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Protein

Beta-1,4-galactosyltransferase 4

Gene

B4galt4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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.By similarity

Catalytic activityi

UDP-alpha-D-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine.
UDP-alpha-D-galactose + N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide = UDP + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide.

Cofactori

Mn2+By similarity

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi196 – 1961ManganeseBy similarity
Binding sitei224 – 2241UDP-alpha-D-galactoseBy similarity
Binding sitei256 – 2561UDP-alpha-D-galactoseBy similarity
Metal bindingi289 – 2891Manganese; via tele nitrogenBy similarity
Binding sitei301 – 3011N-acetyl-D-glucosamineBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-2022854. Keratan sulfate biosynthesis.
R-MMU-975577. N-Glycan antennae elongation.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT7. Glycosyltransferase Family 7.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-1,4-galactosyltransferase 4 (EC:2.4.1.-)
Short name:
Beta-1,4-GalTase 4
Short name:
Beta4Gal-T4
Short name:
b4Gal-T4
Alternative name(s):
UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 4
UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 4
Including the following 2 domains:
N-acetyllactosamine synthase (EC:2.4.1.90)
Alternative name(s):
Nal synthase
Lactotriaosylceramide beta-1,4-galactosyltransferase (EC:2.4.1.275)
Alternative name(s):
Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase
Gene namesi
Name:B4galt4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:1928387. B4galt4.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1212CytoplasmicSequence analysisAdd
BLAST
Transmembranei13 – 3826Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini39 – 344306LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 344344Beta-1,4-galactosyltransferase 4PRO_0000080543Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi77 ↔ 118By similarity
Disulfide bondi189 ↔ 208By similarity
Glycosylationi220 – 2201N-linked (GlcNAc...)Sequence analysis
Glycosylationi335 – 3351N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ9JJ04.
PaxDbiQ9JJ04.
PRIDEiQ9JJ04.

PTM databases

iPTMnetiQ9JJ04.
PhosphoSiteiQ9JJ04.

Expressioni

Gene expression databases

BgeeiQ9JJ04.
ExpressionAtlasiQ9JJ04. baseline and differential.
GenevisibleiQ9JJ04. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000023482.

Structurei

3D structure databases

ProteinModelPortaliQ9JJ04.
SMRiQ9JJ04. Positions 77-344.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni129 – 1335UDP-alpha-D-galactose bindingBy similarity
Regioni168 – 1703UDP-alpha-D-galactose bindingBy similarity
Regioni195 – 1962UDP-alpha-D-galactose bindingBy similarity
Regioni258 – 2614N-acetyl-D-glucosamine bindingBy similarity
Regioni289 – 2913UDP-alpha-D-galactose bindingBy similarity

Sequence similaritiesi

Belongs to the glycosyltransferase 7 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3916. Eukaryota.
ENOG410ZYYA. LUCA.
GeneTreeiENSGT00760000119140.
HOGENOMiHOG000231027.
HOVERGENiHBG058334.
InParanoidiQ9JJ04.
KOiK07969.
OMAiHTRDKGN.
OrthoDBiEOG7060R0.
PhylomeDBiQ9JJ04.
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.

Q9JJ04-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGCNPPYHLS YRLRLLLLFT LCLTVVGWAT SNYFVGAIQV IPKAKDFMAS
60 70 80 90 100
FHKVIHLGNE ETLGHDGATK KPELANCPSV SPNLRGQSKL VFKPDLTLEE
110 120 130 140 150
IEAENPKVSR GRYHPEECKA LQRVAILIPH RNREKHLIYL LEHLHPFLQR
160 170 180 190 200
QQLDYGIYII HQTGSKKFNR AKLLNVGYLE ALKEENWDCF VFHDVDLVPE
210 220 230 240 250
NDFNLYTCGD QPKHLVVGRN STGYRLRYSK YFGGVTALSR EQFLKVNGFS
260 270 280 290 300
NNYWGWGGED DDLRLRVELH KMKISRPKPD VGKYTMIFHT RDKGNEVNMG
310 320 330 340
RMKLLQQMSR VWKTDGLSSC SYRLLSVEHN PLYANITVDF WTAA
Length:344
Mass (Da):39,700
Last modified:October 1, 2000 - v1
Checksum:i74FA110191A4BCC8
GO

Sequence cautioni

The sequence BAC32433.1 differs from that shown. Reason: Frameshift at position 321. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti238 – 2381L → F in AAF22222 (PubMed:9597550).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF142672 mRNA. Translation: AAF22222.1.
AF158746 mRNA. Translation: AAF80363.1.
AK041692 mRNA. Translation: BAC31035.1.
AK045602 mRNA. Translation: BAC32433.1. Frameshift.
AK050005 mRNA. Translation: BAC34028.1.
AK052013 mRNA. Translation: BAC34832.1.
AK053603 mRNA. Translation: BAC35443.1.
AK085368 mRNA. Translation: BAC39433.1.
BC013492 mRNA. Translation: AAH13492.1.
BC031115 mRNA. Translation: AAH31115.1.
CCDSiCCDS28173.1.
RefSeqiNP_001272722.1. NM_001285793.1.
NP_062778.2. NM_019804.4.
XP_006522462.1. XM_006522399.2.
UniGeneiMm.182377.

Genome annotation databases

EnsembliENSMUST00000023482; ENSMUSP00000023482; ENSMUSG00000022793.
ENSMUST00000114712; ENSMUSP00000110360; ENSMUSG00000022793.
GeneIDi56375.
KEGGimmu:56375.
UCSCiuc007zfi.3. mouse.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

b4GalT4

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF142672 mRNA. Translation: AAF22222.1.
AF158746 mRNA. Translation: AAF80363.1.
AK041692 mRNA. Translation: BAC31035.1.
AK045602 mRNA. Translation: BAC32433.1. Frameshift.
AK050005 mRNA. Translation: BAC34028.1.
AK052013 mRNA. Translation: BAC34832.1.
AK053603 mRNA. Translation: BAC35443.1.
AK085368 mRNA. Translation: BAC39433.1.
BC013492 mRNA. Translation: AAH13492.1.
BC031115 mRNA. Translation: AAH31115.1.
CCDSiCCDS28173.1.
RefSeqiNP_001272722.1. NM_001285793.1.
NP_062778.2. NM_019804.4.
XP_006522462.1. XM_006522399.2.
UniGeneiMm.182377.

3D structure databases

ProteinModelPortaliQ9JJ04.
SMRiQ9JJ04. Positions 77-344.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000023482.

Protein family/group databases

CAZyiGT7. Glycosyltransferase Family 7.

PTM databases

iPTMnetiQ9JJ04.
PhosphoSiteiQ9JJ04.

Proteomic databases

MaxQBiQ9JJ04.
PaxDbiQ9JJ04.
PRIDEiQ9JJ04.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023482; ENSMUSP00000023482; ENSMUSG00000022793.
ENSMUST00000114712; ENSMUSP00000110360; ENSMUSG00000022793.
GeneIDi56375.
KEGGimmu:56375.
UCSCiuc007zfi.3. mouse.

Organism-specific databases

CTDi8702.
MGIiMGI:1928387. B4galt4.

Phylogenomic databases

eggNOGiKOG3916. Eukaryota.
ENOG410ZYYA. LUCA.
GeneTreeiENSGT00760000119140.
HOGENOMiHOG000231027.
HOVERGENiHBG058334.
InParanoidiQ9JJ04.
KOiK07969.
OMAiHTRDKGN.
OrthoDBiEOG7060R0.
PhylomeDBiQ9JJ04.
TreeFamiTF312834.

Enzyme and pathway databases

UniPathwayiUPA00378.
ReactomeiR-MMU-2022854. Keratan sulfate biosynthesis.
R-MMU-975577. N-Glycan antennae elongation.

Miscellaneous databases

PROiQ9JJ04.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JJ04.
ExpressionAtlasiQ9JJ04. baseline and differential.
GenevisibleiQ9JJ04. MM.

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(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Molecular cloning of mouse beta-1,4-galactosyltransferase 4."
    Schwientek T., Clausen H.
    Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Embryo.
  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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Corpora quadrigemina, Hippocampus, Kidney and Thymus.
  4. "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].
    Strain: FVB/N.
    Tissue: Colon and Mammary tumor.

Entry informationi

Entry nameiB4GT4_MOUSE
AccessioniPrimary (citable) accession number: Q9JJ04
Secondary accession number(s): Q8BR54, Q9QY12
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: October 1, 2000
Last modified: June 8, 2016
This is version 125 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

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 one 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.