA-86; SER-88; THR-100 AND ASP-124.
Strain: BFM/2Msf, BLG2/Msf, C57BL/10SnJ, CAST/Ei, HMI/Msf, MSM/Msf, NJL/Msf, Pgn2 and SWN/Msf.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF029791 Genomic DNA. Translation: AAC53524.1.
AK034371 mRNA. Translation: BAC28688.1.
AK036141 mRNA. Translation: BAC29317.1.
AK083168 mRNA. Translation: BAC38793.1.
BC046322 mRNA. Translation: AAH46322.1.
AB039144 Genomic DNA. Translation: BAB68668.1.
AB039145 Genomic DNA. Translation: BAB68669.1.
AB039146 Genomic DNA. Translation: BAB68670.1.
AB039147 Genomic DNA. Translation: BAB68671.1.
AB039148 Genomic DNA. Translation: BAB68672.1.
AB039149 Genomic DNA. Translation: BAB68673.1.
AB039150 Genomic DNA. Translation: BAB68674.1.
AB039151 Genomic DNA. Translation: BAB68675.1.
AB039152 Genomic DNA. Translation: BAB68676.1.
CCDSCCDS15342.1.
RefSeqNP_064409.3. NM_020025.4.
UniGeneMm.285580.

3D structure databases

ProteinModelPortalO54905.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGT31. Glycosyltransferase Family 31.

PTM databases

PhosphoSiteO54905.

Proteomic databases

PRIDEO54905.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000038252; ENSMUSP00000046118; ENSMUSG00000033849.
GeneID26878.
KEGGmmu:26878.
UCSCuc007cwy.2. mouse.

Organism-specific databases

CTD8707.
MGIMGI:1349461. B3galt2.

Phylogenomic databases

eggNOGNOG331548.
GeneTreeENSGT00740000114871.
HOVERGENHBG101354.
InParanoidO54905.
KOK07820.
OMACCFAKMS.
OrthoDBEOG7C2R1D.
PhylomeDBO54905.
TreeFamTF318639.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

BgeeO54905.
GenevestigatorO54905.

Family and domain databases

InterProIPR002659. Glyco_trans_31.
[Graphical view]
PANTHERPTHR11214. PTHR11214. 1 hit.
PfamPF01762. Galactosyl_T. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio304691.
PROO54905.
SOURCESearch...

Entry information

Entry nameB3GT2_MOUSE
AccessionPrimary (citable) accession number: O54905
Secondary accession number(s): Q8BH19 expand/collapse secondary AC list , Q8CBX4, Q91V19, Q91V58, Q91VE9, Q920V3, Q920V4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: July 9, 2014
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot