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Protein

Beta-1,4-galactosyltransferase 2

Gene

B4galt2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. Can produce lactose (By similarity).By similarity

Catalytic activityi

UDP-alpha-D-galactose + D-glucose = UDP + lactose.
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.

Cofactori

Mn2+By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi215 – 2151ManganeseBy similarity
Binding sitei275 – 2751UDP-alpha-D-galactoseBy similarity
Metal bindingi308 – 3081Manganese; via tele nitrogenBy similarity
Binding sitei320 – 3201N-acetyl-D-glucosamineBy similarity

GO - Molecular functioni

  1. beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity Source: UniProtKB-EC
  2. lactose synthase activity Source: UniProtKB-EC
  3. metal ion binding Source: UniProtKB-KW
  4. N-acetyllactosamine synthase activity Source: UniProtKB-EC

GO - Biological processi

  1. protein glycosylation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_308816. N-Glycan antennae elongation.
REACT_346228. Keratan sulfate biosynthesis.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT7. Glycosyltransferase Family 7.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-1,4-galactosyltransferase 2 (EC:2.4.1.-)
Short name:
Beta-1,4-GalTase 2
Short name:
Beta4Gal-T2
Short name:
b4Gal-T2
Alternative name(s):
UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 2
UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 2
Including the following 4 domains:
Lactose synthase A protein (EC:2.4.1.22)
N-acetyllactosamine synthase (EC:2.4.1.90)
Alternative name(s):
Nal synthase
Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase (EC:2.4.1.38)
Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase (EC:2.4.1.-)
Gene namesi
Name:B4galt2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1858493. B4galt2.

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1515CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei16 – 3621Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini37 – 369333LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. Golgi cisterna membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 369369Beta-1,4-galactosyltransferase 2PRO_0000080534Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi63 – 631N-linked (GlcNAc...)Sequence Analysis
Glycosylationi68 – 681N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi94 ↔ 136By similarity
Disulfide bondi208 ↔ 227By similarity
Glycosylationi354 – 3541N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ9Z2Y2.
PRIDEiQ9Z2Y2.

PTM databases

PhosphoSiteiQ9Z2Y2.

Expressioni

Gene expression databases

BgeeiQ9Z2Y2.
ExpressionAtlasiQ9Z2Y2. baseline and differential.
GenevestigatoriQ9Z2Y2.

Structurei

3D structure databases

ProteinModelPortaliQ9Z2Y2.
SMRiQ9Z2Y2. Positions 94-362.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni147 – 1515UDP-alpha-D-galactose bindingBy similarity
Regioni186 – 1883UDP-alpha-D-galactose bindingBy similarity
Regioni214 – 2152UDP-alpha-D-galactose bindingBy similarity
Regioni277 – 2804N-acetyl-D-glucosamine bindingBy similarity
Regioni308 – 3103UDP-alpha-D-galactose bindingBy similarity

Sequence similaritiesi

Belongs to the glycosyltransferase 7 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG327897.
GeneTreeiENSGT00760000119140.
HOGENOMiHOG000231027.
HOVERGENiHBG058334.
InParanoidiQ9Z2Y2.
KOiK07967.
OMAiEQPRHFA.
OrthoDBiEOG7060R0.
PhylomeDBiQ9Z2Y2.
TreeFamiTF312834.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR003859. Galactosyl_T.
IPR027791. Galactosyl_T_C.
IPR027995. Galactosyl_T_N.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR19300. PTHR19300. 1 hit.
PfamiPF02709. Glyco_transf_7C. 1 hit.
PF13733. Glyco_transf_7N. 1 hit.
[Graphical view]
PRINTSiPR02050. B14GALTRFASE.
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9Z2Y2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRLLGGTLE RVCKAVLLLC LLHFLVAVIL YFDVYAQHLA FFSRFSTRSP
60 70 80 90 100
AHALYPAASS STNCSRPNAT AASSGLPEVP SARPGPTAPV IPPCPDVPPG
110 120 130 140 150
LVGRVVIEFT SPMPLERVQR ENPGVLLGGR YSPPDCTPAQ TVAVIIPFRH
160 170 180 190 200
REHHLRYWLH YLHPMLRRQR LRYGVYVINQ HGEETFNRAK LLNVGFLEAL
210 220 230 240 250
KEDAAYDCFI FSDVDLVPMD DRNLYRCGDQ PRHFAIAMDK FGFRLPYASY
260 270 280 290 300
FGGVSGLSKA QFLRINGFPN EYWGWGGEDD DIFNRISLTG MKISRPDVRI
310 320 330 340 350
GRYRMIKHDR DKHNEPNPQR FNKIQNTKMS MKWDGIGSVR YRVLEVSRQP
360
LFTNITVDIG QPMSWLTQG
Length:369
Mass (Da):41,909
Last modified:April 30, 1999 - v1
Checksum:iEF4465AFE51C6C30
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF142670 mRNA. Translation: AAF22220.1.
AB019541 mRNA. Translation: BAA34385.1.
AK165829 mRNA. Translation: BAE38399.1.
CCDSiCCDS18539.1.
RefSeqiNP_001240310.1. NM_001253381.1.
NP_059073.1. NM_017377.5.
XP_006503293.1. XM_006503230.2.
UniGeneiMm.123843.

Genome annotation databases

EnsembliENSMUST00000030266; ENSMUSP00000030266; ENSMUSG00000028541.
ENSMUST00000084325; ENSMUSP00000081352; ENSMUSG00000028541.
ENSMUST00000106421; ENSMUSP00000102029; ENSMUSG00000028541.
GeneIDi53418.
KEGGimmu:53418.
UCSCiuc008ujb.2. mouse.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

b4GalT2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF142670 mRNA. Translation: AAF22220.1.
AB019541 mRNA. Translation: BAA34385.1.
AK165829 mRNA. Translation: BAE38399.1.
CCDSiCCDS18539.1.
RefSeqiNP_001240310.1. NM_001253381.1.
NP_059073.1. NM_017377.5.
XP_006503293.1. XM_006503230.2.
UniGeneiMm.123843.

3D structure databases

ProteinModelPortaliQ9Z2Y2.
SMRiQ9Z2Y2. Positions 94-362.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGT7. Glycosyltransferase Family 7.

PTM databases

PhosphoSiteiQ9Z2Y2.

Proteomic databases

MaxQBiQ9Z2Y2.
PRIDEiQ9Z2Y2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030266; ENSMUSP00000030266; ENSMUSG00000028541.
ENSMUST00000084325; ENSMUSP00000081352; ENSMUSG00000028541.
ENSMUST00000106421; ENSMUSP00000102029; ENSMUSG00000028541.
GeneIDi53418.
KEGGimmu:53418.
UCSCiuc008ujb.2. mouse.

Organism-specific databases

CTDi8704.
MGIiMGI:1858493. B4galt2.

Phylogenomic databases

eggNOGiNOG327897.
GeneTreeiENSGT00760000119140.
HOGENOMiHOG000231027.
HOVERGENiHBG058334.
InParanoidiQ9Z2Y2.
KOiK07967.
OMAiEQPRHFA.
OrthoDBiEOG7060R0.
PhylomeDBiQ9Z2Y2.
TreeFamiTF312834.

Enzyme and pathway databases

UniPathwayiUPA00378.
ReactomeiREACT_308816. N-Glycan antennae elongation.
REACT_346228. Keratan sulfate biosynthesis.

Miscellaneous databases

NextBioi310245.
PROiQ9Z2Y2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Z2Y2.
ExpressionAtlasiQ9Z2Y2. baseline and differential.
GenevestigatoriQ9Z2Y2.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR003859. Galactosyl_T.
IPR027791. Galactosyl_T_C.
IPR027995. Galactosyl_T_N.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR19300. PTHR19300. 1 hit.
PfamiPF02709. Glyco_transf_7C. 1 hit.
PF13733. Glyco_transf_7N. 1 hit.
[Graphical view]
PRINTSiPR02050. B14GALTRFASE.
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Mouse beta-1,4-galactosyltransferase II (beta-1,4-GalT II)."
    Sato T.
    Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  3. "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.
    , 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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.

Entry informationi

Entry nameiB4GT2_MOUSE
AccessioniPrimary (citable) accession number: Q9Z2Y2
Secondary accession number(s): Q3TMP2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2005
Last sequence update: April 30, 1999
Last modified: March 31, 2015
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.